Datasets:
habdine
/
Prot2Text-Data

Dataset card Data Studio Files
xet
Community
1
accession
stringlengths
6
10
name
stringlengths
6
11
Full Name
stringlengths
1
147
⌀
taxon
stringlengths
3
46
⌀
sequence
stringlengths
16
2.75k
function
stringlengths
6
5.51k
AlphaFoldDB
stringlengths
6
10
A6LJ74
RPOZ_THEM4
Transcriptase subunit omega
Thermosipho
MNPVINYDELLKKIPYKFAIPIAVAKRAENLKEFAHSYVETWDNNYVSIALKELSEGYIRIKNEEILKVLIPNVK
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
A6LJ74
Q0TBG2
LIGB_ECOL5
Polydeoxyribonucleotide synthase [NAD(+)] B
Escherichia
MKVWMAILISILCWQSSAWAVCPAWSPARAQEEISRLQQQIKQWDDDYWKEGESEIEDGVYDQLSARLTQWQRCFGNEPRDAMMPPLAGTVMHPVAHTGVRKLADKNALRLWMREHNDLWVQPKVDGVAVTLVYRDGKLNKAISRGNGLKGEDWTQKVSLISAVPQTVSGPLANSTLQGEIFLKRKGHIQQQMGGINARAKVAGLMMRQGNSDTLNSLAVFVWAWPDGPHLMTDRLKDLATAGFTLTQTYTRAVKNADEVAHVRNEWWKAKLPFVTDGVVVRAAKEPESRHWLPGQAEWLVAWKYQPVAQVAEVKAIQFAVGKSGKISVVASLAPVMLDDKKVQRVNIGSVRRWQEWDIAPGDQILVSLAGQGIPRIDDVVWRGAERTKPTPPENRFNSLTCYFASDVCQEQFISRLVWLGSKQVLGLDGIGEAGWRALHQTHRFEHIFSWLLLTPEQLQNTPGIAKSKSAQLWHQFNLARQQPFTRWVMAMGIPLTRAALNASDERSWSQLLFSTEQFWQQLPGTGSGRARQVIEWKENAQIKKLGSWLAAQQITGFEP
Catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction.
Q0TBG2
Q4JBK2
COBS_SULAC
Cobalamin-5'-phosphate synthase
Sulfolobus
MGRILKAILGQLSFFTIIPSPSASLEEIAEFSFISPLMVGIITGIIDWFVVLLGIRLIGSLGALLLIPTVEIIRGFHHLDGLLDMGDALMVGKERRPQVLHDLQTGSGAIGLFLVYFSIFLIATLNLNVSNLWFFLPSEVLARASAISLLGLMKPIPGSYLGKVFHDKMRDKLFSIKFLLVQVFAILFSSPVLILAYVILLLVFYLMAKLVFDGMSGDIVGAIITLSFPIYLLVAEKTCYHYFIFQYSLTLP
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Q4JBK2
Q5FLV7
IXTPA_LACAC
Nucleoside-triphosphate pyrophosphatase
Lactobacillus
MSQKILFATGNKGKARELKEAFKTAGVDVEIITNSDLDNPPHPIESGRTFEANAKIKAHELADYSKLPTIADDSGLMVDALNGEPGVRSARYAGEAHNDAKNNAKLLANLGGIPDEKRTAKFWTTIVVSMPGEFEKDLVVSGTCSGRILAAPRGDDGFGYDPLFFVPKKDKTFAQMTTDEKNEISHRGNVVRELLKVLPALA
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Q5FLV7
C0HK90
CPFB3_XENBO
Caerulein precursor fragment B3
Xenopus
GLGSLLGSLFKFIPKLLPSIQQ
Has antibacterial and antifungal activity.
C0HK90
Q589B1
PSBK_SILLA
Photosystem II reaction center protein K
Silene sect. Melandrium
MLNIFSLIGLNSALYSSSCFFAKLPEAYAFLSPIVDFMPVIPLLFFLLAFVWQAAVSFR
One of the components of the core complex 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.
Q589B1
Q8Z171
ULAB_SALTI
Ascorbate-specific phosphotransferase enzyme IIB component
Salmonella
MTVRILAVCGNGQGSSMIMKMKVDQFLTQSNIDHTVNSCAVGEYKSELSGADIIIASTHIAGEITVTGNKYVVGVRNMLSPADFGPKLLEVIKAHFPQDVK
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 UlaABC PTS system is involved in ascorbate transport.
Q8Z171
Q8VP65
AROA_PHODP
5-enolpyruvylshikimate-3-phosphate synthase
Photobacterium
MESLTLQPINLINGEVNLPGSKSVSNRALLLAALAQGTTRLTNLLDSDDIRHMLNALQQLGVQYQLSADKTECTVEGLGQPFSVKDFTCLYLGNAGTAMRPLAAALCLGQGEFELTGEPRMKERPIGHLVDALRSAGADITYLENEHYPPLKIKGTGLDGGEVSIDGSISSQFLTAFLMAAPLAKSDTTILIKGDLVSKPYIDITLNIMAQFGVQVENQNYQKFIVPAGQVYQSPGEFLVEGDASSASYFLAAGAIKGGEVKVTGIGKNSIQGDIQFADALEAMGAEIEWGEDYIIARHRQLNAIDMDFNHIPDAAMTIATAALFAPGTTSIRNVYNWRVKETDRLHAMATELRKLGAEVEEGDDYITITSPTQLKHVAIDTYDDHRMAMCFSLVALSDTAVTINDPKCTSKTFPDYFTKLEQLSR
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Q8VP65
A2BZA6
PURL_PROM1
Phosphoribosylformylglycinamidine synthase subunit II
Prochlorococcus
MTVSFENKDFNQFINSSKFLVEYDVMSALKQEGLKQSDYVEICRRLNRGPNRNELGMFGVMWSEHCCYRNSRPLLKNLPTTGSRILVGPGENAGVVDIGFGQRLVFKIESHNHPSAVEPFQGAATGVGGILRDIFTMGARPIALLNALRFGPLDDEKNISLLEGVVAGISHYGNCVGVPTIGGEVGFDSSYSGNPLVNVMGLGLMETEEIVCSGASGIDFPVLYVGNTTGRDGMGGASFASSELSKTSIDDRPAVQVGDPFLEKGLIEACLEAFKTGYVIAAQDMGAAGLTCSCSEMASKGEVGIELNLDLVPAREKGMTAYEFLLSESQERMLFVVKPGSEEELRELFIRWGLYVEVVGKVLKEKVVRVIHKGEVVANLPASALADDTPIEEHLLINSTPEYLQEHWKWTEDLLPKTLDNGIINIKNNLFISWNNVLLDLLSMPSIASKNWIYKQYDYQVQSNTVVSPGEADAAVIRIRSQNDFLTKPKKDRGIASVVDCNDRWVYLDPLRGSMSAVAEAARNLSSVGAEPIAITNNLNFSSPDKPVGFWQLSMSCEGITKACLALSTPVTGGNVSLYNDTKLQNNTVLPIHPTPVIGMVGLIEDINKICKKSWVKAEDQIWMIGLPLENNINQDERISLSASSFLEYIHGLKTGRPPEIDLNLEKQVHAFLREVIKQGIVNSAHDLGDGGLAVAIAECCISSGYGANIILPPSQSRLDRLLFAEGGARVLVSCSTDQSEELKKYYKNISLQGSNLFSISHLGNVNNQKKLLVSQSNNTIIDVNILDLKDTYKDAIHKKITK
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.
A2BZA6
P31440
ADEQ_ECOLI
Adenine permease AdeQ
Escherichia
MNNDNTDYVSNESGTLSRLFKLPQHGTTVRTELIAGMTTFLTMVYIVFVNPQILGAAQMDPKVVFVTTCLIAGIGSIAMGIFANLPVALAPAMGLNAFFAFVVVGAMGISWQTGMGAIFWGAVGLFLLTLFRIRYWMISNIPLSLRIGITSGIGLFIALMGLKNTGVIVANKDTLVMIGDLSSHGVLLGILGFFIITVLSSRHFHAAVLVSIVVTSCCGLFFGDVHFSGVYSIPPDISGVIGEVDLSGALTLELAGIIFSFMLINLFDSSGTLIGVTDKAGLIDGNGKFPNMNKALYVDSVSSVAGAFIGTSSVTAYIESTSGVAVGGRTGLTAVVVGVMFLLVMFFSPLVAIVPPYATAGALIFVGVLMTSSLARVNWDDFTESVPAFITTVMMPFTFSITEGIALGFMSYCIMKVCTGRWRDLNLCVVVVAALFALKIILVD
High-affinity transporter for adenine.
P31440
Q1I7T2
GLO2_PSEE4
Glyoxalase II
Pseudomonas
MIQIDALPAFSDNYIWLLQDTANRRCAVVDPGDDAPVLAWLGKHPGWVLEAILVTHHHHDHVGGVEALKHATGAQVFGPANERIPARDIALEDGAQVHVLGLAFDVLAMPGHTLGHIAYYTAQSPTPLLFSGDTLFAAGCGRLFEGTPEQMHHSLQRLAALPEQTQVYCAHEYTLSNLRFARAVEPHSEPVQQRFEAVTQLRADNRISLPSTIGIERQTNPFLRTAEISVKQKADEWKGHSNPTQASVFAALRSWKDVF
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Q1I7T2
Q5FFA3
PTH_EHRRG
Peptidyl-tRNA hydrolase
Ehrlichia
MLHLLVGLGNPGKEYELTRHNVGFMIIDAIMHHFLFPDFKKKHNALISSGSIQSYKVILAKPYTFMNNSGAPISSIVKLYKIPLDNIIVFHDETDIDFCTIRIKKGGGNAGHNGLKSIDTLLGRDYWRIRFGIGHPSNGYDLSYHVLSQFNNLNAVNNTISNIIEHISLLFENDKSIFKNKVKDLIKYTDISS
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Q5FFA3
Q9R061
NUBP2_MOUSE
Nucleotide-binding protein 2
Mus
MEAAAGERAEPGNLAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQCDNGWVPVFVDQEQSISLMSVGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMATMEALRPYRPLGALVVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLGSVPLDSQLTRSLEEGRDFIQEFPKSTAYSALTSIAQRVVHRMSALCS
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Negatively regulates cilium formation and structure .
Q9R061
B1KP09
MOAC_SHEWM
Molybdenum cofactor biosynthesis protein C
Shewanella
MSNEFTHINADGNAHMVDVTEKAVTEREARAEAFIEMAPATLEMIMSGSHHKGDVFATARIAGIQAAKKTSDLIPLCHPLMLTKVEVELEAQPEHSRVRITSLCKLSGKTGVEMEALTAASVAALTIYDMCKAVQKDMVISQTRLLEKRGGKSGHFKV
Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
B1KP09
B1LMN0
HEM6_ECOSM
Oxygen-dependent coproporphyrinogen-III oxidase
Escherichia
MKPDAHQVKQFLLNLQDTICQQLSAVDGAEFVEDSWLREAGGGGRSRVLRNGGVFEQAGVNFSHVHGEVMPASATAHRPELAGRSFEAMGVSLVVHPHNPYVPTSHANVRFFIAEKPGAEPVWWFGGGFDLTPFYGFEEDAIHWHRTARDLCQPFGEDVYPRYKKWCDEYFYLKHRNEQRGIGGLFFDDLNTPDFDHCFAFMQAVGKGYTNAYLPIVERRKTMAYGERERNFQLYRRGRYVEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYQPKDGSPEAALNEFIKVRDWV
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.
B1LMN0
Q9CQ56
USE1_MOUSE
USE1-like protein
Mus
MAQAEGAYHRPLATSRLELNLVRLLCRCESMAAEKREPDEWRLEKYVGALEDMLQALKVQASKPASEVISEYSRKVDFLKGMLQAEKLTSSSEKALANQFLAPGRVPTTAKERVPATKTVHLQSRARYTSEMRSELLGMEPSGECEVDMRKRAAKGSRPADERQSASELDLVLQRHQGLQEKLAEEMLGLARSLKTNTLAAQSVIKKDNQTLSHSLKMADQNLEKLKLESERLEQHAQKSVNWLLWAMLIVVCFVFISMILFIRIMPRLK
SNARE that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER.
