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sequence
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2.75k
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5.51k
AlphaFoldDB
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P83504
PSBO_BRACM
Oxygen-evolving enhancer protein 1, chloroplastic
Brassica
EGAPKRLTYDEIQSKTYMEVKGTGTANQCPT
Stabilizes the manganese cluster which is the primary site of water splitting.
P83504
O82302
P2C29_ARATH
Protein phosphatase 2C PLL1
Arabidopsis
MGSGFSSLLPCFNQGHRNRRRHSSAANPSHSDLIDSFREPLDETLGHSYCYVPSSSNRFISPFPSDRFVSPTASFRLSPPHEPGRIRGSGSSEQLHTGFRAISGASVSANTSNSKTVLQLEDIYDDATESSFGGGVRRSVVNANGFEGTSSFSALPLQPGPDRSGLFMSGPIERGATSGPLDPPAGEISRSNSAGVHFSAPLGGVYSKKRRKKKKKSLSWHPIFGGEKKQRPWVLPVSNFVVGAKKENIVRPDVEAMAASSGENDLQWALGKAGEDRVQLAVFEKQGWLFAGIYDGFNGPDAPEFLMANLYRAVHSELQGLFWELEEEDDNPTDISTRELEQQGEFEDHVNEMASSSCPATEKEEEEMGKRLTSSLEVVEVKERKRLWELLAEAQAEDALDLSGSDRFAFSVDDAIGAGNAVSVGSKRWLLLSKLKQGLSKQGISGRKLFPWKSGVEENETEEVDNVGVEEGVDKRRKRRKAGTVDHELVLKAMSNGLEATEQAFLEMTDKVLETNPELALMGSCLLVALMRDDDVYIMNIGDSRALVAQYQVEETGESVETAERVEERRNDLDRDDGNKEPLVVDSSDSTVNNEAPLPQTKLVALQLTTDHSTSIEDEVTRIKNEHPDDNHCIVNDRVKGRLKVTRAFGAGFLKQPKLNDALLEMFRNEYIGTDPYISCTPSLRHYRLTENDQFMVLSSDGLYQYLSNVEVVSLAMEKFPDGDPAQHVIQELLVRAAKKAGMDFHELLDIPQGDRRKYHDDCTVLVIALGGSRIWKSSGKYL
Involved in the regulation of pedicel length and of CLAVATA pathways controlling stem cell identity at shoot and flower meristems.
O82302
Q8DVB5
EX7L_STRMU
Exodeoxyribonuclease VII large subunit
Streptococcus
MSDYLSVSSLTKYLKLKFDRDPYLERVYLTGQVSNFRRRPNHQYFSLKDEKAVIQATMWSGIYRKLGFELEEGMKINVIGRVQLYEPSGSYSIIIEKAEPDGIGALAVQFEQLKKKLAEAGYFDDRHKQRLSQFVKKIGVVTSPSGAVIRDIITTVSRRFPGVDILLFPTKVQGEGAAQEVADNIRLANERTDLDLLIVGRGGGSIEDLWAFNEEIVVQAIFESHLPIISSVGHETDTTLADFAADRRAATPTAAAELATPVTKADLLAFLKERQMRSYQAVMRLIRQKDEQVKKLQRSVIFRQPERLYDAYVQKLDHLRTHLLTKVRQVYDVYDSKEHLLRQRLLSFNLSGCIQRYQAQLKQDQRLLLSHMSSQYDSKLARFEKAQDALLSLDTTRIVARGYAIVQKDNHIIQSTQQIKKGDRLHLEMKDGQVQVEVENVKQEENI
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Q8DVB5
Q6D0G6
LEUC_PECAS
Isopropylmalate isomerase
Pectobacterium
MGKTLYQKLFDAHIVHEAPNETPLLYIDRHLVHEVTSPQAFDGLRAMGRKVRQPGKTFATMDHNVSTQTKDINASGEMARIQMQELIKNCAEFGVQLYDLNHPYQGIVHVIGPEQGMTLPGMTIVCGDSHTATHGAFGSLAFGIGTSEVEHVLATQTLKQGRAKTMKIEVTGDAAHGITAKDIVLAIIGKTGSAGGTGHVVEFCGKAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYLKGRQFAPKDANWDAAVAYWSTLKSDDDAQFDTIVTLDAAQIAPQVTWGTNPGQVIAVNQEIPNPDSFSDPVERASAAKALAYMDLQPGIKLTDVKIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAAGVQAIVVPGSGPVKTMAELEGLDKVFIEAGFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRAGRTHLVSPAMAAAAAVTGRFADVRELN
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Q6D0G6
Q38S35
COX2_APOMY
Cytochrome c oxidase polypeptide II
Sylvaemus group
MAYPFQLGLQDATSPIMEELMNFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAVILILIALPSLRILYMMDEINNPVLTVKTMGHQWYWSYEYTDYEDLCFDSYMIPTNDLKPGELRLLEVDNRVVLPMELPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQATVTSNRPGLFYGQCSEICGSNHSFMPIVLEMVPLKNFENWSTSMI
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Q38S35
P16550
APA1_YEAST
Diadenosine tetraphosphate alpha,beta-phosphorylase (ADP-forming)
Saccharomyces
MSIPADIASLISDKYKSAFDNGNLKFIQTETTKTKDPKTSMPYLISHMPSLIEKPERGQTPEGEDPLGKPEEELTVIPEFGGADNKAYKLLLNKFPVIPEHTLLVTNEYQHQTDALTPTDLLTAYKLLCALDNEESDKRHMVFYNSGPASGSSLDHKHLQILQMPEKFVTFQDRLCNGKEHFLPTFNTEPLQDAKVSFAHFVLPMPESEETVDEDLLAMCYISILQRALTFFQDWLNENPELKKSYNLMLTKEWICVVPRSKAFSDEMKIGFNSTGYCGMILTKNDEVFSKITEKPELINDILLECGFPNTSGQKPNEYNY
Ap4A phosphorylase catalyzes the phosphorolytic degradation of bis(5'-adenosyl) tetraphosphate (Ap4A) into ADP and ATP. Can also use other Np4N' nucleotides (where N and N' stand for A,C,G or U) as substrates with equal efficiency. Cannot catalyze the reverse reaction. Additionally, this enzyme can also catalyze the phosphorolytic degradation of adenosine 5'-phosphosulfate (AMPS) into ADP and sulfate, the reversible exchange reaction between inorganic phosphate and the beta-phosphate of a nucleoside diphosphate (NDP), and the synthesis of Ap4A from AMPS plus ATP.
P16550
Q9BEA8
TNFL6_PIG
SPPL2A-processed FasL form
Sus
MQQPFNYPYPQIFWVDSSATSPWASPGSVFPCPASVPGRPGQRRPPPPPPPPPPPPTLLPSRPLPPLPPPSLKKKRDHNAGLCLLVMFFMVLVALVGLGLGMFQLFHLQKELTELRESASQRHTESSLEKQIGHPNLPSEKKELRKVAHLTGKPNSRSIPLEWEDTYGIALVSGVKYMKGSLVINDTGLYFVYSKVYFRGQYCNNQPLSHKVYTRNSRYPQDLVLMEGKMMNYCTTGQMWARSSYLGAVFNLTSADHLYVNVSELSLVNFEESKTFFGLYKL
Cytoplasmic form induces gene transcription inhibition.
Q9BEA8
B2V4G5
RIMP_CLOBA
Ribosome maturation factor RimP
Clostridium
MRKDMLLEKVEVLVKPIVEELSYELYYLEYVKENGEYYLRIYIDKEEDSISLNDCEKVSRRVSEILDVEDPIEDSYYLEVSSPGLNRGLYKEEHFKKFIGREVLVRFNGSLEGMKKIQGILKEAENEFITVEGEKELKIPTEKIKGANLEGEI
Required for maturation of 30S ribosomal subunits.
B2V4G5
Q65WA7
HLDD_MANSM
ADP-L-glycero-beta-D-manno-heptose-6-epimerase
Basfia
MIIVTGGAGMIGANIVKALNDMGRKDILVVDNLKDGTKFINLVDLDIADYCDKEDFISSVIAGDDLGDIDAVFHEGACSATTEWDGKYLMHNNYEYSKELLHYCLDREIPFFYASSAATYGDKTDFIEEREFEGPLNAYGYSKFLFDQYVRAILPEANSPVCGFKYFNVYGPREQHKGSMASVAFHLNNQILKGENPKLFAGSEHFLRDFVYVGDVAEVNLWAWENGVSGIFNLGTGNAESFKAVAEAVVKFHGKGEIETIPFPDHLKSRYQEYTQANLTKLRAAGCDFKFKNVAEGVAEYMAWLNRK
Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
Q65WA7
Q97BX7
RL3_THEVO
50S ribosomal protein L3
Thermoplasma
MATPHHSRRGSMAYYPRVRAKSIEPRIRSWPEISGPVKVQGFAGFKVGMTHVEMVDYRKTSVTAGQPIFVPVTVIEVPPLDVIGIRLYDEDEEGNMVVVYEKWTQNLDKELFKKITTFKEVKEKPVPETYADVRLIVATRNKDVPGIPSKKPEIFELRIGGGNSVKERFEYATAHLGKTIRFEDFSKPGKFVDVLSVTKGKGFTGHVQRFGVKLLPRKNRKHRRMIGTLGPWHPDWVRNTVPQAGQMGYQQRTISNVRVLKYSKGEDADTINVRGGFLHYGLVKNDYVLLFGSVPGPAKRLIKMRDPARQKVPDIDNVKLDYISLESKQGD
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.
Q97BX7
Q32BP9
MUG_SHIDS
Mismatch-specific uracil DNA-glycosylase
Shigella
MVEDILAPGLRVVFCGINPGLSSAGTGFPFAHPANRFWKVIYQAGFTDRQLKPQEAQHLLDYRCGVTKLVDRPTVQANEISNQELHAGGRKLIEKIEDYQPQALAILGKQAYEQGFSQRGAQWGKQTLSIGSTQIWVLPNPSGLSRVSLEKLVEAYRELDQALVVRGR
Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells.
Q32BP9
O32999
RL18_MYCLE
50S ribosomal protein L18
Mycobacterium
MVQSVSAIRRVSRLRRHARLRKKVSGTSERPRLVVNRSARHIHVQLVNDVTGTTVAAASSIEADVRGLQGDKKVRSVRVGQLIAERAKAAGINTVVFDRGGYTYGGRIAALADSVRENGLNF
This is one 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.
