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A0DTY1

MGPYLSQPNKNKTTTSGEGKSIIFAASEMQGWRNTMEDAHIHVCDLQQDLSIFGVFDGHGGKEVAQFVEKHFIEELQKNKNFKDQKFEDALRETFLKMDELLLTPEGQKEIIQIKGGDDEASYAGCTANVALFHKNVLYVANAGDSRSVLCRNNTNYDMSVDHKPDNYEEKSRIERAGGFVSDGRVNGNLNLSRALGDLEYKRDSKLRSNEQLIIALPDIKKVELNQTDKFLLMGCDGVFETLDHQDLLKFINQKLGNQQITPQLLGRVAEDLLDNLIAPDTSAGTGCDNMTTLIIYLKGK

Enzyme with a broad specificity. H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate Binds 2 magnesium or manganese ions per subunit. Belongs to the PP2C family.

P71148

MTLTSAEKEMSGVLTFFQKEIRGFRTGKAHPALVETVTVEVYGTTMRLSDIASISVSDTRQLLISPYDAGNVSAISKGILAANLNLQPIVEGATVRINVPEPTEEYRREVIKQLKRKSEEAKVSIRNIRRTCNDRLKKDDSLTEDAVKGLEKKIQELTDKFCKQIEELAKQKEAELSSI

Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another. Belongs to the RRF family.

P54390

MQTPVSVNEKKDFIRWFLNHYQLKRRECVWILNYLMSHDSLMEKVHFVEQAEFCPRGIIMSTHCVEEVPFRFYKENVMTTDAEKSFHDIRLNKQQDLFIQLNFRSAYSSPEYAAVLESNPHIPKNLFENKKDQGLAEQILEHAISTFQREKLLKDIDDALDRHDKEAFEQLSRQLNQLT

Belongs to the UPF0302 family.

Q8IZS9

MVCGCSALLPLPNPRPTMPATPNFLANPSSSSRWIPLQPMPVAWAFVQKTSALLWLLLLGTSLSPAWGQAKIPLETVKLWADTFGGDLYNTVTKYSGSLLLQKKYKDVESSLKIEEVDGLELVRKFSEDMENMLRRKVEAVQNLVEAAEEADLNHEFNESLVFDYYNSVLINERDEKGNFVELGAEFLLESNAHFSNLPVNTSISSVQLPTNVYNKDPDILNGVYMSEALNAVFVENFQRDPTLTWQYFGSATGFFRIYPGIKWTPDENGVITFDCRNRGWYIQAATSPKDIVILVDVSGSMKGLRMTIAKHTITTILDTLGENDFINIIAYNDYVHYIEPCFKGILVQADRDNREHFKLLVEELMVKGVGVVDQALREAFQILKQFQEAKQGSLCNQAIMLISDGAVEDYEPVFEKYNWPDCKVRVFTYLIGREVSFADRMKWIACNNKGYYTQISTLADTQENVMEYLHVLSRPMVINHDHDIIWTEAYMDSKLLSSQAQSLTLLTTVAMPVFSKKNETRSHGILLGVVGSDVALRELMKLAPRYKLGVHGYAFLNTNNGYILSHPDLRPLYREGKKLKPKPNYNSVDLSEVEWEDQAESLRTAMINRETGTLSMDVKVPMDKGKRVLFLTNDYFFTDISDTPFSLGVVLSRGHGEYILLGNTSVEEGLHDLLHPDLALAGDWIYCITDIDPDHRKLSQLEAMIRFLTRKDPDLECDEELVREVLFDAVVTAPMEAYWTALALNMSEESEHVVDMAFLGTRAGLLRSSLFVGSEKVSDRKFLTPEDEASVFTLDRFPLWYRQASEHPAGSFVFNLRWAEGPESAGEPMVVTASTAVAVTVDKRTAIAAAAGVQMKLEFLQRKFWAATRQCSTVDGPCTQSCEDSDLDCFVIDNNGFILISKRSRETGRFLGEVDGAVLTQLLSMGVFSQVTMYDYQAMCKPSSHHHSAAQPLVSPISAFLTATRWLLQELVLFLLEWSVWGSWYDRGAEAKSVFHHSHKHKKQDPLQPCDTEYPVFVYQPAIREANGIVECGPCQKVFVVQQIPNSNLLLLVTDPTCDCSIFPPVLQEATEVKYNASVKCDRMRSQKLRRRPDSCHAFHPEENAQDCGGASDTSASPPLLLLPVCAWGLLPQLLR

The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Dimer formed of alpha-2-2 and delta-2 chains; disulfide-linked. Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1 (CACNA1), alpha-2 (CACNA2D), beta (CACNB) and delta (CACNA2D) subunits in a 1:1:1:1 ratio (Probable). Interacts with CACNA1C and CACNB3. Predominantly expressed in certain types of endocrine cells. Present in the Paneth cells of the small intestine. Also present in the erythroblasts in the fetal liver, in the cells of the zona reticularis of the adrenal gland and in the basophils of the pituitary. Present at low level in some brain regions such as the cerebellum (at protein level). The MIDAS-like motif in the VWFA domain binds divalent metal cations and is required to promote trafficking of the alpha-1 (CACNA1) subunit to the plasma membrane by an integrin-like switch. May be proteolytically processed into subunits alpha-2-4 and delta-4 that are disulfide-linked. It is however unclear whether such cleavage really takes place in vivo and has a functional role (By similarity). The disease is caused by variants affecting the gene represented in this entry. In contrast to CACNA2D1 and CACNA2D2, it does not bind gabapentin, an antiepileptic drug. May be due to an intron retention. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the calcium channel subunit alpha-2/delta family. Wrong choice of frame. Truncated N-terminus.

Q8PM31

MLTPPINLHAWIEEHRHLLKPPVGNKCIQQDGFIIMVVGGPNARTDYHYDEGPEWFFQLEGEMVLKVQDEGVARDIPIRAGEVFLLPPKVPHSPQRADGSIGLVIERERLPTEQDGLQWYCPQCNHKLYEAMFPLKNIETDFPPVFDRFYRSPALRTCSQCGHLHPAPERYATVEG

Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate. 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde Binds 2 Fe(2+) ions per subunit. Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. Homodimer. Belongs to the 3-HAO family.

Q11HR0

MKAADVRAMTTDQLDDELANLKKEQFNLRFQKATGQLEKTARVKQIRRDIARIKTIAAEKSAGKKA

Belongs to the universal ribosomal protein uL29 family.

A9VRF1

MSLMLEPNPTQIKEERIYAEMGLTDEEFAMVEKILGRLPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTTGERVLQGPGEGAGIVDIGDNQAVVFKMESHNHPSAIEPYQGAATGVGGIIRDVFSMGARPVALLNSLRFGELQSPRVKYLFEEVVAGIAGYGNCIGIPTVGGEVQFDPCYEGNPLVNAMCVGLINHEDIKKGQAHGAGNTVMYVGASTGRDGIHGATFASEELSESSEAKRPAVQVGDPFMEKLLIEACLELIQSDALVGIQDMGAAGLTSSSAEMASKAGMGIEMYLDDVPQRETGMTPYEMMLSESQERMLIVVKKGREQEIVDLFEKYGLAAVTMGKVTEDKMLRLFHKDEMVAEVPADALAEEAPIYHKPSKEAAYFAEFQQMKMETPKVEDYKETLLALLQQPTIASKEWVYDQYDYQVRTSTIVTPGSDAAVIRVRGTEKGLAMTTDCNSRYIYLDPEVGGKIAVAEAARNIVCSGGEPLAITDCLNFGNPEKPEIFWQIEKSVDGMSEACRKLQTPVIGGNVSMYNERSGEAVYPTPTVGMVGLVHDLKHVTTQEFKQAGDLVYVIGETKAEFGGSELQKMIYGKIFGQSPSIDLDVELKRQKQVLAAIQAGLVQSAHDVAEGGLAVAITESAIGAKGLGATVKLDGEATAVLFAESQSRFVITVKRENKEAFEKAVEAIQVGEVTNTNEVTIHNEENEVLLTANVDEMRKAWKGAIPCLLK

Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL. ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2. Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits. Belongs to the FGAMS family.

Q97U21

MKAIVVNPPNKGVHVKEINDIHRSLTADEVLVKTIANGICGTDRGIVSGLLKFSRPPNGKNDLVLGHENLGQVIDKGPEVHGLGKGDYVVSIVRRGCGKCSNCLAGRQDFCETGEFVEAGIRGLDGFMREFYIDNASYLVKIPDEIVDIAVLLEPLSNVVKAYSELMLVQRRMTWWCKDGSYNCRNVAIVGSGPIGLMFSLMFSIQGFNAFVLNKRDPFPIEAEIVEKSNAKFINTNKDRLPNTIDLLIDTSGYPSAFIPLMSRLNKNSAIILFGTTGGEKFEVNADLITYLVENNILLFGSVNASKKDFENGVNYLTIWKYRYPSVLNRMITRVIKPEQAPEVLYTKPKGEIKTVISWV

Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a non-phosphorylative variant of the Entner-Doudoroff pathway. D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH Binds 2 Zn(2+) ions per subunit. One of the zinc atoms is essential for catalytic activity while the other has a structural function. Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.

Q95TJ0

MGDSDDEYDRKRRDKFRGERESYRTERRDDRRPVGGSAGARDEWAERNPFRGGASAGGGGARHRPDYSDYRGPGARPRYGSPVRDLPPAKRMRPDWGDGDVRANPRFGGYDPYLMQAWNDHYQSMHSAYSHGGHAPPVRESIGGGGGDTLTQPAMLNLKQFLDTQDENISDSEVMRKYTEYKTDFKRQQLNEFFVAHKDEEWFKNKYHPEDSVKRSEEQRGFLQRRTDVFMELLENGTIGSVKVDSSQADALIRVLDTCVIKLEGGTDEDLKVLDEKPKDPVVYERKAEQMQSVKEVEKTINSPKEEMSEADPVSTQRKPVRPVNSDGENWDDDDAENSAPKKELAEDSKDSDSKPEDKQLNKKKTKKRKRNSSDDDSSSSESSSSSDEEKLKEKYDVEDGLRAEQKTEAEKDRQEATKAKQGPQSPKLDEDEGNENTEPKGLDSKINTYEEIDNTLKSPEISSNPIKNTDNGDGSKVEEDGEKPSVGKDKVVETETIDLDKVKDGQPRALHRTSSIFLRNLAPSITRSEIEAVCNRFSGYLRVAIADPLVERRWYRRGWITFMRDVNIKEICWGLNNQRLRDCEMGAIVNRDLSRRVRPANGITAHKQVVRSDIKLCAKIALNLDEKFRLWAEGPKDDSNSARANESSENGSGSTYGFNSQNPVLQNITDYLIEEASAEEEELLGLTGENKDTEGEPIERDEQLISVLDRLVLYLRIVHSVDYYNHCEYPYEDEMPNRCGIIHARGPPPVRVTNNDVQEYIKIYESKLQQFLTKTVPLSDEEIKNLGAKDAETEVEKFVQANTQELAKDKWLCPLSGKKFKGPEFIRKHIFNKHEEKVDEVRKEVQYFNNYLRDPKRPQLPEHPGTSKRPESESARGGGGGYRPPMYPPFSAMPYGFGPPMMGGGRGGRNFPPARRELPLEHQRRLIGYHDLDAPANSDMFD

Acts as a mediator between the cap-binding complex (CBC) and RNA-mediated gene silencing (RNAi). Involved in innate immunity via the short interfering RNAs (siRNAs) processing machinery by restricting the viral RNA production. Also involved microRNA (miRNA)-mediated silencing by contributing to the stability and delivery of primary miRNA transcripts to the primary miRNA processing complex containing drosha and pasha. Interacts with cbp20, Dcr-2 and pasha. Lethality. Belongs to the ARS2 family. Contaminating sequence. Potential poly-A sequence.

Q6KMR8

MGKEKWCYINSGQCSPAFNMALDECLLNWQSEKKMPPTIRFYEWEVPTLTVGYFQRVEKDINMDVVNEKKYGFVRRQTGGRGVLHDKELTYSVIVSEDHPNMPKTVTEAYRVISQGLLDGFKALGLEAYYAVPKTEADRENLKNPRSGVCFDAPSWYEIVVEGRKIAGSAQTRQKGVILQHGSIPLEIDLDELYDLFLFPNERVKERMKSMFASKAVAINELTDRTFTIEQLIKAFEVGFEKGLDVELVPYELTEEQLHEVQTLAKEKYESKEWNYKK

Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domain of GcvH, an intermediate carrier during protein lipoylation. L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein] Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]. Monomer. In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes. The reaction proceeds via an octanoyl-thioester enzyme intermediate. Belongs to the octanoyltransferase LipM family.

Q9UT41

MKDDKGRSDTVNGYYISNSKLSSGFYKRNNANTASNDEKPNLEQNDIPSVTSSGSSTPSSISIEKEIKISKGNVIVKAIRSWSLYVAIIAILLLLVILHSFQGRPQDNGCGKSYVWPSYVRFVDFDERYTRFANKYSLYLYREKSVEESDEPSGIPILFIPGNAGSYKQVRAFAAQAAHVYANAYAEDADGTLNAGKLVPDFFVVDFNEDFSAFHGQTLLDQAEYVNDAIPYILSLYRQNRKISSEYDNEAFPPPTSVILLGHSMGGIVAQATFTMKNYVDGSVNTLITLATPHAMAPLPFDRHLVEFYESIKNFWSQSFLLSPEENSLDDVLLVSIAGGGLDTHVVPEYSSISTFVPPSNGLMVFTSGIPSVWAEIDHQAMAWCENFRRVLIRGIFAIMDARTSKCTVSLNLRKELLSRAYIQGSSFQNDITQISKPIAQYKALDLDLTYVYSEMPGQLLFLNQLGVSYIRHHIFPIPKPTSSIDRFELLTDQPIDLSSSNIKVLACRLDPKIDNTISALLENGNNKVINANCHLLRELVTLLPASTAYTSSPYGGDSFYNYVLPKEKMDDYHFILVSDDSKAPASGFVVGGFSNVSLDPKTIKGSQIELFKSGRKFQFDTKGSISKRFRFPGIQSSIMAYTISVTYELYPGAVPQKEFTPMLKQSIESPFETKYHVNMSNTELSVHGISPFMEFFGKESEKSLTLEFFLNPAIYKSVYVSIQPSYYRSAGRLLMRYRTLLASFPVVVISLAAYNQFRYFHYGSAYLSMSAALEVMIRKGLIKLLFLVSILSIAFSYLISRVELIVADGADPVASWKIFAMMVPKSFWKQNHLLFGLQTAQFWFLAPLLTLMFVGLVITASVIILCVMHLLAFIYGIYLRYKGLTFTGVCQAVKFSFQCLRTRNTRKLDHGEFKKLSSFLSQRNMYYANPSLCYVYGKKHMQARIIGIMLLLLMAMTVVPFQLVYGVALCTQTVTTAKALHLARFCTKSSHYRKKLWDFYNFSCTITILMLLLAPLDFPVLIVWARNLSMHWSIPFPTHHNFFSIIPFILLTEILRTGKMLPRLNDVEYYINNVFLFLLSFYSLIYGAEKPYLIHNVVGLYFFWLLFLYAKNGFFVQNISKWPIIPRMKYFIKHKFLRSIS

Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins. Belongs to the GPI inositol-deacylase family.

F4IYY1

MHSSYSLSKCLVCFTILAIQTLIRRVSSLNRTNAYLNHKCLVIQGKYKRQSEYEENLNYIIDHISSTQKFPDGFTHTSRGEAPNFVTIVFQCRGDSYGSKCRSCYATPISGIRRRCQGYKGAIIWDQCFLDISTINSPPTMIDYENTFSMHNQNNVNEDAESFNKKTRDFLYNLMLKADKPKAGSYAAGEMRLGTKNLYAMVQCALDIFECKVCLEWSINELSKCCHSKKGARFLGTSCNIRYELYPFLST

Belongs to the cysteine-rich repeat secretory protein family. Could be the product of a pseudogene.

Q7VRR2

MIYGIGIDIVEINRIKKIVIRSGDKLAKRILRKSELKLYYSKEYPVRFLSKRFAAKEAVLKAFGTGMSQGITFSQFEIFNDDLGRPMLRFFSQAAVLAKKLDLVRTHVSVSDTGLYACSIVIFEC

Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP] Belongs to the P-Pant transferase superfamily. AcpS family.