Q9CQ56
B8H6U2
HIS6_PSECP
ImGP synthase subunit HisF
Pseudarthrobacter
MAVAVRVIPCLDVDAGRVVKGVNFEGLRDAGDPVELAHRYDNAGADELTFLDVTASSGNRETTFDVVRRTAEEVFIPLCVGGGVRGVAEVDKLLRFGADKAAINTAAVARPDVIDEITRHFGSQVLVLSVDARRTRPGSKPTPSGFEVTTHGGRTGTGIDAIEWAKEAADRGVGEILLNSIDADGTKDGFDLEMIRMVRAAVKVPLIASGGAGEPAHFPPAVAAGADAVLAASIFHWGPNDMMHQVKDAIRNAGFEVR
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
B8H6U2
P21916
NEU2_STRCA
MSEL-neurophysin
Struthio
ALADAALRQCMPCGPGDRGNCFGPSICCGAELGCYVGTAETLRCAEENYLPSPCRAGGQPCGAGGRCAAPGICCSDETCSLEPACLEEAGERGGEPAQKNLTGLDASAGDFLLKLMHLAANRQQQGGKGPLL
Neurophysin 2 specifically binds vasopressin.
P21916
Q6ZN68
D19P2_HUMAN
Protein dpy-19 homolog 2-like 2
Homo
MADSRRVIIASWYRTFMGIVNLFGLETKTCWNVTRIEPLNEVQSCEGLRDPACFYVGVIFILNGLMMGLFFIYGTYLSGTELGGLITVLCFFFNHGEATCVMWTPPLRESFSYPFLVLQMYVLTLILRTSSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNCWLIQGSAWWCGTIILKFLTSKILGVSDHICLSDLIAAGILRYTDFDTLKYTCSPEFDFMEKATLLIYTKTLLLPVVMVITCFIFKKTVGDISRVLATNVYLRCCLCRCHAYNGKCQAVYTSSHCESSTLRRCRLEAWLQHA
Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins.
Q6ZN68
P02707
LECH_CHICK
Hepatic lectin
Gallus
MDEERLSDNVRLYKGGSIRQGLRSFAAVYVLLALSFLLLTLLSSVSLARIAALSSKLSTLQSEPKHNFSSRDSLLFPCGAQSRQWEYFEGRCYYFSLSRMSWHKAKAECEEMHSHLIIIDSYAKQNFVMFRTRNERFWIGLTDENQEGEWQWVDGTDTRSSFTFWKEGEPNNRGFNEDCAHVWTSGQWNDVYCTYECYYVCEKPLPK
Hepatic lectin is a membrane receptor protein that recognizes and binds exposed N-acetylglucosamine moieties of plasma glycoproteins, thus mediating their clearance (from the circulation) and endocytosis.
P02707
B2U9Q0
ACCA_RALPJ
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Ralstonia
MKTTFLEFEQPIAELEAKIEELRFVQDDSAVDISEEISRLASKSQQLTKDLYANLTPWQVAQIARHPQRPYTLDYVREIFTDFHELHGDRTFADDLSIVGGLARFNGQACMVIGHQKGRDTKERALRNFGMSKPEGYRKAKRLMELADKFGLPIFTFVDTPGAFPGIDAEERGQSEAIGHNLFVMAGLKVPLIATIIGEGGSGGALAIAMGDSVIMLQFATYAVISPEGCASILWKTAEKAPEAAEALGLTAHRLKALGLIDKIVNEPLGGAHRDPKSMATMLKRALAESLRQFQGMKTSELQARRHERLMAYGKFKETEGR
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
B2U9Q0
P37451
PDUF_SALTY
Propanediol uptake facilitator PduF
Salmonella
MNDSLKAQCGAEFLGTGLFLFFGIGCLSALKVAGASLGLWEICIIWGLGISLAVYLTAGISGGHLNPAVTIALWLFACFPKQKVLPYIIAQFAGAFGGALLAYVLYSSLFTEFETAHHMVRGSVESLQLASIFSTYPAAALNVWQAALVEVVITSILMGMIMALTDDGNGIPKGPLAPLLIGILVAVIGASTGPLTGFAMNPARDFGPKLFTWLAGWGNMAMSGGREIPYFIVPIVAPVIGACAGAAIYRYFIGKNLPCNRCEL
The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low.
P37451
Q5HUF2
TGT_CAMJR
tRNA-guanine transglycosylase
Campylobacter
MEFKLKHKDGMARVCEITTAHSTFLTPVFMPVGTVGAVKSLDANDMKNELDAKIILANTYHMYLRPTSKVVKDFGGLHGFTKFDRSFLTDSGGFQAFSLSKNSKHFNEGIEFKSHIDGSRHLFTPKSVLDAQYDFNSDIMMILDDLVALPATKERVKISVDRTILWAKEAITYHKNMQNKGIGIGQNIFGIIQGGTDYEERKRCALSLNEMPFDGLAIGGLSVGEENALMYETVQNLNPYLDENRPRYLMGVGTPEDLVENVERGVDMFDCVMPTRNARNGTFFTSFGKFNIKKAEFINDHEVIDPTCSCYTCRNFSRGYLNHLFKAKELTFFRLASLHNLHYYLELARKMREAILNNSFTQFKRNFYHLRGK
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Q5HUF2
Q5LC42
PYRG_BACFN
UTP--ammonia ligase
Bacteroides
MGETKYIFVTGGVASSLGKGIISSSIGKLLQARGYKVTIQKFDPYINIDPGTLNPYEHGECYVTVDGHEADLDLGHYERFLGIQTTKANNITTGRIYKSVIDKERRGDYLGKTIQVIPHITDEIKRNVKLLGNKYKFDFVITEIGGTVGDIESLPYLESIRQLKWELGQNALCVHLTYVPFLSAAQELKTKPTQHSVKELQSLGVQPDILVLRTEHDLNTNLRKKVALFCNVAENAVVQSIDASTIYEVPLLMQEQGLDETILQKMGLPVGERPPLGPWKDFLNRRANATETVTIAMVGKYVELQDAYKSILESLSQAATYNDRKVKIEYVSSEHLTPDNVDEQLGHVNGVVICPGFGSRGIEGKFVAAKYTREHNIPTFGICLGMQCMAIEFARNVLGYADANSIEMDEKTKHNVIDIMEEQKAITNMGGTMRLGAYECVLKKDSKVYEAYKEEHIQERHRHRYEFNNDYRKQFEEAGMKCVGINPESDLVEIVEIPTLKWYIGTQFHPEYSSTVLHPHPLFVSFIKAAIDK
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Q5LC42
Q75D30
ERI1_ASHGO
Endoplasmic reticulum-associated Ras inhibitor protein 1
Eremothecium
MNDKVAATLVLVVTYSIVGASLWCLTYAWHDETKLYYWCIVQLLPVMLWVWCVISWCGAQLFGYAKRGKAD
Probable component of the GPI-GlcNAc transferase (GPI-GnT) complex in the endoplasmic reticulum, a complex that catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI-anchors for cell surface proteins.
Q75D30
B5XWP0
SYY_KLEP3
Tyrosyl-tRNA synthetase
Klebsiella
MASSNLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTADSLHLGHLVPLLCLKRFQQAGHKPVALVGGATGLIGDPSFKAAERKLNTEDTVQEWVDKIRKQVAPFLDFDCGDNSAIAANNYDWFGSMNVLTFLRDIGKHFSVNQMINKEAVKQRLNRDDQGISFTEFSYNLLQGYDFACLNKLHGVALQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTEGGAVWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMDMAEINALEEEDKNSGKAPRAQYVLAEQVTRLVHGEEGLEAAKRITESLFNGNLSDLSESDFEQLAQDGMPMVELEKGTDLMQALVESELQPSRGQARKAIAANGVTVNGIKQPDPDYVLNENDRYFSNYTLLRRGKKNWCLIKWKSK
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
B5XWP0
A1USB4
GATB_BARBK
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Bartonella
MQMIDIRPPDPRHFISGSTGDWEVVIGMEVHAQIVSDSKLFSGASTKFGAEPNNHVSLIDAAMPGMLPVVNQECIRQAIRTGLGLKAQINLKSVFDRKNYFYPDLPQGYQISQFHYPIVGEGKVTISIGPDSNGQFEDVEIGIERLHLEQDAGKSIHDQHPTMSFVDLNRSGVALMEIVSKPDMRSSEEAKAYITKLRMILRYLGTCDGNMDEGSIRADVNVSVRRPGEPLGTRCEIKNVNSIRFIGQAIEYEARRQIAVLEDGGVIDPETRLFDAAKCETRSIRLKEEAHDYRYFPDPDLLPLEFDQAFVDALASELPELPDDIKARFINDMGLTVYDASILITEKEIADYFQKVARGRDGKMVANWVINDLLGALNKNNCKIEDTPVKPDQLGAIIDLIEEGIISGKIAKDLFEIIWHEGGDLRQIVEERGMKQVTDTGAIQSAVDEIMANNPDKVSQAKEKPALVGWFVGQVMKETGGKANPQTVNKLVKMKLEID
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
A1USB4
A6SZM5
GUAA_JANMA
Glutamine amidotransferase
Janthinobacterium
MHSKILILDFGSQVTQLIARRVRDSGVFSEVFPYDVSDEFVRNYGAAGVILSGGPNSVIEGDESPRVPQAVFELGVPVMGICYGMQAMAEQLGGKVENGKVREFGYAEVRAHGHTALLKDISDFTTPEGHGMLKVWMSHGDKVNEMPPGFKLMASTPNCPIAGMADEERRMYAFQFHPEVTHTVQGKAIIARFVHDICGCKSDWNMPDYIAEAVEKIRQQVGSDEVILGLSGGVDSSVAAALIHRAIGDQLTCVFVDHGLLRLDEGKMVMEMFAESLGVNVIHIDAVDQFMGHLAGVSDPEAKRKIIGREFVEVFQVEAGKRKNAKWLAQGTIYPDVIESAGKGKKGHTIKSHHNVGGLPETLNLQLLEPLRELFKDEVRKLGVALGLPHDMVYRHPFPGPGLGVRILGEVKKEFADLLRRADAIFIEELRKTPFVATPGASEATDNGIPHRNWYDATSQAFAVFLPVKSVGVMGDGRTYEYVVALRAVQTQDFMTAHWAHLPHELLGNVSNRIINEVRGINRVVYDISGKPPATIEWE
Catalyzes the synthesis of GMP from XMP.
A6SZM5
Q1G9R3
DNAJ_LACDA
Chaperone protein DnaJ
Lactobacillus
MAANRDYYDVLGVSRDASDAEISKAYRKLAKKYHPDLNHEAGAEEKYKEVNEAYEVLHDPQKRQQYDQFGQAGMNGQGGFGGQYGGQGFGGADFGDFGDIFSSFFGGARQQVDPTAPQRGADLDYTMTIDFMDAIKGKTSEISYSRSTTCEVCKGSGAEKGTHPITCDKCGGSGMMTITQRSVLGMIQRQTTCDKCTGSGVIIQHPCHNCHGKGVKTQKQTLQVKVPAGIDNGQQIRLAGQGEAGKNGGPYGDLYIVFRVRPSKDFTRRGQTIYTTVPISFAQATLGDEINVKTVYGDTKLKIPAGTQPNQKFTLKEKGVPSLRGGSTGDQVTTVEIVIPKSINEAQRKALLEFVKASGGSIAPQEKGFFERLKEKLS
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Q1G9R3
B1Z181
SELD_BURA4
Selenophosphate synthase
Burkholderia cepacia complex
MTEATLTPPAVPRLTSLSHGGGCGCKIAPGVLSELLKRATPPALFPDLLVGTETSDDAAVYRLNDEQAIVATTDFFMPIVDDPFDFGRIAATNALSDVYAMGGKPILALALVGMPINVLPHETIAAILRGGESVCAEAGIPVAGGHSIDSVEPIYGLAAIGVVHPSRVKRNAAARAGDVLVLGKPLGVGVLSAALKKNQLDAAGYAQMVATTTKLNRPGAELAALPGVHALTDVTGFGLLGHTLELARGANLTARVHYASLPWLAGVEAFVADGVFTGASGRNWAAYGTDVRLADGLPPVAQALLTDPQTSGGLLVACAPEAVDDVLACFRADGFDRAAVIGEMVDGPSRVDVA
Synthesizes selenophosphate from selenide and ATP.