O32999
A4G8R4
OBG_HERAR
GTP-binding protein Obg
Herminiimonas
MKFIDEAKIEVIAGDGGNGVASFCREKFRPFGGPDGGDGGKGGSIWAVADRNINTLVDFRYSKMHKARDGENGRGADCYGKGADDIKLRMPVGTLIIDNNDGELIADLTEHGQEVLIAKGGEGGWGNIHFKSSTNRAPRQKSEGKEGERRELRLELKVLADIGLLGMPNAGKSTFISAVSNARPKIADYPFTTLHPNLGVVRVSHEKSFVIADIPGLIEGASDGAGLGIQFLRHLQRTRLLLHIVDLAPFDNVDPVKEAKAIVKELKKYDESLFDKPRWLVLNKLDMVPEEERKKRVKDFIKRFGWKGPVFEISALTHEGCSELVTEIYDYIAVQRQAEQRSEETPQMVEAARGIDSIDPDDPRFKIID
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
A4G8R4
P29668
CYB_MEGAT
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Megalops
FGSLLGLCLATQILTGLFLAMHYTSDISTAFSSVTHICRDVNYGWLIRNIHANGASFFFICIYLHIGRGLYYGSYLYKETWNIGVVLLLLVMMTAFVGYVLP
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
P29668
Q06128
TRPE_SACS2
Anthranilate synthase component 1
Saccharolobus
MEVHPISEFASPFEVFKCIERDFKVAGLLESIGGPQYKARYSVIAWSTNGYLKIHDDPVNILNGYLKDLKLADIPGLFKGGMIGYISYDAVRFWEKIRDLKPAAEDWPYAEFFTPDNIIIYDHNEGKVYVNADLSSVGGCGDIGEFKVSFYDESLNKNSYERIVSESLEYIRSGYIFQVVLSRFYRYIFSGDPLRIYYNLRRINPSPYMFYLKFDEKYLIGSSPELLFRVQDNIVETYPIAGTRPRGADQEEDLKLELELMNSEKDKAEHLMLVDLARNDLGKVCVPGTVKVPELMYVEKYSHVQHIVSKVIGTLKKKYNALNVLSATFPAGTVSGAPKPMAMNIIETLEEYKRGPYAGAVGFISADGNAEFAIAIRTAFLNKELLRIHAGAGIVYDSNPESEYFETEHKLKALKTAIGVR
Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.
Q06128
Q05584
GLO2_YEAST
Glyoxalase II
Saccharomyces
MQVKSIKMRWESGGVNYCYLLSDSKNKKSWLIDPAEPPEVLPELTEDEKISVEAIVNTHHHYDHADGNADILKYLKEKNPTSKVEVIGGSKDCPKVTIIPENLKKLHLGDLEITCIRTPCHTRDSICYYVKDPTTDERCIFTGDTLFTAGCGRFFEGTGEEMDIALNNSILETVGRQNWSKTRVYPGHEYTSDNVKFVRKIYPQVGENKALDELEQFCSKHEVTAGRFTLKDEVEFNPFMRLEDPKVQKAAGDTNNSWDRAQIMDKLRAMKNRM
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Q05584
Q29W37
PANB_CAMJJ
Ketopantoate hydroxymethyltransferase
Campylobacter
MRKSMISFLEKKAKNEKITMVSAYDYHSAKILDNCDIDIILVGDSLAMTVLGMQDTLSVTMDEMLIFTKAVSRGAKKSFVLADMPFMSYQSSDRDAILNASRFIKESHANGVKVEGGIEIASKIKLISQSGIPVVAHLGLTPQAVNMLGGYRVQGKDLQSAQKIIDDAKAVQDAGACMLVVECVPVKLAQKISSILEIPTIGIGSGKYCDGQVLVYHDLLGLNKDFKAKFVKHFDKIDPQVGVEKYRDEVKSGIFPSQEHSFDYLDDELLDKLY
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Q29W37
Q52107
MERP_ACICA
Periplasmic mercury ion-binding protein
Acinetobacter calcoaceticus/baumannii complex
MKKLFASLALAAFVAPVFAATQTVTLSVPGMTCASCPITVKHALSKVEGVSKTDVSFDKRQAVVTFDDAKTNVQKLTKATEDAGYPSSLKR
Involved in mercury resistance. Acts as a mercury scavenger that specifically binds to a mercuric ion in the periplasm and probably passes it to the cytoplasmic mercuric reductase MerA via the mercuric transport protein MerT.
Q52107
O49066
SODM_CAPAN
Superoxide dismutase [Mn], mitochondrial
Capsicum
MALRNLMTKKPFAGILTFRQQLRCVQTFSLPDLSYDYGALEPAISGEIMQLHHQKHHQTYITNYNNALQQLHDAINKGDSPTVAKLQGAIKFNGGGHINHSVFWKNLAPTREGGGEPPKGSLGSAIDTNFGSLEAVIQKMNAEGAALQGSGWVWLGLDKELKRLVIETTANQDPLVIKGPNLVPLLGIDVWEHAYYLQYKNVKPDYLKNIWKVINWKYAAEVYEKECP
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
O49066
A5F543
RS3_VIBC3
30S ribosomal protein S3
Vibrio
MGQKVHPNGIRLGIVKPWNATWFANTKDFADNLDGDFKVRQYLSKELANASLSRIVIERPAKSIRVTIHTARPGVVIGKKGEDVEKLRAAVAKIAGVPAQINIAEVRKPELDGQLVADSIASQLERRVMFRRAMKRAVQNAMRLGAKGIKVEVSGRLGGAEIARSEWYREGRVPLHTLRADIDYATSSAHTTYGVIGVKVWIFKGEILGGMPAATEAAEPKADKPKKQRKGRK
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
A5F543
Q9PQV8
PFKA_UREPA
Phosphohexokinase
Ureaplasma
MNQVNFLNLDKNILIITSGGDAPGMNASLISLIHRLMNNNFNVFIGIEGLLGLYNNLIEPIKDKRVFDVYFNEQGTVIKTSRFIKLDINDKKTQIIKDNLLSHNIQKIIILGGQGSMQAGLVLTKMGFEVFGILHTIDNDFSETQMCIGALSAASFNQKLLKCLNYTAKAHCAFNLVELMGRECSWLVNNSVGKLKPILMLTNQDNKYTVDEVIDLIKDKINSIKEYDPLIIVQELIYDQKWYELLVKTFEQKLHKSLRITILNYLQRGAPVSDFDLQLAKDSANVLVDFIVNQNDIKNTNNMYVVINKFDNKLEVIKFNK
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Q9PQV8
Q4KLH4
PSPC1_RAT
Paraspeckle component 1
Rattus
MMLRGNLKQVRIEKNPARLRALESAAGESEPVAAAAMALTLAGEQPPPPAPSEEHPDEEMGFTIDIKSFLKPGEKTYTQRCRLFVGNLPTDITEEDFKRLFERYGEPSEVFINRDRGFGFIRLESRTLAEIAKAELDGTILKSRPLRIRFATHGAALTVKNLSPVVSNELLEQAFSQFGPVEKAVVVVDDRGRATGKGFVEFAAKPPARKALERCGDGAFLLTTTPRPVIVEPMEQFDDEDGLPEKLMQKTQQYHKEREQPPRFAQPGTFEFEYASRWKALDEMEKQQREQVDRNIREAKEKLEAEMEAARHEHQLMLMRQDLMRRQEELRRLEELRNQELQKRKQIQLRHEEEHRRREEEMIRHREQEELRRQQEGFKPNYMENREQEMRMGDMGPRGAINMGDAFSPAPAGTQGPPPMMGMNMNNRGTIPGPPMGPGPAMGPEGAANMGTPMIPDNGAVHNDRFPQGPPSQMGSPMGNRTGSETPQAPMSAVGPVSGGPGGFGRGSQGGNFEGPNKRRRY
Together with NONO, required for the formation of nuclear paraspeckles. Regulates, cooperatively with NONO and SFPQ, androgen receptor-mediated gene transcription activity in Sertoli cell line. Binds to poly(A), poly(G) and poly(U) RNA homopolymers. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway.
Q4KLH4
Q5NR75
RUVA_ZYMMO
Holliday junction ATP-dependent DNA helicase RuvA
Zymomonas
MIARLVGFLVEKNSDSAVIDVNGVGYLVQLSGRALDYFSEIEGEITVHIETQIREDSITLFGFASYLERDWFRLLTSVQGVGGKAALAILTALTCDAISVAISSGDKTMICRANGIGPKIAQRIINELKEKPAAIALFSSAKGDHLAVEDISQPAASAHHAGNFMADAVSALLNLGFKPAEAQRVVQLASEELGDQATLDSLVRLALRLSSKH
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
Q5NR75
B1XT37
RPPH_POLNS
(Di)nucleoside polyphosphate hydrolase
Polynucleobacter
MLDREGYRPNVGIVLLNSRNEVFWGKRVGQHSWQFPQGGIQHGESPEQAMYRELHEEVGLLPEHVQIIGRTRDWLRYDVPEEYLRRQNSTRVHRAAYRGQKQIWFLLRLVGLDSDIQLRAFEHPEFDAWRWVPFWIQLDAVIGFKREVYQLALSELARYLSRGMRMQQLAWGTPLDLFQSFYAGNEDQSKSSEKSDK
Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage.
B1XT37
B3EEB5
RL9_CHLL2
50S ribosomal protein L9
Chlorobium
MKIILRKDVAALGDAGDVVAVKNGYANNYLIPQGMAIRATEGTLKALETEKKQQAKKIEQQRKNARDLAQKIEQMTLKVYAKAGESGKLFGTVTSADIAEALSAQGVEIDRRKITLEAPVKLLGKYEADAKLFMDVTVKVNFEVEAESSAS
Binds to the 23S rRNA.