P47196

MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVEQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKRQEEETMDFRSGSPSDNSGAEEMEVALAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA

AKT1 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis (PubMed:11882383, PubMed:21620960, PubMed:21432781). This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates (PubMed:11882383, PubMed:21620960, PubMed:21432781). Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported (PubMed:11882383, PubMed:21620960, PubMed:21432781). AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface (PubMed:9632753, PubMed:10400692). Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling (By similarity). Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport (By similarity). AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven (By similarity). AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating the TORC1 signaling pathway, and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Also regulates the TORC1 signaling pathway by catalyzing phosphorylation of CASTOR1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1 (By similarity). AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis (PubMed:12107176). Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis (By similarity). Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity (PubMed:15546921). The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth (By similarity). AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity). Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I) (By similarity). AKT mediates the antiapoptotic effects of IGF-I (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly (By similarity). May be involved in the regulation of the placental development (By similarity). Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro-apoptotic activity. Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53. Phosphorylates palladin (PALLD), modulating cytoskeletal organization and cell motility. Phosphorylates prohibitin (PHB), playing an important role in cell metabolism and proliferation. Phosphorylates CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization. These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation. Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation (By similarity). Phosphorylates PCK1 at 'Ser-90', reducing the binding affinity of PCK1 to oxaloacetate and changing PCK1 into an atypical protein kinase activity using GTP as donor (By similarity). Also acts as an activator of TMEM175 potassium channel activity in response to growth factors: forms the lysoK(GF) complex together with TMEM175 and acts by promoting TMEM175 channel activation, independently of its protein kinase activity (By similarity). Acts as a negative regulator of the cGAS-STING pathway by mediating phosphorylation of CGAS during mitosis, leading to its inhibition (By similarity). ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Three specific sites, one in the kinase domain (Thr-308) and the two other ones in the C-terminal regulatory region (Ser-473 and Tyr-474), need to be phosphorylated for its full activation. Interacts (via the C-terminus) with CCDC88A (via its C-terminus). Interacts with GRB10; the interaction leads to GRB10 phosphorylation thus promoting YWHAE-binding. Interacts with AGAP2 (isoform 2/PIKE-A); the interaction occurs in the presence of guanine nucleotides. Interacts with AKTIP. Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B. Interacts with CDKN1B; the interaction phosphorylates CDKN1B promoting 14-3-3 binding and cell-cycle progression. Interacts with MAP3K5 and TRAF6. Interacts with BAD, PPP2R5B, STK3 and STK4. Interacts (via PH domain) with SIRT1. Interacts with SRPK2 in a phosphorylation-dependent manner. Interacts with TNK2 and CLK2. Interacts with RAF1. Interacts (via the C-terminus) with THEM4 (via its C-terminus). Interacts with TRIM13; the interaction ubiquitinates AKT1 leading to its proteasomal degradation. Interacts with and phosphorylated by PDPK1 (By similarity). Interacts with BTBD10 (By similarity). Interacts with KCTD20 (By similarity). Interacts with PA2G4 (PubMed:16832058). Interacts with KIF14; the interaction is detected in the plasma membrane upon INS stimulation and promotes AKT1 phosphorylation (By similarity). Interacts with FAM83B; activates the PI3K/AKT signaling cascade (By similarity). Interacts with WDFY2 (via WD repeats 1-3) (By similarity). Forms a complex with WDFY2 and FOXO1 (By similarity). Interacts with FAM168A (By similarity). Interacts with SYAP1 (via phosphorylated form and BSD domain); this interaction is enhanced in a mTORC2-mediated manner in response to epidermal growth factor (EGF) stimulation and activates AKT1 (By similarity). Interacts with PKHM3 (By similarity). Interacts with FKBP5/FKBP51; promoting interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1 (By similarity). Interacts with TMEM175; leading to formation of the lysoK(GF) complex (By similarity). Nucleus after activation by integrin-linked protein kinase 1 (ILK1). Nuclear translocation is enhanced by interaction with TCL1A (By similarity). Phosphorylation on Tyr-176 by TNK2 results in its localization to the cell membrane where it is targeted for further phosphorylations on Thr-308 and Ser-473 leading to its activation and the activated form translocates to the nucleus. Colocalizes with WDFY2 in intracellular vesicles (By similarity). Widely expressed. Low levels found in liver with slightly higher levels present in thymus and testis. Binding of the PH domain to phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) following phosphatidylinositol 3-kinase alpha (PIK3CA) activity results in its targeting to the plasma membrane. The PH domain mediates interaction with TNK2 and Tyr-176 is also essential for this interaction (By similarity). The AGC-kinase C-terminal mediates interaction with THEM4. O-GlcNAcylation at Thr-305 and Thr-312 inhibits activating phosphorylation at Thr-308 via disrupting the interaction between AKT1 and PDPK1. O-GlcNAcylation at Ser-473 also probably interferes with phosphorylation at this site. Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for full activity (PubMed:10400692). Activated TNK2 phosphorylates it on Tyr-176 resulting in its binding to the anionic plasma membrane phospholipid PA. This phosphorylated form localizes to the cell membrane, where it is targeted by PDPK1 and PDPK2 for further phosphorylations on Thr-308 and Ser-473 leading to its activation. Ser-473 phosphorylation by mTORC2 favors Thr-308 phosphorylation by PDPK1. Phosphorylated at Thr-308 and Ser-473 by IKBKE and TBK1 (By similarity). Ser-473 phosphorylation is enhanced by signaling through activated FLT3 (By similarity). Ser-473 is dephosphorylated by PHLPP (By similarity). Dephosphorylated at Thr-308 and Ser-473 by PP2A phosphatase. The phosphorylated form of PPP2R5B is required for bridging AKT1 with PP2A phosphatase. Ser-473 is dephosphorylated by CPPED1, leading to termination of signaling (By similarity). Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT1 ubiquitination is critical for phosphorylation and activation. When ubiquitinated, it translocates to the plasma membrane, where it becomes phosphorylated. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome. Ubiquitinated via 'Lys-48'-linked polyubiquitination by ZNRF1, leading to its degradation by the proteasome. Also ubiquitinated by TRIM13 leading to its proteasomal degradation. Phosphorylated, undergoes 'Lys-48'-linked polyubiquitination preferentially at Lys-284 catalyzed by MUL1, leading to its proteasomal degradation (By similarity). Acetylated on Lys-14 and Lys-20 by the histone acetyltransferases EP300 and KAT2B. Acetylation results in reduced phosphorylation and inhibition of activity. Deacetylated at Lys-14 and Lys-20 by SIRT1. SIRT1-mediated deacetylation relieves the inhibition (By similarity). Cleavage by caspase-3/CASP3 (By similarity). Cleaved at the caspase-3 consensus site Asp-462 during apoptosis, resulting in down-regulation of the AKT signaling pathway and decreased cell survival (By similarity). Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily. In light of strong homologies in the primary amino acid sequence, the 3 AKT kinases were long surmised to play redundant and overlapping roles. More recent studies has brought into question the redundancy within AKT kinase isoforms and instead pointed to isoform specific functions in different cellular events and diseases. AKT1 is more specifically involved in cellular survival pathways, by inhibiting apoptotic processes; whereas AKT2 is more specific for the insulin receptor signaling pathway. Moreover, while AKT1 and AKT2 are often implicated in many aspects of cellular transformation, the 2 isoforms act in a complementary opposing manner. The role of AKT3 is less clear, though it appears to be predominantly expressed in brain.

B5ZJZ7

MSSLQPVRGTHDLIGETQLRHAHVVETARRIAGLYGFDEWATPIFEDTRVFARSLGDTSDVVSKEMYSFEDRGGESLTLRPEGTAGVCRALVTNGLTQSLPQKVFYAGPMFRYERPQKGRYRQFHQIGAELIGAAEPLADAEAIAMGRDVLKALGIADETILDLNTLGDTESRAAWRTALIGYFTECRDQLSDDSRARLERNPLRILDSKAPQDRALVADAPRIGAFLTPEAVAFWDGLRSALDLMGVPFRENPGIVRGLDYYGHTAFEFVTERLGAQGTVLAGGRYDGLVAEMGGPRTPAIGWAGGIERLSMLLDATPAAPRPVAVVPMGEGAMGAAILLLQALRAGGVRAEIAYRGNTKKRLERANRIGATHAVLIGEDEVARGVAQVKALDDGSQAELALDAVTPYLAGLAG

ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His) Homodimer. Belongs to the class-II aminoacyl-tRNA synthetase family.

Q03AP4

MANILRKWVESDKREIARLGKIADKVQQYEDEYAALSDEQLKANTPKLKDRLAAGATLDDILPEAFATAREGAKRVLGLFPFRVQIIGGIVLHEGNIAEMKTGEGKTLTATMPVYLNALTGKGVHVVTVNEYLSTRDATEMGELYNWLGLSVGLNLNSKNSDEKREAYNCDITYSTNSELGFDYLRDNMVVYKEQMVQRPLNFAIVDEVDSILIDEARTPLIISGGAEKTTGLYIRADRFVKTLKAETDYKIDWPTKTISLTESGIRKAEKNFGLDNLYDTENTALTHHIDQALRANYIMLKDIDYMVSDGEVLIVDQFTGRAMEGRRYSDGLHQAIEAKEGVQIQDENKTMANITYQNFFRMYTKLAGMTGTAKTEQEEFREIYNMEVISVPTNKPVIRVDSPDVLYPTLDAKFNAVVEDIKARHEKGQPMLIGTVAIESSERLSKQLDEAKIPHTVLNAKNHFKEAEIIMNAGQRGAVTIATNMAGRGTDIKLGPGVTELGGLAVIGTERHESRRIDNQLRGRSGRQGDPGSTQFYLSLEDDLMKRFGSDRIKAMLDRFKVADDDQVIQSRMISRQVESAQKRVEGNNYDTRKNTLQYDDVMREQREVIYKQRQQVINEQETLKPVLMAMINRTITRIVQTHTQGDQKDWNLDALYAWVTANMIDPEKFKRSQLDGKSQDELIGLLAEMAETNFQQKNKQLGDDAQMLEFEKVVILRVVDSAWTDHIDAMDQLRQSIGLRGYGQMNPLVEYQEEGYRMFEEMIASIDDDVTRLFMKAEIRQNIRR

Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2. Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved. Distribution is 50-50. Belongs to the SecA family.

A7MIX7

MAVTKLVLVRHGESQWNNENRFTGWYDVDLSEKGVSEAKAAGKLLKDEGYSFDFAYTSVLKRAIHTLWNILDGLDQAWLPVEKSWKLNERHYGALQGLNKAETAEKYGDEQVKQWRRGFAVTPPALTKDDERYPGHDPRYAKLSEQELPLTESLALTIDRVIPYWNETILPRLKSGERVIIAAHGNSLRALVKYLDNMSEEEILELNIPTGVPLVYEFDENFKPIKHYYLGNADEIAAKAAAVANQGKAK

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Homodimer. Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

B2UDT8

MALMQDFKKFAMRGNVIDLAVGVIIGAAFGKIVDSLVNDLIMPLISRIVGKLDFSNLFIQLAEAPAGVPHTLADLKKAGVPVFAYGNFITVAVNFLILAFIVFLMVRAITRMIDANPPAAPAETPEDIQLLREIRDSLKNKP

Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell. Homopentamer. Belongs to the MscL family.

Q9ET51

MEIGGSGAPPPLLLLPLLLLLGTGLLPASSHIETRAHAEERLLKRLFSGYNKWSRPVANISDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPGDYENVTSIRIPSELIWRPDIVLYNNADGDFAVTHLTKAHLFYDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMKFGSWTYDKAKIDLVSMHSRVDQLDFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFIIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKVTLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPRTHTMPAWVRRVFLDIVPRLLFMKRPSVVKDNCRRLIESMHKMANAPRFWPEPESEPGILGDICNQGLSPAPTFCNRMDTAVETQPTCRSPSHKVPDLKTSEVEKASPCPSPGSCHPPNSSGAPVLIKARSLSVQHVPSSQEAAEGSIRCRSRSIQYCVSQDGAASLTESKPTGSPASLKTRPSQLPVSDQTSPCKCTCKEPSPVSPITVLKAGGTKAPPQHLPLSPALTRAVEGVQYIADHLKAEDTDFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPWLAGMI

After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane permeable to sodium ions. Neuronal AChR is composed of two different types of subunits: alpha and beta. Alpha-4 subunit can be combined to beta-2 or beta-4 to give rise to functional receptors, complexes with beta-2 may be heteropentamers. Interacts with RIC3; which is required for proper folding and assembly. Interacts with LYPD6. The heteropentamer alpha-4-beta-2 interacts with alpha-conotoxins PnIA, GID and MII (By similarity). Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-4/CHRNA4 sub-subfamily.

B8IUY7

MTRKQRRLMLIGVCGAVLAVALGLVLWAMRGTIVFFRSPSEIASQAVAPGVRFRLGGLVQEGSVQRGPDGRVAFVVTDNGATVPVRYQGLLPDLFREGQGVVAEGMLEPGGMFRADTVLAKHDETYMPREVADALKKQGHWQGEAKHPGGTAPAPQTASGEKPALRQQ

Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. Belongs to the CcmE/CycJ family.

C7GLC0

MSVYHLPTLLNPLVNAIFNCPEPERSPLKKLFANLKTRRFILLAPPSEYLLNYHDVKSKLPLHDLCYNAEFINSYILLMTENSYINTNSRDSHYETLDGKTVVIQWKNNVIHALNGFHIRRRLKILETKILPNFNDYFEGAADFIILFIDQPLNCEFVPNDYLQCFHNYEKIPKNAHAMPNLSIDSFQQERSSFENILHIHPARLTQLGQLFSSYRTLAPGDDPSRSIFESIVQQAFDGMKSDSLFKNFSNLYDLIHDYFELNLYDDIWSRLTTHFKGHEVDTEKYKYFSVNQLLTDFYSKDYGEFKLHDITLIERRLHLASKHLQKLALTHSYAEKSKILVETLQKLSGTTEMDSHQLELPDGLNNMTMDADTLISLFVLVVCRSEQKHLKSHLYYLQNFSNNSSSTKFGILGYAVSTLEAVVCYFEDFNKNTGNVAKANTLCEKTKNLLDKLSCENPTNEVEDLATYKDILTYRNEQGQSIPSICITNHKNYILLDILSEYENDFPVEDLLEDETIDGSTLLIESIKAGNLEAAKVLIKIMLFNCTEEELVSYINKTDKYARTVAHYLTHEMDILKSIGNYIDWKRKNSSGQTPLFSIFRSYDQPNYEEMVKTAFDIANTWYRKHNSLFDYLDHTDNKGNSLLHVLKTNIPILLQLTKLDINEENYKGLTPLMVYVKYKRLSNIDAITKDRRLILEKVQNSTFFTCFDYAKDHSVLSKIGERGVKDSLFGLIYFHSLRYHNLNATTNITSVSNAEKPFATTVINMKTIQGLLRSILKDNPFTFLPLNTYIDEISHLNRSDLTIIGKTDVTSLLHQLTNCFNVLLFLKKIPENLFTDEASILYWMRINTSKRNQKPSGKENPKTMEPEEINMIQSFLRFNFDEISSFKASLNILRKVLIFINLKSDDFEDAYKGLNEMGRKLINSEASSAFKGIITNHNMFSELSLAELLENVRFLEQCTIQLSSFVQIILFEKIPNWWKHYGEFLALHKSYRKAFPNMVKPKSASDTSSRAPLGGFIETKREQSEQRLAVQIKASSKMLKELGSEIFVAHERLAEELSNYMEFRKACLDQRSLVAFATTNISVLQECV

Belongs to the UPF0507 family.

Q32ME1

MTNPPGQSVSANTVAESHEGEFGCTLMDLRKLMELRGADAVAQISAHYGGVQEICTRLKTSPIEGLSGNPADLEKRRLVFGKNVIPPKRPKTFLELVWEALQDVTLIILEIAAIISLVLSFYRPPGGDNEICGHIASSPEEEEEGETGWIEGAAILASVIIVVLVTAFNDWSKEKQFRGLQSRIELEQKFSIIRNGQLIQLPVAEIVVGDIAQIKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKTLDKDPMLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGASEEEDDDDKKKKGKKQGAPENRNKAKTQDGVALEIQPLNSQEGLDSEDKEKKIARIPKKEKSVLQGKLTRLAVQIGKAGLIMSVLTVVILILYFVVDNFVIQRREWLPECTPVYIQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMTVVQAYIGGTHYRQIPQPDVFPPKVLELIVNGISINCAYTSKIQPPEKEGGLPRQVGNKTECGLLGFVTDLKQDYQAVRNEVPEEKLFKVYTFNSVRKSMSTVIRKPEGGFRMFSKGASEIMLRRCDRILNKEGEIKSFRSKDRDNMVRNVIEPMASEGLRTICLAYRDFDGTEPSWDIEGEILTSLICIAVVGIEDPVRPEVPDAIAKCKRAGITVRMVTGDNVNTARAIATKCGILTPKDDFLCLEGKEFNSLIRNEKGEVEQEKLDKIWPKLRVLARSSPTDKHTLVKGIIDSTAGEQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTFASLALATEPPTESLLRRRPYGRNKPLISRTMMKNILGHAVYQLLIVFLLVFAGDTLFDIDSGRKAPLNSPPSQHYTIVFNTFVLMQLFNEINARKIHGEKNVFAGVYRNIIFCTVVLGTFFCQIMIVELGGKPFSCTSLTMEQWMWCLFIGIGELLWGQVISAIPTKSLKFLKEAGHGSDKEDISRDTEGMDEIDLAEMELRRGQILWVRGLNRIQTQIRVVKLFHNNHEVAHKPKNRSSIHTFMTQPEYPADDELSQSFLDIQEGNPELVSKAGTSVLLLDGEAASHDNINNNAVDCHQVQIVASHSDSPLPSLETPV

Calcium/calmodulin-regulated and magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell (By similarity). By regulating sperm cell calcium homeostasis, may play a role in sperm motility (PubMed:15078889). ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate Activated by calcium/calmodulin. Interacts with PDZD11. Interacts with SLC35G1 and STIM1. Interacts with calmodulin. Specifically expressed by sperm in testis (at protein level). Male mice lacking Atp2b4 are infertile with severe reduction of sperm motility. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIB subfamily.