B1Z181
P66878
COBIJ_MYCBO
S-adenosyl-L-methionine--precorrin-3B methyltransferase
Mycobacterium tuberculosis complex
MSARGTLWGVGLGPGDPELVTVKAARVIGEADVVAYHSAPHGHSIARGIAEPYLRPGQLEEHLVYPVTTEATNHPGGYAGALEDFYADATERIATHLDAGRNVALLAEGDPLFYSSYMHLHTRLTRRFNAVIVPGVTSVSAASAAVATPLVAGDQVLSVLPGTLPVGELTRRLADADAAVVVKLGRSYHNVREALSASGLLGDAFYVERASTAGQRVLPAADVDETSVPYFSLAMLPGGRRRALLTGTVAVVGLGPGDSDWMTPQSRRELAAATDLIGYRGYLDRVEVRDGQRRHPSDNTDEPARARLACSLADQGRAVAVVSSGDPGVFAMATAVLEEAEQWPGVRVRVIPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWDVIAARLTAAAAADLVLAIYNPASVTRTWQVGAMRELLLAHRDPGIPVVIGRNVSGPVSGPNEDVRVVKLADLNPAEIDMRCLLIVGSSQTRWYSVDSQDRVFTPRRYPEAGRATATKSSRHSD
Methylates precorrin-2 at the C-20 position to produce precorrin-3A.
P66878
B7JYV9
RF3_RIPO1
Peptide chain release factor 3
Rippkaea orientalis
MSSELQTEIQEAVEKRRNFAIISHPDAGKTTLTEKLLLYGGAIHQAGAVKARRDQRKATSDWMEMEKQRGISITSTVLQFEYRNFQINLLDTPGHQDFSEDTYRTLAAADNAVMLIDAAKGLEPQTRKLFEVCRLRGLPIFTFINKLDRPTREPLELLDEIEQELGLKTYAVNWPIGTGDRFKGVFDRRHQGIHLFERRAHGSQQAQETAIKLGDPKIEAHLEQELYYQLKEELEILQELGGDLDLKELHDGQITPVFFGSAMTNFGVQLFLEAFLEYALQPEGRNSSVGVVDPTHPEFSGFVFKLQANMDPKHRDRVAFVRVCTGKFEKDMTVSHARTGKTVRLSRPQKLFAQDRESIEEAYGGDVIGLNNPGVFAIGDTIYSGTKLEYEGIPCFSPEIFAYLKNPNPSKFKQFQKGIQELREEGAIQIMYSTDDFKRDPILAAVGQLQFEVVQFRMLSEYGVETNLEPLPYSVARWVTGGWTALEKAGRIFNSMTVKDNWDRPVLLFKNEWNLNQVKADKPELGLSSTAPVGSGINE
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.
B7JYV9
Q08A71
ANM6_ARATH
Probable protein arginine N-methyltransferase 6
Arabidopsis
MQSGGDFSNGFHGDHHRELELEDKQGPSLSSFGRAKKRSHAGARDPRGGLANVLRVSDQLGEHKSLETSESSPPPCTDFDVAYFHSYAHVGIHEEMIKDRARTETYREAIMQHQSLIEGKVVVDVGCGTGILSIFCAQAGAKRVYAVDASDIAVQAKEVVKANGLSDKVIVLHGRVEDVEIDEEVDVIISEWMGYMLLYESMLGSVITARDRWLKPGGLILPSHATLYMAPISHPDRYSHSIDFWRNVYGIDMSAMMQLAKQCAFEEPSVESISGENVLTWPEVVKHIDCKTIKIQELDSVTARYKFNSMMRAPMHGFAFWFDVEFSGPASSPAKNTSETSIASGSSSISPSGEVNQKKRTNPSDALVLSTSPESPPTHWQQTIVYFYDPIDVEQDQVIEGSVTLSQSKENKRFMNIHLEYSSAGRSFVKESVMR
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA).
Q08A71
A1KVS7
MTGA_NEIMF
Peptidoglycan glycosyltransferase MtgA
Neisseria
MFRIVKWLIALPVGIFIFFNAYVYGNIITYRAVAPHRTAFMSMRMKQFEQEGRDVALDYRWVPYNRISVNLKKALIASEDAHFAGHGGFDWGGIQNAIRRNRNSGKVKAGGSTISQQLAKNLFLNESRSYIRKGEEAAITAMMEAVTDKDRIFELYLNSIEWHYGVFGAEAASRYFYQIPAAKLTKQQAAKLTARVPAPLYYADHPKSKRLRNKTNIVLRRMGSAELPESDTD
Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
A1KVS7
Q8DPQ5
PYRC_STRR6
Dihydroorotase
Streptococcus
MLLIKNGRVMDPKSGLDQVCDVLVQDGKIIKIAPEITEEGAETIDATGHVVAPGLVDIHVHFREPGQTHKEDIHTGALAAAAGGFTTVVMMANTSPTISDVETLQAVLQSAAKEKINVKTVATITKNFNGKNLTDFKALLEAGAVGFSDDGIPLESSKIVKEAMEEAKKLNTFISLHEEDPGLNGVLGFNENIAREHFHICGATGVAEYAMMARDVMIAYATKAHVHIQHLSKEESVKVVEFAQGLGAEVTAEVAPQHFSKTEALLLTQGSNAKMNPPLRLESDRRAVIEGLKSGVITVIATDHAPHHVDEKNVEDITKAPSGMTGLETSLSLGLTYLVEAGELSLMELLEKMTYNPAKLYNFEAGYLAENGPADITIFDAKADRLVDSHFASKAANSPFIGETLKGQVKYTICKGQIVYQA
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Q8DPQ5
P80563
PGTL_PELAC
Transhydroxylase subunit alpha
Pelobacter
MGEVVRLTNSSTGGPVFVYVKDGKIIRMTPMDFDDAVDAPSWKIEARGKTFTPPRKTSIAPYTAGFKSMIYSDLRIPYPMKRKSFDPNGERNPQLRGAGLSKQDPWSDYERISWDEATDIVVAEINRIKHAYGPSAILSTPSSHHMWGNVGYRHSTYFRFMNMMGFTYADHNPDSWEGWHWGGMHMWGFSWRLGNPEQYDLLEDGLKHAEMIVFWSSDPETNSGIYAGFESNIRRQWLKDLGVDFVFIDPHMNHTARLVADKWFSPKIGTDHALSFAIAYTWLKEDSYDKEYVAANAHGFEEWADYVLGKTDGTPKTCEWAEEESGVPACEIRALARQWAKKNTYLAAGGLGGWGGACRASHGIEWARGMIALATMQGMGKPGSNMWSTTQGVPLDYEFYFPGYAEGGISGDCENSAAGFKFAWRMFDGKTTFPSPSNLNTSAGQHIPRLKIPECIMGGKFQWSGKGFAGGDISHQLHQYEYPAPGYSKIKMFWKYGGPHLGTMTATNRYAKMYTHDSLEFVVSQSIWFEGEVPFADIILPACTNFERWDISEFANCSGYIPDNYQLCNHRVISLQAKCIEPVGESMSDYEIYRLFAKKLNIEEMFSEGKDELAWCEQYFNATDMPKYMTWDEFFKKGYFVVPDNPNRKKTVALRWFAEGREKDTPDWGPRLNNQVCRKGLQTTTGKVEFIATSLKNFEEQGYIDEHRPSMHTYVPAWESQKHSPLAVKYPLGMLSPHPRFSMHTMGDGKNSYMNYIKDHRVEVDGYKYWIMRVNSIDAEARGIKNGDLIRAYNDRGSVILAAQVTECLQPGTVHSYESCAVYDPLGTAGKSADRGGCINILTPDRYISKYACGMANNTALVEIEKWDGDKYEIY
Isomerization of pyrogallol to phloroglucin.
P80563
P13582
EAST_DROME
Serine protease easter
Sophophora
MLKPSIICLFLGILAKSSAGQFYFPNEAAQVPNYGRCITPNRERALCIHLEDCKYLYGLLTTTPLRDTDRLYLSRSQCGYTNGKVLICCPDRYRESSSETTPPPKPNVTSNSLLPLPGQCGNILSNRIYGGMKTKIDEFPWMALIEYTKSQGKKGHHCGGSLISTRYVITASHCVNGKALPTDWRLSGVRLGEWDTNTNPDCEVDVRGMKDCAPPHLDVPVERTIPHPDYIPASKNQVNDIALLRLAQQVEYTDFVRPICLPLDVNLRSATFDGITMDVAGWGKTEQLSASNLKLKAAVEGSRMDECQNVYSSQDILLEDTQMCAGGKEGVDSCRGDSGGPLIGLDTNKVNTYYFLAGVVSFGPTPCGLAGWPGVYTLVGKYVDWIQNTIES
Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo . Three proteases; ndl, gd and snk process easter to create active easter . Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo .
P13582
Q8NQV2
DDL_CORGL
D-alanylalanine synthetase
Corynebacterium
MSNSNSGKVRVAVVYGGRSSEHSVSCVSAGAIMAHLDPEKYDVIPVGITVDGAWVVGETDPQKLTLIDRTMPEVEHHEEVRPSLDPAHRGEFHFSDGSLYATADVIFPVLHGRFGEDGTVQGLFALSDIPVVGPGVLASAAGMDKEYTKKLMAAEGLPVGREVILRDRTELTEAEKNLLGLPVFVKPARGGSSIGISRVTAWEDFNKAVGLARAHDEKVIVESEIVGSEVECGVLQYPDGRIVASVPALLSGTESGAGGFYDFDTKYLDNVVTAEIPAPLDEKTTELIQSLAVESFQALACEGLARVDFFVTANGPVLNEINTMPGFTPISMYPQMFTASGVAYEELLDVLVQQALHRDN
Cell wall formation.
Q8NQV2
Q8VTT5
HYDA_RALPI
D-hydantoinase
Ralstonia
MDIIIKNGTIVTADGISRADLGIKDGKITQIGGALGPAERTIDAAGRYVFPGGIDVHTHVETVSFNTQSADTFATATVAAACGGTTTIVDFCQQDRGHSLAEAVAKWDGMAGGKSAIDYGYHIIVLDPTDSVIEELEVLPDLGITSFKVFMAYRGMNMIDDVTLLKTLDKAVKTGSLVMVHAENGDAADYLRDKFVAEGKTAPIYHALSRPPRVEAEATARALALAEIVNAPIYIVHVTCEESLEEVMRAKSRGVRALAETCTHYLYLTKEDLERPDFEGAKYVFTPPARAKKDHDVLWNALRNGVFETVSSDHCSWLFKGHKDRGRNDFRAIPNGAPGVEERLMMVYQGVNEGRISLTQFVELVATRPAKVFGMFPQKGTIAVGSDADIVLWDPEAEMVIEQTAMHNAMDYSSYEGHKVKGVPKTVLLRGKVIVDEGSYVGEPTDGKFLKRRKYKQ
Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives.
Q8VTT5
D5FM34
NAS35_HAECO
Procollagen C-proteinase
Haemonchus
MSLLRSASLLLVVVTAALPPCTLGYSLHDGSRLDDVIAEFTAERRPRRLATPAQRRLMGLTEEQHKTVQFYLDKLRELGNRRHPESYNKDSPKNEAYKWRKQMRDDLKTELLNPEKYGRHFEGDIILFPEQAKQIYENALKTGQRRVKRKFIGSDLRRWDPTRPIIYSFDGSHTSREQRIIELALEHRHNITCLNFVRNDNANKGNRIVFTDVDGCASNVGRHPLGEEQLVSLAPECIRLGVIAHEVAHALGFWHEQSRPDRDQFVNVRWENIDKDSKGQFLKEDPDDVDNAGVPYDYGSIMHYRSKAFSRYDDLYTISTFVTDYQKTIGQRDQLSFNDIRLMNKIYCSNVCSRKLPCQRGGYTDPRRCDRCRCPDGFTGQFCEQVMPGYGAVCGGRIQVNSGWTRFSSPGYPREFKEGQECSWLLVAPPGQVVEMQFIGEFEMYCKVRHSLCMDYVEVRNSTDFANTGMRYCCYGTPSTSIRSATTDLVVLFRSFYRGGRGFEARARALPANGQWASWTPWTPCTASCGACGSRMRTRVCPHGACPC
Metalloprotease which cleaves the carboxyl terminus of procollagens to mature collagens. Probably involved in cuticular collagen maturation.