B3EEB5
Q05910
ADAM8_MOUSE
Macrophage cysteine-rich glycoprotein
Mus
MLGLWLLSVLWTPAVAPGPPLPHVKQYEVVWPRRLAASRSRRALPSHWGQYPESLSYALGTSGHVFTLHLRKNRDLLGSSYTETYSAANGSEVTEQLQEQDHCLYQGHVEGYEGSAASISTCAGLRGFFRVGSTVHLIEPLDADEEGQHAMYQAKHLQQKAGTCGVKDTNLNDLGPRALEIYRAQPRNWLIPRETRYVELYVVADSQEFQKLGSREAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWNKDKFYISRYANVTLENFLSWREQNLQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSRHSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEDIPGCYCPEPREGGGCIMTESIGSKFPRIFSRCSKIDLESFVTKPQTGCLTNVPDVNRFVGGPVCGNLFVEHGEQCDCGTPQDCQNPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPEDAFQQNGTPCPGGYCFDGSCPTLAQQCRDLWGPGARVAADSCYTFSIPPGCNGRMYSGRINRCGALYCEGGQKPLERSFCTFSSNHGVCHALGTGSNIDTFELVLQGTKCEEGKVCMDGSCQDLRVYRSENCSAKCNNHGVCNHKRECHCHKGWAPPNCVQRLADVSDEQAASTSLPVSVVVVLVILVAAMVIVAGIVIYRKAPRQIQRRSVAPKPISGLSNPLFYTRDSSLPAKNRPPDPSETVSTNQPPRPIVKPKRPPPAPPGAVSSSPLPVPVYAPKIPNQFRPDPPTKPLPELKPKQVKPTFAPPTPPVKPGTGGTVPGATQGAGEPKVALKVPIQKR
Possible involvement in extravasation of leukocytes.
Q05910
A7ZLA2
PYRF_ECO24
OMP decarboxylase
Escherichia
MTLTASSSSRAVTNSPVVVALDYHNRDDALSFVDKIDPRDCRLKVGKEMFTLFGPQFVRELQQRGFDIFLDLKFHDIPNTAAHAVAAAADLGVWMVNVHASGGARMMTAAREALVPFGKDAPLLIAVTVLTSMEASDLADLGVTLSPADYAERLAALTQKCGLDGVVCSAQEAVRFKQVFGQEFKLVTPGIRPQGSDAGDQRRIMTPEQALAAGVDYMVIGRPVTQSVDPAQTLKAINASLQRSA
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
A7ZLA2
Q5WLQ0
RL5_ALKCK
50S ribosomal protein L5
Alkalihalobacillus
MNRLKEKYQNEIVSSLTEKFNYPSVMAVPKIEKIVVNMGIGDAVQNAKVLDKAVEELQAITGQKPVITKAKKSIAGFKLREGMPIGAKVTLRGERMYDFLDKLVSVSLPRVRDFRGVSKKAFDGRGNYTLGVREQLIFPEIDYDKVDKVRGMDIVIVTTAKTDEEARELLTQVGMPFQK
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.
Q5WLQ0
Q6F2A3
MNME_MESFL
tRNA modification GTPase MnmE
Mesoplasma
MNNLNQTIVAPTTNISTQAISLIRISGDDSFNIINKLLKTKIKEEKNVWVRKMFDGQELVDEVVITSFVSPASFTGENVVEIACHGGILNTQRIINLIIKNGARMANKGEFSQRAFLNNKIDLIQAEGINDLIFAKNELALKIGVNNMSGAHNQSIINLKGNLLDIISRIQVSIDYPDYDDVEGSSIPELAKALSGINEEVNNLLKRSKMAIKNTNGIKTAIVGKTNVGKSSLLNALLNEDKAIVTDIHGTTRDIVTGEINLENISLNLIDTAGIRETTDIVEGLGIEKSLKIIDEAELVLFVVDFKSINDEENKMIFDKLENKNYILVFNKSEFINDIERNKIKDLHNNFVYTSAINNDIDNLIMKIEQMHINEEIINNDSLILINLQQITLVEQVKDRLEKSLNAIIGGMPIDIVNVDLHEAWDYLNQLIGEQYDEEIIDNIFKKYCLGK
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.
Q6F2A3
P0CZ76
AROE_STRP3
Shikimate dehydrogenase (NADP(+))
Streptococcus
MSERLSGHTLLVSLLATPIRHSLSPKMHNEAYAKLGLDYAYLAFEVGTEQLADAVQGIRALGIRGSNVSMPNKEAILPLLDDLSPAAELVGAVNTVVNKDGKGHLVGHITDGIGALRALADEGVSVKNKIITLAGVGGAGKAIAVQLAFDGAKEVRLFNRQATRLSSVQKLVTKLNQLTRTKVTLQDLEDQTAFKEAIRESHLFIDATSVGMKPLENLSLITDPELIRPDLVVFDIVYSPAETKLLAFARQHGAQKVINGLGMVLYQGAEAFKLITGQDMPVDAIKPLLGDE
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
P0CZ76
Q4SSF5
LTOR3_TETNG
Late endosomal/lysosomal adaptor and MAPK and MTOR activator 3
Tetraodon
MADDLKRYLYKQLQSVEGLHAIVVTDRDGVPVVKVANDNAPVPALRPGFLSTFALATDQGSKLGLSKNKSIICYYNDYQIVQFNRLPLVISFIARSSANTGLIMSLENELAPLIEELKQVVEVT
Regulator of the TOR pathway, a signaling cascade that promotes cell growth in response to growth factors, energy levels, and amino acids. As part of the Ragulator complex, may activate the TOR signaling cascade in response to amino acids. Adapter protein that may regulate the MAP kinase cascade.
Q4SSF5
A7HGZ2
PANB_ANADF
Ketopantoate hydroxymethyltransferase
unclassified Anaeromyxobacter
MSSQTAPRRRVTIHELRRMKDAGEKIAVVTAYDATAARLADAAGVDVVLVGDSLGMVVQGHESTLPVTLEHMIYHSAAVRRGLARSSGRAHLVGDMPFGSYQASADEAVKSAMRLVAEGGVESVKLEGGAEFVEVIRRIARAGVPVMGHIGLTPQAVHRMGGYVVQGKDSEKAQQLLRDARALELAGCYAIVLECIPAELARIISSQLRIPTIGIGAGLHCDGQVLVLNDLLGMDDAFTPKFVKRFGEIGQAISTAVGAYVGEVKRRVFPDDAHSFHSSTVRLVPAAPVDEDDGEPSGGVMGAPV
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
A7HGZ2
Q75VR0
TPC1B_TOBAC
Voltage-dependent calcium channel protein TPC1B
Nicotiana
MEEYLLPGESSNSCRTRRRSGSIFDRRDAIAHGSAYQKAAALVDLAEDGIGLPEEILEGASFEKAAELYFMFTRFDFLWSLNYLALVVLNFFEKPLWCSKHLAESCNNRDYYYLGELPFLTGAESLIFEGVTLLLLIIHILFPISYEGFNLYWRSLLNRLKVILLLILVADIVVYILLPADFYYLPFRIAPYLRVVFFILNIRELRDSFFILAGMLGTYLNVVALSALFLLFSSWLAYVFFEDTRQGKTTFTSYGTTLYQMFVLFTTSNNPDVWIPAYKDSRWYCLFFVLYVLLGVYFVTNLILAVVYDSFKSELVKQVADKDRLRLRTLKKAFSLIDEANNGLLNEKQCTLLFEELNKYRTLPKISGDDFKSIFNELDDTGDFKINLEEFADLCSAIGLRFQKEDSLPIFEACPNFYHSPASEKLRGFIRGATFEYIIVFVLLVNLVAVIIETTLDIQNNSGQTFWQKVEFTFGWLYVIEMALKVYTYGFENYWRDGQNRFDFIVTWVIVIGETTTFVAPDDLTFLSNGEWIRYLLIARMLRLIRLLMHVERYRAFVATFLTLIPSLMPYLGTIFCILCFYCSLGLQIFGGIVNTGNPNLAQTDLAGNDYLLFNFNDYPNGMVTLFNILVMGNWQVWMQSYKELTGTSWTYAYFVSFYLISVLWLLNLIVAFVLEAFQAEMDLEASARCVDGDDKEAKRERRRNVGTKTRSQRVDFLLHHMLRSELTECSNDNP
Functions as a voltage-gated inward-rectifying Ca(2+) channel (VDCC) across the plasma membrane that mediates sucrose-induced Ca(2+) influx in autotrophically grown leaf cells. Acts as the major ROS-responsive Ca(2+) channel and is the possible target of Al-dependent inhibition. Plays a regulatory role in defense responses.
Q75VR0
A5GMW9
ISPD_SYNPW
MEP cytidylyltransferase
unclassified Synechococcus
MHLLIAAAGSGRRMGADRNKLLLAVHGRPVLAWTLEAAGAAQSIDWIGVIGQPLDHSAMAALFHHAGQPVTWIEGGSTRQESVERGLQALPGDARHVLIHDGARCLVAPQVFNRCAEALLEGGAVIAATPVSDTIKRVDAQGVITDTPDRSELWAAQTPQGFSVSELREGHAQARARNWVVTDDASLFERLGWPVRVLDAGPGNIKVTTPFDLTVAAAVLAQR
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
A5GMW9
Q8R5X5
EFP_FUSNN
Elongation factor P
Fusobacterium
MKIAQELRAGSTIKIGNDPFVVLKAEYNKSGRNAAVVKFKMKNLISGNISDAVYKADDKMDDIKLDKVKAIYSYQNGDSYIFSNPETWEEIELKGEDLGDALNYLEEEMPLDVVYYESTAVAVELPTFVEREVTYTEPGLRGDTSGKVMKPARINTGFEVQVPLFVEQGEWIKIDTRTNEYVERVKK
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Q8R5X5
Q9CCT0
SYA_MYCLE
Alanyl-tRNA synthetase
Mycobacterium
MQTHEIRKRFLDHFVKAGHTEVPSASVILDDPNLLFVNAGMVQFVPFFLGQCTPPYATATSIQKCIRTPDIDDVGITTRHNTFFQMAGNFSFGDYFKRGAIELAWALLTNSFADGGYGLDPERLWATVYLDDDEAAGLWQEIAGLPPERIQRRGMADNYWSMGIPGPCGPSSEIYYDRGPEFGPEGGPIVNEDRYLEVWNLVFMQNERGEGTTKEDYEIRGPLPRKNIDTGMGVERIALVLQGVHNVYEIDLLRPVIDLVATRAPRPYDPENEDTNHADNVRYRIIADHSRTAAILIGDGVSPVNDGRGYVLRRLLRRIIRSAKLLGIDSPIVGDLMATVCNAMGRAYPGLVTDFDRINRIAVAEETAFNRTLTSGSKLFDDVVGATVASGSTVVAGLDAFTLHDTYGFPIELTLEMAAEAGLTVDEKGFHELMLQQRQRAKVDAAARKQAHVDLTAYRELVDAGPTEFTGFDELTTEARILGIFVEGKRVPVVAHAVRGQAGITNRVELVLDRTPLYAESGGQIADAGTISGIGAGASSRAAVTDVQKIAKTLHVHRVNLESGEFVEGDTVVAVVDPGWRRGAAQGHSGTHIVHAALRQVLGPNAVQAGSLNRPGYLRFDFNWQGSLTGEQRTQIEEVTNEAVQADFEVHTFTEKLDTAKAMGAIALFGEAYPDEVRVVEMGGPFSLELCGGTHVHNTAQIGPVTILGESSIGSGVRRVEAYVGLDSFRHLAKERALMAGLASSLQVPSEEVHARVATLVERLKAAEKELERARQANVQAAATKAAAGAEWIGNVRVVVQRMSGPIAPDDLRFLVGDIRGKLGSDPAVVALIAVTSDGPTATVPYAVAANPAAQDLGIRANDLVEQLAMVVDGRGGGKADLAQGSGKDPTGIDAALDTVRAQIAQVG
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.