A2BWM0

MNVAIVGATGYGGIQSVNLLKDNKNYKISYLGGYKTSGTKWSDNFPFIKLDSNNLIEKISIDRIADKADVALLCLPNGISSTLTRGLLEKGVKVIDLSADYRYKSLEQWKRIYSNEAAKYKRDDDDLCKEAVYGLPEINNKDISKARLIACPGCYPTSALIPLIPFLSQGIIDNEGIIIDSKSGTSGGGRESSQKLLFSECGDGLSAYGLINHRHTSEIEQIASFISGNDIELLFTPHLLPMIRGMHSTIYGRLRDPGLTSSDCRIILENFYRNYSNIRVLPVDIYPSTKWVKNTNEIHLSVKVDNRNGRIILLSVIDNLLKGQTGQAIQNLNLISGLPLNNGLEMINHYP

Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.

Q5YQF7

MFSNIGWGEMMILLVAALVILGPERLPGAVRWTTRSLRQLRDYASGATAQLKEELGPEFDDLRKPLAELNELRGMTPRGLVTKHLLNGDDTVLRDLEKAVPTTADLYGTNSGMPDFPKPKMEKPLARNEHPPIDTDAT

Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation. The Tat system comprises two distinct complexes: a TatABC complex, containing multiple copies of TatA, TatB and TatC subunits, and a separate TatA complex, containing only TatA subunits. Substrates initially bind to the TatABC complex, which probably triggers association of the separate TatA complex to form the active translocon. Belongs to the TatB family.

Q2QXB2

MSFRSIVRDVRDGFGSLSRRGFEVRLVGHRRGRSHSAVHELRDGHAAAAAADVVQSSCWANLPPELLRDVIERLEASEAAWPSRKNVVACAAVCRTWRDMCREIVKNPEFCGKITFPVSLKQPGPRNGAIQCFIKRDKSTQTYNLYLCLSSAVLVESGKFLLSAKRYSRATCTEYTIFMSADNTSRSSNMYIGKLRSNLLGTKFVIYDTQPPCNTANVSQSGKTSRRFYSRKVSPKNPSSTYSIAQVSYELNVLGTRGPRRMNCVMHSIPASSLEAGGTVPCQPDSVLARSLDESFGSISFSKSSIMDRSIRFSSSRYSDISVGGPMVGGQALGDSDESKERPLILRNKAPRWHEQLQCWCLNFKGRVTVASVKNFQLVAATQPAAGAPTPSQPAPPPPPDHDKVILQFGKVAKDMFTMDYRYPLSAFQAFAICLSSFDTKLACE

Ubiquitous. Belongs to the TUB family.

B5Z2K3

MLSKQIPLGIYEKALPAGECWLERLQLAKTLGFDFVEMSVDETDERLSRLDWSREQRLALVNAIVETGVRVPSMCLSAHRRFPLGSEDDAVRAQGLEIMRKAIQFAQDVGIRVIQLAGYDVYYQEANNETRRRFRDGLKESVEMASRAQVTLAVEIMDYPLMNSISKALGYAHYLNNPWFQLYPDIGNLSAWDNDVQMELQAGIGHIVAVHVKDTKPGVFKNVPFGEGVVDFERCFETLKQSGYCGPYLIEMWSETAEDPAAEVAKARDWVKARMAKAGMVEAA

Catalyzes the isomerization of L-xylulose-5-phosphate to L-ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization. L-ribulose 5-phosphate = L-xylulose 5-phosphate Cofactor degradation; L-ascorbate degradation; D-xylulose 5-phosphate from L-ascorbate: step 3/4. Induced by L-ascorbate. Repressed by UlaR. Belongs to the L-ribulose-5-phosphate 3-epimerase family.

A4G9I7

MLLIPAIDLKDGHCVRLKQGDMDQATVFSEDPADMARHWLEQGARRLHLVDLNGAFAGKPKNEPAVKAILQAVREYAEKNGIEEIPVQLGGGIRDLDTIERYLDDGLSYIIIGTAAVKNPGFLHDACSAFPGQIIVGLDAKDGKVATDGWSKLSGHEVIDLAKKFEDYGCESIIYTDIGRDGMMGGVNIEATVKLAQSMTIPVIASGGVHNIKDVEALCAVQEEGIEGVICGRSIYEGTLDLRSAQDRADELSGVGPETEAEAGE

1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. Belongs to the HisA/HisF family.

B9JH59

MVANSGGGLTDADGGPVRHIPVLLKEVLEALAPAPGKLILDGTFGAGGYTSAILAAGADMIALDRDPTAIAAGQSMVAAHAGRLTLIQSQFSQLADHAPQGGLDGVVLDIGVSSMQLDEAERGFSFSKNGPLDMRMSASGVSAADVVNHAKLADLIRIFVFLGEEKQAPRIAHAIEKRRAEAPFVTTRDLAGLIEIVTPRKAKDKIHPATRVFQALRIFVNDELGELAQALFAAERALKPGGRLVVVTFHSLEDRIVKKFFADRSGRAGGSRHMPMVHERLATFDPIGKPMISASDAEAEINPRARSAKLRAGLRTSVQAEAADLSIFDLPNLASLGKLGG

Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine Belongs to the methyltransferase superfamily. RsmH family.

Q99XG3

MTLYLDGETLTIEDIKSFLQQQSKIEIIDDALERVKKSRAVVERIIENEETVYGITTGFGLFSDVRIDPTQYNELQVNLIRSHACGLGEPFSKEVALVMMILRLNTLLKGHSGATLELVRQLQFFINERIIPIIPQQGSLGASGDLAPLSHLALALIGEGKVLYRGEEKDSDDVLRELNRQPLNLQAKEGLALINGTQAMTAQGVISYIEAEDLGYQSEWIAALTHQSLNGIIDAYRHDVHSVRNFQEQINVAARMRDWLEGSTLTTRQAEIRVQDAYTLRCIPQIHGASFQVFNYVKQQLEFEMNAANDNPLIFEEANETFVISGGNFHGQPIAFALDHLKLGVSELANVSERRLERLVNPQLNGDLPAFLSPEPGLQSGAMIMQYAAASLVSENKTLAHPASVDSITSSANQEDHVSMGTTAARHGYQIIENARRVLAIECVIALQAAELKGVEGLSPKTRRKYEEFRSIVPSITHDRQFHKDIEAVAQYLKQSIYQTTACH

L-histidine = NH4(+) + trans-urocanate Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3. Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly. Belongs to the PAL/histidase family.

Q7A6M2

MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKRQKVNMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRFVKEDLNDDFETSLTELEPLEKDAYIVRLVFAGSTTTEPIVSSLSTAYDIKINILEANIKNTKNGTVGFLVLHIPYISSVDFGKFEKELIERQVKMEVLRHG

Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system. ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate ATP + D-methionine(out) + H2O = ADP + D-methionine(in) + H(+) + phosphate The complex is composed of two ATP-binding proteins (MetN), two transmembrane proteins (MetI) and a solute-binding protein (MetQ). Belongs to the ABC transporter superfamily. Methionine importer (TC 3.A.1.24) family.

Q95X69

MTDVEIKAENGSGDASLEPENLRKIFVGGLTSNTTDDLMREFYSQFGEITDIIVMRDPTTKRSRGFGFVTFSGKTEVDAAMKQRPHIIDGKTVDPKRAVPRDDKNRSESNVSTKRLYVSGVREDHTEDMLTEYFTKYGTVTKSEIILDKATQKPRGFGFVTFDDHDSVDQCVLQKSHMVNGHRCDVRKGLSKDEMSKAQMNRDRETRGGRSRDGQRGGYNGGGGGGGGWGGPAQRGGPGAYGGPGGGGQGGYGGDYGGGWGQQGGGGQGGWGGPQQQQGGGGWGQQGGGGQGGWGGPQQQQQGGWGGPQQGGGGGGWGGQGQQQGGWGGQSGAQQWAHAQGGNRNY

This protein is a component of ribonucleosomes. Overexpression gradually increases telomere length, leading to increase lifespan. Binds to telomeres.

A4WWP0

MFNVTKKSIEWGGETLTLETGKVARQADGSVIATLGETSVMANVTFAKAAKPGQDFFPLTVHYQERYYAAGKVPGGFFKREARPSEKETLTSRLIDRPIRPLFVDGFKNEVLLIVTVLSHDLVNEPDIVAMIAASAALTISGVPFMGPIGAARVGYANGEYVLNPDVDDMQKLRENPEQRLDLVIAGTKDAVMMVESEAYELSEAEMLGAVKFGHEAMQPVIDMIIDFAEEAAKEPFDFSPPDYAALYAKVKSLGEAQMRAAFAIREKQERVNAIDAARAAIKAQLSDAELADENLGTAFKKLESSILRGDIINGGARIDGRDTKTVRPIISETSVLPRTHGSALFTRGETQALVVTTLGTGEDEQIIDALHGNSRSNFLLHYNFPPYSVGEVGRFGPPGRREIGHGKLAWRALQAVLPAATDFPYTIRVVSEITESNGSSSMASVCGGSLSMMDAGVPLKAPVAGVAMGLILEDDGKWAVLTDILGDEDHLGDMDFKVAGTENGITSLQMDIKVAGITPAIMEQALAQAKDGRMHILGEMSKALSSANSFSAYAPKIETLTIPTDKIREVIGSGGKVIREIVETSGAKVDINDDGVIKIASNDQAAIKKAYDMIWSIVAEPEEGQIYTGKVVKLVDFGAFVNFFGKRDGLVHVSQIANKRLTHPNEVLKEGQEVKVKLLGFDERGKVRLGMKMVDQETGQEIAPEKKEEATEA

Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n) Belongs to the polyribonucleotide nucleotidyltransferase family.

A5IHQ2

MARLKEFYKKDVVTMMMKRFNYSSVMEVPRILKITLNMGVGEAVGDKKVMNHAIEDMTLISGQKPVVTKARKSIAGFKIREGWPIGCKVTLRRERMYEFLDRLISITLPRVRDFRGLNPKSFDGTGNYSMGIHEQIVFPEIDYDKTDGIRGLDICITTSAKTNEEAKALLEAFNLPLKDKDRK

This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome. Belongs to the universal ribosomal protein uL5 family.

Q0BP04

MANIKAKKYYSYAKINLFLHILNKRTDGYHNLQTWFTFLDLKDQLTFSFNNSREINISSNISIAAKQDNLVYKAIKKFQQSYRVQDIGVDIEIKKNIPMGAGLGGGSSNAATTLIALRDYYLPQLSNEEMIPLAVKLGADVPIFVYGKSAWAEGIGEILYHKDFSPQYALLIKPDIHISTKEFFTSEDLIKSSVLISKDLGFDKSIMHNDFENVFYAKYPEFSQYLKELDSDFRMTGTGSCFYLLSADKNKLEQLTRKINKPLDKWLVKTLNYVY

Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+) Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. Belongs to the GHMP kinase family. IspE subfamily.

Q4PNI0

MGLMLIDWCALALVVFIGLPHGALDAAISFSMISSAKRIARLAGILLIYLLLATAFFLIWYQLPAFSLLIFLLISIIHFGMADFNASPSKLKWPHIIAHGGVVTVWLPLIQKNEVTKLFSILTNGPTPILWDILLIFFLCWSIGVCLHTYETLRSKHYNIAFELIGLIFLAWYAPPLVTFATYFCFIHSRRHFSFVWKQLQHMSSKKMMIGSAIILSCTSWLIGGGIYFFLNSKMIASEAALQTVFIGLAALTVPHMILIDFIFRPHSSRIKIKN

Catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal. Exhibits the highest activity for beta-carotene, followed by beta-cryptoxanthin, beta-apo-4'-carotenal, alpha-carotene, and gamma-carotene in decreasing order, but has no activity on beta-apo-8'-carotenal, beta-apo-12'-carotenal, lutein, zeaxanthin, or lycopene, suggesting that the presence of one unsubstituted beta-ionone ring in a substrate with a molecular weight greater than C35 seems to be essential for enzyme activity. all-trans-beta-carotene + O2 = 2 all-trans-retinal Binds 1 Fe(2+) ion per subunit. The kcat is 4.5-fold higher with beta-carotene than with beta-cryptoxanthin as substrate. Optimum pH is 8.0. Optimum temperature is 40 degrees Celsius. Above this temperature, the enzyme activity decreases significantly, exhibiting 66% of the maximum activity at 50 degrees Celsius. Below 40 degrees Celsius, the enzyme activity decreases with decreasing temperature, exhibiting 15% of the maximum activity at 25 degrees Celsius. The half-lives of the enzyme at 35, 40, 45, 50, and 55 degrees Celsius are 17.6, 15.0, 12.5, 6.1, and 1.5 hours, respectively. Homodimer. Could be used for high retinal production. Belongs to the Brp/Blh beta-carotene diooxygenase family.

B0K5X4

MARLFGTDGVRGIANYDLTPQLAFELGRAGAYVLTHGTHRPKVVVGKDSRISGDMLECALTAGLTSVGAEVISVGIIPTPAVAYLTRLYQADAGVMISASHNPVEYNGIKFFDKDGYKLPDEVEDRIENIIKEKIELPSPIGTGIGTRKEYTNSHRDYIEFLKSTIDGDLKGMKIVIDCAYGASSTIAPILFKELGAEVILHGAEPIGEKINVNCGSTHPEKLQQLVIENGADIGLAFDGDADRLIAVDEKGNVVDGDHIMAICAIDLKKKGRLKNNTVVATVMSNIGFEIALKEQGINLIRTKVGDRYVLEEMTKGGYSIGGEQSGHIIFLDDNTTGDGEITALKLCSISKESGKKLSELAACMITYPQVLINAKVKNELKNAYLEDEEIKREIENLEREMRGEGRVLIRPSGTEPLVRVMVEGKDYDKISQMAKELAELIERKLN

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate Binds 1 Mg(2+) ion per subunit. Activated by phosphorylation. Belongs to the phosphohexose mutase family.