D5FM34
Q6C093
UBC2_YARLI
Ubiquitin-protein ligase UBC2
Yarrowia
MSTTARRRLMRDFKRMQQDPPQGVSASPVADNVLTWNAVIIGPAETPFEDGTFRMVLQFDEQYPNKPPAVKFVSQMFHPNVYSSGELCLDILQNRWSPTYDVAAILTSVQSLLNDPNTSSPANVEASMLYKDHRQQYEKRVRDTVEASWTD
Catalyzes the covalent attachment of ubiquitin to other proteins. Plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. Also involved in postreplication repair of UV-damaged DNA, in N-end rule-dependent protein degradation and in sporulation.
Q6C093
Q51463
FLIF_PSEAE
Flagellar M-ring protein
Pseudomonas
MADALIDSQVPAKSGGAGMLKKSFPGLSFLDNLSEMTMLRQIGLLVGLAASVAIGFAVVLWSQQPDYKPLYGSLNGVDANRVVEALTAADIPYKVEPNSGALLVKADDLGRARMKVASAGVAPTDNNVGFEILDKEQALGTSQFMEATNYRRGLEGELARTVSSLNNVKAARVHLAIPKSSVFVRDDRKPSASVLVELYPGRSLEPSQVMAIVNLVATSVPELDKSQVTVVDQKGNLLSDQQELSELTMAGKQFDFTRRMEGLLTQRVHNILQPVLGNGRYKAEVSADVDFSAVESTSEMYNPDQPALRSEQRNNEERQNSSGPQGVPGALSNQPPGPASAPQQATASAPADYVAPGQPLKDANGQTIIDPKTGKPELAPYPTDKRDQTTRNYELDRSISYTKQQQGRLRRLSVAVVLDDQMKVDAKTGEVSHQPWSADELARFTRLVQDSVGYDASRGDSVSVINAPFAPAQAEEIDSIPFYSQPWFWDIVKQVLGVLFILVLVFGVLRPVLSNITGGGKGKSLAGGGGRDGDLALGESGLEGSLADDRVSIGGPSSILLPSPTEGYDAQLNAIKNLVAQDPGRVAQVVKEWINADE
The M ring may be actively involved in energy transduction.
Q51463
P36053
ELF1_YEAST
Transcription elongation factor 1
Saccharomyces
MGKRKKSTRKPTKRLVQKLDTKFNCLFCNHEKSVSCTLDKKNSIGTLSCKICGQSFQTRINSLSQPVDVYSDWFDAVEEVNSGRGSDTDDGDEGSDSDYESDSEQDAKTQNDGEIDSDEEEVDSDEERIGQVKRGRGALVDSDDE
Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions.
P36053
P07947
YES_HUMAN
p61-Yes
Homo
MGCIKSKENKSPAIKYRPENTPEPVSTSVSHYGAEPTTVSPCPSSSAKGTAVNFSSLSMTPFGGSSGVTPFGGASSSFSVVPSSYPAGLTGGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEIRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHYTEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMSKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGENLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILQTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELMNLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQPGENL
Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis.
P07947
Q8DSG3
SYDND_STRMU
Non-discriminating aspartyl-tRNA synthetase
Streptococcus
MKELFIGNYGLEQVGQKVTAKGWVANIRNHGKLAFIELRDREGLLQVFVDSAVADFDKLHDLHKESILAVTGEIVARDERFVNPHIKSGQVELRAETIEIIASSKLLPFELDNHAHAGEDIRQKYRYLDLRREKMTANLKLRHQVTKAIRDYLNQADFIDVETPYLTKSTPEGARDFLVPSRVFKNQFYALPQSPQMLKQLLMGAGLERYYQIVRCFRDEDLRGDRQPEFTQVDLEMSFVSEEDVRNLVEGMLKAVVKASKGIELTEAFPIISYAQAMRRFGSDKPDTRFAMELKDLTELSRGNTSLFLQKGLKKENGVVMGICAKNAAKAFTNRQMATLKQLVMDFGVAGFATATIEKGQVTGSLKSTFKDHNTELLELFEAEDGDMIFFVTGSLKRVQEALGGLRVRLAKDLELIDNDKLNFLWVVDWPLLEWNEDLNRYQAMHHPFTQGAFEDGSDWKENPEKMMSRAYDIVLNGYEIGGGSLRIHKRSAQEAMFELLGMKKEDYERDFGFFLEALEYGFPPHGGLALGLDRLVMILAEEGNIREVIAFPKNGQGADAMLESPSLVADQQLAELRLALRD
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Q8DSG3
Q2GHV0
ISPF_EHRCR
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Ehrlichia
MNQHPNKPIFKVGIGYDVHKFDNTCYNDANTFITICGIKINYHKKIIAHSDGDVGLHALTDAILGAVGCGSIGQHFPNTDNTWKNIKSDYFLIEAQKKAQEKGYSISNADITIICEQPKIMPHALEMQEYIANLICIDPSCINVKATTTEKLGFLGRKEGIAAQAIVLCCLQN
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Q2GHV0
A1UCA4
ADD_MYCSK
Adenosine aminohydrolase
unclassified Mycobacterium
MTTPLTLENISQAPKALLHDHLDGGLRPSTVLELAGQYGYDDLPADDVDELATFFRTAAHSGSLVRYLEPFAHTVGVMQTAEALHRVAFECVEDLAGDNVVYAEVRFAPELHIEGGMGLDAVVDAVLAGFADGEKAAASAGRTITVRCLVTAMRHAARSREIAELAIRFRDRGVVGFDIAGAEAGYPPTRHLDAFEYMRGNNARFTIHAGEAFGLPSIHEAIAFCGADRLGHGVRIVDDITVAPDGQVKLGRLAAILRDKRIPLELCPSSNVQTGAVASIAEHPFDLLARTRFRVTVNTDNRLMSDTSMSQEMLRLVEAFGYGWSDLARFTINAMKSSFIPFDERLALIDDVIKPRYAVLAG
Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine.
A1UCA4
B6YVT5
RNH2_THEON
Ribonuclease HII
Thermococcus
MKLAGIDEAGRGPVLGPMVIAAVVVDEGNVPKLEELGVKDSKKLTPKRRERLFDEIVQLLDDYVILELWPEEIDSREGTLNEFEVENFVKALNSLKVKPDVVYIDAADVKEARFGEEIKAKLDFEADIIAEHKADDKFVPVSAASILAKVARDRAIEKLKDQYGEIGSGYPSDPRTRTFLEEYYRKHGEFPPIVRRTWKTLKKIEEKLAKEMKKRRGQTSLEEFFGK
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
B6YVT5
Q4L7U0
LEU1_STAHJ
Alpha-isopropylmalate synthase
Staphylococcus
MESHIQIFDTTLRDGEQTPGVNFSFDERLKIAKQLETWGVDILEAGFPASSAGSFKSVQAISNTLTKTAVCGLARCKKSDIDAVYEATKDAVKPVIHVFIATSPIHLTHKLKMTQQQVLESIKEHVSYAKQYFDVVQFSPEDATRTDTDFLIKCVQMAVDCGATIINIPDTVGYSYPNEYGRIFKTLIENINSKQDITYSAHCHDDLGMAVANSLAAIENGAKRIEGTVNGIGERAGNTAIEELALALYVRKDHYGNETRLKLSETKNTSDIISRYAGIRVPRNKAIVGQNAFSHESGIHQDGVLKNPETYEIMTPQLVGISKNDLPLGKLSGKHAFAEKLKSLGYDIEPQNQAELFKQFKAIADKKKSVTDRDIHAIIQGTEHEQNAIYQVDTLQLQFVSNGLQSAVVVIKDKNGNIYQDSSIGTGSIVAIYNAVDRIFKHKSELIDYRIDSVTEGTDAQAEVHVSLTIEGQPVNGIGIDHDVLYASCKAYVEAHAKYASEINKKEGNH
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Q4L7U0
Q96EH3
MASU1_HUMAN
Mitochondrial assembly of ribosomal large subunit protein 1
Homo
MGPGGRVARLLAPLMWRRAVSSVAGSAVGAEPGLRLLAVQRLPVGAAFCRACQTPNFVRGLHSEPGLEERAEGTVNEGRPESDAADHTGPKFDIDMMVSLLRQENARDICVIQVPPEMRYTDYFVIVSGTSTRHLHAMAFYVVKMYKHLKCKRDPHVKIEGKDTDDWLCVDFGSMVIHLMLPETREIYELEKLWTLRSYDDQLAQIAPETVPEDFILGIEDDTSSVTPVELKCE
Required for normal mitochondrial ribosome function and mitochondrial translation . May play a role in ribosome biogenesis by preventing premature association of the 28S and 39S ribosomal subunits (Probable). Interacts with mitochondrial ribosomal protein L14 (MRPL14), probably blocking formation of intersubunit bridge B8, preventing association of the 28S and 39S ribosomal subunits (Probable). Addition to isolated mitochondrial ribosomal subunits partially inhibits translation, probably by interfering with the association of the 28S and 39S ribosomal subunits and the formation of functional ribosomes (Probable). May also participate in the assembly and/or regulation of the stability of the large subunit of the mitochondrial ribosome . May function as a ribosomal silencing factor (Probable).
Q96EH3
P0DN22
ALMA1_DURXX
Symbiodinium-A1
Symbiodinium
MPLILGGLAGAAAGYGAAAWLERRKPPPGKDPNIKHASLGVVRLDWHYHPLPGDVGSPDSFEYPVYYRAVPGLTFEICQSGKMSPEIQQNFKDAIEFLDKERGVSVITSDCGFFMWFQKEARLYTSKPVVMSSLALLPSLHAAIGTDGKIAIFSANSTSLGPMHDTVAKECGVDWDEACYVLVGCQDVEGFEAVASGEPLDLEKVTPGIVRKAKQVIAEHPDIHAILMECTQLPPFSDDVRAATGLPVYDAIVSADFFIRGFVDNPRFGLNDWHRPWDGHQEKYKLGDNVQDKEKLLHYKP
Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle.
P0DN22
Q63AJ1
KYNB_BACCZ
N-formylkynurenine formamidase
Bacillus cereus group
MKTSEWIDISQPLNNDIATWPGDTPFSYEVSWSKEESGSVNVGKLTMSIHTGTHIDAPFHFDNEGKKVIDLDVQVYVGPARIIDVSNLESIGKKELENFHLEGVERLLLRTSSHGKANEFPDVIPHLRADIAPFLSEKGIRLIGVDVPSVDPLDDKELAAHHQLFKHGIHILENVVLDHVADGDYELIALPLALSDADGSPVRAVIRPI
Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.
Q63AJ1
O82139
CAS1_PANGI
Phytosterol synthase
Panax
MWKLKIAEGGNPWLRTLNDHVGRQIWEFDPNIGSPEELAEVEKVRENFRNHRFEKKHSADLLMRIQFANENPGSVVLPQVKVNDGEDISEDKVTVTLKRAMSFYSTLQAHDGHWPGDYGGPMFLMPGLVITLSITGVLNVVLSKEHKREICRYLYNHQNRDGGWGLHIEGPSTMFGTVLNYVTLRLLGEGANDGQGAMEKGRQWILDHGSATAITSWGKMWLSVLGVFEWSGNNPLPPETWLLPYILPIHPGRMWCHRRMVYLPMSYLYGKRFVGPITPTVLSLRKEVFSVPYHEIDWNQARNLCAKEDLYYPHPLIQDILWASLDKVWEPIFMHWPAKKLREKSLRTVMEHIHYEDENTRYICIGPVNKVLNMLCCWVEDPNSEAFKLHLPRLHDFLWLAEDGMKMQGYNGSQLWDTAFAVQAIISTNLAEEYGPTLRKAHTFMKNSQVLDDCPGDLDAWYRHVSKGAWPFSTADHGWPISDCTAEGFKAVLQLSKLPSELVGEPLDAKRLYDAVNVILSLQNSDGGYATYELTRSYSWLELVNPAETFGDIVIDYPYVECTSAAIQALTAFKKLFPGHRREEIQHSIEKAALFIEKIQSSDGSWYGSWGVCFTYGTWFGIKGLVTAGRTFSSCASIRKACDFLLSKQVASGGWGESYLSCQNKVYTNLEGNRSHVVNTGWAMLALIDAGQAERDATPLHRAAKLLINSQMENGDFPQEEIMGVFDKNCMITYAAYRNIFPIWALGEYRCRVLQGPS
Component of the phytosterols biosynthetic pathways (Probable). Oxidosqualene cyclase converting oxidosqualene to cycloartenol .