Q9CCT0
P48971
OPCA_NOSP7
Putative OxPP cycle protein OpcA
Nostoc
MTKSKISNPKLPMALQTSTIFSLQAPKDISLNEIDAELNQIWQSYGITGEDGGLPSATRATTFTLVVYEPEETQYLLAALGFYNGPIDGILGPQMAAALREVQKKHKLPETGTATQETLTILREEFAKGQRGGTGGEHAIAGLNSGSPRIADEIALRNPCRIIALFPITGEDEGVKAQVSAYCPIQKQSSSTLICCEYITLSGTAAALERIGGMIPALLIGGLPKFLWWKATPDPNNGLFKRLAAICNNVIVDSCNFNEPESDLLRLEELVEAGVPLADLNWRRLASWQELTAEAYDSPKRRAALREIDRVTIDYEKGNPAQALLFLGWLASRLEWQPVSYQKESGDYDITRIHFISQDQRQVEAELAGVPVADVGDIIGDLIALRLSSTNPQADCGTVICSETGGCMRMETHGGAQSAGLFQQVTSLSEQKAEALLSQQVQRWGRESLFEESLGVTANIFKLAN
May be involved in the functional assembly of glucose 6-phosphate dehydrogenase.
P48971
A0A0C4DH36
HV338_HUMAN
Probable non-functional immunoglobulin heavy variable 3-38
Homo
MQFVLSWVFLVGILKGVQCEVQLVESGGGLVQPRGSLRLSCAASGFTVSSNEMSWIRQAPGKGLEWVSSISGGSTYYADSRKGRFTISRDNSKNTLYLQMNNLRAEGTAVYYCARY
Probable non-functional open reading frame (ORF) of V region of the variable domain of immunoglobulin heavy chains . Non-functional ORF generally cannot participate in the synthesis of a productive immunoglobulin chain due to altered V-(D)-J or switch recombination and/or splicing site (at mRNA level) and/or conserved amino acid change (protein level) . Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen .
A0A0C4DH36
Q24SV0
RECO_DESHY
Recombination protein O
Desulfitobacterium
MGVYHADALVIRSREYGESDRLLTLFSREYGKIQAVAKGVRKPKSRQRAGAQLFTYAEYLLHKGKSLDTVNQVSPRESFPHLWTDLDMSMAATAMAELLDLATLPGQPHPELFTLTFSSLFLVESCDPALVQCTYALKLMNYLGYRPRLVECAECGQRVQGERLLFSPDAGGVVCRQCQTQGSSPAVGRWVSGGSLGLMRQLLQGELEKLNRLRWNQWSKKEILEASQYFCEQTLDKSLRSWSMGNRLVNVGQNPSGKDDLNERRDVDGTGES
Involved in DNA repair and RecF pathway recombination.
Q24SV0
A0A023FFD0
EV991_AMBCJ
Evasin P991
Amblyomma
MHSTIVYACLLALAVFVALHGTPLAALAENGEGTTQPDYDNSTDYYNYEDFKCTCPAPHLNNTNGTVMKPIGCYYTCNVTRCTAPDTYPCYNLTEHQAKNLTTSPTTLCAVGNCDHGICVPNGTKELCFKAPNLEE
Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CCL2, CCL3, CCL3L1, CCL4, CCL4L1, CCL5, CCL6, CCL7, CCL8, CCL9, CCL11, CCL12, CCL13, CCL14, CCL16, CCL17, CCL18, CCL19, CCL22, CCL23, CCL24 and CCL27.
A0A023FFD0
B8E9H2
CH10_SHEB2
Chaperonin-10
Shewanella
MNIRPLHDRVIVKRLEVESTSAGGIVLTGSAAEKSTRGEILAVGNGRILENGTVKPLDVKVGDVVIFNEGYGVKKEKIDGQEVLILSEADLMAVVG
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.
B8E9H2
Q5KWE8
CRCB2_GEOKA
Putative fluoride ion transporter CrcB 2
Geobacillus thermoleovorans group
MVYLAVGIAGMIGALVRYGLGLVVPAAAVGGFPLGTLFINWTGSFLLSWFTVMFTRRPAWPPWLKTAVTTGFVGSYTTFSTLSVECVELMEQGRFGMAAVYIAASLFGGLLASWAGYAAAQPERKEGIG
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Q5KWE8
Q927E5
DHAL1_LISIN
PEP-dependent dihydroxyacetone kinase 1, ADP-binding subunit DhaL
Listeria
MTYDKDWALRWLNDFGERVQENKQLLSDLDQAIGDGDHGINMARGLSELKKAFTEKEPADLTDVFKTAGMTMVSKVGGASGPLYGTAFLNMSKAVDSETIDAEGLTKVIEAGLEGIEKRGKSHAGEKTMIDVWEPVVNALHQEDLTDDVVEAALQKTKDLKATKGRASYLGERSIGHLDPGAYSSALLFHAMLQTEVS
ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone binds to DhaK.
Q927E5
Q9KS67
CRY2_VIBCH
Cryptochrome-like protein cry2
Vibrio
MEKINLVWLKRDLRLTDHAPLQAALTSGRPTLLLYLFEPMLLGDAHYSERHWRFVWQSLQAINRDLAQSKGEVLIVTSDWQTCFARIAERYAIEAIYSHQEVGLACTFQRDLALAQWCQQHDIVWHEFPYAAVIRGAQTRKNWDEHWQQVMRSPCCDPDLTRANWLKLDAATLGLRSDIPATWQSKQAGMQTGGSDMAWATLEDFFARRGREYYRSISSPSLARHACSRMSPYLAWGNISLREMYQTLLKHWSVAGFRRSLIALSSRLHWHCHFIQKFESECEMEFRCVNRAYDSLLQQSSDAPAAQLAAWQTGHTGIPLVDACMRCLIQTGYLNFRMRAMLVSVLTHHMNVDWRAGVTYLAQLFLDFEPGIHYPQFQMQAGVTGTNTIRIYNPTKQAQEHDSEGQFIHKWVPELAQVPVPLLFEPWLMTPLEAQMYQVPLESPYLKPVMDLEASAKQARDRLWQWQKLPAVQAEAMRILARHVRQAKPRTSPRQPNKRQPEMD
Has no photolyase activity.
Q9KS67
Q9PT40
VSPH2_MACLB
Venom serine proteinase-like protein 2
Macrovipera
MVLIRVLANLLVLQLSYAQKSSELVIGGDECNINEHPFPVALHTARSKRFYCAGTLINQEWVLTAARCDRKNIRIILGVHSKNVPNEDQQIRVPKEKFFCLSSKTYTRWDKDIMLIRLKKPVNDSTHIVPLSLPSSPPSVGSVCRIMGWGTITTTKVTYPDVPHCANINMFDYSVCRKVYRKLPEKSRTLCAGILQGGIDSCKVDNGGPLICNGQIQGIVSWGGHPCAQPHKPALYTNVFDYTDWIQSIIAGNITATCPP
Snake venom serine protease homolog that may act in the hemostasis system of the prey.
Q9PT40
Q50773
MTRF_METTM
N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit F
Methanothermobacter
MIILSNKPNIRGIKNVVEDIKYRNQLIGRDGRLFAGLIATRISGIAIGFLLAVLLVGVPAMMSILGVI
Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Q50773
Q65PA7
RL3_BACLD
50S ribosomal protein L3
Bacillus
MTKGILGRKIGMTQVFAENGDLIPVTVIEAAPNVVLQKKTSENDGYEAIQIGFDDKREKLANKPEKGHVAKAETAPKRFVKELRGVDMDAYEVGQEVKVDIFSNGEIVDVTGTSKGKGFQGAIKRHGQSRGPMSHGSRYHRRPGSMGPVDPNRVFKGKLLPGRMGGEQITVQNLEIVKVDAERNLLLVKGNVPGAKKSLVTVKSAVKSK
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.
Q65PA7
P44651
NAPD_HAEIN
NapA signal peptide-binding chaperone NapD
Haemophilus
MNNTNLILENARDWHVVGLIVQGNPKKLSAIQTALLAIEHTEIPTLDEKLGKFVVVMQSNDQHLLLEKMESVKDIDGVINVSLVYHEQDEQNK
Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin-arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export.
P44651
Q7AP54
HBP2_LISMO
Surface virulence-associated protein A
Listeria
MKKLWKKGLVAFLALTLIFQLIPGFASAADSRLKDGGEYQVQVNFYKDNTGKTTKESSEADKYIDHTATIKVENGQPYMYLTITNSTWWQTMAVSKNGTRPEKPAQADVYQDRYEDVQTVSTDAAKDTRVEKFKLSSLDDVIFSYMHIKVDAISYDHWYQVDLTIDPSTFKVISEPAVTTPVTLSDGIYTIPFVAKKANDDSNSSMQNYFNNPAWLKVKNGKKMVAMTVNDNKTVTALKTTLAGTLQDVKVVSEDKDANTRIVEFEVEDLNQPLAAHVNYEAPFNGSVYKGQADFRYVFDTAKATAASSYPGSDETPPVVNPGETNPPVTKPDPGTTNPPVTTPPTTPSKPAVVDPKNLLNNHTYSIDFDVFKDGTTETSMMESYVMKPALIKVENNQPYVYLTLTNSSWIKTFQYKVNGVWKDMEVVSGDINKNTRTVKYPVKDGTANTDVKTHVLIEDMPGFSYDHEYTVQVKLNAATIKDITGKDVTLKEPVKKDILNTGNVASNNNAGPKLAKPDFDDTNSVQKTASKTEKNAKTNDSSSMVWYITLFGASFLYLAYRLKRKRLS
Acts as an extracellular and cell wall-bound hemophore; scavenges host heme and hemoglobin from the environment and also serves as a cell wall receptor for both (Probable). At low hemin (Hn) and hemoglobin (Hb) concentrations adsorbs Hn/Hb and presumably directs it to membrane transporters (Probable). Soluble Hbp2 can probably pass Hn/Hb to cell wall-anchored Hbp2, and both forms can accept Hn/Hb from Hbp1 . May be involved in crossing the digestive barrier in infected animals . Binds host hemin (Probable) . Binds host hemoglobin with affinity in the nanomolar range .