Q8CFL0

MANVQVAVRVRPLSKRETKEGGRIIVEVDDKVAKIRNVKVDSRPESFGDTREKVVAFGFDYCYWSVNPEDPHYASQEVVFRDLGTEVLSGAAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFIREDDCASQPCSRSIKVSFLEIYNERVRDLLKQSNQNKSYTLRVREHPEMGPYVQGLSQHVVTNYQQVIQLLEAGIANRITAATHVHEASSRSHAIFTIHCTQAILQNNLPSETASKINLVDLAGSERADPSYCKDRITEGANINKSLVTLGIVISTLAQNSQVFSSCQSLSSAASSGGDSGVPSTTSGASSGGGPARRQSYIPYRDSVLTWLLKESLGGNSKTIMVATVSPAHTSYSETMSTMRYASNAKNIINKPRVNEDANVKLIRELREEIERLKAVLLNFELIDTLTQHWTEKRNDRQALMEHYGVDINRKRARVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSTCGVVILRPTQGARCTVNGREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLRHQRLKVGEALGSSGSLEWLDLDGDVSASRLGLCPVLRKERRVLEEQCDRDQQPSRHSEIPYRAQPEQQQCHVEALKQQAKEGQSRVQKELELDHTHISQQIKDNQQWLLTEETWLASLRETQQEGNCGEEKELEASVAPDAWLPTVPQTPPSPLVQSQKRVVQPQCSPRHTTRATVWNIRQKKVSFQLERIIKKRRLLEAQRRLEQLSTFFWIQDDGASRAPSWASSSNTSGPGSQRRSRWTTCSSLSLQRLGCRRLPQLHSDFMNWDPSAMSPPVPELTHQMPEKTLSTDCIPPKAGRLGRNSFHSSRWRKFSPARRASTQGTHLTVSHKSVSSQEIESLGKQPCQMSSQGQSTKKQKARDGSRTFIPAAQTRWASVNTKTGWQKEGTCGTYKDPKETTSQSTDLSGLEPAAGHRKVVKTFQAESKPSPSSRASKKHQRVLAARARDIVKTFSRLPHGGPLKNQPRAGDPGTPASFTDSRPIKDPVREEDRDLSDTESSYSVDSLSYIYAKVPKKLLKPEDLQGKWNLPDSENSESDNSQISEDSLAGKGHKSLPENSRGEYSMKDHGHSRARTSASVRGLPMPSDSSLCTQKYRSFSLDSLIDPENRQGEPFLGSADEMPTETFWHLQNATPSSVDQEAMDRPSPTNHRMGVGVNVLLPKSNSFYLDPQFQPPCEQLESEMEASYSEHTNPLRGLQLARESPLLSVDSWFSCDSKVSPSSPSGDIHSLCPSPDIHEIQPHDEKPKHWLSIEEPKPPGTCKLPQSSTEPPCSSDLYATSASDTSKPSVCESQGLLQPGDGGFFQGREMPDMTNQGISEESHNSDMSSVLAPSATSFTQVCSVNKDWAALHQEYLLELSDSGFEAVGEPRPAFPFLEEDSSSLAEASDKVDTQLPTGPGLPRNLDFSSFPVHISKIGHLRAEKDHDSLSAKVESASDLLSTVERMSSNGTYPADIESLTSGSINAQPYTAGNVIPSSMTEAWEVHRASLEGCLQGDRHSVLITSSGQKRAYHNDDTLATEGDCLPQDGALLGKNTKVQPGLLSHNSYQQPLLEEKAASQQCTDGEVAGTRIDACCAFPSGPELFLHSTPWSSSPSSLQPPPLETFYVTKSRDALTETALEIPACREAWVPSPPPREAWGFDHSHQVSQKAHWKNNLPKLSQSQNSKIDSPQQTTTKRPTDLDTGEGTEELGKHSRNMREEENHDSAYSFVAQNRQHLPSTRLKVCECGNQLGILNKEYSLSVHQDEEGASAWHHGSVAFNGSEPKTLLFICDSKASGEEQSLLLPQIQSCGMHSQSPGARSDFIGKIANLDPEKVIPEEAAVSLKSRSLHCLSSPVIVAGGRSPTRRREGRNETGLLREVISKDIQEEFSLPGTQYICERCHLLLCSRERKPTECKAHGQSQEVQSKEEPLEEKQNKRVNNIDEMARLMRSVMQLETGILEIESKHNKHLHASHMPSTELMLQDLEDQEKADHVPTPESSGEHLCFEDQPSFPIQIKDDIFEDSKAREIEVTNATSNNNTQIQKLTGSPFRSREYVQTRESESEHSYPPPGADRLARDTCDSLGKGTALRKPSNISLHSRTMRGLARALPLQPSIERPKKDNELLKASAKFQGQTWALESLEELESMERFQESQIVVVPSGSELEDAKTQGGVEEMTVDRRGSLQEKEDMVSSTQKVPTPSQHWKGTFFSQEAVSPFYYQTGFSAALPHGELSGTQPVHSLSFPRSGLHGSDTKGVSSFEYILEPVMLKTNRNSLATGVGDQDHSGETRSSSPQERASGDVSTTHTPLGGSVMPVVVRASGQAVTSDSTLLNTEDWITVSTSSQEDQEGDFRDTSTGSTTQEALGSEAEATVQKERKNSSLDRISRQAEKRVSFLLQEDSNQGEEERQKAEETSEDQQLPNSAYLTPISELKGPDAEPLLLPDSSINASICLGILAEIRQAKTQRKQLTDLVAEGTVLPYETLQEAEWFSEAAGKPQTQKVKLGWGSTRNDAKAQRLHEASPSAVSADLLADERKAQVSAGSFHHLPNPETDRGPQHHLLASPHIVSELEKRYCTGKPRQFCGASGRSDSSEVIEKRKEASRTKSSVDPLPSDRLLSIPAVEQDGGLGSEKVSVLPSQTSYAPGRILHGQGQLTARETVKGLSFGGKDSILGHQEPRSLDSTHGGGSEKISVTTQKENAVFSECPSVICTVDNAVDLSQSKQDHVQGLDASTGLEETKASPKSGAVHPEAPGNVGAEANIRHPVKWKNVDSGLACGGDSKNPWSTPFLDQRPSLHPSGVREEAPGPCPKECLVFERNTGGSRPLGSSYEEAENRTIPCPHLSGSQPTTAVHACCSHSSTLLCCRDGVLRKGTPWAAAPPDHSLCIVPSTVCEVDGTGECLSRVSLAHDLKHKCGPVDNSIPNPPTTTPVSSPAQNCSCLSTSEMRARCLTHTFARGRSVEGSGEETTGKKVTTAPEDTFPSSPAGMSSEPLRTLKNNSVDENGQASQTMPEPPAVTQGPGTLNSNECVDSKLVIAAQFGHLENTKCCSEKMQPSTKVRGHSCLAPQARFVDMLKPTCHPKIETSWEEEEQQRDQVSGDGKDHAQVRNLVPSNVGGFDGYQTRDGETKSSVPQTFFSDFEAQTEPSQPAAQTHSQHCSDREQLPRSHRHLLPVIAIFSGPKHARYSPRPQFTVVSSSRSLQELNLSVEPPSPTDEDAQRPDSSWRPHLRGYSSEKPISTSLKTQDCSQKALCNLNNSSSNHRPLNPVIPPYPTSSTVSCMPTPEFMTTWMPGALEQAHQGKTDKLSVQGMPENWHSQTDEEMLHFGSSELSPSVLSSCPQGLVHIGWKQYVFGSAVDVSCSQKPQCLIQSNMAQCSSIDNVLEDKKSPFHSHPKTDAQTQDLPNIHSDVENDQSSNELPLVGGSATAQVDEILLLCPPEMGCAGGEASVNTFEQGTQALGSRRHWCCTDVSLQPEARTMSDSELASWTSMHNLSVHLSQLLHSTSELLGSLSHPGVVIKEQNVKRDSLDEAQQALRMDGSASTTVDEGIQTDLALPPLAFQGPEVKSEEVSVILDMMDSGITTVAQEKGDVPVVFQKREAEGAAETPGLHEESTHNKLQSPPLPSPHLRVQKADLGQNFTFMSPPASPDGSPPPSLRPEESCMVVNMPRFSPHSGLSLGAFESTQEPRTQKRLCGSRAVLVDRASSPILTFSASIQELSNPLACVTLSAPSVHPLEDFQKLDDINSDLAVGDPRPPVDNSQATDESGDSQRAESLDREGKSPLGKSSERLLLDNSSSCSPQQSSSLQVSFLGIAPQQLQPKTTTGDQSKLPSPPPRHKNPKLDDSCVSEKVTSVEHGPLRPSQWQGRTTNKDWGSEFMVEPQPNLDQPSSRRGLQPLSPCQISDTTGLQSPAVDPPQACHPVGLLCSGSHMHVAPGPQHYNLRDLPVHNNFNNLYGVQGGPGRGLHEGESLGVRCDSSSVGTHRPPQLSDKYSQNLEWLRLEHIPLQAGVQKLALSVELTEAKLHHGFGETDALLKVLQSGTGEVLAPQEPAVPSSEEFYTRQKKTIETLRRQRAERLHNFRRTRSLSPQKQLGLLPSKDLPTWELDLPSRRQEYLQQLRKHIVDTTRIPEPAPGLARPPSDIELMLQEYRRAREEAKVEIAQARDRLKERTEQEKMRIRQQIISQLLKEEEKLQTLANFSSLYTSSNGSISSGVTSGYNSSPAFSGHLQSLEVSGDSQVPDSQDTWIGDWQDQSTVRNSYLYLTGSSWKSLAHSRRASMGSGCCSASSLSSLGACFSFPYQDLAKHIVSTSMADVMAACSDNLHNLFIRQATDGWNYQGEEQEVQLYYKEFSSTRHGFLGASVVSQPLSQVWAAVSDPTLWPLYHKPIQTARLHQRVTNSISLVYLVCNTTLCELKQLRDFCCVCVEAKEGCLSIMAAQSVYDASMPRPSRKMVRGEILPSAWVLQPVIIEGKEITRVISLVQVELGAPGFPPHLLNSCIKQQPLVVAKLASFLRS

Microtubule-dependent motor protein required for spindle pole assembly during mitosis. Required to stabilize the pericentriolar material (PCM) (By similarity). Interacts with ATAD3A. Localizes throughout the cytoplasm and nucleus during interphase. Localizes to the daughter centriole during mitosis. Disappears in cytokinesis (By similarity). Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.

Q9AL01

MAVTYEKTFEIEIINELSASVYNRVLNYVLNHELDTKNTRLLEVNLLNQLEVAQEVDLFQQPFEELQAIHEYWRSMNQYSKQILNKEKVA

Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the toxic effect of zeta toxin. Part of a postsegregational killing (PSK) system involved in the killing of plasmid-free cells. Continuous synthesis of the epsilon antitoxin is required to counteract the zeta toxin (By similarity). In the presence of the zeta toxin, forms an inactive PezA(2)PezT(2) heterotetramer. Belongs to the epsilon antitoxin family.

B7NKV0

MRSSAKQEELVKAFKALLKEEKFSSQGEIVAALQEQGFDNINQSKVSRMLTKFGAVRTRNAKMEMVYCLPAELGVPTTSSPLKNLVLDIDYNDAVVVIHTSPGAAQLIARLLDSLGKAEGILGTIAGDDTIFTTPANGFTVKDLYEAILELFDQEL

Regulates arginine biosynthesis genes. Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Belongs to the ArgR family.

Q01833

MEGMALYLVAALLIGFPGSSHGALYTLITPAVLRTDTEEQILVEAHGDSTPKSLDIFVHDFPRKQKTLFQSRVDMNQAGSMFVTPTIKVPAKELNKDSKQNQYVVVKVTGPQVALEKVVLLSYQSGFVFIQTDKGIYTPGSPVRYRVFSVDHNMHRMDKTVIVEFQTPEGIVVSSKPVNPSGSIRPYNLPELVSFGTWKAVAKYEHSPEESYTAYFDVREYVLPSFEVRLQPSDKFLYIDGNKNFHVSITARYLYGKKVEGVAFVVFGVKIDDAKKSIPDSLTRIPIIDGDGEATLKRDTLRSRFQDLNQLVGHTLYVSVTVITESGSDMVVTEQGGIHIVTSPYQIYFTKTPKYFKPGMPYELTVYVTNPDGSPAAHVPVVSEAIHSEGTTLSDGTAKLILNTPLNIQSLPITVRTNHGDLPRERQAIKSMTATAYQTQGGSENYLHVAITSTEIKPGDNLPVNFNVRGNANSLNQIKYFTYLILNKGKIFKVGRQPRRDGQNLVTMNLHITPDLIPSFRFVAYYQVGNNEIVADSVWVDVKDTCMGTLVVKGASSRDDRIQKPGAAMKIKLEGDPGARVGLVAVDKAVYVLNDKYKISQAKIWDTIEKSDFGCTAGSGQNNLGVFEDAGLALTTSTNLNTKQRSAAKCPQPANRRRRSSVLLLDSKASKAAQFQDQGLRKCCEDGMHENPMGYTCEKRAKYIQEGDACKAAFLECCHYIKGIRDENQRESELFLARSDFEDELFGDDNIISRSDFPESWLWLTEELTGEPNNQGISSKTVPFYLRDSITTWELLAVGLSPTKGICVAEPYEITVMKDFFIDLRLPYSVVKNEQVEIRAILYNYADEDIYVRVELIYNPAFCSASTEGQRYRQQFPIKALSSRAVPFVIVPLEQGLHDVEVIASVRGELASDGVRKKLKVVPEGERKNIVTIIELDPSVKGVGGTQELTVIANKLDDKVPDTEVETRISVLGDPVAQIIENSIDGSKLNHLIITPSGCGEQNMITMTPSVIATYYLDATGQWENLGVDRRTEAIKQIMTGYAQQMVYKKADHSYAAFTNRASSSWLTAYVVKVLAMASNMVKDISHEIICGGVKWLILNRQQPDGVFKENAPVIHGEMLGGTKGAEPEASLTAFIVTALLESRSVCKEQINILDSSINKATDYLLKKYEKLQRPYTTALTAYALAAADRLNDDRVLMAASTGRNRWEEYNARTHNIEGTSYALLALLKMKKFAEVGPVVRWLIDQKYYGGTYGQTQATVMVFQALAEYEIQMPTHQDLNLDISIKLPEREVPERYSINDRNAVQARTVETKLNEDFTVSASGDGKATMTILTVYNAQLREDANVCNKFHLDVSVENVELNLKQAKGGKAALRLKICTRYLGEVDSTMTIIDISMLTGFFPDAEDLKRLSNGVDRYISKFEIDNNMAQKGTVVIYLDKVSHSEDECLHFKIHKHFEVGFIQPGSVKVYSYYNLDEQCTKFYHPDKETGLLNKICHGNICRCAEETCSLLNQQKKIDLQLRIQKACAQNVDYVYKTKLLRIEEKDGNDIYFMDVLEVIKGGTDRNAQAKARQYVSQRKCQEALNLKLDNDYLIWGLSSDLWPMKDDISYLITKNTWIERWPNEDECQDEEFQNLCDDFAQLSNTLTIFGCPT

C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates. Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. C3 precursor is first processed by the removal of 4 Arg residues, forming two chains, beta and alpha, linked by a disulfide bond. C3 convertase activates C3 by cleaving the alpha chain, releasing C3a anaphylatoxin and generating C3b (beta chain + alpha' chain) (By similarity).

B1MY04

MAKETYVRTKPHVNIGTIGHVDHGKTTLTAAISKVLAEKQGITATDFAEIDNAPEEKERGITINTSHIEYETETRHYAHIDAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVEYLVVFLNKTDLVDDEELVELVEMEVRELLSEYDFPGDDIPVIKGSALKALEGDPEQVKVIEELMDTVDSYIPEPKRETDKPFLMPVEDVFTITGRGTVASGRVDRGVLTTGTEIEIVGLKDEIKKTTVTGIEMFRKTLDEAQAGDNIGALLRGVDRNEIERGQVLAKPGSIKTHKKFKAEVYVLSKEEGGRHTPFFTNYRPQFYFHTTDVTGVVELPAGVEMVMPGDQVTFEIELISPVAIEQGLKFTVREGGHTVGAGTVTEIED

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Monomer. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.

Q9H5T4

MLSSGVETQPVPLDSSMSAVVQELYSELPVSVSRELHADPEPSVIPDVKPGASSSLLSQNRALPLELQRTHVESCCEETYETLDHGSEPGRCGLVDSTAGGSVASGILDRAKRSESMEPKVFRDPGGQAGIIREPSEGAKEDPHQHSTAAEEKTSPSQEDLLMQSSKELSHVDLPEDFLRSKEGNVQITAETLLKSAEVQGMKVNGTKTDNNEGHKNGNVSKDLSAGCGEFQEVDKIMTSDEVSETSTLVTPEPLTFVDPVLTEATPKEKECEELKSCPWLSLPGNSAISNVDNGKEELCKPNLVCEADDNHQQLHGHHNEQPSSTHDSPTATSPLKENSEVSCFTSDLSGPESRTISLENCGFEGGGLLKRSAEKTDSSYFYRGDDQGKNLASREENEERLLIPRSERGGPFLFNAREPEKEISGRCSGEKEPVVSPKENIHNNCIQDSLHTGNSSSLMPNSFTEATEVMLNKNDLKITVHVQGNLTNPEDHKETFTNMSHPGGHSEESSFSSLMQIEEAGQTTPVEPNILSKSFYTKDCNSLVSIQRNLEGNTQLNEASCNDFLFERKSIVSLMPEDQISPVSEVLKPKQGTALLLPSPEFDYRPESEKVIQTSHDDIPLLDEQSIACEMNELSCTNELVVNKVESECVLNQQVSLNSQEHANLPTDSLLHLNKEMPLATGRDAHQSHHPPLEGRADVIADIQTIPIQTKIKDISPPGNQTCGASSNCPTLNIKPVSLERKKEMADSGTKALHSRLRSNKREAAGFPQVVSVIECHSVQSQDISSCHRVRKNVSQENMCSASAAFKSSKISLQVDNSLITKYENAFQHRDHCCQGTGHSVEKSSCKVSYTSQERELDGKETNGSLPGDKIRNKMVAGLLNSGISNKTIHTSSSIKLSEEGLEGKEQDVSKETVFCKYNISDHAIQELNQTVNIPGPEKVLDQSPTVMFSSFKNVKSVETLDQKADEVLDCQSNQNRPDECKSEGQSAKEMLSSDQRETVTEPHGEVNHNQKDLLVSSGSNNSLPCGSPKKCNLKGAFVKMSGCDESTEGMVDIVYTDCSNKLAEGVLDVKASNLLDCGARQEKLAFQEDSRSTLSRRELDAAHTGTTGQDSDFPVTAASTVDFLKIKKSCEENVCRSLKDCEMEKCPDSCAHEMESVADHEPNKRILGRVNLSLNDSHYGQQDKGTSLRETQEMTEGSRLEPNSEFGKESTFGISSKESMSCHDESSVSLRSLKSIEIMPSQENSETNVNSEETDLKNLCKPKDGEMLCENVKDCTVLPEMKEIVSRDWSNSSDRDSVCTCVEKNACKACHPHENSSDRHLPLTVKTDIKVKGEETEEHQRGRLGYLTVGEQSEELVTRETGDGDPVSNISQTHFKCRGILNHAEKQQSPEVLDYMLQKEEKYIRQQKAHTISQQCISSSLLLDDAQNQNQPKADKDESTMINEITLAKLAKDSIVAQTQKLEDQKEERLHHPLRKDTESCTSPCLLGAPRKAQDPSSAGCDQIHGAFAKKGVLPLKKQPHRTCKKVSYQEQIIVGRKIGKIRSSAFLKSSSNPIPTKAHRLLSLCTLSAPTRLEPETAPTKSLVSHIPKQMSTPCHPLRSLNFRKTTKESALLNKLSILASKLAPAMKTQKLRYRRCSSELLPMAKSYKRLRYKRLLDGFSSSTEQLNPYLAASGWDKRPNSKPMALYSLESIKMTFIDLSNKMPSLLFGSEIFPVSFHVKSSSSDCTTESSRTFPEHCAPARLALGEALQCPSQPPKWTFSFFLSHGCPGMATFREDTGVHSQTHTQAPPQPPAPLQDYGGTAIVQTRADCSVLGLHTLLALCSPGCYRIWTKKRSFSSHMPTMQRLFMTQFTQGLKGLRSPASIADKVFCSLPYSVGRVLSIWSQHGPSVCSFEISSLHSPHCKRQPSLGTTSSHTMLPYVPLPGMEATYNTSGSQTRLEPPFPALVPKSCLVAESAVSKLLLSASEFQVRGLDELDGVKAACPCPQSSPPEQKEAEPEKRPKKVSQIRIRKTIPRPDPNLTPMGLPRPKRLKKKEFSLEEIYTNKNYKSPPANRCLETIFEEPKERNGTLISISQQKRKRVLEFQDFTVPRKRRARGKVKVAGSFTRAQKAAVQSRELDALLIQKLMELETFFAKEEEQEQSSGC

Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus.