O82139
Q9NYL5
CP39A_HUMAN
Oxysterol 7-alpha-hydroxylase
Homo
MELISPTVIIILGCLALFLLLQRKNLRRPPCIKGWIPWIGVGFEFGKAPLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFELAVQNIVYRTASIPKNVFLALHEKLYIMLKGKMGTVNLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQLPECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLDIVETETSKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSLLDPLPKQSYLHLVGVPQPEGQCRIEYKQRI
A cytochrome P450 monooxygenase involved in neural cholesterol clearance through bile acid synthesis . Catalyzes 7-alpha hydroxylation of (24S)-hydroxycholesterol, a neural oxysterol that is metabolized to bile acids in the liver . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) .
Q9NYL5
B0BWS2
DDL_RICRO
D-alanylalanine synthetase
spotted fever group
MHKYQTHWVEHSIVKILSSTGKKHIALMAGGMSAEREVSLVSSEGVSKALIELGYRVTFIDMGADIAVRLQEIKPDIVFNCLHGTYGEDGGLPGLLNIMRIPYTHSGVLSSALAFDKIHSRIWFLTNNINMAESIVVNKSDNIKNDPMKRPYVIKPLTQGSSIGVEVIFAEDDFNFADYDFPYGDQVIIEQYIKGRELQVAVLNGKALGALEIKLLKNRFYDYETKYTAGFADHLCPAPLPANLYEKLLIESEKIYKTMNCKGPARAEFILEEQTNKLYALEINTHPGMMSLSIVPEIAAYAGINFTNLIEEIIKTASFES
Cell wall formation.
B0BWS2
Q0SWX6
DNAA_CLOPS
Chromosomal replication initiator protein DnaA
Clostridium
MDAQLNNLWEQALNIIKGEISEISFNTWIKSCTPISISDNILKLSVPNEFTKGILDTRYKDLLIQALKIVTSRKFKIEFYLESDLEEEKENEEKQKEEKKDNTNDVDGSIVVSDEMSATLNPKYTFQSFVIGNSNRFAHAASLAVAESPAKAYNPLFIYGGVGLGKTHLMHAIGHYILQENPKAKVVYVSSEKFTNELINAIKDDKNEEFRNKYRKVDVLLIDDIQFIAGKERTQEEFFHTFNALHEENKQIILSSDRPPKEIPTLEDRLRSRFEWGLIADIQPPDFETRMAILKKKADVEGLSVPNEVMVYIATKIKSNIRELEGALIRIIAYSSLTNRDVSVDLASEALKDIISNKESAPVTVKTIQESVANYYNLRIEDLKSQRRTRNIAYPRQIAMYLSRKLTDMSLPKIGEEFGGRDHTTVIHAYEKISENLKTDEGLQSMINDITKKLTQK
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
Q0SWX6
P35223
CTNB_TRIGR
Beta-catenin
Tripneustes
MEQARYSNQQSVNPQQKGFGGPGLQDLPKQDPMQNTMEWQHHGYGMDSGFQSSATSHPPSVSSKSRHEDGGEEAQAQGMFEWDAGYGQAYTQEQVDEMNQQLTQTRSQRVRAAMFPETLEEGVQIPSTQFDPAHPTAVQRLSEPSQMLKHAVVNLINYQDDADLATRAIPELTKLLNDDDLVVVNQAAMMVHQLSKKEASRHAIMNSPQMVAALVRAMSNSNDAETTRCAAGTLHNLSHHRAGLLQIFKSGGIPALIKLLSSPVESVLFYAITTLHNLLLHQEGSKMAVRLAGGLQKMVALLSRNNPKFLAITTDCLQILAYGNQESKLIILASGGPAALVHIMRTYDYEKLLWTTSRVLKVLSVCHNNKPAIVEAGGMSALGLHLGHHSNRLVQNCLWTLRNLSDCHRGTDDIEPLLQMLVQLLASNDINVVTCACGILSNLTCNNSRNKMIVSQMAGVEALVQTLMKAGDREEITEPAVCALRHVTSRHPGAEMGQNTVRLNYGIPVIVKLLHPPSRWPLIKATVGLIRNLALCSANHAPLREQGALHRLVQLLMRAHQDTQRRSSMGSTGSQGGNYADGVRMEDIVEGTTGALHILARDSHNRALIQGLNCIPLFVQLLYNNIENIQRVAAGVLSELSLEKQGAEMIEQEGATAPLTELLHSRNEGVATYAAAVLYRMSDDKPQDYKKRISVELGNSLFRGDSVPWGDPLDMPSDNQILPPSSMGGHPPDPGYPQPGSVHSLHSNHGEYRQPPPPMQGYHDGTGPIEPMMQDLDLGGGGDFGMDPGLPDMGPPASDLNLDSIPPADNTGLAFFDTDL
Binds to the cytoplasmic domain of the cell-cell adhesion molecule E-cadherin, and perhaps to other (membrane) proteins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties.
P35223
P29540
T2EB_XENLA
Transcription initiation factor IIE subunit beta
Xenopus
MDPALLRDRELFKKRALTTPAVEKRPSASSESSKKKRAKLELSSTSGSKPSSDGSNGSFNLKSLSGSSGYKFGVLAKIVNYMKTRHQRGDTYPLTLEEILDETQHLDIGIKQKQWLMSEALVNNPKIEIIDGKYAFKPKYNLKDKKALLRLLDKHDQRGLGGILLEDIEEGLPNAQKAIKALGDQIVFVTRPDKKKILFYNDKSCQFTVDEEFQKLWRSVPVDSMDDEKIEEYLKRQGISSMQESGPKKIIPVQKRKKATSQRRRFKTHNDHLAGVLKDYTDVASGKP
Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.
P29540
Q59542
DHMH_METME
Methylamine dehydrogenase (amicyanin)
Methylophilus
MTTFDHPSMIRQPKPTGLAGGLVLAALMLSSSLALADATPNQLGSEITAKLQDETSIAIAPASDSKRVYVLDPGNFHMTSTVYTIDGKSSKLLGMTDAGKLPNVMVASDGKFLAIANTMYSRVARGKRDDYLELIDTKTHQPIADIDIPEGRFLTGVFERTAGLSVDDKHLLFQQFSPSPGVGLVDLQQKAFVKIMNVPDCYHIFPTANQNFFMHCRDGSLMQFTYDSKGNTKQKPTKIFHAEKEYLLNNPYYSNSNNHLTWPTYEGKIFQAKLSESGAEFLKPIEVFTDKEKADKWRPGGWQTIAFHKARNELYLLADQREKWTHKLPSRFVFVVDATSGKRLRRIELKHEINSIAVSQDDKPYLYAVSEEAKTLFTFDAVNGKALSSIDELGRAPSMIFIADK
Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.
Q59542
A2RE43
UVRB_STRPG
Excinuclease ABC subunit B
Streptococcus
MIDKRDDKPFKLKSKYKPSGDQPQAIESLVDNIEGGEKAQILLGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEFFPDNAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSSLLERNDVIVVASVSCIYGLGSPKEYADSAVSLRPGQEISRDTLLNQLVDIQFERNDIDFQRGCFRVRGDVVEVFPASRDEHAFRVEFFGDEIDRICEIESLTGKTIGEVDHLVLFPATHFVTNDEHMEQSIAKIQAELAEQLQLFESEGKLLEAQRLRQRTEYDIEMLREMGYTSGVENYSRHMDGRSPGEPPYTLLDFFPEDFLIMIDESHMTMGQIKGMYNGDQARKQMLVDYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGEYEMSQTNTIIEQIIRPTGLLDPEIDVRPSMGQIDDLLGEINQRVARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNVDGHVIMYADKMTDSMQRAIDETARRREIQIAYNKAHGIVPQTIKKDIRGLISISKTSHNDISKEEMDYESMSRGERKEAINALQKQMQEAAELLDFELAAQMRDLILELKLMD
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
A2RE43
P24624
RBL_ANTSP
Ribulose bisphosphate carboxylase large chain
unclassified Antithamnion
MSNSVEERTRIKNERYESGVIPYAKMGYWDPEYAVKDTDILALFRVSPQPGVDPIEASAAVAGESSTATWTVVWTDLLTACDLYRAKAYKVDAVPNTSDQYFAYIAYDIDLFEEGSIANLTASIIGNVFGFKAIKALRLEDMRIPVAYLKTIQGPATGIIVERERMDKFGRPFLGPTVKPKLGLSGKNYGRVVYEGLRGGLDFLKDDENINSQPFMRWKERFLYSMEAVNRSIAATGEVKGHYMNVTASTMEDMYERAEFAKQLGTVIIMIDLVIGYTAIQSMGIWARKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIRGFYNTLLLSELAIDLPKGIFFEQDWAALRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMVIARNEERDYVAEGPQILLDAAKTCGPLQTALDLWKDITFNYTSTDTADFVETPTANV
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
P24624
P42788
CBPZ_SIMVI
Zinc carboxypeptidase
Simulium
QYHTLPEIYSWLDRLVQEHPEHVEPVVGGKSYEGREIRGVKVSYKKGNPVVMVESNIHAREWITAATTTYLLNELLTSKNSTIREMAENYDWYIFPVTNPDGYVYTHTTDRMWRKTRSPNPDSLCAGTDPNRNWNFHWMEQGTSSRPCTETYGGKKAFSEVETRSFSDFLKTLKGQIKVYLAFHSYSQLLLFPYGHTCQHTYNHDDLQAIGDAAARSLAQRYGTDYTVGNIYDAIYPASGGSMDWAYDTLDIPIAYTYELRPRDGWNGFQLPANQIIPTGEETVDSVVTILKESRRLGYFNTSD
Involved in the digestion of the blood meal.
P42788
Q97F64
RL31_CLOAB
50S ribosomal protein L31
Clostridium
MQKDIQPEYHQDAVVKCACGNTFTTGSTKKELKVDICSKCHPFFTGQQKIVDVGGRVEKFRKKYNLSADK
Binds the 23S rRNA.
Q97F64
A6VUP6
RNC_MARMS
Ribonuclease III
Marinomonas
MSSLYQKLSRRIGYFFADLGLLELALTHRSFGGKNNERLEFLGDSILNYVIAEDLFHRFPKAKEGELSRLRASLVKGDTLAELAREFELGDYLKLGAGELKSGGFRRDSILADTVEGIIGAMYLDAGMDVCRQHILAWYKERLDATSLKIVTKDAKTRLQEFLQARKHALPQYDVVNIVGEPHDQTFYVHCHIELCEEFIEGKGNSRRIAEQNAAAKALKKLEKKDV
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
A6VUP6
B2V049
GLGA_CLOBA
Starch [bacterial glycogen] synthase
Clostridium
MRVLFVASEAHPFIKSGGLGDVAGALPKELARKGVDVRVVIPKYREINNELKNKLRFNKWFNVDVGWRNQYCGILEYEYDGVIYYFVDNEYYFSRGGMYGHYDDAERFAFFDRAVLDMIKQLDWKPNIIHCNDWQTGMIPVLLKLEYMRKDMFYWDIKSVFSIHNIAFQGVFDPVILPELFGYDYEQYTNTNLKFDDGVGFMKGAINYSDMITTVSYSYAEEIKTPEFGERLDWLLREKSYMLRGILNGIDYDEFNPKNDNLINKNYDVNNINDKYENKRNLQSELGLNVNENIPIIAMVTRLTSQKGLDLLVNISERLLQNDIQLVIVGTGDKHYEDHFKWLDYKYGNKVSANIRFDNNLAHKVYAASDMFLMPSLFEPCGLGQLIALRYGSIPIVRETGGLKDTIRAYNEYTGEGNGFSFYNYNADELLHIIEYALKIYYDKNKWSNLVKNAMNSNNSWSKSADEYLNMYKELSYR
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
B2V049
Q5XCL9
ENGB_STRP6
Probable GTP-binding protein EngB
Streptococcus
MAEEQVLNTHNASILLSAANKSHYPQDDLPEIALAGRSNVGKSSFINTILGRKNLARTSSKPGKTQLLNFFNIDNKLRFVDVPGYGYAKVSKSERAKWGKMIEEYLTSRDNLRAVVSLVDLRHAPSKEDIQMYDFLKYYDIPVIVVATKADKIPRGKWNKHESVVKKALNFDKSDTFIVFSSVERIGIDDSWDAILEQV
Necessary for normal cell division and for the maintenance of normal septation.