Q7AP54
Q32001
DNE1_CHLAP
DNA endonuclease I-ChuI
Chlamydomonas
MSLTQQQKDLIFGSLLGDGNLQTGSVGRTWRYRALHKSEHQTYLFHKYEILKPLCGENTLPTESIVFDERTNKEVKRWFFNTLTNPSLKFFADMFYTYDQNTQKWVKDVPVKVQTFLTPQALAYFYIDDGALKWLNKSNAMQICTESFSQGGTIRIQKALKTLYNIDTTLTKKTLQDGRIGYRIAIPEASSGAFREVIKPFLVDCMRYKVSDGNKGHL
Probable endonuclease involved in intron homing. Encoded in the group-I intron of the subunit rRNA-encoding gene (rrnL), it generates a staggered cut with 4-nt (CTCG) 3'-OH overhangs 2 bp downstream from the intron insertion site.
Q32001
Q9JW46
RNPA_NEIMA
Protein C5
Neisseria
MDYRFGRQYRLLKTDDFSSVFAFRNRRSRDLLQVSRSNGNGLDHPRIGLVVGKKTAKRANERNYMKRVIRDWFRLNKNRLPPQDFVVRVRRKFDRATAKQARAELAQLMFGNPATGCRKQA
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Q9JW46
Q8N0X4
CLYBL_HUMAN
Malate synthase
Homo
MALRLLRRAARGAAAAALLRLKASLAADIPRLGYSSSSHHKYIPRRAVLYVPGNDEKKIKKIPSLNVDCAVLDCEDGVAANKKNEARLRIVKTLEDIDLGPTEKCVRVNSVSSGLAEEDLETLLQSRVLPSSLMLPKVESPEEIQWFADKFSFHLKGRKLEQPMNLIPFVETAMGLLNFKAVCEETLKVGPQVGLFLDAVVFGGEDFRASIGATSSKETLDILYARQKIVVIAKAFGLQAIDLVYIDFRDGAGLLRQSREGAAMGFTGKQVIHPNQIAVVQEQFSPSPEKIKWAEELIAAFKEHQQLGKGAFTFQGSMIDMPLLKQAQNTVTLATSIKEK
Mitochondrial citramalyl-CoA lyase indirectly involved in the vitamin B12 metabolism . Converts citramalyl-CoA into acetyl-CoA and pyruvate in the C5-dicarboxylate catabolism pathway . The C5-dicarboxylate catabolism pathway is required to detoxify itaconate, a vitamin B12-poisoning metabolite . Also acts as a malate synthase in vitro, converting glyoxylate and acetyl-CoA to malate . Also displays malyl-CoA thioesterase activity . Also acts as a beta-methylmalate synthase in vitro, by mediating conversion of glyoxylate and propionyl-CoA to beta-methylmalate . Also has very weak citramalate synthase activity in vitro .
Q8N0X4
Q2T3J4
4HYPE_BURTA
4-hydroxyproline 2-epimerase
pseudomallei group
MKHLHIIDSHTGGEPTRVVVSGFPPLGDGPMAERLAALARDHDRYRTACILEPRGSDVLVGALLCEPVSAGAAAGVIFFNNAGYLGMCGHGTIGLVRTLHHMGRIAPGVHRIETPVGDVEATLHDDLSVSVRNVLAYRHAKDVVVEVPGHGSVTGDVAWGGNWFFLVSDHGQRIAGENVAALAAYASAVRAGLERAGVTGRDGAPIDHIELFADDPEHDSRSFVLCPGHAYDRSPCGTGTSAKLACLAADGKLAPGAAWRQASVIGSVFSASYERAESGVVPTIRGSAHLSAEATLLIEDDDPFGWGIVS
Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Can also catalyze the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C), albeit with 42-fold lower efficiency. Displays no proline racemase activity.
Q2T3J4
C5MH59
ASA1_CANTT
ASTRA-associated protein 1
Candida
MSQQFTLRSHNSSITFIYPSPTSSLHLYTADSTGLIIEWDLITRRPVITWQAHNDTILSMSTIHNHLLTHSRDNTIKIWNNTDCIMEIPCNSLNFSNVVVVHDEILITPASINSNNLDVYKITSDWQLTRLISDINVYQLVEKGIQFEEIGSRNDYGIIMKIHLVDNIIYVGFESGDIVGLELILPKPIVKENSNIDKLIINQSPKLIVKYHNSIHVPNPIISMSTFQDILVSGSTTNKIVIHKHPVEIIKVTHSGVQSIVNYKNENLIIGFWNGEIRYDENVIKRDVPMIQNNDNDDRSKSIKKLTFMTLLVPQKVESTTTGKNKYSQLIRGKKILTTDTLLVGYEDGSIVAYKV
Component of the ASTRA complex involved in chromatin remodeling.
C5MH59
B1LWS9
RL2_METRJ
50S ribosomal protein L2
Methylobacterium
MALKTFKPVTPSLRQLVLVDRRELYKGKPVKALTEGKSSSGGRNNLGRITVRFRGGGHKRVLRNVDFKRRDQLGVAATVERIEYDPNRTAFIALINFPDGKQSYILAPQRLQPGDKVVAGESVDIKPGNAGPVGSMPVGTIVHNVELKIGKGGAIARSAGNYAQIVGRDQGYVTLRLNSGEQRLVHGQCFASVGAVSNPDHMNISLGKAGRNRWLGKRPHNRGVAMNPVDHPHGGGEGRTSGGRNPVTPWGVPTKGKKTRSNKRTDVFILSSRHNRKK
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
B1LWS9
B1LFX6
FIXB_ECOSM
Protein FixB
Escherichia
MNTFSQVWVFSDTPSRLPELMNGAQALANQINTFVLNDADGAQAIQLGANHVWKLSGKPDERMIEDYAGVMADTIRQHGADGLVLLPNTRRGKLLAAKLGYRLKAAVSNDASTVSVQDGKATVKHMVYGGLAIGEERIATPYAVLTISSGTFDAAQPDASRTGETHTVEWQAPAVAITRTATQARQSNSVDLDKARLVVSVGRGIGSKENIALAEQLCKAIGAELACSRPVAENEKWMEHERYVGISNLMLKPELYLAVGISGQIQHMVGANASQTIFAINKDKNAPIFQYADYGIVGDAVKILPALTAALAR
Required for anaerobic carnitine reduction. May bring reductant to CaiA.
B1LFX6
Q254H4
IF2_CHLFF
Translation initiation factor IF-2
Chlamydia
MEKAKLTKNLKLKIKNAQLTKAAGLDKLKQKLAQAGSSDTKNSSEKPSAKVAEKVVKKKSVVDPSVSATPESVSSETSPRRIRAKNRSSFVSEDLEVSSPVPVDSDTTSSMPPVEEEIASSTDSEPEVIEVTQPPIEEKSEVVTKVPPTPLKEPEVVVKKDPPKSVVGIKSNFGPTGKHINHLLAKTFKAPKKEDKPAPKERSGQAQAKPQQSSEASSENKPHSPNNNRSSQPFYRRDTSKKPGSDFRDRAKKDDNPKAFTGRDRYGLNDGSDDDKWRKKRVQKTKKHYDEHTIQRPTHIKVPLPITIKDLAAEMKLKASELIQKMFIHGMTYVVNDVLDNETTVQFIGLEFGCTIDIDSSEQDKLCIESNTVKEEIQETDPSKLIIRPPIVAFMGHVDHGKTTLIDSLRKSNIAAVEAGAITQHMGAFCCSTPVGNITILDTPGHEAFSAMRARGAEVCDIVVLVVAGDEGIKEQTLEAVKHARAANITIVVAINKCDKPNFNAETIYRQLSEINLLPEAWGGTTVTVNTSAKTGEGLPELLEMLALQAEVLELKANPSARARGIVIESELHKGLGAVATILVQNGTLHLGEALVFNDCYGKVKTMHDEHNRLMKVASPSVPALITGLSSMPKAGDPFVVVKNEKIAKDIIGARLAGQQKFALQKKRPNFDAMLQNKKILKLIIKADVQGSIEALASSILKIVSDKVSAEILSNSVGEISESDIRLAAASKAVIIGFHTGIESHAESLIKSLGVKVQLFNIIYHAVDAVKEMMTALLDPIAEEKNLGSAEIKETFKSSQLGTIYGCLVSEGVMTRNQKVRVVRNNDVLWKGTLSSLKRIKEDVKEVKKGLECGILLEGYQNAQVGDILQCYEVIYHPQKL
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Q254H4
P85258
CTX17_LACTA
Cytoinsectotoxin-1f
Lachesana
MKYFVVALALVAAFACIAESKPAESEHELAEVEEENELADLEDAVWLEHLADLSDLEEARGFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYLLKHYGKKALQKASEKL
Insecticidal, cytolytic and antimicrobial peptide. Has insecticidal activity against the flesh fly S.carnaria. Has antibacterial activity against the Gram-negative bacteria E.coli. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis.