Q6C7X8

MSDSEVEYDIAGSLNPGVDSEDDYSSGSESDSEIPDIIEDSEDETGPQQGEPGTMTFPNLELSDDDDDDDDDDEGRKKKKKKTDDSVESYFGAPQTGKKSSGSFAGLGLSQLVLKNIARKGFKQPTPIQRKTIPLVLEGKDVVGMARTGSGKTAAFVLPMLEKLKVHSAKVGARAVILSPSRELALQTLKVVKDFSAGTDLRLAMLVGGDSLEEQFKMMMSNPDIIIATPGRFLHLKVEMELSLASVEYICFDEADRLFELGFGEQMNELLASLPSNRQTLLFSATLPKTLVEFAKAGLHDPILVRLDAETKLPEHLEMTFFAVKENQRDACLAFILKEVIQMPFATPEQLKELERLDERAIDDGERDEDRKQKRPKFKKERLPPAHQLPSEKSTIVFCPTKHHVEYVIVLLQTLGYAVSYIYGTLDQHARKNQLYRFRTGKTSILVVTDVAARGIDVPVLANVINYSLPPSPKVFIHRVGRTARAGNRGWAYSIIKDNDIPYLLDLEVFLGRKLLTPRLFKQQNPDPSAEPDYVNTLTIGAPPRQALEIHGEELAQMVKDSYELQQLSEVAVKGERMYNKTKGSASQESAKRSKQIMALGWDDHHLMFGEDGESAKDALLARLGQKRIRETVFEFRKSKTTSGAEMMATRRAQLAPIQRRAAEKRAIQEKERLAGLVHSQDAEIARSTEEDMATEADLTGFTTEEDLRAAKKAQKSKKRSFRDSENFMSHYAPTNDDKGYAVGNFAGAASNATFDLINDGSEMQQKQGMKWDKKKGKFINAGSEGGKKFIRGEGGQRIAASFRSGRFDKWKAAHKVGNLKVGALEESGPATKRVLSAREFKHNKNEAPKRADKYRDDFHKQKTKVAAAKEDGRIQKPQPKSELKSTADVRKSRILAEKRKQKNARPSRGGRGGGRGGRGGGRGGR

ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs. ATP + H2O = ADP + H(+) + phosphate The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis. Belongs to the DEAD box helicase family. DDX54/DBP10 subfamily.

Q1RGM8

MATKKAGGSSRNGRDSAGRRLGVKKADGQYVIPGNIIVRQRGTKIHPGVNVGIGKDHTIFALTSGRVEFLTKRDHKIVNVTEIASA

Belongs to the bacterial ribosomal protein bL27 family.

Q47921

MSDERIRQIAFYGKGGIGKSTTSQNTLAAMAEMGKRILIVGCDPKADSTRLILHCKAQTTVLHLAAEKGAVEDLELEEVVINGFRNIRCVESGGPEPGVGCAGRGIITAINFLEENGAYQDLDFVSYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMAMFAANNISRGILKYAHSGGVRLGGLICNSRKTDREWDLISELARRISTQMIHFVPRDNIVQHAELRRMTVNEYAPDSNQANEYRTLATKIIDNEFMAVPTPLEMDELEELLIEFGILESDEQVKQLTETDKAAKESEKKQEDAEGEA

The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein. 16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate Binds 1 [4Fe-4S] cluster per dimer. Homodimer. The reversible ADP-ribosylation of Arg-104 inactivates the nitrogenase reductase and regulates nitrogenase activity. Belongs to the NifH/BchL/ChlL family.

P57957

MPKLRSATSTQGRNMAGARALWRATGMKENDFGKPIIAVVNSFTQFVPGHVHLKDMGQLVAREIEKAGGVAKEFNTIAVDDGIAMGHGGMLYSLPSRDLIADSVEYMVNAHCADAMVCISNCDKITPGMLMAALRLNIPCVFVSGGPMEAGKTKLSDKIIKLDLVDAMIQGANPNVSDEDSAQIERSACPTCGSCSGMFTANSMNCLTEALGLSLPGNGSCLATHADRKQLFLDAGKQVVELCKRYYEQEDDSVLPRSIANKKAFENAMSLDIAMGGSTNTVLHLLAAAQEAEVDFTMADIDRLSRQVPCLSKVAPNTQKYHMEDVHRAGGIMAILGELDRANLLHNDTRTVLGMSLAEQIAKYDIVLTKDEAVHKFFRAGPAGIRTTEAFSQDCRWDTVDDDRENGCIRSKTFAYSQDGGLAMLSGNLAMDGCIVKTAGVDESILKFTGDAIVFESQEDAVAGILGGKVQAGHVVVIRYEGPKGGPGMQEMLYPTSYLKSMGLGKACALLTDGRFSGGTSGLSIGHCSPEAAAGGLIGLVKDGDKIEIDIPNRSIQLCVAEEELAQRRAEQDKLGWQPVNRQREVSFALKVYGHFATSADKGAVRDKTKI

Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively. (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O (2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2-oxopentanoate + H2O Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor. Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 3/4. Homodimer. Belongs to the IlvD/Edd family.

A1KIC8

MNSPLAPVGVFDSGVGGLTVARAIIDQLPDEDIVYVGDTGNGPYGPLTIPEIRAHALAIGDDLVGRGVKALVIACNSASSACLRDARERYQVPVVEVILPAVRRAVAATRNGRIGVIGTRATITSHAYQDAFAAARDTEITAVACPRFVDFVELGVTSGRQVLGLAQGYLEPLQRAEVDTLVLGCTHYPLLSGLIQLAMGENVTLVSSAEETAKEVVRVLTEIDLLRPHDAPPATRIFEATGDPEAFTKLAARFLGPVLGGVQPVHPSRIH

Provides the (R)-glutamate required for cell wall biosynthesis. L-glutamate = D-glutamate Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the aspartate/glutamate racemases family.

B2SBS0

MSIFRFFTRQQASAPQARERLQVLLAHERASYGGQSDLVAVLREEILAVIAKHIKVDREKVSVKMDRGDQVSTLEVDIELPLTAKKGRAA

Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell. Belongs to the MinE family.

Q5GWS1

MARKINCYIKLQVKAGQANPAPPVGPALGQRGLNIMEFCKAFNAATSKLEPGLPTPVIITAYSDRTFTFVTKSTPASVLLKKAAGVTSGSKRPNTDKVGKVTRKQLEEIVKVKEADLTAADLEAAVRTIAGSARSMGLTVEG

Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex. One or more lysine residues are methylated. Belongs to the universal ribosomal protein uL11 family.

A4IZ92

MKALAKLKKQPGIWIINDAPIPEYGYNDVLIKIKKTAICGTDLHIYNWDKWSQNTIPVPMITGHEFAGEVVAKGDGVTSVDIGDRVSGEGHLVCGQCRNCRAGKRHLCRKTIGIGVNVQGAFAEYLVMPAVNVFKIPDSISDDIASTFDPMGNAIHTALSFNLTGEDVLITGAGPIGLMAVKIARFCGARRIVITDINEYRLQMARDFGATVALNVAPFKNQDELVKQMRKVMSDIGMTEGFDVGLEMSGINSAISMMLDVMNHGGKLSLLGISAGDISVDWGAILFKGLTLKGIYGREMFETWYLMTSMLQAGMDMNPIITHRLHIDEFQKGFEIMKSGQCGKVILDWSS

Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate. L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) + NADH Binds 2 Zn(2+) ions per subunit. Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2. Homotetramer. Belongs to the zinc-containing alcohol dehydrogenase family.

Q2RPU7

MAVYTDVSDDDLTTFLEGYDIGRLRACKGIAEGVENSNFLLVTDRGPHILTLYEKRVNPDDLPFFLGLLRHLAARDIPCPQPVAGRDGAVLHTLCDRPAAIVTFLDGVWPKRPEVRHCAQLGEALARLHLAGGDYAPTRRNSLSVDGWRPLFDAAAERADSVKPGLRAELETELDALEALWPHDLPTGIIHADLFPDNVFFVDDTLSGLIDFYFACDDFLAYDLAVCLNAWCFEGEREFNVTKARHMLTRYEKVRPLSDAEFAALPLLARGAAMRFLLTRLYDWLNTPPGAMVRPKDPMEYYHKLAFHRAVSGPGAYGLSR

ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5. Belongs to the pseudomonas-type ThrB family.

Q8KF03

MNLKPLADRVIVKPAPAEEKTKGGLYIPDTGKEKPMYGEVVAVGPGKVSDAGQVVAMQVKAGDKVLYGKYSGTEVHVEGEDYLIMRESDIFAILG

Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel. Heptamer of 7 subunits arranged in a ring. Interacts with the chaperonin GroEL. Belongs to the GroES chaperonin family.

A7J3A7

MAYRKRGARREANLNNNDRMQEKNDEKQDSNKIQLSDKVLSKKEEIVTDSHEEVKITDEVKKSTKEESKQLLEVLKTKEEHQKEIQYEILQKTIPTFEPKETILKKLEDIKPELAKKQTKLFRIFEPKQLPIYRANGERELRNRWCWKLKKDTLPDGDYDVREYFLNLYDQVLTEMPDYLLLKDMAVENKNSRDAGKVVDSETASICDAIFQDEETEGAVRRFIAEMRQRVQADRNVVNYPSILHPIDYAFNEYFLQHQLVEPLNNDIIFNYIPERIRNDVNYILNMDRNLPSTARYIRPNLLQDRLNLHDNFESLWDTITTSNYILARSIVPDLKELVSTEAQIQKMSQDLQLEALTIQSETQFLTGINSQAANDCFKTLIAAMLSQRTMSLDFVTTNYMSLISGMWLLTVIPNDMFIRESLVACQLAIVNTIIYPAFGMQRMHYRNGDPQTPFQIAEQQIQNFQVANWLHFVNNNQFRQAVIDGVLNQVLNDNIRSGHVINQLMEALMQLSRQQFPTMPVDYKRSIQRGILLLSNRLGQLVDLTRLLAYNYETLMACITMNMQHVQTLTTEKLQLTSVTSLCMLIGNATVIPSPQTLFHYYNVNVNFHSNYNERINDAVAIITAANRLNLYQKKMKAIVEDFLKRLYIFDVSRVPDDQMYRLRDRLRLLPVEIRRLDIFNLILMNMDQIERASDKIAQGVIIAYRDMHLERDEMYGYVNIARNLDGFQQINLEELMRSGDYAQITNMLLNNQPVALVGALPFITDSSVISLIAKLDATVFAQIVKLRKVDTLKPILYKINSDSNDFYLVANYDWVPTSTTKVYKQVPQQFDFRNSMHMLTSNLTFTVYSDLLAFVSADTVEPINAVAFDNMRIMNEL

Inner capsid protein that self-assembles to form an icosahedral capsid with a T=2 symmetry, which consists of 120 copies of VP2, with channels at each of its five-fold vertices. This capsid constitutes the innermost concentric layer of the viral mature particle. It encapsidates the polymerase VP1, the capping enzyme VP3 and the genomic dsRNA, thereby defining the core. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels formed by VP2 N-termini. VP2 is required for the replicase activity of VP1 polymerase. Probably recruits a copy of a VP1-VP3 complex, potentially along with a segment of plus-strand RNA, as a decamer of VP2 assembles. May activate the autoinhibited VP1/RNA complex to coordinate packaging and genome replication. Homodecamer; each decamer is made up of two conformers of VP2, called VP2A and VP2B. Interacts with a VP1-VP3 complex. Interacts with the intermediate capsid protein VP6. Interacts with NSP5. Interacts (via N-terminus) with NSP2. Inner capsid protein. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. The N-terminus binds RNA. It is necessary for encapsidation of VP1 and VP3. The N-termini of 10 VP2 molecules form a cylindrical hub underneath each 5-fold axis of the inner capsid. Sumoylated with SUMO1 and SUMO2. Sumoylation of viral proteins seems to have a positive role on viral replication. Belongs to the rotavirus VP2 family.

Q9RX68

MSQTDVLDLYKQAGAFHEGRFLLASGRQSPYFMQSTTLLQHPRALMELGGLMSQKILDAGLKPDFIVGPAMGGVTLAYEVARQLSETLPDVRAIFAEKDGSGGMKLREAFAVRPGETFVAVEDVLTTGGSLLRAVRAVEGQGGQCIGLCCIIDRRQQTGPLSGYPLMSLKELYFDTYASHEVPGWLAERPLQEI

Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.

B0TW17

MSKEKALESALSQIEKQFGKGSIMRLGDQETAHDIDVIPSGIIALDVALGIGGYPKGRIIEIYGHESSGKTTLTLLAIAQCQKQGGVAAFIDAEHALDPKYAKLLGVDVDNLIVSQPDTGEQALEIADMLVRSGGIDIVVIDSVAALTPKAEIEGDMGDSHMGLQARLMSQALRKLTANIKRSNTLVMFINQIRMKIGVMFGNPETTTGGNALKFYASVRLEVRKGGSIKDGVDVSGNEIKVKIVKNKVAPPFKQAEFELIYGEGISLEAELIDLGAKYEIIEKSGAWYSYKGKKIGQGKEKSKEYLKENTLERDEIEKALLQLLLPQKYAVQEQVQPEPKSKQSKSKQASEQATQDELI

Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. Belongs to the RecA family.

B0U6B6

MSNVNMDFEQAGELKIGQVGIATLRIRTLNVPRLIQEMSDRVTRAPKLFRRTAVILDFGELPHPPDLTTAKALVDGLRAANVLPVAIAYGTNEIDLLSQQLGLPLLSKFRAHYERQEVAAPPPQSTPPINTGRIQHTTVRSGQQLYAEHCDLTILNTVGAGAEVIADGNIHIYGTLRGRAMAGARGNAEMRIFCRDFQAELIAIAGRYKVLDDIPTELRGKAVQVWLEQNQIKIAALD

Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. Interacts with MinD and FtsZ. Belongs to the MinC family.

O26820

MEMMVLLSQEHPELPSAELRSVLMSEGIDFSVIESGSGYEVIDAPRSTWKILKKRLAYAHEISEVIGYAAADDLDDAAEEIDWSKYVRESFAVRIRKLCGDVDSRTLERTIGAIIKEDTGLKVDLEKPWTLIRPVLINDRFILTRRLAVISKEHFNQARPHKRPFFYPGSMSPKLARCMVNLSGVKAGDRILDPFCGTGGILIEAGLMGVRVVGADIDWRMVEGTRENLQHYGITDFEVIRSDARDLRLDEKVDAIVTDPPYGISASTAGEKSEKLYREFLDSAHSNLAEGGMICMAAPHYLDLESLIDERFSIRERYSMRMHRSLTRVIRVIERV

Catalyzes the adenosylmethionine-dependent methylation of the exocyclic amino group (N(2)) of guanosine at position 10 of various tRNAs. Acts via a two-step process that leads to the formation of either N(2)-monomethyl (m(2)G) or N(2)-dimethylguanosine (m(2)(2)G) (By similarity). guanosine(10) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(10) in tRNA + 2 S-adenosyl-L-homocysteine Monomer. Belongs to the methyltransferase superfamily. Trm-G10 family.