Q5XCL9
P0A234
PGTC_SALTI
Phosphoglycerate transport regulatory protein PgtC
Salmonella
MFGSCQAYSRELVMATTFSPSATAWIIQRWQTEPGSVMIRTLNRTSGSLEQLLDTANAENVDLILTSSPMLLQHLQEHQKLALLDSAPAASQKLVPRSIRSTSVAVAVSGFGLLINRSALAARHLPPPADWQDMGLPSYQGALLMSSPSRSDTNHLMVESLLQQKGWTAGWATLLAISGNLVTISSRSFGVADKIKSGLGVAGPVIDNYANLLLNDPNLAFTYFPYSAVSPTYVAVLKNSRHADEARAFIHYLLSPKGQRILADANTGKYPVAPLSADNPRAAQQQRLMAQPPLNYRLILKRQQLVQRMFDTAISFRLAQLKDAWRALHSAETRLKRPLPEIRALLTSVPVDAASSEDETWLAQFDNKSFAEQKMMEWQIWFLNNQRLAIHKLEELK
Required for pgtP expression, it may act jointly with the PgtA/PgtB signaling proteins.
P0A234
Q9MUS4
PETN_MESVI
Cytochrome b6-f complex subunit VIII
Mesostigma
MDIISLGWVFLMVFFSFSLSLVVWARNGL
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Q9MUS4
Q85XY8
MATK_MIMPU
Intron maturase
Mimosa
MKEYQVYLERDRSRQQDFLYPLIFREYVYGLAYSHDFNRSTFVENVGYDNKYSLLIVKRLITRMYQQNHLIISANDSKKNPFLGYNKNFYSQIISEGFAIIVEIPFFLQFSSSLEAAEIVKSYKNLRSIHSIFPFLEDKFPYLNYVSDIRIPYPIHLEILVQILRYWVKDAPFFHLLRLFLYNFCNRNSFLTPKKSISTFSKSNPRLFLFLYNFYVCEYESIFLFLRKKSSHLRLKSFSVFFERIFFYAKREHLVEVFAKDFSSTLTFFKDPLIHYVRYQGKSILASKNAPLLMNKWKHYFIHLWECFFDVWSQPGTIHIKQLSEHSFYLLGYFSNVRLNRSVVRSQMVQNTFLIEIVSKKLDIIVPIIPIIRSLAKAKFCNVLGHPISKAVWADSSDFDIIDRFLRICRNISHYYNGSSKKKSLYRIKYILRLSCIKTLACKHKSTVRAFLKRSGSEELLEEFFTEEEEILSLIFPRASSTLQKLHGNRIWYLDILFSNDLVNHE
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
Q85XY8
Q3Z4A7
KDPC_SHISS
Potassium-translocating ATPase C chain
Shigella
MSGLRPALSTFLFLLLITGGVYPLLTTALGQWWFPWQANGSLIREGDTVRGSALIGQNFTGNGYFHGRPSATAEMPYNPQASGGSNLAVSNPELDKLIAARVAALRAANPDASASIPVELVTASASGLDNNITPQAAAWQIPRIAKARNLSVEQLTQLIAKYSQQPLVKYIGQPVVNIVELNLALDKLDE
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
Q3Z4A7
P52897
PGFS2_BOVIN
Prostaglandin-D2 11 reductase 2
Bos
MDPKSQRVKFNDGHFIPVLGFGTYAPEEVPKSEALEATKFAIEVGFRHVDSAHLYQNEEQVGQAIRSKIADGTVKREDIFYTSKLWCNSLQPELVRPALEKSLQNLQLDYVDLYIIHSPVSLKPGNKFVPKDESGKLIFDSVDLCHTWEALEKCKDAGLTKSIGVSNFNHKQLEKILNKPGLKYKPVCNQVECHPYLNQSKLLEFCKSHDIVLVAYAALGAQLLSEWVNSNNPVLLEDPVLCAIAKKHKQTPALVALRYQVQRGVVVLAKSFNKKRIKENMQVFDFELTPEDMKAIDGLNRNTRYYDFQQGIGHPEYPFSEEY
Catalyzes the reduction of PGD(2) and PGH(2) to PGF(2 alpha) and a stereoisomer, respectively. It has a broad substrate specificity and reduces also other carbonyl compounds.
P52897
P9WQH7
ACCD5_MYCTU
Propionyl-CoA carboxylase
Mycobacterium tuberculosis complex
MTSVTDRSAHSAERSTEHTIDIHTTAGKLAELHKRREESLHPVGEDAVEKVHAKGKLTARERIYALLDEDSFVELDALAKHRSTNFNLGEKRPLGDGVVTGYGTIDGRDVCIFSQDATVFGGSLGEVYGEKIVKVQELAIKTGRPLIGINDGAGARIQEGVVSLGLYSRIFRNNILASGVIPQISLIMGAAAGGHVYSPALTDFVIMVDQTSQMFITGPDVIKTVTGEEVTMEELGGAHTHMAKSGTAHYAASGEQDAFDYVRELLSYLPPNNSTDAPRYQAAAPTGPIEENLTDEDLELDTLIPDSPNQPYDMHEVITRLLDDEFLEIQAGYAQNIVVGFGRIDGRPVGIVANQPTHFAGCLDINASEKAARFVRTCDCFNIPIVMLVDVPGFLPGTDQEYNGIIRRGAKLLYAYGEATVPKITVITRKAYGGAYCVMGSKDMGCDVNLAWPTAQIAVMGASGAVGFVYRQQLAEAAANGEDIDKLRLRLQQEYEDTLVNPYVAAERGYVDAVIPPSHTRGYIGTALRLLERKIAQLPPKKHGNVPL
Component of a biotin-dependent acyl-CoA carboxylase complex. This subunit transfers the CO2 from carboxybiotin to the CoA ester substrate . When associated with the alpha3 subunit AccA3, is involved in the carboxylation of acetyl-CoA and propionyl-CoA, with a preference for propionyl-CoA . Is also required for the activity of the long-chain acyl-CoA carboxylase (LCC) complex .
P9WQH7
P60364
CH601_RHOPA
Chaperonin-60 1
Rhodopseudomonas
MAAKDVKFSGDARDRMLRGVDVLANAVKVTLGPKGRNVLIEKSFGAPRITKDGVTVAKEVELEDKFENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIEIAVAAVVKDIQKRAKPVASSAEIAQVGTISANGDAPIGKMIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQSMLPVLEAVVQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVSAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLETVTLKMLGRAKKVVIDKENTTIVNGAGKKPEIEARVSQIKAQIEETSSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDALNATRAAVQEGIVPGGGVALLRAKKAVGRISNDNPDVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKTETFGFDAQTEEYVDMLAKGIVDPAKVVRTALQDASSVASLLVTTEAMVAELPKADAPAMPAGGGMGGMGGMGF
Together with its co-chaperonin GroES, 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.
P60364
Q8YFR1
ISPH_BRUME
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
Brucella
MTQHRPPLEIRLCGPRGFCAGVDRAIQIVVLALKKYGAPVYVRHEIVHNRYVVEGLQARGAIFVEELDEIPAAHRNQPVVFSAHGVPKSVPADAEAKNLFYLDATCPLVSKVHKQAMRHQRLGRHVILIGHSGHPEVIGTMGQLPDGAVTLIETVEDAHTCHFDDEDNLGFVTQTTLSVDDTAGIIKELQARFPNLAAPAAESICYATTNRQDAVRAAAPGCDLFLIVGAPNSSNSKRLVEVAEKAGARMSMLVQRAEDIEWEQIGDISVVGLSAGASAPEIIVDEIIDAFKARFDVKIELAETTVETENFLVNREIRDVELTVKDMAFVNGEHRVVGISKLMQGK
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Q8YFR1
P35872
NUSG_THET8
Transcription termination/antitermination protein NusG
Thermus
MSIEWYAVHTLVGQEEKAKANLEKRIKAFGLQDKIFQVLIPTEEVVELREGGKKEVVRKKLFPGYLFIQMDLGDEEEPNEAWEVVRGTPGITGFVGAGMRPVPLSPDEVRHILEVSGLLGKKEAPKAQVAFREGDQVRVVSGPFADFTGTVTEINPERGKVKVMVTIFGRETPVELDFSQVVKA
Participates in transcription elongation, termination and antitermination.
P35872
A8L6J3
RNY_FRASN
Ribonuclease Y
unclassified Frankia
MVADLRREARDVEEEVERIRRRAEQDAAEQTERVRREAEQIRRHAEEAAEAIRERAVADAELRASRAEAAARDAIHAEREQIRAELDEDLRTQRTELRGWDSRLTQREQRVTDQAASVEERLRRLETREAELAVREAGLDSRESDLGELEEARRRELERVAGLTSAEARTELVKVVEDQARLDAAVRVRDIEARAEEEAEDRARRIVTLAIQRVASDQTAESVVSVLHLPSDEMKGRIIGREGRNIRAFESVTGVNVLIDDTPEAVLLSCFDPVRREMGRITLTALVSDGRIHPHRIEEEYARAEREVAAKCVRAGEDALIDVGIAEMHPELINLLGRLRYRTSYGQNVLAHLVESAHLAGIMAAELRLPPAIAKRGTLLHDLGKALTHEVEGSHAIVGAEIARRYGEHEDVVHAIEAHHNEVEPRSIGAVLTQAADQISGGRPGARRDSLESYVKRLERIEQIAAERPGVEKVFAMQAGREVRVMVVPELVDDVAAHLLARDVAKQIEDELTYPGQIRVTVVRETRAVGMAR
Endoribonuclease that initiates mRNA decay.
A8L6J3
A1JL26
NAPA_YERE8
Periplasmic nitrate reductase
Yersinia
MKLSRRDFMKANAAVAAAAAAGLTIPTVAKAVVGETTNAIKWDKAPCRFCGTGCGVLVGTQNGRIVASQGDPDSPVNRGLNCVKGYFLPKIMYGKDRLTQPLLRMKDGQYDKEGDFTPISWEKAFDIMELKFKNALKEKGPTAVGMFGSGQWTVWEGYAASKLLKAGFRSNNLDPNARHCMASSVVGFMRTFGMDEPMGCYDDIEEADAFVLWGSNMAEMHPILWSRMTSRRLTNEHVRIAVLSTFEHRSFELADNPIVFTPQTDLVIMNYIANYIIQNNAVDQGFLDRHVNFRRGATDIGYGLRPTHPLEKAAKNPGSDASEPMSFDDFKAFVAEYTLEKTAKMSGVPEDQLESLAQLYADPKVKLVSYWTMGFNQHTRGVWANNMCYNLHLLTGKISKPGSGPFSLTGQPSACGTAREVGTFSHRLPADMVVTNEKHRQIAETKWQLPAGTIPEKVGLHAVAQDRALKDGTLNAYWVMCNNNMQAGPNINEERMPGWRDPRNFIVVSDPYPTISALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVPAPGEAKSDLWQMVEFAKRFKVEEVWPDELINKKPEYRGKTLYDVLFANNVVNKYPLSEIPADQLNDEARDFGFYIQKGLFEEYADFGRGHGHDLAPFDRYHQERGLRWPVVNGKETLWRYREGFDPFVPKGEDVRFYGKPDGKAVIFALPYEPAAESPDQEYDLWLSTGRVLEHWHTGSMTRRVPELHRAFPEAVLFIHPLDAKARGLRRGDKVKVISRRGEVISLVETRGRNRPPQGLVYMPFFDAAQLVNNLTLDATDPLSKETDFKKCAVKLARVVA
Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.
A1JL26
Q5PLN6
DLGD_SALPA
3-dehydro-L-gulonate 2-dehydrogenase
Salmonella
MKVTFEELKGAFYRVLRSRNIAEDTADACAEMFARTTESGVYSHGVNRFPRFIQQLDNGDIIPDAKPQRVTSLGAIEQWDAQRAIGNLTAKKMMDRAIELASDHGIGLVALRNANHWMRGGSYGWQAAEKGYIGICWTNSIAVMPPWGAKECRIGTNPLIVAIPSTPITMVDMSMSMFSYGMLEVNRLAGRELPVDGGFDDNGQLTKEPGVIEKNRRILPMGYWKGSGLSIVLDMIATLLSNGSSVAEVTQENSDEYGVSQIFIAIEVDKLIDGATRDAKLQRIMDFITTAERADDNVAIRLPGHEFTKLLDDNRRHGITVDDSVWAKIQAL
Catalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH, to form 3-keto-L-gulonate.