P85258
B4S6J0
MURA_PROA2
UDP-N-acetylglucosamine enolpyruvyl transferase
Prosthecochloris
MDKLVINGGHRLTGSVAASGSKNSALPLIAATLLCDNGTCRLERIPDLKDTRTFQELLAYLGADISYSGSRLSVSTQNLRAIQAPYELVKKMRASIYVLGPLLARFGRAEVSLPGGCAFGPRPIDLHLMAMEKLGASISIKNGYIEASIAKGRLTGGHIEFPVSSVGATGNALMAASLAEGTTTITNASIEPEITALCDFLMAMGADIKGAGTTALTIEGVPSLHPVAFTNIFDRIEAGTLLAAAAITKGTISITGIDHTHMGAVLKKFKQAGCRITIDDDSLTLQSPDRLEPTDIIASPYPFFPTDMQAQWIALMTQANGSSRIIDKVYHERFNHIPELNRLGAKIEINNNEAIVHGPQLLTGTTVMSTDLRASACLVLAGLVAQGTTEVLRVYHLDRGYEKIEEKLRHLGADIQRENYQEFST
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
B4S6J0
P28605
GLN1B_SYNP2
Glutamine synthetase I beta
unclassified Synechococcus
MTQTATDVLRLIQEENIQIIDLKFVDLPGIWQHCSFYQDQLDEASFVDGVPFDGSSIRGWKAINESDMAMVPDPTTAWIDPFCKEKTLSLICSIKEPRTGEWYSRDPRSIAQKAVDYLAASGIGDTAYFGPEAEFFVFDDVRFDQTENKGFYYVDSVEGRWNSGRKEPGGNLAHKPGYKQGYFPVPPTDTLQDMRTEMLLTMAKCGVPIEKHHHEVATGGQNELGFRFATLLKAADYLMTYKYVIKNVARKYGRTVTFMPKPLFNDNGSGMHTHQSLWKEGQPLFWGDRYANLSQLALHYIGGILKHAPALLAFSNPSTNSYKRLVPGFEAPVNLAYSQGNRSASVRIPLSGPNPKAKRLEFRCPDATANPYLAFAAMLCAGIDGIKNAIDPGDPLDVDIYDLTPEELSKIPSTPASLEAALEALQQDHDFLTAGGVFTTDFIENWIEYKLDAEVNPLRLRPHPYEFALYYDC
Involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
P28605
Q4L4R1
AROD_STAHJ
Type I dehydroquinase
Staphylococcus
MTNVEVAATVAPNQLLDTLTLDNIKEYSNDIDIIELRIDQWEDRHLELLKSNLEQLQELNINANVLVTYRTISQGGKGEMTHEAYMTLLKEIIKNHHCQMIDIEWDSDFDVFAHRDLINLAHRYNKQVVISYHNFQETPDIDILKFTYYKMNQLNPDYVKIAVMPQDKEDVATLLEAVATSADTLDAKVIGISMSKVGLVSRTAQGVFGGTVSYGCLGEPQAPGQIHVKTLKQQLLFYSNH
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Q4L4R1
Q822M2
RF1_CHLCV
Peptide chain release factor 1
Chlamydia
MEKKILEYLKRLEEVEVKISNPEIFENPKEYSSLSKEHARLSELKNVYDKVLGQEKILNDDKEALAQEKDPEMIAMLEEGIQLGKAEVDKLYKVLENLLVPPDPDDDLNVIMELRAGTGGDEAALFVGDCVRMYHLYASTKGWKYEVLSASESDIGGYKEYVMGISGAAVKRLLQYEAGTHRVQRVPETETQGRVHTSAITVAVLPEPAEDDEEVFIDEKDLKIDTFRASGAGGQHVNVTDSAVRITHLPTGVVVTCQDERSQHKNKAKAMRILKARIRDAEMQRRQKEASAMRSAQVGSGDRSERIRTYNFSQNRVTDHRIGLTLYNLDKVMEGDLDAITSALVSHAYHQLLQHGNEENS
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Q822M2
Q03WX7
PYRH_LEUMM
Uridine monophosphate kinase
Leuconostoc
MTDIKYKRVLMKLSGEALAGDKGQGIDLETVSAIAEELKDVHDLGTQIAIVVGGGNLWRGEPASKIGMERSRADYTGMLGTTMNALVLQDSLERAGVQTRVQTAITMQQIAEPYIRGRAIRHLEKGRIVIFAAGTGSPYFSTDTTAALRANEINADAILMGKNGVDGIYDSDPNKNANAVKFTELTHLDILQKGLKVMDSTASSLSMDNNMPLVVFNLNTPGNLKRVVLGEAIGTTVTGEK
Catalyzes the reversible phosphorylation of UMP to UDP.
Q03WX7
Q96IZ6
MET2A_HUMAN
Methyltransferase-like protein 2A
Homo
MAGSYPEGAPAVLADKRQQFGSRFLRDPARVFHHNAWDNVEWSEEQAAAAERKVQENSIQRVCQEKQVDYEINAHKYWNDFYKIHENGFFKDRHWLFTEFPELAPSQNQNHLKDWFLENKSEVPECRNNEDGPGLIMEEQHKCSSKSLEHKTQTLPVEENVTQKISDLEICADEFPGSSATYRILEVGCGVGNTVFPILQTNNDPGLFVYCCDFSSTAIELVQTNSEYDPSRCFAFVHDLCDEEKSYPVPKGSLDIIILIFVLSAIVPDKMQKAINRLSRLLKPGGMMLLRDYGRYDMAQLRFKKGQCLSGNFYVRGDGTRVYFFTQEELDTLFTTAGLEKVQNLVDRRLQVNRGKQLTMYRVWIQCKYCKPLLSSTS
S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Thr)(UGU) and tRNA(Arg)(CCU) . N(3)-methylcytidine methylation by METTL2A requires the N6-threonylcarbamoylation of tRNA (t6A37) by the EKC/KEOPS complex as prerequisite .
Q96IZ6
Q9P0J0
NDUAD_HUMAN
NADH-ubiquinone oxidoreductase B16.6 subunit
Homo
MAASKVKQDMPPPGGYGPIDYKRNLPRRGLSGYSMLAIGIGTLIYGHWSIMKWNRERRRLQIEDFEARIALLPLLQAETDRRTLQMLRENLEEEAIIMKDVPDWKVGESVFHTTRWVPPLIGELYGLRTTEEALHASHGFMWYT
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis . Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone . Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes .
Q9P0J0
Q0C093
KGUA_HYPNA
GMP kinase
Hyphomonas
MSNSGHPKDRGNRRGLMLVLSSPSGAGKTTLSRMLLEEFGDVKLSISATTRPPRPNEVHGEDYYFKTPDEFHRMIERREFLEWAHVFDKHYGTPKADTVARLEAGEDVLFDVDWQGADALHDQMPNDVVSVFILPPSIEALQARLMGRPGSTPELVARRMEDAKREIMHWRRYDYVIVNDDLNVAYQRLKRILLVERLKRLRQIDLEDHVRALLGEA
Essential for recycling GMP and indirectly, cGMP.
Q0C093
Q753D9
PKH3_ASHGO
Serine/threonine-protein kinase PKH3
Eremothecium
MSKRKSPHDFLFREELGHGSYSTVYRVVERSSQHQYAIKICSKRHIIGENKVKYVTIEKNTLNLLGQANHPGIIKLYYTFHDQENLYFVMDLAPGGELLQLLRRQRVFSEAWARHYMCQLVDTVEYIHSMGVIHRDLKPENVLLDKEGRLMIADFGAAYTVGQSDAGSDGDKPATSFVGTAEYVSPELLLENKSYYSSDVWALGCMLYQFLQGTPPFRGQNEMETFEQIVNLDYTWRIPANPLAAGLVSKILVLDPSQRYTLEQIKKHKWFSGVDWNNKEKIWRGSWTIASESTPRPRVGYKSRELLDTPIKNIPVVTQRNKKPTKMNTTSSIVEWRKMLGLSGNDLGIKATLGGNGLPIAPFTPTSGITPDNRGDNAVAPAKTRDAFRPMSSRVISSPHSKPSGRPAALPLPLQTGTPSHNVVQQIVVNTPGRTETSSPYVSPTVPVRNAIWKQDWVQLHEIPYSAKYSGLTLAGFSQVSDTLIADLISHHANELRTLSRTGILSLDNTGYLSFIEQGRARPLSRIIDPDLSIYEYQLGHSTEDDFLILEKYKQSIWIVWPNKPTSASRRIPIKETWAQTLSKYKKQVSDEEELSAKLNRTCVSSWGSRTPSPTYPAEGKTRVAVQPQDIPLPSPAKSSSNSGVSEPISKIPPRQLVSASEQSHKAKSEAHTKKANSYSYIAPNDMVLSSSRYEVLRTASNNDSKSNGAAVSGASAAFRTLRVNK
Serine/threonine-protein kinase.
Q753D9
Q722V6
METXA_LISMF
Homoserine transacetylase
Listeria
MTLQQKELFQKSPLLLENGETLSPVLVGYETYGTLSASRDNCILLEHALTGTAHAAKHFESDAPGWWDDYIGPGKTIDTDKYFLVCTNVFGGCSGTTGPSSINPKTGEPFRLQFPGFSIKDIIKVQRELLEQLGVTRIVSVIGGSMGGMQATEWAIDYADITDSIINIASPLAAGPDAIGYNLIMRMAILNDPDFNGGNYVGQPEGGLATARMVGMMTYRTSELFSKRFERFTVAESSPAAFSKEHFQIESYLQYQGDTFVERFDANSYLYLTKAIDLFDVTAPAKDDLPAFAKIKIPYLLIGITTDQLFRIHDLRRGYELLKEWDVPVTYHEVASEYGHDAFLVEKEVPKFEPLIRSFLSNLPVKSI
Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Q722V6
P56251
HBB_LEIXA
Hemoglobin beta chain
Leiostomus
VDWTDAERAAIKALWGKIDVGEIGPQALSRLLIVYPWTQRHFKGFGNISTNAAILGNAKVAEHGKTVMGGLDRAVQNMDNIKNVYKQLSIKHSEKIHVDPDNFRLLGEIITMCVGAKFGPSAFTPEIHEAWQKFLAVVVSALGRQYH
Involved in oxygen transport from gills to the various peripheral tissues.
P56251
P52901
ODPA1_ARATH
Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
Arabidopsis
MALSRLSSRSNIITRPFSAAFSRLISTDTTPITIETSLPFTAHLCDPPSRSVESSSQELLDFFRTMALMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAIGMEAAITKKDAIITAYRDHCIFLGRGGSLHEVFSELMGRQAGCSKGKGGSMHFYKKESSFYGGHGIVGAQVPLGCGIAFAQKYNKEEAVTFALYGDGAANQGQLFEALNISALWDLPAILVCENNHYGMGTAEWRAAKSPSYYKRGDYVPGLKVDGMDAFAVKQACKFAKQHALEKGPIILEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERIKKLVLSHDLATEKELKDMEKEIRKEVDDAIAKAKDCPMPEPSELFTNVYVKGFGTESFGPDRKEVKASLP
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
P52901
Q25055
HOL3_HOLDI
Holotricin-3
Holotrichia
MNKLIILGLACIIAVASAMPYGPGDGHGGGHGGGHGGGHGNGQGGGHGHGPGGGFGGGHGGGHGGGGRGGGGSGGGGSPGHGAGGGYPGGHGGGHHGGYQTHGY
Has antifungal activity against C.albicans.