Q93DY6

MKFENCRDCREEVVWWAFTADICMTLFKGILGLMSGSVALVADSLHSGADVVASGVTQLSLKISNKPADERYPFGYGNIQYISSAIVGSLLLIGASFLMYGSVVKLISGTYEAPSIFAALGASVTVIVNELMYRYQICVGNENNSPAIIANAWDNRSDAISSAAVMVGVIASVIGFPIADTIAAIGVSALVGHIGLELIGKAVHGLMDSSVDTELLQTAWQIATDTPLVHSIYFLRGRHVGEDVQFDIRLRVDPNLRIKDSSMVAEAVRQRIQDEIPHARDIRLFVSPAPAAVTVRV

Plays a dual, essential role in magnetosome formation; required for magnetosome vesicle formation as well as biomineralization (Probable) (PubMed:29243866). Requires heterodimerization with MamM for stability (PubMed:22007638). Probably binds and transports iron (Probable). One of 7 genes (mamLQBIEMO) able to induce magnetosome membrane biogenesis; coexpression of mamLQRBIEMO in a deletion of the 17 gene mamAB operon restores magnetosome vesicle formation but not magnetite biosynthesis (PubMed:27286560). Forms homodimers via its C-terminal domain, may form higher order multimers that are sensitive to reducing agent. Probably interacts with MamE (Probable). Interacts with MamM via their C-terminal domains (PubMed:22007638, PubMed:29243866). Purified magnetosomes remain attached to each other (PubMed:11571158). Tagged protein has several locations; most is in 1-3 dots in the cell, also seen as patchy membrane localization, while about 20% localizes with magnetosomes in a straight line running through the center of the cell (PubMed:22007638). Upon induction in a non-magnetic deletion mutant this protein is first found in the cell inner membrane, then collects into foci along the entire cell length from which magnetosome vesicle formation and subsequent clustering occur (at protein level). Part of the probable 17 gene mamAB operon. The C-terminal domain (CTD) is probably responsible for hetero- and homodimerization and binds 1 Fe cation per subunit (Probable). The CTD assumes a V-shaped, dimeric metallo-chaperone-like fold (By similarity). The most severe single mam gene deletion. Single gene disruption has no accumulation of magnetite, no intracellular magnetosome vesicles form, wild type levels of MamM, mislocation of MamC in 1-3 foci, MamI mislocalized in 1 to a few patches (PubMed:22007638, PubMed:27286560, PubMed:29243866). Deletion of approximately 80 kb of DNA, including this operon, leads to cells that are non-magnetic, lack internal membrane systems, grow poorly, have reduced mobility and take-up and accumulate iron poorly (PubMed:13129949). This bacteria makes up to 60 cubo-octahedral magnetosomes of about 45 nm in diameter which contain membrane-bound crystals of magnetite (Fe(3)O(4)). Expression of just the minimal mamAB gene cluster (MGMSRv2__2365 to MGMSRv2__2381), including this gene, is sufficient to form a minimal magnetosome chain with small magnetite particles. Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. A sense of direction - Issue 217 of September 2019

E7KDX7

MGFEWGFKPSSKITQSTVSSQGTGNVMIPTAGVKQKRRYANEEQEEEELPRNKNVMKYGGVSKRRPQPGSLIRGQPLPLQRGMELMNKNQLQQLLVDLMTKHPEIQQSVHTRVIGLDFSIQKCLDMLKQKSEAVYQSIPYNRSYESNKLDDYAFVRMKPQILEFLNCLVDFILDNIPPRLENLHASLKFLDICTELVIKLPRFELASNNYYYDKCIEQLSHVWCTLIEHVARDRIILLADNSSVWKSHMTRLQVYNEHSNGLLERPLQLFKSLDMGSPSAASSSTLSLQESIIYHHDTMTANENNNNSGSAATDSPFN

Involved in ubiquitin-mediated protein degradation. Regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates. Targets proteasomes to the nucleus and facilitates the degradation of nuclear proteins (By similarity). Binds the proteasome. Interacts with karyopherin SRP1 and Proteasome subunit RPN11. Belongs to the cut8/STS1 family.

O84510

MADLIMGIDPGTLVCGYALIKVENRYHIHPHSFGKVKLSQKLALAHRYKQLFTEISTILQQESPKAVVLETQYVHKNPQSTIKLGMARGVLLLAASLQDVPVFEYAPNTAKKAAVGKGNASKKQVQLMVSKLLRVPDLLAEDNEDIADAFALAMCHAHLAPYQDLKKTLV

Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group (By similarity). Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction). Binds 1 Mg(2+) ion per subunit. Belongs to the RuvC family.

Q3MC10

MTSGNNINQPVTYPIFTVRWLAVHTLAVPTVFFLGAIASMQFIQR

This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. With its partner (PsbE) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids. Heterodimer of an alpha subunit and a beta subunit. Cyanobacterial PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. Belongs to the PsbE/PsbF family.

D3DM03

MSQVQEQHISESQLQYGNGSLMSTVPADLSQSVVDGNGNGSSEDIEATNGSGDGGGLQEQAEAQGEMEDEAYDEAALGSFVPIEKLQVNGITMADVKKLRESGLHTAEAVAYAPRKDLLEIKGISEAKADKLLNEAARLVPMGFVTAADFHMRRSELICLTTGSKNLDTLLGGGVETGSITELFGEFRTGKSQLCHTLAVTCQIPLDIGGGEGKCLYIDTEGTFRPVRLVSIAQRFGLDPDDALNNVAYARAYNADHQLRLLDAAAQMMSESRFSLIVVDSVMALYRTDFSGRGELSARQMHLAKFMRALQRLADQFGVAVVVTNQVVAQVDGGMAFNPDPKKPIGGNIMAHSSTTRLGFKKGKGCQRLCKVVDSPCLPEAECVFAIYEDGVGDPREEDE

Required both for recombination and for the repair of DNA damage caused by X-rays. Its function may be modulated by interaction with other repair proteins. RAD52 interacts directly with RAD51, via its C-terminus. Forms a nucleoprotein filament with DNA as an early intermediate in recombination. Part of a repair/recombination complex that includes RAD51, RAD52 and RAD54. Interacts with HED1, RDH54 and SAW1. Localizes as foci on meiotic chromosomes. RAD51 is cell cycle regulated, peaking around the G1-to-S transition. By X-rays. Present with 6960 molecules/cell in log phase SD medium. Belongs to the RecA family. RAD51 subfamily.

Q9GF45

MEKFQGYLEFDGARQQSFLYPLFFREYIYVLAYDHGLNRLNRNRSIFLENADYDKKYSSLIVKRSILRMYEQNRLIIPTKDLNQNPFFGHTNIFYYQIISVLFAVIVEIPFSLRLGSYFEGKKFKKSYNLQSIHSIFPFLEDKLSHFNYVLDVLIPYPIHLEILVQILRYWVKDASSLHFFRFCLYEYCNWKNFDIKKKCILNPRFFLFLYNSHVCEYESIFFFLRKRSSHLRSTSYEVLFERILFYGKVQHFLKVFVNNFPAIPGLLTDPFLHYVRYHGKCILATKDTPLLMNKWKFFFVYLWQCYFSVWFQSQKVNINQLSKDNLEFLGYLSSLRLNPLVVRSQMLENSFIIDNVRIKLDSKIPISSIILSLAKDKFCNVLGHPISKATWTDSSDSDILNRFVRICRNISHYYSGSSKKKNLYRIKYILRLCCVKTLARKHKSTVRAFLKRLGSGLLEEFLTGEDQVLSLIFPRSYYASKRLYRVRIWYLDILYLNDLVNHE

Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. Belongs to the intron maturase 2 family. MatK subfamily.

Q9QXL0

MNWRFVELLYFLFVWGRISVQPSRQEPAGTDQHVSKEFDWLISDRGPFHHSRSYLSFVERHRQGFTTRYKIYREFARWKVRNTAIERRDLVRHPVPLMPEFQRSIRLLGRRPTTQQFIDTIIKKYGTHLLISATLGGEEALTMYMDKSRLDRKSGNATQSVEALHQLASSYFVDRDGTMRRLHEIQISTGAIKVTETRTGPLGCNSYDNLDSVSSVLLQSTESKLHLQGLQIIFPQYLQEKFVQSALSYIMCNGEGEYVCQNSQCRCQCAEEFPQCNCPITDIQIMEFTLANMAKAWTEAYKDLENSDEFKSFMKRLPSNHFLTIGSIHQHWGNDWDLQSRYKLLQSATEAQRQKIQRTARKLFGLSVRCRHNPNHQLPRERTIQQWLARVQSLLYCNENGFWGTFLESQRSCVCHGSTTLCQRPIPCIIGGNNSCAMCSLANISLCGSCNKGYKLYRGRCEPQNVDSERSEQFISFETDLDFQDLELKYLLQKMDSRLYVHTTFISNEIRLDTFFDPRWRKRMSLTLKSNKNRMDFIHMVIGMSMRICQMRNSSLDPMFFVYVNPFSGSHSEGWNMPFGEFGYPRWEKIRLQNSQCYNWTLLLGNRWKTFFETVHIYLRSRTRLPTLRNETGQGPVDLSDPSKRQFYIKISDVQVFGYSLRFNADLLRSAVQQVNQSYTQGGQFYSSSSVMLLMLDIRDRINRLAPPVAPGKPQLDLFSCMLKHRLKLTNSEIIRVNHALDLYNTEILKQSDQMTAKLC

Inhibits cell proliferation by negative regulation of the G1/S transition. Mediates cell death which is not of the classical apoptotic type and regulates expression of components of the plasminogen pathway. Expressed in brain. Weakly expressed in embryonic stem (ES) cells and in ES-derived neural stem cells (NSCs). Expressed from 9.5 dpc. Up-regulated upon differentiation into neuronal cells in the presence of retinoic acid and BDNF. Up-regulated upon differentiation into astroglial cells. Belongs to the BRINP family.

Q7C4D6

MAGINRAGPSGAYFVGHTDPEPVSGQAHGSGSGASSSNSPQVQPRPSNTPPSNAPAPPPTGRERLSRSTALSRQTREWLEQGMPTAEDASVRRRPQVTADAATPRAEARRTPEATADASAPRRGAVAHANSIVQQLVSEGADISHTRNMLRNAMNGDAVAFSRVEQNIFRQHFPNMPMHGISRDSELAIELRGALRRAVHQQAASAPVRSPTPTPASPAASSSGSSQRSLFGRFARLMAPNQGRSSNTAASQTPVDRSPPRVNQRPIRVDRAAMRNRGNDEADAALRGLVQQGVNLEHLRTALERHVMQRLPIPLDIGSALQNVGINPSIDLGESLVQHPLLNLNVALNRMLGLRPSAERAPRPAVPVAPATASRRPDGTRATRLRVMPEREDYENNVAYGVRLLNLNPGVGVRQAVAAFVTDRAERPAVVANIRAALDPIASQFSQLRTISKADAESEELGFKDAADHHTDDVTHCLFGGELSLSNPDQQVIGLAGNPTDTSQPYSQEGNKDLAFMDMKKLAQFLAGKPEHPMTRETLNAENIAKYAFRIVP

Effector protein involved in gene-for-gene resistance in tomato plants. It is recognized by the host Pto resistance protein and elicits Pto and Prf-dependent hypersensitive response (HR) and programmed cell death (PCD), resulting in host immunity. In susceptible plants, acts as a virulence factor by suppressing PCD and HR-based plant immunity. This function requires its E3 ubiquitin ligase activity probably by recruiting E2 enzymes and transferring ubiquitin molecules to cellular proteins involved in regulation of PCD and targeting them for degradation. Also, induces expression of host genes involved in ethylene biosynthesis and signaling, in particular ACO1 and ACO2, encoding the ethylene-forming enzyme ACC oxidase. Interacts physically with plant cell Pto. Secreted via type III secretion system (TTSS). Localized to the plant cell cytoplasm. Transcriptionally induced by HrpL. Auto-ubiquitinated. Unlike many effector proteins, it is widely conserved among diverse genera of plant pathogens including Xanthomonas, Erwinia and many strains of Pseudomonas. Acts as a general eukaryotic PCD inhibitor in plants and yeast. Belongs to the HopAB family.

Q5NCN1

MKALPALPLMLMLLSMPPPCAPQASGIRGDALEKSCLQQPLDCDDIYAQGYQEDGVYLIYPYGPSVPVPVFCDMTTEGGKWTVFQKRFNGSVSFFRGWSDYKLGFGRADGEYWLGLQNLHLLTLKQKYELRVDLEDFENNTAYAKYIDFSISPNAISAEEDGYTLYVAGFEDGGAGDSLSYHSGQKFSTFDRDQDLFVQNCAALSSGAFWFRSCHFANLNGFYLGGSHLSYANGINWAQWKGFYYSLKRTEMKIRRA

Could be involved in calcium-dependent cell adhesion or intercellular interactions. May contribute to the elastic fiber assembly and/or maintenance. Homodimer. Can also form higher oligomers. Interacts with FBN1, FBN2 and LOX. Interacts with COL1A1 in a Ca (2+)-dependent manner. Interacts with ELN in a Ca (2+)-dependent manner; this interaction promotes ELN self-assembly.

B2K8G1

MKQAFRVALGFLVLWASVLHAEVRIEITQGVDSARPIGVVPFKWMGPGTPPEEIGAIVGADLRNSGKFNPIDAARMPQQPSTAAEVTPAAWTALGIDAVVVGQVQPSADGSYVVSYQLVDTSGSAGSILAQNQYKVTKQWLRYSAHTVSDEVFEKLTGIKGAFRTRIAYVVKTNGGKFPHELRVSDYDGYNQFVVHRSPEPLMSPAWSPDGSKIAYVTFESGKSALVIQTLANGAIRQVASFPRHNGAPAFSPDGTKLAFALSKSGSLNLYVMDLASGQISQVTDGRSNNTEPSWFPDSQNLAYTSDQGGRPQVYKVNINGGVPQRITWEGSQNQNADVSPDGKFLVLVSSNGGAQHIAKQDLETGAVQVLTDTLLDETPSIAPNGTMVIYSSTQGLGSVLQLVSTDGRFKARLPATDGQVKFPAWSPYL

Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane. The Tol-Pal system is composed of five core proteins: the inner membrane proteins TolA, TolQ and TolR, the periplasmic protein TolB and the outer membrane protein Pal. They form a network linking the inner and outer membranes and the peptidoglycan layer. Belongs to the TolB family.

Q80VL1

MSTERTSWTNLSTIQKIALGLGIPASATVAYILYRRYRESREERLTFVGEDDIEIEMRVPQEAVKLIIGRQGANIKQLRKQTGARIDVDTEDVGDERVLLISGFPVQVCKAKAAIHQILTENTPVFEQLSVPQRSVGRIIGRGGETIRSICKASGAKITCDKESEGTLLLSRLIKISGTQKEVAAAKHLILEKVSEDEELRKRIAHSAETRVPRKQPISVRREEVTEPGGAGEAALWKNTNSSMGPATPLEVPLRKGGGDMVVVGPKEGSWEKPNDDSFQNSGAQSSPETSMFEIPSPDFSFHADEYLEVYVSASEHPNHFWIQIIGSRSLQLDKLVSEMTQHYENSLPEDLTVHVGDIVAAPLSTNGSWYRARVLGTLENGNLDLYFVDFGDNGDCALKDLRALRSDFLSLPFQAIECSLARIAPTGEEWEEEALDEFDRLTHCADWKPLVAKISSYVQTGISTWPKIYLYDTSDEKKLDIGLELVRKGYAVELPEDMEENRTVPNMLKDMATETDDSLASILTETKKSPEEMPHTLSCLSLSEAASMSGDDNLEDDLF

Participates in the primary piRNA biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Required for the final steps of primary piRNA biogenesis by participating in the processing of 31-37 nt intermediates into mature piRNAs. May act in pi-bodies and piP-bodies by transferring piRNA precursors or intermediates to or between these granules. Interacts with (symmetrically methylated) PIWIL1, PIWIL2 and PIWIL4. Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Colocalizes with pi- and piP-bodies, a subset of the nuage which contains secondary piRNAs. Associated with mitochondria in the germline. Highly expressed in testis, present at lower level in brain. Weakly or not expressed in other tissues (at protein level). Present at low level in male gonads in postnatal day 7 (P7) Expressed at higher level in P14, P21 and adult testes, correlating with the onset of meiosis (at protein level). Expressed in spermatogonia, spermatocytes and round spermatids, but not in elongating spermatids. Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. Male mice are sterile due to defects in male meiosis, piRNA production defects, DNA demethylation of LINE-1 (L1) transposable elements and an increase in L1 expression in the adult testis. Mutants have severely reduced levels of mature piRNAs and accumulate 1'U-containing, 2'O-methylated 31-37 nt RNAs that complement the missing mature piRNAs. Belongs to the Tdrkh family.