Q5PLN6
Q7NGW6
KATG_GLOVI
Peroxidase/catalase
Gloeobacter
MDVEAKCPMGGGKVEGRAVLFEMTNRLWWPNHLDLSVLHQNPPAGNPMGEGFNYAAEFESLDLAAVKQDIFALMTESQDWWPADYGHYGPLFIRMAWHAAGTYRIGDGRGGAGAGTQRFAPLNSWPDNANLDKARLLLWPIKEKYGRKLSWGDLLILAGNCALESMGFKTAGFAGGRVDIWEPENDIFWGPEREWLGDERYSSDRDLAHPLAAVQMGLIYVNPEGPNGKPDPMAAAHDIRETFGRMAMNDEETVALIAGGHTFGKCHGAAEPSQYVGAEPEGAGIERQGLGWDNSFGSGRGVHTITSGLEGAWTKNPIQWDNGYFENLFEYEWELTKSPAGAHQWTPKNPEAASTVPDAHDPHKRHAPMMATTDLAMRADPAYEKISRRFYDNPDQLAHAFAEAWYKLTHRDMGPYARLLGPEVPSEPRIWQDPVPASDHPLIDDADIAELKAQILAAGLSIARLVTTAWASASTFRGTDKRGGANGARIRLVPQKDWAVNEPTELATALAKLEAIQQDFNAGQTGGKQVSLADLIVLGGCAAVEQAAKKAGHDITVPFTPGRTDASPDQTDVESFAPLEPKIDGFRNYVGEKSVYSAEEMLVDRAHLLTLSAPEMTVLVGGLRVLGANYGGSKLGVFTERPETLTNDFFVNLLKTSTSMKWEASPDADVFEASDRATGEKKWAGTRVDLIFGSNSQLRALSEAYATADAQQTFVDAFVAAWTKVMNLDRFDLPR
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
Q7NGW6
Q60870
REEP5_MOUSE
Protein TB2 homolog
Mus
MRERFDRFLHEKNCMTDLLAKLEAKTGVNRSFIALGVIGLVALYLVFGYGASLLCNLIGFGYPAYISMKAIESPNKDDDTQWLTYWVVYGVFSIAEFFSDLFLSWLPFYYMLKCGFLLWCMAPSPANGAEMLYRRIIRPIFLRHESQVDSVVKDVKDKAKETADAISKEVKKATVNLLGDVKKST
Plays an essential role in heart function and development by regulating the organization and function of the sarcoplasmic reticulum in cardiomyocytes.
Q60870
B2T2A0
RLMH_PARPJ
rRNA (pseudouridine-N3-)-methyltransferase RlmH
Paraburkholderia
MKLHILAVGHKMPDWIATGFDEYTKRMPPELRIELREIKPEQRSSGRQADSVMAAERLKIEAALPKNARIVALDERGKDWTTMQLAGALPGWQQDGRDVAFLIGGADGLDPQLKARSDMLLRVSSLTLPHAMVRVLLAEQLYRAWTITQNHPYHRV
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
B2T2A0
Q83IN9
G6PI_SHIFL
Phosphohexose isomerase
Shigella
MKNINPTQTAAWQALQKHFDEMKDVTIADLFAKDGDRFSKFSATFDDQMLVDYSKNRITEETLAKLQDLAKECDLAGAIKSMFSGEKINRTENRAVLHVALRNRSNTPILVDGKDVMPEVNAVLEKMKTFSEAIISGEWKGYTGKAITDVVNIGIGGSDLGPYMVTEALRPYKNHLNMHFVSNVDGTHISEVLKKVNPETTLFLVASKTFTTQETMTNAHSARDWFLKAAGDEKHVAKHFAALSTNAKAVGEFGIDTANMFEFWDWVGGRYSLWSAIGLSIVLSIGFDNFVELLSGAHAMDKHFSTTPAEKNLPVLLALIGIWYNNFFGAETEAILPYDQYMHRFAAYFQQGNMESNGKYVDRNGNVVDYQTGPIIWGEPGTNGQHAFYQLIHQGTKMVPCDFIAPAITHNPLSDHHQKLLSNFFAQTEALAFGKSREVVEQEYRDQGKDPATLDYVVPFKVFEGNRPTNSILLREITPFSLGALIALYEHKIFTQGVILNIFTFDQWGVELGKQLANRILPELKDDKEISSHDSSTNGLINRYKAWRG
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Q83IN9
G0S1B3
CMS1_CHATD
Protein CMS1
Thermochaetoides
MSLDNDINTKKRKLQDDEKPRKKRKHKRPTRDDDADLDVEAGLNRAFARMDGQLLADHLAQKTRRFGTELSSVELNDLYISAASIRDSSSFEKDRTLENLPSFLEKFAQEKEKLDEAPKKNGSPHTLIVAAAGLRAADLVRACRKFQKKGSPVAKLFAKHFKLEEQVAFLNKTRTGIAVGTPQRLIDLIEHGALSVENLRRIVVDASHIDQKKRNITDMRETMMPLAKLLARADFKERYTDEKKHIDLLFY
May play a role in the regulation of DNA replication and cell cycle control.
G0S1B3
A4WQY3
PURL_CERS5
Phosphoribosylformylglycinamidine synthase subunit II
Cereibacter
MTEPEITPELIAAHGLKPDEYERILGIIGREPSFTELGIFSAMWNEHCSYKSSKKWLRTLPTTGPQVICGPGENAGVVDIGDGQAVIFKMESHNHPSYIEPYQGAATGVGGILRDVFTMGARPIAAMNALSFGEPNHSKTAHIVKGVVEGIGGYGNAFGVPTVGGEVRFHRAYNGNCLVNAFAAGLADADKIFYSAASGVGMPVVYLGAKTGRDGVGGATMASAEFDDTIEEKRPTVQVGDPFTEKRLLEACLELMASDSVISIQDMGAAGLTCSAVEMGDKGDLGIKLQLDNVPQREANMTAYEMMLSESQERMLMVLKPEKEAVARAIFEKWDLDFAIVGETIPEDRFLILHGNEVKADLPLKALSGTAPEYDRPWVETPAAAPMAPVAEVDPIEGLKALIGSPSYAHKAWVWEQYDSQVMADTVRAPGLGAGVVRVHGTPKALAFTSDVTPRYVKANPFEGGKQAVAEAYRNLTAVGAKPLATTDNMNFGNPEKPEIMGQFVGAIKGIGAAVAALDMPIVSGNVSLYNETDGVAILPTPTIGAVGILQSLDELIAGQPEEGDVALVIGETKGHLGQSALLAELLGREDGDAPHVDLDAEKRHGEFLRANRKLVSAATDLSDGGLALAAFEMAEGAGLGLTLTVTGTAQLFGEDQARYLVAVHPDQTKALQAAAEAAGVPLQQVGQFGGEEVTLGTVSAPLVDLSRLHRGAFAAAIG
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.
A4WQY3
Q2G9L1
TOLB2_NOVAD
Tol-Pal system protein TolB 2
Novosphingobium
MKIRHLLLLAGLVSAPAIVAAQQTALPSSSAAQASGDDDGGLTGSVSDESEWQDLGIAIPSFPTNASVPTAAEGGTTEALGRNVARVVFNDLKNNGLFKPVGPDALPAIAFPQVAAPAFDAWRGRSAEMLVQGFVKANEDGRLTVGCYLYDVALGSELARQGYVVKPEEWRRAAHKCADMVYSRLSGESPFFDSKIAYIAETGPKDRRRKQLAIMDSDGANHRFITNGQATALTPRYSPDYSQIVYLSYLNGAPRIYIYNIGTGQQKLVTSSTNPTFAPRWSPDGKWILYSMSVAGNTDIYRVSVNGGASTRLTDSPGIDVGGSYSPDGSRIVFESDRSGSQQLYVMNADGSNQKRISFFGGRAATPEWSPRGDQIAFTHLGGNFRIAVTDPSGGNMRFLTDSWQDEAPTWSPNGRIVQFFRTERGSGKTGIWQVDLTGRNERKLNTPVDGSDPAWGPVLP
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.
Q2G9L1
A4SCQ9
RL3_CHLPM
50S ribosomal protein L3
Chlorobium
MGAILGKKIGMTRLYNEKREAVPCTIIQAGPCFVTQVKSAGIDGYDAYQVGIGERKEAKVTKPMLGHYKKAGVAPGYMTAEFDTSMFDGELTAGSPVLVESFTEGEIVKVQGVSKGKGFAGVVKRHNFGGGQRTHGQSDRLRAPGSIGGASDPSKTFKGTKMGGRMGSDTITVRNLQVIKIMPESSLIMVKGSVPGPKNSYVRIVSTKK
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
A4SCQ9
B4EVU5
MDTJ_PROMH
Spermidine export protein MdtJ
Proteus
MIYWIFLVLAIICEVIGTLSMKYASVSGGYTGMIVMWLMIATSYIFLAIAVKKVALGVAYALWEGIGIVIITTFSVLWFGESLSALKLGGLAMLIAGITLIKSGTKKSVVAKKTTDSVKNIAGKAKQVATVVKGVNKPISSNVKEA
Catalyzes the excretion of spermidine.
B4EVU5
Q2YY85
MENG_STAAB
Demethylmenaquinone methyltransferase
Staphylococcus
MADNKANKEQVHRVFQNISKKYDRLNNIISFEQHKVWRKRVMKDMGVRKGTKALDVCCGTGDWTIALSKAVGPTGEVTGIDFSENMLEVGKEKTASMENVKLVHGDAMELPFGDNSFDYVTIGFGLRNVPDYLVALKEMNRVLKPGGMVVCLETSQPTLPAFKQMYALYFKFVMPIFGKLFAKSKEEYEWLQQSTFNFPGKEELKRMFEEAGFINVRVRSFTGGVAAMHLGYKEKDNTKGD
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Q2YY85
C7R400
ARC_JONDD
Proteasomal ATPase
Jonesia
MTETHNDPEELARRVASLSAQNERLAQILVEARSKIVGLQQQIDDLAQPPSTYATFIRSYSDGTADVMVQGRKMRLTSLPAAMVSTARPGQQVRLNEAMAIVETMTYDHTGELVTVKELIGTHRAMVVGRGDDERVVNLAGSLIGRDGPTIRTGDSVLVDLKAGYALEKIDKSEVEELVLEEVPRVAYEDIGGLSRQIDTIKDAVELPFLHPDLYREHGLKAPKGILLYGPPGCGKTLIAKAVAHSLAQTVGQGNNTPTDDTRGYFLNIKGPELLNKYVGETERQIRLIFTRARDKAAQGHPVVVFFDEMESLFRTRGTGLSSDVETTIVPQLLAEIDGVERLDNVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAEAALDIFSKYLTPDLPIHPVDLAEHGGNAQDAVTAMGQRVVEHMYATTPDNQFLEVTYASGDKETLYFKDFSSGAMIQNIVDRAKKAAIKGYLSHGTRGLQVEHLLAACDDEFQENEDLPNTTNPDDWARISGKKGERIVFIRTIVQRKGEGKNPTPAKAIETPHNTGPYL
ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.
C7R400
Q9PBK1
PSTA_XYLFA
Phosphate transport system permease protein PstA
Xylella
MSTASQHLYKRRRLINATAITISCIAALFGLFFLIWILWTLISKGLPGIGLDLFTKITPPPMQKGGLANAFFGSAIMCLLAIVIGTPLGIAAGTWLAEYGNTSKTSAVVRFVNDILLSAPSIVLGLFVYTLYVMHTGGHFSAFSGALALVFIVLPIVVRTTDEMLRLVPGQMREAALSLGIPQWKMIIQVLYRSASAGILTGILLALARISGETAPLLFTAFGNQYWSSNIFQPIASLPLVMNQFASSPYKSWQLLAWSGALVLTVFVLLVSLGARTLLLRNKIPNE
Part of a binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Q9PBK1
Q16558
KCMB1_HUMAN
Slo-beta-1
Homo
MVKKLVMAQKRGETRALCLGVTMVVCAVITYYILVTTVLPLYQKSVWTQESKCHLIETNIRDQEELKGKKVPQYPCLWVNVSAAGRWAVLYHTEDTRDQNQQCSYIPGSVDNYQTARADVEKVRAKFQEQQVFYCFSAPRGNETSVLFQRLYGPQALLFSLFWPTFLLTGGLLIIAMVKSNQYLSILAAQK
Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Increases the apparent Ca(2+)/voltage sensitivity of the KCNMA1 channel. It also modifies KCNMA1 channel kinetics and alters its pharmacological properties. It slows down the activation and the deactivation kinetics of the channel. Acts as a negative regulator of smooth muscle contraction by enhancing the calcium sensitivity to KCNMA1. Its presence is also a requirement for internal binding of the KCNMA1 channel opener dehydrosoyasaponin I (DHS-1) triterpene glycoside and for external binding of the agonist hormone 17-beta-estradiol (E2). Increases the binding activity of charybdotoxin (CTX) toxin to KCNMA1 peptide blocker by increasing the CTX association rate and decreasing the dissociation rate.