Q25055
I1JIC4
ERD15_SOYBN
Protein EARLY RESPONSIVE TO DEHYDRATION 15
Glycine subgen. Soja
MEVISASSLNPNAPMFVPLAYRTVEDFSDQWWNLVHSSPWFRDYWLRECFQDPQFQNDDAFDFDFDLDLQDEDEKERKEGKEVVSLGVLKWRSCGGGWAQAPRYVEKAPKFVKPKVSPRAIHQPR
DNA-binding protein that binds to the NRP-B promoter to activate the NRP-B-mediated cell death response . Functions as an upstream component of stress-induced NRP-B-mediated signaling to connect stress in the endoplasmic reticulum (ER) to an osmotic stress-induced cell death signal . Exhibits transactivation activity in yeast .
I1JIC4
B7I2C3
FMT_ACIB5
Methionyl-tRNA formyltransferase
Acinetobacter calcoaceticus/baumannii complex
MKIIFAGTPEFAATALAALLKTSHEIIAVYTQPDRKAGRGQKLTPSPVKQLALEHNIPVYQPLHFKASTEEGLAAQQELAALGADVMVVAAYGLILPQAVLDTPKYGCLNIHGSLLPRWRGAAPIQRAIATGDDETGITIMQMAAGLDTGDMMYKTYCPIASEDTSATLHDKLAAQGATAICAVLESEETLQKYLAEREVQDESLTVYAHKLVKSEARIDWSMNAVQVDRNIRAFNPWPVAFIQLDENNALRVWNSIISSQSKVNAQAGEIIAIDKQGVHVACGENTFICLTSVQWPGGKALNAQQIAQTQKLHVGQILP
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
B7I2C3
P58982
MTTC1_METMA
Trimethylamine corrinoid protein 1
Methanosarcina
MANKEEIIAKAKDAITDFDDELAAEVAAEALAAGVDPVELIEKGFTAGMQEVGEQFEQGTLFLPHVLAAAEAMNAGIEVIKPEMEKRKSQTKSLGTIVIGTIEGDIHSIGKDIVASMLNIAGFKVVDLGRDVPIKTFVEKAKEIKPQIIASSALMTTTMVNQIQIEEQLKEAGIRGQVKTMVGGAPVTQDWADKIGADIYGESATDVVSKVKAALL
Acts probably as a methyl group carrier between MttB and either MtbA or MtaA.
P58982
Q89AZ8
FLIH_BUCBP
Flagellar assembly protein FliH
Buchnera
MSKNFLNKAWEKWNPGEIDTTTNITHNNFKKSDQVSNFSNTFTAEQNNDNLNNIKKNGYEDGFKRGKKEGFEAGFKKSFAEFEKKNREILNKMEDFLSNFRQSLSLFDEKVSSKIINTVLKISKKVLETTTLANDDSSFLKKIETIFQDRMFSLENPKLFISPNNQLLVKKYFGKIFSQYGWTICYNHYIPSGEFIISSGDTILDSTSSTRWNKLCKLVYFQEKQ
Needed for flagellar regrowth and assembly.
Q89AZ8
Q2LTB9
EFG1_SYNAS
Elongation factor G 1
Syntrophus
MKNDIKKVRNIGISAHIDSGKTTLTERILFYTKRIHAMHDVKGKDGVGATMDSMELERERGITISSAATFCTWGDHEVNIIDTPGHVDFTIEVERALRVLDGAILVLCAVGGVQSQSITVDAQMKRYKVPCVAFVNKCDRSGANPARVVEQLKTRLGHNALLMQLPIGLEADFQGIVDLISMKAVYFDGAGGELLRTEAVPESLLPEAISRREELIDSVSLFSDSLTEAILEGTEISEVMIMEAVRQGTLERKITPVFIGSAYKNKGIQPLLDAVTRYLPCPADIENSALDLSREEAPVQLTSNTEDPVVALAFKLEDGIYGQLTYIRVYQGILSRGATVVNARDGKKVRIGRLVRMHADQMEDIEAIHAGYIGALFGLECQSGDTFAAQGLNLAMTSMFVPEPVISLAIVPKDKKSMVNMSKALNRFTKEDPTFRTHLDPETSETIIEGMGELHLDIYVERIRREYNAEVTTGNPRVAYRETITQKAAFNYTHRKQTGGSGQYGRVAGYIEPLSDEDFLFENKITGGAIPTQFIPACEKGFRMSMAKGPKMEFPVTGVKVVIDDGAFHAVDSSDMAFQAAARGAFREAYNKAKPVILEPIMKVVVETPNEFQGAVMGLLNQRRGMIVGTQDEGQTCVIEAQTPLAEMFGFSTVIRSATQGKAQFTMEFSAYRQVPQSIAEKITEEVAKRKKSAA
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Q2LTB9
P15772
RL12_HALMA
Hmal12
Haloarcula
MEYVYAALILNEADEEINEDNLTDVLDAAGVDVEESRVKALVAALEDVDIEEAVDQAAAAPVPASGGAAAPAEGDADEADEADEEAEEEAADDGGDDDDDEDDEASGEGLGELFG
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
P15772
Q9ER60
SCN4A_MOUSE
Voltage-gated sodium channel subunit alpha Nav1.4
Mus
MASSSLPTLVPPGPHCLRPFTPESLAAIEQRAMEEEARLQRNKQMEIEEPERKPRSDLEAGKNLPLIYGDPPPEVIGVPLEDLDPYYSDKKTFIVLNKGKAIFRFSATPALYMLSPFSIVRRVAIKVLIHALFSMFIMITILTNCVFMTMSNPPSWSKDVEYTFTGIYTFESLIKMLARGFCIDDFTFLRDPWNWLDFSVITMAYVTEFVDLGNISALRTFRVLRALKTITVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALVGLQLFMGNLRQKCVRWPPPMNDTNTTWYGNDTWYGNDTWYGNDTWYGNDTWNSQESWVSNSTFDWEAYINDEGNFYFLEGSNDALLCGNSSDAGHCPEGYECMKAGRNPNYGYTSYDTFSWAFLALFRLMTQDYWENLFQLTLRAAGKTYMIFFVVIIFLGSFYLINLILAVVAMAYAEQNEATLAEDQEKEEEFQQMLEKFKKHQEELEKAKAAQALEGGEEADGDPTHSKDCNGSLDTSGEKGPPRPSCSAESAISDAMEELEEAHQKCPPWWYKCAHKVLIWNCCAPWVKFKHIILLIVMDPFVDLGITICIVLNTLFMAMEHYPMTEHFDNVLSVGNLVFTGIFTAEMVLKLIAMDPYEYFQQGWNIFDSFIVTLSLVELGLANVQGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKIASDCSLPRWHMHDFFHSFLIVFRILCGEWIETMWDCMEVAGQAMCLTVFLMVMVIGNLVVLNLFLALLLSSFSADSLAASDEDGEMNNLQIAIGRIKWGIAFAKTFLLGLLHGKILSLKDIMLSLGEPGGAGENGESPPEDEKKEPPPEDGNKELKDNHILNHVGLTDGPRSSIEMDHLNFINNPYLTIHVPIASEESDLEMPTEEETDTFSEPEDIKKPLQPLYDGNSSVCSTADYKPPEEDPEEQAEENPEGELPEECFTEACVKRCPCLYVDISQGRGKMWWTLRRACFKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRRVIRTILEYADKVFTYIFILEMLLKWVAYGFKVYFTNAWCWLDFLIVDVSIISLVANWLGYSELGPIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYYCINTTTSERFDISVVNNKSECESLMYTGQVRWMNVKVNYDNVGLGYLSLLQVATFKGWMDIMYAAVDSREKEEQPDYEVNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGKDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPQNKIQGMVYDFVTKQVFDISIMILICLNMVTMMVETDDQSQLKVDILYNINMVFIIVFTGECVLKMFALRHYYFTIGWNIFDFVVVILSIVGLALSDLIQKYFVSPTLFRVIRLARIGRVLRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMSNFAYVKKESGIDDMFNFETFGNSIICLFEITTSAGWDGLLNPILNSGPPDCDPTLENPGTNIKGDCGNPSIGICFFCSYIIISFLIVVNMYIAIILENFNVATEESSEPLCEDDFEMFYETWEKFDPDATQFIDYSRLSDFVDTLQEPLKIAKPNKIKLITLDLPMVPGDKIHCLDILFALTKEVLGDSGEMDALKQTMEEKFMAANPSKVSYEPITTTLKRKQEEVCAIKIQRAYRRHLLQRSVKQASYMYRHSQEGNGDGAPEKEGLLANTMNKMYGSEKEDNGVQSQGEKEKDSTEDAGPTTEVTAPSSSDTALTPPPPSPPPPSSPPQGQTVRPGVKESLV
Pore-forming subunit of a voltage-gated sodium channel complex through which Na(+) ions pass in accordance with their electrochemical gradient. Alternates between resting, activated and inactivated states . Required for normal muscle fiber excitability, normal muscle contraction and relaxation cycles, and constant muscle strength in the presence of fluctuating K(+) levels .
Q9ER60
Q06911
CARS_MYXXA
Antirepressor protein CarS
Myxococcus
MIQDPSLIICHDVDGAPVRIGAKVKVVPHSEDGTISQRFLGQTGIVVGLVFDDPATQYPDDPLIQVLVEGLGEDLFFPEELELAPEWARNRIAQHRQAVRTGGRSSLERLP
Involved in carotenoid biosynthesis. Antagonizes the transcriptional repressor proteins CarA and CarH by preventing their binding to DNA. Can also dissociate preformed CarA-DNA complexes. Does not bind DNA.
Q06911
P54969
ILL1_ARATH
IAA-amino acid hydrolase ILR1-like 1
Arabidopsis
MALNNFLTFQLLLLLLRVSSESPWIVAGDVSRIPINFLELAKSPEVFDSMVRIRRKIHENPELGYEEFETSKFIRSELDLIGVKYRFPVAITGIIGYIGTGEPPFVALRADMDALPIQEAVEWEHKSKNPGKMHACGHDGHVAMLLGAAKILQQHRQHLQGTVVLIFQPAEEGLSGAKMMREEGALKNVEAIFGIHLSPRTPFGKAASLAGSFMAGAGAFEAVITGKGGHAAIPQHTIDPVVAASSIVLSLQHLVSRETDPSDSKVVTVTKVNGGNAFNVIPDSITIGGTLRAFTGFTQLQERIKEIITKQAAVHRCNASVNLAPNGNQPMPPTVNNMDLYKKFKKVVRDLLGQEAFVEAVPEMGSEDFSYFAETIPGHFSLLGMQDETQGYASSHSPHYRINEDVLPYGAAIHATMAVQYLKDKASKGSVSGFHDEL
Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA), including IAA-Ala, IAA-Asn and IAA-Tyr.