Q7WUL3

MIDLTAAPFSLDDDGIAWVRTTLAEMGEDEKLGQLFCLITYTSDPEYLGYLTRGLHVGGVMLRTMTAADAAATVTTLQSTATVPLLISANLEGGASQTVQEATHVGSNMALAATGSTDHVRRAATVIGREARALGINWAFTPVVDIDLNFRNPITNTRTFGADAATVAAMGAEYVEAIQAQGLAASAKHFPGDGVDERDQHLLASVNTMSVEEWDDSFGVVYRAAIAAGVKTVMVGHIMLPAYSRALRPGVADRDILPGVVAEELLNDLLRDRLGFNGLVVSDSTTMAGLASVLPRSQAVPRVIAAGCDMFLFTKNLDEDFGYMRAGIRDGVITPERLDEAVTRILALKASLGLHRGTNLPAQGAAGVLADPDHSATAREVAASSITLVKEEPGVLPITRERYPRVLVYDLQNGGSPIGQGARAGAVEQFVDALVEAGHDVTRFEPGGGWEGMAAPTTDVTERHDLVLYLANLSTRSNQTVVRIEWAEPMGANVPAYVHSVPTVFVSFENPYHLFDVPRVRTLINTYGSSPVVLETLLAALQGKAPFAGSSPVDAFCGQWDTHL

Catalyzes the cleavage of beta-N-acetyl-D-glucosaminides and beta-D-glucosides. Might be involved in the degradation of glucuronic acid-containing glycosaminoglycans such as hyaluronic acid. Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. The catalytic efficiencies against 4'-nitrophenyl beta-N-acetyl-D-glucosaminide and 4'-nitrophenyl beta-D-glucopyranoside are similar. Optimum pH is 7.3 with 4'-nitrophenyl beta-D-glucopyranoside as substrate. Precipitates below pH 6 and stable from pH 6.8 to 8.4. Catalyzes hydrolysis by a double-displacement mechanism via a covalent glycosyl-enzyme intermediate, involving the participation of a catalytic nucleophilic group in the enzyme active site. Belongs to the glycosyl hydrolase 3 family.

A6TC33

MTKFALVGDVGGTNARLALCDLASGEISRAKTYSGLDYPSLEAVVRVYLEEHQVTVNEGCIAIACPITGDWVAMTNHTWAFSIAEMKRNLGFAHLEIINDFTAVSMAIPMLKAEHLIQFGGSAPVAGKPIAVYGAGTGLGVAHLVHVDKRWVSLPGEGGHVDFAPNSEEEGIILEELRAELGHVSAERVLSGPGLVNLYRAIVKSDGRLPENLQPREVTERALADSCTDCRRALSLFCVIMGRFGGNLALTLGTFGGVYIAGGIVPRFLEFFKASGFRGGFEDKGRFKAYVQDIPVYLIVHDNPGLLGSGAHLRQTLGQVL

ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+) Belongs to the bacterial glucokinase family.

A8AGR2

MARAMDNSILETILQQVRPLIGQGKVADYIPALASVDGSKLGIAICTVDGQYYQAGDAQERFSIQSISKVLSLVVAMRHYPEEEIWQRVGKDPSGSPFNSLVQLELEQGIPRNPFINAGALVVCDMLQGRLSAPRQRMLEVVRALSGVSDIAYDVTVARSEFEHSARNAAIAWLMKSFGNFQHDVTTVLQNYFHYCALKMSCAELARTFVFLARQGQAFHLDEPVVTSMQARQINALMATSGMYQNAGEFAWRVGLPAKSGVGGGIVAIVPHEMAIAVWSPELDPAGNSLAGIAVLEQLTQQLGRSVY

H2O + L-glutamine = L-glutamate + NH4(+) Homotetramer. Belongs to the glutaminase family.

Q4R6Q9

MNEIKDTDSKKSEEYEDDFEKDLEWLINENEKSDASIIEMACEKEENINQDLKENETVIEHTKQHSDPDKSLQDDVSPRRNDIISVPGIQPLDPISDSDSENSFQESKLESQKDLEEEEDEEVRRYIMEKIVQANKLLQNQEPVNDKRERKLKFKDKLADLEVPPLEDTNTSKNYFENERNMFGKLSQLCISNDFGQENVLLSLTNASCEENKDRTILVERDGKFELLNLQDIASQGFLPPINNANSTENDPQHLLLRSSNSSVSGTKKEDSAAKIHAVTHSSTGEPLVYIPQPPLNRKTCPSSAANSDRSKGKGKYNHRTQSARISPVTSTYCLSPRQKELQKQLEQKREKLKREEEQRKIEEEKEKKRENDIVFKAWLQKKREQVLEMRRIQRAKEIEDMNSRQENRDPQQAFRLWLKKKHEEQMKERKTEELRKQEECLFFLKGTEGRERAFKQWLRRKRIEKIAEQQAVRERTRQLRLEAKHSKQLQHHLYMSEAKPFRFTDHYN

Microtubule-binding protein that localizes to the microtubular manchette of elongating spermatids. Homodimer. Interacts with HOOK1. Interacts with HOOK2. Interacts with HOOK3. Localizes to the microtubular manchette of elongating spermatids. Localizes to the sperm flagella and to the basal half of motile cilia. Belongs to the CCDC181 family.

Q8NES7

MKLLFPIFASLMLQYQVNTEFIGLRRCLMGLGRCRDHCNVDEKEIQKCKMKKCCVGPKVVKLIKNYLQYGTPNVLNEDVQEMLKPAKNSSAVIQRKHILSVLPQIKSTSFFANTNFVIIPNATPMNSATISTMTPGQITYTATSTKSNTKESRDSATASPPPAPPPPNILPTPSLELEEAEEQ

Has antibacterial activity. Expressed specifically in testis. Belongs to the beta-defensin family.

Q1KN14

IQSTSMDQGSLSEDSMNSFIRTLIQAGIWKNKVPKQTARTKDGMQTTVKKTEAEPDVRLGFQPIVSVDAELLRQQRRFSSPRVLLSENTPLEPPPLYLMEEPMVLNRTSRRKRFAEGKSHRGEYSVCDSESRWVTDKSSAVDIRGHQVTVLGEIRMGPS

Seems to promote the survival of visceral and proprioceptive sensory neurons. Belongs to the NGF-beta family.

P82642

MRCTTLIMVSFVVSCLLLSLVEESEAGAPPVECWSEILFSGKCGFHGKKKCYKEMESKLKQRVLKCRCEDVKKDSNTSKDEHYCGCQRENPYECN

Flower buds. Belongs to the DEFL family.

A6T0H2

MMKNQLAGLMKQAQAMQDNMKKMQDQLASIEVEGQSGAGLVKVVMSCKNDVKRVSIDPSLLADDKDMLEDLVAAAFNDAVRKAEATSQEKMSGVTAGMPLPPGFKMPF

Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. Homodimer. Belongs to the YbaB/EbfC family.

Q3Z504

MRVTDFSFELPESLIAHYPMPERSSCRLLSLDGPTGALTHGTFTDLLDKLNPGDLLVFNNTRVIPARLFGRKASGGKIEVLVERMLDDKRILAHIRASKAPKPGAELLLGDDESINATMTARHGALFEVEFNDERSVLDILNSIGHMPLPPYIDRPDEDADRELYQTVYSEKPGAVAAPTAGLHFDEPLLEKLRAKGVEMAFVTLHVGAGTFQPVRVDTIEDHIMHSEYAEVPQDVVDAVLAAKARGNRVIAVGTTSVRSLESAAQAAKNDLIEPFFDDTQIFIYPGFQYKVVDALVTNFHLPESTLIMLVSAFAGYQHTMNAYKAAVEEKYRFFSYGDAMFITYNPQAINERVGE

Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + H(+) + L-methionine tRNA modification; tRNA-queuosine biosynthesis. Monomer. Belongs to the QueA family.

O52715

MASYDLVERLNNTFRQIELELQALQQALSDCRLLAGRVFELPAIGKDAEHDPLATIPVVQHIGKTALARALRHYSHLFIQQQSENRSSKAAVRLPGAICLQVTAAEQQDLLARIQHINALKATFEKIVTVDSGLPPTARFEWVHRHLPGLITLSAYRTLTPLVDPSTIRFGWANKHVIKNLTRDQVLMMLEKSLQAPRAVPPWTREQWQSKLEREYQDIAALPQRARLKIKRPVKVQPIARVWYAGEQKQVQYACPSPLIALMSGSRGVSVPDIGELLNYDADNVQYRYKPEAQSLRLLIPRLHLWLASE

Trans-acting protein required for termination of DNA replication. Binds to DNA replication terminator sequences (terA to terF) to prevent the passage of replication forks. The termination efficiency will be affected by the affinity of this protein for the terminator sequence. Belongs to the Tus family.

P87324

MVEVRHSIPCEETKRLELSLSQQTYSQQYASIYFARLTALRPRITEAASKKWPDKQRLERVLDVKSDEDCWVVATAYMTTALKPNVMNDVTQLHTIVTTTEESPYVSPEDAASGDIEYALEDDYGRIDCSGSFLYDAGVVTGVVLAVLGHEDEQGRFVVVDVCFPGIFSHSIPMTTDESQAQPEYIAAVSGLGLSNDGIEGIQVHQLVDFLRGTLPHVSSFSPSSIKRLIILGNCLAPSIEIADSASASVPIGKKKVKRYGYDTSAYNPNPTFQLDNFLDQVCSSIDVTLMPGPYDYSSTILPQQPLHPALLTKSKVWLGSSLQTVTNPTWLSLGNHFVLATSGQNINDLRKYHPKKSSLQCMENTLLWNHITPTSPDTLWCYPFTDKDTFVMEEMPDLYLCGNQPKFGCKTVINEGNRIQLVSVPEFRKTGVLVLINMHTLNVEIIQFRPMSVKAETPITS

Required for replication of the leading DNA strand and for completion of lagging strand synthesis. It is essential for cell cycle progression. a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Heterodimer with subunits of 125 kDa and 50 kDa. Interacts with cdc27, however the function of this complex is not known. Belongs to the DNA polymerase delta/II small subunit family.

P79062

MQFLSSFVFAALALLPLSAMAVDEAASEIASSTKPASTNGTLSFCLGVKHADGTCKYTDDYLADFEVLAPYTNMIRTYATSDCNTLEYLLPALAQSPYNFSAILGVWPTDDAHYDLEKQALMQYLPQYGVDHVRAITVGSEVLYRNDLPADVLAERIYDVRGLVQQKLGFDVPVGTADSWNLWAGGSGDVVITASDFIMSNDFPYWQGQNTSNMTNTFISDTLAALERVQSVKGTNNVTFWVGETGWPTDGPSYGEADATVDIASEFFQEALCNIRRKGIDIFFFEAFDEDWKGDSSSVEPYFGAMYSNRTLKYNLNCTSE

Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase. Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose. Tightly bound to cell wall. Belongs to the glycosyl hydrolase 17 family.

Q87WH1

MTQQAAEVAKRRTFAIISHPDAGKTTITEKLLLMGKAISVAGTVKSRKSDRHATSDWMEMEKQRGISITTSVMQFPYRDHMINLLDTPGHEDFSEDTYRTLTAVDSALMVLDGGKGVEPRTIALMDVCRLRDTPIVSFINKLDRDIRDPIELLDEIEAVLKIKAAPITWPIGCYRDFKGVYHLADDYIIVYTAGHGHERTDTKIIQNLDSDEARAHLGDEYDRFVEQLELVQGACHEFNQQEFIDGQLTPVFFGTALGNFGVDHVLDAVVNWAPMPLARVANERTVEPEEEKFAGFVFKIQANMDPKHRDRIAFMRICSGRYEKGMKMRHVRLGKDVRIGDALTFFSSEREQLEEAYAGDIIGLHNHGTIQIGDTFTEGEALGFTGIPHFAPELFRRVRLKDPLKSKQLRQGLQQLAEEGATQVFFPQRSNDIILGAVGVLQFDVVASRLKEEYKVECAYEPITVWSARWIDCADKKKLEEFENKAVENLAVDGGGHLTYLAPTRVNLALMEERWPDVKFSATREHH

Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. PrfC subfamily.

A7EBU5

MLLQSLFAWALAIGPCIAQNSTNSTWPIHNNGLTTQVEWDHYSLMVDGQRFFLWSGEFHYWRIPVPELWVDVLQKVKAAGFNTFAIYTHWYFHNPNPNTLDFENAAHNFTKIFDLAKELGMFVVFRPGPYVNAESNAGAFPLWLTTGAYGALRNNDERYTEAWTPFWEKVASIVAPYQFTNGGNVLTYQIENELGSQWRGTPSNKVPNLSSVEYMEALEASARAHGITIPFQANDPNLNSDSWSKDFYDGYGSVDIYGMDSYPACWTCNLTECDSTNGAYKAFNVIDYYDHFEAISPTQPSFLPEFQGGSFNPWGGPEGGCPENSPADFANLFYRNNVGQRVTAMSLYMIYGGTNWGWLAAPVVATSYDYSSPISENRMINDKYAETKLFGHFLRVAKDLTKTDRIGTGKTASTNPNVVYSEIRNPDTNAAFYVTIHKESTVGTREEFYINANTSKGAFKIPQKAASIVLNGFQSKIIVTDFNFGSHSLLYSTAEVLSHSIVDDQDILALWMPTGEAGEFVVTGAKSGSVSSCGGCSSVGFYPQGDDLLVTISQSKGISVLTFDDGLRVLVMDRSFAYEFWVPVLTADPFSPANETVFVQGPSLVRSAAYSSDGSTLDLTGDNNGTSTQIQVFPPKSVSKVTWNGQVITTEKTDYDSLIGSLTGPALDSLTLPTISGWKANDSLPERLPTYDDSWWVAADHMNTSNPTKPETLPVLYIDDYGYHVGNHLWRGRFEGSASGVYLSVTGGRAFGYSAWLNGEFIGSYLGAAYPDTGKLTLSFSNVTVNSNSTNILLVLQDNSGHDETSEALNPRGINNATLISSSTKNFTSWKVTGTAGKPDTAIDPVRGILSEGGLYAERLGWHLPDFDDSEWSSASPSNVSSSAGVTFYRTTVSLAIPTGLDVAISFTLKASPSNAALRVLLFVNGYQYGRFSPWIGNQVEFPVPPGILNYDGDNVIGLSVWRQEEGDESMGVNVGWKVTEAFASSFEPIFDAAYLQPGWTDERLQYA

Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Belongs to the glycosyl hydrolase 35 family.

Q399X3

MQPDLTPNPAPPLIALTGIGKRFPGVQALDDCHFDLRAGEVHALMGENGAGKSTLMKILAGVYQRDDGEIRMDGRAVEIADPRAAQALGIGIIHQELNLMNHLSVAQNIFIGREPRGRFGVFVDEAALNRDAAAIFARMRLDLDPRTPVGQLTVAKQQMVEIAKALSFDSRVLIMDEPTAALNNAEIAELFRIIGDLRAHGVGIVYISHKMDELRQIADRVTVMRDGKYVATVPMADTSMDAIIAMMVGRQLATEFRTPPDTSANDVALEVRGLSRGRAIRDVGFTLRRGEILGFAGLMGAGRTEVARAVFGADPVDAGEIRVHGKTVSIRSPADAVRHGIGYLSEDRKHFGLAVGMDVQNNIALSSMRRFVRRGLFLDARALRDTAQSYVRQLAIRTPSVTQPARLLSGGNQQKIVIAKWLLRDCDILFFDEPTRGIDVGAKSEIYKLLDALAADGKAIVMISSELPEVLRMSHRILVMCEGRVTGELRAADATQEKIMQLATQRESTVLS

Part of an ABC transporter complex involved in carbohydrate import. Could be involved in ribose, galactose and/or methyl galactoside import. Responsible for energy coupling to the transport system. ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) + phosphate Belongs to the ABC transporter superfamily. Carbohydrate importer 2 (CUT2) (TC 3.A.1.2) family.

Q1GCM0

METIFALATAQGKAGVAVIRVSGPHAIEIGEKLTRRTLPARGMIFSKLKDSAGEILDEALVLSFTSPDSFTGENIVEFQLHGSIAVVSAVMSAIEETGVARLADPGEFTRRALDNGKLDLTQVEGLADLIDAETEAQRKQAQVILAGTLGDLADRWRTDLIRAASLIEVTIDFADEEVPVDVTPEVKQLLSGVLHDIEKEVDGVAIAERIREGFEVAIVGSPNVGKSTLLNALAGRTAAITSEYAGTTRDVIEVRMDLAGLPVTLLDTAGLRETDDHVEGIGIRLAQERAERADIRVFLAEEDESFSIQMREGDLRLLPKADERRSAKGAISGRTGQGVDDLVSRISDTLRNRTAHDGIATRARHRETMNRAVLSLRQAIEVVEQGPEFYDLAAEDMRSAIRALELLVGRINVENLLDEIFSSFCLGK

Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. Binds 1 potassium ion per subunit. Homodimer. Heterotetramer of two MnmE and two MnmG subunits. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.

Q5FCY8

MLIIDIGNTNIKFGICINNQIIQTLRISSQPRRTADEYFFFLNTIINQLNINNFTITHIIISSVVPSITKPMIELSTHYFNITPTIINNQHADICNIKIDLNDKLLGSDRLASIIGAVTLYPNKNLLVISMGTATVFNLISKERSIYGQVITPGAHIMAQSMRQHTALLPEISQIKVNKVVHNTLFYAIEAGVYWGYIAMVEGIVKQILHEENKDLHIVATGGNSILFIDHKNFIKNIDPDLTMKGMIYLHNMLFNK

Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+) A monovalent cation. Ammonium or potassium. Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. Homodimer. Belongs to the type III pantothenate kinase family.