Q16558
O28339
PURL_ARCFU
Phosphoribosylformylglycinamidine synthase subunit II
Archaeoglobus
MYRKVDVPFELYEVEILDASEEELAKISEEMGLALSVDEMKRIQDYFRQKGRNPYDIELQSLAQAWSEHCCYKSSKYYLRQYLLEASKADYVISAIEEDAGVVEFDDEYAYVTAFESHNHPSAIEPYGGAATGIGGILRDVLCMGAQPIALIDPLFFGNLDTPYEKLPRGTKHPLYLLKGVVAGIRDYGNRVGIPTVAGMVFFDNSYLTNCLVNVGCVGIVRKDRIIHSRAGGAGDLFVLAGGKTGRDGIHGVTFASAELDEKSEEEARGAVQLGNPIMKEPLIHACLEVVEKGLLTGMKDLGGGGLSCVIGEMALAAGFGAEVYLDKVPLKEEGMAPWEIWISESQERMMLTVRPEHIDEVLYIFQKWDVPATVVGKVIPEKITRIYYKGYKIYEMDTEFVTSGPEYCRPYVARKPEKELHEEVEPPADYVKTFMKMLSHPNAAFKEWIVRQYDHEVRASTVLKPLQGKMNFETHGDAAVIKPTRSFRGLAITADVNPWMCKVDPYWGAASSFDEMVRNLVAVNAVPHSFNDCLNFGNPEKPERMGEFVEAVKALGWMAKGVGVPCVSGNVSFYNETPYGAVAPTPSLLGVGIVEDVRKAITSEFKGRGAVILVGETHNEFGGSLYSAVMGQRCHKVPRTSPERLKTYSDAMLESFRKFEVKACHDVSMGGLAVCIAEMSFGRGLGFEAARELSFVELFSESNTRWVVEVPESVAEGYAEFFRAKELKAEVIGYSGGERLDFGAFSVELGEADKSWREGLTKFL
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.
O28339
A4SUY3
RS13_POLAQ
30S ribosomal protein S13
Polynucleobacter
MARIAGVNIPNHQHTVIGLTAIFGIGTTRANKICQTTGVAIDKKVKDLTDADLEKLRDEVGKFITEGDLRREVTMSIKRLMDLGCYRGVRHRKGLPVRGQRTKTNARTRKGPRKSGVQLKK
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
A4SUY3
Q9ZVR7
PSKR1_ARATH
Protein serine-threonine kinase
Arabidopsis
MRVHRFCVIVIFLTELLCFFYSSESQTTSRCHPHDLEALRDFIAHLEPKPDGWINSSSSTDCCNWTGITCNSNNTGRVIRLELGNKKLSGKLSESLGKLDEIRVLNLSRNFIKDSIPLSIFNLKNLQTLDLSSNDLSGGIPTSINLPALQSFDLSSNKFNGSLPSHICHNSTQIRVVKLAVNYFAGNFTSGFGKCVLLEHLCLGMNDLTGNIPEDLFHLKRLNLLGIQENRLSGSLSREIRNLSSLVRLDVSWNLFSGEIPDVFDELPQLKFFLGQTNGFIGGIPKSLANSPSLNLLNLRNNSLSGRLMLNCTAMIALNSLDLGTNRFNGRLPENLPDCKRLKNVNLARNTFHGQVPESFKNFESLSYFSLSNSSLANISSALGILQHCKNLTTLVLTLNFHGEALPDDSSLHFEKLKVLVVANCRLTGSMPRWLSSSNELQLLDLSWNRLTGAIPSWIGDFKALFYLDLSNNSFTGEIPKSLTKLESLTSRNISVNEPSPDFPFFMKRNESARALQYNQIFGFPPTIELGHNNLSGPIWEEFGNLKKLHVFDLKWNALSGSIPSSLSGMTSLEALDLSNNRLSGSIPVSLQQLSFLSKFSVAYNNLSGVIPSGGQFQTFPNSSFESNHLCGEHRFPCSEGTESALIKRSRRSRGGDIGMAIGIAFGSVFLLTLLSLIVLRARRRSGEVDPEIEESESMNRKELGEIGSKLVVLFQSNDKELSYDDLLDSTNSFDQANIIGCGGFGMVYKATLPDGKKVAIKKLSGDCGQIEREFEAEVETLSRAQHPNLVLLRGFCFYKNDRLLIYSYMENGSLDYWLHERNDGPALLKWKTRLRIAQGAAKGLLYLHEGCDPHILHRDIKSSNILLDENFNSHLADFGLARLMSPYETHVSTDLVGTLGYIPPEYGQASVATYKGDVYSFGVVLLELLTDKRPVDMCKPKGCRDLISWVVKMKHESRASEVFDPLIYSKENDKEMFRVLEIACLCLSENPKQRPTTQQLVSWLDDV
Phytosulfokine receptor with both a serine/threonine-protein kinase activity and a guanylate cyclase activity . Regulates, in response to phytosulfokine binding, a signaling cascade involved in plant cell differentiation, organogenesis, somatic embryogenesis, cellular proliferation and plant growth. Involved in plant immunity, with antagonistic effects on bacterial and fungal resistances . Not involved in PSY perception. CNGC17 and AHAs form a functional cation-translocating unit that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes .
Q9ZVR7
P32414
ES1_PELLE
Esculentin-1
Pelophylax
GIFSKLGRKKIKNLLISGLKNVGKEVGMDVVRTGIDIAGCKIKGEC
Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity.
P32414
A1AHQ2
BGLH_ECOK1
Putative outer membrane porin BglH
Escherichia
MFRRNIITSAILLMAPLAFSAQSLAESLTVEQRLELLEKALRETQSELKKYKDEEKKKYTPATVNRSVSTNDQGYAANPFPTSRAAKPDAVLVKNEEKNASETGSIYSSMTLKDFSKFVKDEIGFSYNGYYRSGWGTASHGSPKSWAIGSLGRFGNEYSGWFDLQLKQRVYNENGKRVDAIVMMDGNVGQQYSTGWFGDNAGGENFMQFSDMYVTTKGFLPFAPEADFWVGKHGAPKIEIQMLDWKTQRTDAAAGVGLENWKVGPGKIDIALVREDVDDYDRSLQNKQQINTNTIDLRYKDIPLWDKVTLMVSGRYVTANESASEKDNQDNNGYYDWKDTWMFGTSLTQKFDKGGFNEFSFLVANNSIASNFGRYAGASPFTTFNGRYYGYHTGGTAVRLTSQGEAYIGDHFIVANAIVYSFGNDIYSYETGAHSDFESIRAVVRPAYIWDQYNQTGVELGYFTQQNKDANSNKFNESGYKTTLFHTFKVNTSMLTSRPEIRFYATYIKALENELDGFTFEDNKDDQFAVGAQAEIWW
May be a sugar porin with a broad carbohydrate specificity.
A1AHQ2
Q38XB6
SYD_LATSS
Aspartyl-tRNA synthetase
Latilactobacillus
MKTRTTYSGLVDETFVGQTVTLHGWVQKRRSLGNLIFVDLRDREGLVQLVFNQDNADILALANTLRNEYVIEVTGMVQARDEAAINPDMKTGKVEVIVSELTILNEAKNLPFEIKDGITTSEETKLKYRYLDLRRPEMQQAIIRRSQITQAAHKYLDNNGFLNIETPDLTRSTPEGARDYLVPSRVYPGSFYALPQSPQVFKQLLMDAGFDRYYQMARCFRDEDLRGDRQPEFTQIDVETSFMSAEEIQEQAEGIIKQVMQDVMHIDVPTPFKRMKWQEAMDRYGSDKPDIRFDLEIQDLTEMMKTSSFKVFSDTANSGNLVRAIVVPEGAAKYSRKMLDEQTEYIKRYGARGMAWVKVVDGELTGPAAKFLKEQEAELLSALSAKDGDLVLFVADKFQVVCDSLGYLRKHFAHDMGLVDESQFAYLWVVDWPLFEYDEGFGRWIAAHHPFTRPNDSDVDLLETDPHKAHAQSYDIILNGYELGGGSLRIYQRDIQERMFKALGISPETYEEQFGHLLSAMDYGFPPHGGFAIGLDRFAMLLAGRDNIRDVIAFPKNSHASEPMTNAPSRVAPAQLDELGLEVEPEVEKD
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Q38XB6
Q02394
HMD_METKA
N(5),N(10)-methenyltetrahydromethanopterin dehydrogenase
Methanopyrus
MVEINKVAILGAGCWRTHAATGITTFKRACEVADETGIKEAALTHSSVTYAVELKHLAGVDEVVLSDPVFDADGFTVVDIEEDCDVDLDEFIKAHLEGNPEDVMPKLRDYVNDIADDVPKPPKGAIHFLSPEEMEDKLDIVVTTDDAEAVEDADMIISWLPKGGVQPDIFKKIIDDIPEGCIVANTCTIPTRQFKEMFEDMGRDDLQVTSYHPATVPEHKGQVFVAEGYADEEVVEAVYELGEKARGLAFKVPGYLLGPVCDMASAVTAIVYAGLLTFRDACTDILGAPVDFTQNMAVEALQMMAKFMEEEGLDKLEEALDPAALTNTADSMNFGPLADTEILPKALEVLEKYSKKAE
Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
Q02394
Q8L5W8
PIL1_ARATH
bHLH transcription factor bHLH124
Arabidopsis
MEAKPLASSSSEPNMISPSSNIKPKLKDEDYMELVCENGQILAKIRRPKNNGSFQKQRRQSLLDLYETEYSEGFKKNIKILGDTQVVPVSQSKPQQDKETNEQMNNNKKKLKSSKIEFERNVSKSNKCVESSTLIDVSAKGPKNVEVTTAPPDEQSAAVGRSTELYFASSSKFSRGTSRDLSCCSLKRKYGDIEEEESTYLSNNSDDESDDAKTQVHARTRKPVTKRKRSTEVHKLYERKRRDEFNKKMRALQDLLPNCYKDDKASLLDEAIKYMRTLQLQVQMMSMGNGLIRPPTMLPMGHYSPMGLGMHMGAAATPTSIPQFLPMNVQATGFPGMNNAPPQMLSFLNHPSGLIPNTPIFSPLENCSQPFVVPSCVSQTQATSFTQFPKSASASNLEDAMQYRGSNGFSYYRSPN
Transcription factor. Involved in responses to transient and long-term shade. Required for the light-mediated inhibition of hypocotyl elongation. Necessary for rapid light-induced expression of the photomorphogenesis- and circadian-related gene APRR9. Seems to play a role in multiple PHYB responses, such as flowering transition and petiole elongation.
Q8L5W8
A5ILF1
Y1006_THEP1
Nucleotide-binding protein Tpet_1006
Thermotoga
MKRIVVVSGLSGAGKTTAMGFLEDLGYFCVDNVPGNILEELLKLFMSSDLEKMAMAIDVRSEHLGDPISTVERIKEKTNALVIFLEASTEELLRRYALTRRRHPLQKDGLGLEDAIEKEKEILSHIKEIADVVIDTTRMNTHQLRETLAHFLVNQAGGTSVRIMSFGFKHGIPMDADFVFDARFLPNPHYVPELSSKTGLDSEVEAYFKNYPVVEEFIEKIFEVLKVAIEEYQRTGRRIITVGIGCTGGKHRSVYITHRLKEMLEREGFTVIEKHRDIEKV
Displays ATPase and GTPase activities.
A5ILF1