Q9WVH0

MGRMHAPGKGLSQSALPYRRSVPTWLKLASDDVKEQIYKLAKKGLTPSQIGVILRDSHGVAQVRFVTGNKILRILKSKGLAPDLPEDLYHLIKKAVAVRKHLERNRKDKDAKFRLILIESRIHRLARYYKTKRVLPPNWKYESSTASALVA

Belongs to the universal ribosomal protein uS15 family.

Q8R0T2

MEREASSWGLESRDVHSPNAVGSPEGSLKDPAGNTSENEEGEISQREGNGDYEVEEIPFGLEPQSPEFEPQSPEFESQSPRFEPESPGFESRSPGFVPPSPEFAPRSPESDPQSPEFESQSPKYEPRSPGCHPRSPGCEPGSPRYEPKSPGYGSKSPEFESQSPGYESQSPGYEPQNSGDGVQNSEFKTHSPEFETQSSKFQEGAEMPLSPEEKNPLSISLGVHPLDSFTQGFGEQPTGALPPFDMPSGALLAAPQFEMLQNPLNLTGTLRGPGRRGGRARGGQGPRPNICGICGKSFGRGSTLIQHQRIHTGEKPYKCEVCSKAFSQSSDLIKHQRTHTGERPYKCPRCGKAFADSSYLLRHQRTHSGQKPYKCPHCGKAFGDSSYLLRHQRTHSHERPYSCPECGKCYSQNSSLRSHQRVHTGQRPFSCGICGKSFSQRSALIPHARSHAREKPFKCPECGKRFGQSSVLAIHARTHLPGRTYSCPDCGKTFNRSSTLIQHQRSHTGERPYRCAVCGKGFCRSSTLLQHHRVHSGERPYKCDDCGKAFSQSSDLIRHQRTHAAGRR

May be involved in transcriptional regulation. Belongs to the krueppel C2H2-type zinc-finger protein family.

P16088

KEFGKLEGGASCSPSESNAASSNAICTSNGGETIGFVNYNKVGTTTTLEKRPEILIFVNGYPIKFLLDTGADITILNRRDFQVKNSIENGRQNMIGVGGGKRGTNYINVHLEIRDENYKTQCIFGNVCVLEDNSLIQPLLGRDNMIKFNIRLVMAQISDKIPVVKVKMKDPNKGPQIKQWPLTNEKIEALTEIVERLEKEGKVKRADSNNPWNTPVFAIKKKSGKWRMLIDFRELNKLTEKGAEVQLGLPHPAGLQIKKQVTVLDIGDAYFTIPLDPDYAPYTAFTLPRKNNAGPGRRFVWCSLPQGWILSPLIYQSTLDNIIQPFIRQNPQLDIYQYMDDIYIGSNLSKKEHKEKVEELRKLLLWWGFETPEDKLQEEPPYTWMGYELHPLTWTIQQKQLDIPEQPTLNELQKLAGKINWASQAIPDLSIKALTNMMRGNQNLNSTRQWTKEARLEVQKAKKAIEEQVQLGYYDPSKELYAKLSLVGPHQISYQVYQKDPEKILWYGKMSRQKKKAENTCDIALRACYKIREESIIRIGKEPRYEIPTSREAWESNLINSPYLKAPPPEVEYIHAALNIKRALSMIKDAPIPGAETWYIDGGRKLGKAAKAAYWTDTGKWRVMDLEGSNQKAEIQALLLALKAGSEEMNIITDSQYVINIILQQPDMMEGIWQEVLEELEKKTAIFIDWVPGHKGIPGNEEVDKLCQTMMIIEGDGILDKRSEDAGYDLLAAKEIHLLPGEVKVIPTGVKLMLPKGYWGLIIGKSSIGSKGLDVLGGVIDEGYRGEIGVIMINVSRKSITLMERQKIAQLIILPCKHEVLEQGKVVMDSERGDNGYGSTGVFSSWVDRIEEAEINHEKFHSDPQYLRTEFNLPKMVAEEIRRKCPVCRIIGEQVGGQLKIGPGIWQMDCTHFDGKIILVGIHVESGYIWAQIISQETADCTVKAVLQLLSAHNVTELQTDNGPNFKNQKMEGVLNYMGVKHKFGIPGNPQSQALVENVNHTLKVWIQKFLPETTSLDNALSLAVHSLNFKRRGRIGGMAPYELLAQQESLRIQDYFSAIPQKLQAQWIYYKDQKDKKWKGPMRVEYWGQGSVLLKDEEKGYFLIPRRHIRRVPEPCALPEGDE

During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase. Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus. 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. dUTP + H2O = diphosphate + dUMP + H(+) a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Cleavage sites that yield the mature proteins remain to be determined. Belongs to the retroviral Pol polyprotein family.

Q31Y44

MKPDAHQVKQFLLNLQDTICQQLTAVDGAEFVEDSWQREAGGGGRSRVLRNGGVFEQAGVNFSHVHGEAMPASATAHRPELAGRSFEAMGVSLVVHPHNPYVPTSHANVRFFIAEKPGAEPVWWFGGGFDLTPFYGFEEDAIHWHRTARDLCLPFGEDVYPRYKKWCDDYFYLKHRNEQRGIGGLFFDDLNTPDFDHCFAFMQAVGKGYTDAYLPIVERRKAMAYGERERNFQLYRRGRYVEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYQPKDGSPEAALSEFIKVRDWV

Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX. coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1. Homodimer. Belongs to the aerobic coproporphyrinogen-III oxidase family.

B3NPV7

MNAAGGGSGSQAAGAAGGNSSLSHNALLATASGATTMPMAQLADGWLELESDPGLFTLLLKDFGCHDVQVEEVYDLQKPIESPYGFIFLFRWIEERRARRKIVETTAEIFVKDEEAISSIFFAQQVVPNSCATHALLSVLLNCNENNLQLGDTLSRLKVHTKGMSPENKGLAIGNTPELACAHNSHAMPQARRRLERTGAGVSSCRFTGEAFHFVSFVPINGQLFELDGLKPYPMNHGGWEDSEDWTDKFRRVMAERLGIATGEQDIRFNLMAVVPDRRIAITHKLKMLRTNQAIVSGTLQKLLKADEQGESGNGDSQRPDTPTTLLEPSAFTARDLQSLLKNLDTEIAINEQHLADENDRRHMFKVDASRRTHNYDKFICTFLSMLAHQGVLGELVSQHLLPSKKVSGQGAANRISKQSTTASAGGSTAGASAATPKTQQQQAAAAKNGKSPSKTPGRRRKGRNKCRKRK

Polycomb group (PcG) protein. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-118' (H2AK118ub1). Does not deubiquitinate monoubiquitinated histone H2B. Required to maintain the transcriptionally repressive state of homeotic genes throughout development. The PR-DUB complex has weak or no activity toward 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Component of the PR-DUB complex, at least composed of calypso and Asx. Localizes to PcG response elements (PREs). Belongs to the peptidase C12 family. BAP1 subfamily.

Q5HM40

MNKLIAWIEKGKPFFEKISRNIYLRAIRDGFIAAIPIILFSSIFILITYVPNVFGFTWSKTMEGILMKPYNYTMGIVGLLVAGTTAKSLTDSYNRKLDKTNQINFISTMMAAICGFLFLAADPVKDGGFSSAFMGTKGLLTAFISAFITVIVYNFFVKRNITIKMPKEVPPNISQVFKDIFPLSAVILILYALDLLSRAIVHTNVANAVLKVFEPLFTAADGWIGVTLIFGAFAFFWFVGIHGPSIVEPAIAAITYANLETNLHLIQAGEHADKVITPGTQMFVATMGGTGATLVVPFMFMWLTKSKRNKAIGRASVVPTFFGVNEPILFGAPLVLNPVFFIPFIFAPIVNIWIFKFFVDVLNMNSFSIFLPWTTPGPLGIVMGTGFAFWSFVLAILLIVVDVIIYYPFLKVYDEQVLEEELGNKEANNELKEKVSANFDTKKADAILATAGASEADTDDTSSVDETTSTSSTDTISEQTNVLVLCAGGGTSGLLANALNKAAEEYEVPVKAAAGGYGAHMDIMKDYQLIILAPQVASNFEDIKQDTDRLGIKLAKTEGAQYIKLTRDGEAALEFVKQQFNN

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II LacEF PTS system is involved in lactose transport. lactose(out) + N(pros)-phospho-L-histidyl-[protein] = L-histidyl-[protein] + lactose 6-phosphate(in) Induced by lactose, galactose and galactose-6-P. Repressed by glucose. The EIIC type-3 domain forms the PTS system translocation channel and contains the specific substrate-binding site. The PTS EIIB type-3 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-3 domain.

Q2T0M6

MTTLADLRTNYSRASLDAADVNPNPFVQFDVWFKEALSAQLPEPNTMTLATVDEAGRPSARIVLIKGVDERGFVFFTNYESRKGRELAHNPNAALLFYWIELERQVRIEGRIEKTTEEESDRYFASRPLGSRIGAWASEQSAVIESRALLEAREKEISARFGENPPRPPHWGGYRLVPSTIEFWQGRPSRLHDRLLYTRDAASASGWRIARLAP

Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-phosphate Binds 1 FMN per subunit. Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1. Homodimer. Belongs to the pyridoxamine 5'-phosphate oxidase family.

Q62KZ3

MKAAEIREKFLKFFESKGHTIVRSSSLVPGNDPTLLFTNSGMVQFKDVFLGAETRPYSRATTAQRSVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKRDAIHYAWELLTSVYKLPADKLWVTVYHDDDEAYDIWAKEVGVPAERIIRIGDNKGARYASDNFWQMGDTGPCGPCSEIFYDHGPDVWGGPPGSPEEDGDRYIEIWNLVFMQFNRDAQGNMTRLPKPCVDTGMGLERIAAVLQHVHSNYEIDLFQQLIKASARETGVADLANNSLKVIADHIRACSFLIVDGVIPGNEGRGYVLRRIVRRAIRHGYKLGRKAPFFHKLVADLVAEMGAAYPELKEAEPRVTDVLRQEEERFFETIEHGMSILEAALAELDAAGGKTLDGELAFKLHDTYGFPLDLTADVCRERGVTVDEPAFDDAMARQREQARAAGKFKATQGLEYTGAKTTFHGYEEIAFDDAKVVALYVEGASVGEVKAGESAVVVLDHTPFYAESGGQVGDQGVLANAATRFAVGDTLKVQADVIGHHGELEQGTLKVGDVVRAEIDAARRARTARNHSATHLMHKALRDVLGSHVQQKGSLVDADKTRFDFAHNAPLTDDEIRRVEAIVNEQVLANAPGIVRVMPYDDAVKGGAMALFGEKYGDEVRVLDLGFSRELCGGTHVHRTGDIGLFKIVAEGGVAAGIRRVEAITGDNAVRYVQALDARVNAAAAALKAQPSELLQRIGQVQDQVKSLEKELGALKSKLASSQGDELAQQAVEVGGVHVLAATLDGADAKTLRETVDKLKDKLKSAAIVLAAVDGGKVSLIAGVTADASKKVKAGELVNFVAQQVGGKGGGRSDMAQAGGTEPAKLPAALAGVKGWVEARL

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala) Binds 1 zinc ion per subunit. Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. Belongs to the class-II aminoacyl-tRNA synthetase family.

Q922Y4

MKYILVTGGVISGIGKGVIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQSRKMLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSTDLEPSTLQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARKQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPKTSHPVVIDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDTDYLEERHRHRFEVNPVLKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLPHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSISQD

This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity. ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate Activated by GTP and inhibited by CTP. Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. Mainly cytosolic but when active detected in long filamentous structures (By similarity). Co-localizes with TNK2 in the cytosolic filaments (PubMed:25223282). Belongs to the CTP synthase family.

Q2Y629

MFRGGTPVSLDNKGRLAVPARYRETLISLCAGHLIVTADPSKCLLIYPQPVWEPIEQKLNSLSSFNPQTRSLQRLLVGNACDVEMDGVGRILVPPSLRAFAGLNKEVVLVGQGAKFELWDSEKWNLQMESALAFRDGIPQELEGFSL

Forms oligomers. Belongs to the MraZ family.

Q5VI41

MLPQRPQLLLLAGLLALQSVLSQECTKYKVSTCRDCIESGPGCAWCQKLNFTGQGEPDSTRCDTRAQLLSKGCPADDIMEPKSLAETRQSQAGKQKQLSPEEVTLYLRPGQAAAFNVTFQRAKGYPIDLYYLMDLSYSMVDDLANVKKLGGDLLRALNDITESGRIGFGSFVDKTVLPFVNTHPEKLRNPCPNKEKQCQPPFAFRHVLKLTDNSKQFETEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKSSNEFDYPSVGQLAHKLAESNIQPIFAVTKKMVKTYEKLTEIIPKSAVGELSEDSKNVVELIKSAYNKLSSRVFLDHNTLPDTLKVAYDSFCSNGVSQVDQPRGDCDGVQINVPITFQVKVTATECIQEQSFTIRALGFTDTVTVRVLPQCECQCRDASRDRSVCGGRGSMECGVCRCDAGYIGKNCECQTHGRSSQELEGSCRKDNSSIICSGLGDCICGQCVCHTSDVPNKKIYGQFCECDNVNCERYDGQVCGGEKRGLCFCGTCRCNEQHEGSACQCLKSTQGCLNLDGVECSGRGRCRCNVCQCDPGYQPPLCIDCPGCPVPCAGFAPCTECLKFDKGPFAKNCSAACGQTKLLSSPVPGGRKCKERDSEGCWMTYTLVQRDGRNRYDVHVDDMLECVKGPNIAAIVGGTVGGVVLVGILLLVIWKALTHLSDLREYHRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES

Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrin ITGAL/ITGB2 is also a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL. Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2 is also a receptor for factor X. Integrin ITGAD/ITGB2 is a receptor for ICAM3 and VCAM1. Contributes to natural killer cell cytotoxicity. Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation. Integrin ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages. In association with alpha subunit ITGAM/CD11b, required for CD177-PRTN3-mediated activation of TNF primed neutrophils. Heterodimer of an alpha and a beta subunit. The ITGB2 beta subunit associates with the ITGAL, ITGAM, ITGAX or ITGAD alpah subunits. Found in a complex with CD177 and ITGAM/CD11b. Interacts with FGR. Interacts with COPS5 and RANBP9. Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23). Interacts with THBD. Belongs to the integrin beta chain family.

B4KCL9

MALTDLSAKVVLVDIEGTTTSITFVHDVLFPYAKANAGQYLSETWETDDTKQIVEELTQLPQYTEYASTLETRPEINAAHIADFSRYLIEKDLKVTPLKTLQGHIWAKGYASGELKGHVYEDVAVAFQAWSDAGLRIAVYSSGSVAAQKLIFQHSIAGDLLPLLSAHFDTNVGHKQQTESYTRIAESLGVEPQHVLFLTDVPEEASAARDAGMQTVLLARPGNAPLTAEHTSAFPVVANFVALQSLKQP

Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate Binds 1 Mg(2+) ion per subunit. Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6. Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6. Monomer. Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.

A6L792

MATKEYFPGIGKIKFEGKESKNPMAFRYYDAEKVINGKKMKDWLKFAMAWWHTLCAEGGDQFGGGTKKFPWNGDADKVQAAKNKMDAGFEFMQKMGIEYYCFHDVDLCEEADTIEEYEANLKEIVAYAKQKQAETGIKLLWGTANVFGHARYMNGAATNPEFDVVARAAVQIKNAIDATIELGGSNYVFWGGREGYMSLLNTDQKREKEHLAQMLTIARDYARSKGFTGTFLIEPKPMEPTKHQYDVDTETVVGFLKTHGLDKDFKVNIEVNHATLAGHTFEHELAVAVDNGMLGSIDANRGDYQNGWDTDQFPIDNYELTQAMMQIIRNGGLGNGGTNFDAKTRRNSTDLEDIFIAHIAGMDAMARALESAAALLNESPYCKMLSDRYASFDSGKGKEFEEGKLTLEDVVAYAKQNGEPKQVSGKQELYEAIVNMYC

alpha-D-xylose = alpha-D-xylulofuranose Binds 2 magnesium ions per subunit. Homotetramer. Belongs to the xylose isomerase family.

Q8ZRQ6

MLFSPPLQRATLIQRYKRFLADVITPDGTTLTLHCPNTGAMTGCATPGDTVWYSTSENTKRKYPHTWELTETQSGAFICVNTLRANQLTKEAIQENRLPALAGYNILKSEVKYGAERSRIDFMLQADFRPDCYIEVKSVTLAEKENGYFPDAITERGQKHLRELMGVAAAGHRAVVVFAVLHSAITRFSPARHIDIKYAQLLSEAQNKGVEVLAYKAELSAQKMELNEPVPITL

Binds to DNA non-specifically. Could be a regulatory factor involved in maltose metabolism. Belongs to the SfsA family.

B5ELX8

MDSSKIRIRLKSYDYRMLDISAAEIVETARRTGARVCGPIPLPTKIERFTVLRSPHVDKNARDQFEQRTHKRLLDILDPNDKTVDALIKLDLAAGVDVEIKL

Involved in the binding of tRNA to the ribosomes. Part of the 30S ribosomal subunit. Belongs to the universal ribosomal protein uS10 family.