P54969
B9JFS7
RECA_AGRRK
Recombinase A
Agrobacterium tumefaciens complex
MSQNSLRLVEDKSVDKSKALEAALSQIERSFGKGSIMKLGSNENVVEIETVSTGSLSLDIALGIGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEHALDPVYARKLGVDLQNLLISQPDTGEQALEITDTLVRSGAIDVLVVDSVAALTPRAEIEGEMGDSLPGLQARLMSQALRKLTASISKSNTMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGAVKEREEVVGNQTRVKVVKNKMAPPFKQVEFDIMYGEGVSKTGELVDLGVKAGIVEKSGAWFSYNSQRLGQGRENAKLFLRDNPDLAREIELSLRQNAGLIADRFLQNGGPDADDGEAAAE
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.
B9JFS7
B4E8S4
LEXA_BURCJ
LexA repressor
Burkholderia cepacia complex
MTKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGVDDAPHQFTLPHAALMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFTSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLMRRPGGLELIAENPDYENIFVKAGSADFALEGIAVGLIRSGEL
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
B4E8S4
Q6GQB9
EDEM3_XENLA
Alpha-1,2-mannosidase EDEM3
Xenopus
MGCPAVEARRWGDMWLVVAFCLLGHGHAAVTKEEKAHLRSQVLEMFDHAYGNYMQHAYPADELMPLTCRGRIRGQEPSRGDVDDALGKFSLTLIDTLDTLVVLNKTKEFEDAVRKVITDVNLDNDIVVSVFETNIRVLGGLLGGHSVAIMLKENGDGMQWYNDELLHMAKELGYKLLPAFNTTSGLPYPRINLKFGIRRPEARTGTETDTCTACAGTMILEFAALSRFTGISVFEEHARKALDFLWDKRQRSSNLVGVTINIHTGDWVRKDSGVGAGIDSYYEYLLKAYVLLGDDSYLERFNTHYDAIMRYISQPPLLLDVHIHKPMLTARTWMDSLLAFFPGLQVLKGDIRPAIETHEMLYQVIKKHNFLPEAFTTDFRVHWAQHPLRPEFAESTYFLYKATGDPYYLEVGKTLIDNLNKYARVPCGFAAVKDVRTGSHEDRMDSFFLAEMFKYLYLLFSEREDLIFDIEDYIFTTEAHLLPLSLSTANPSSTKKNTTTQYTELDDSNFDWSCPNTQILFRNDPMYAQNIREPLKNVVDKNCPRSPSRLDEISGSGKMPPLRARDFMASNSEHLEILKKMGVSLIHLKDGRVQLVQHANQAASSIDAEDGLRFMQEMIELSSQQQKEQQLPPRAVQIVSHPFYGRVVLTAGPAQFGMDLSKHLAGAQGLVARAEPYSGCSDITNGQAIQGKIALMQRGQCMFAEKARNVQKAGAIGGIVIDDNEGSSSDTAPLFQMAGDGKSTDDVTIPMLFLFSKEGNIILDAIREYQQVEVLLSDKAKDRDLESESGEQKPVENDSQKQALEDLFMTPEEIAELLIVHEEESPVSQPEVPSSDSPSGGDRTSERDITPESQEHKTEETEHSPKDNVQTPPENSEDSTEEKMDNKVQPMESILADWKEDIEAFEMMEKDEL
May be involved in endoplasmic reticulum-associated degradation (ERAD).
Q6GQB9
Q97F58
DDL_CLOAB
D-alanylalanine synthetase
Clostridium
MKKKVAILFGGQSTEHEVSRVSAASVLRNIDTSKYDLFPIGITKKGEWFEYTGSADKIENGEWEKDEFYKSPNGQAILFNKEVDVVFPVMHGLYGEDGTIQGLCKLVGVPCVGPSVLSSSVCMDKVYTKYVLEHFNIKQADYVVVHAHEYKTSKEEIIKEIENKLGYAVFIKPSNSGSSVGITKAHNRKELEAGLEEAMKYDRKILVEEALNAREIEVAVLGNEEPKAAIPGEIVPAKEFYDYEAKYENAASKLLIPANLSNENLEKIKNIAIEVYKALDCSGMSRVDFLVDKDTTEMYLNEVNTIPGFTSISMYPKLWAAAGKDYSKLIDELIELAASRNNA
Cell wall formation.
Q97F58
A6T8Y8
SOTB_KLEP7
Probable sugar efflux transporter
Klebsiella
MTTNTVSRKVAWLRVVTLAIAAFIFNTTEFAPVGLLSDIADSFGMETAQVGMMLTIYAWVVALMSLPFMLLTSKVERRRLLIGLFILFIASHVLSFFAWNFDVLVISRIGIAFAHAVFWSITSALAIRMAPPGKRAQALSLIATGTALAMVFGIPIGRIIGQYFGWRMTFLAIGLGALATLACLVKLLPTLPSEHSGSLKSLPVLFRRPALVSVYILTVVVVTAHYTAYSYIEPFVQTVAGLSGNFATVLLLILGGAGIIGSILFGKLGNQHASGLISLAIALLLACLLLLLPASHNPQHLMLLSIFWGVAIMIIGLGMQVKVLASAPDATDVAMSLFSGIFNIGIGAGALVGSQVSLHLSMASVGYVGAIPALVALVWSLMIFRRWPVSLEDHQPHHS
Involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites.
A6T8Y8
Q57979
SURE_METJA
Nucleoside 5'-monophosphate phosphohydrolase
Methanocaldococcus
MEILIVNDDGIYSPSLIALYNALKEKFSDANITIVAPTNQQSGIGRAISLFEPLRMTKVKLAKDIVGYAVSGTPTDCVILGIYQILKKVPDLVISGINIGENLGTEIMTSGTLGAAFEAAHHGAKSIASSLQITSDHLKFKELDIPINFEIPAKITAKIAEKYLDYDMPCDVLNINIPENATLETPIEITRLARKMYTTHVEERIDPRGRSYYWIDGYPIFEEEEDTDVYVLRKKRHISITPLTLDTTIKNLDEFKEKYGKILCEM
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Q57979
A7FN99
UBIA_YERP3
4-HB polyprenyltransferase
Yersinia
MKGSTVHTKWQAYCRLMRIDKPIGSLLLLWPTLWALWLAGRGIPEAKILVVFVLGVFFMRAAGCVVNDYADRHIDGFVKRTASRPLPSGTISEKESKILFVVLILLSFGLVLTLNSMTIWLSLAALALAWIYPFMKRVTHLPQVVLGAAFGWSIPMGFAAVSESLPLVCWLLLLANICWTVAYDTQYAMVDRDDDLRIGVKSTAILFGQHDKLIIGLLQLATLLLMVAIGWLMNLGGAFYWSILLAGALFTHQQKMIAQREREPCFRAFLNNNYVGLILFLGILISYW
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
A7FN99
Q6P5S2
LEG1H_HUMAN
Protein LEG1 homolog
Homo
MAFLPSWVCVLVGSFSASLAGTSNLSETEPPLWKESPGQLSDYRVENSMYIINPWVYLERMGMYKIILNQTARYFAKFAPDNEQNILWGLPLQYGWQYRTGRLADPTRRTNCGYESGDHMCISVDSWWADLNYFLSSLPFLAAVDSGVMGISSDQVRLLPPPKNERKFCYDVSSCRSSFPETMNKWNTFYQYLQSPFSKFDDLLKYLWAAHTSTLADNIKSFEDRYDYYSKAEAHFERSWVLAVDHLAAVLFPTTLIRSYKFQKGMPPRILLNTDVAPFISDFTAFQNVVLVLLNMLDNVDKSIGYLCTEKSNVYRDHSESSSRSYGNNS
May be involved in early liver development.
Q6P5S2
Q00461
T701_MICDP
Probable transposase for insertion sequence element IS701
Microchaete
MVQPRPAAPTVKFVDEYCQWYKSLFPDVRSFEAFKYLHVGCISDLKRKTLPEIAKIVGLDNQQGLHHFLTTSPWDIEKLRTLRLELILQVLKGRPIILIIDETGDKKKGSKTDYVKRQYIGNLGKTDNGIVAVTVYGVFCGMTFPLLFEVYKPRERLQAGDKYRTKPEIAAILIKKLQSMGFKFNLVLADSLYGESGKNFISVLDELNLNYIVAIRSNHYVEILPRQHIQYLKWQKFQRVFSDLSRENRFIREIIPGKRGELRYWQITTDPENLPDNTTWYVMSKYPDITPREVGNFYGLRTWVEYGLKQSKNELGWSDFRLTHYPDIEAMVGNYLQCLFNGVCIRSNCFSLHHNESQNLFHILGGIMEMAGRTFLTIFV
Involved in the transposition of the insertion sequence.
Q00461
A0L1P1
MURC_SHESA
UDP-N-acetylmuramoyl-L-alanine synthetase
Shewanella
MTKTERYLQLRSMIPEMRRIKRIHFVGIGGAGMGGIAEVLVNEGYVVSGSDIAQNAVTDRLCLLGAKIHIGHGADNVQQADVVVVSTAINPENPEIIAAKELRIPIVRRAEMLAELMRYRHGVAIAGTHGKTTTTSLIASLYGQAGRDPTFVIGGLLNSAGTNARLGTSRYLIAEADESDASFLHLQPMVSVVTNIEADHMDTYGGDFEKLKSTFVDFLHNLPFYGVAVVCIDDAVVREIMPRIGRHMITYGFSDDADVQALNFHQQGHQCRFTVRRKGKEDLDLLLNLPGQHNVLNALAAIAVATEDEIDDSAIIQALAEFQGIGRRFQHLGKFATPKGEVMLVDDYGHHPSEVAATIKAARAGWPDKRLVMAYQPHRYTRTRDLYEDFIEVLSQVDCLLLLEVYSAGEAPIPGADGRALCRSIRLRGQLDPIFIASPDQLAEVLPDVLQEGDLLLTQGAGNIGALSRQLAASELGFSIAATTEVKP
Cell wall formation.
A0L1P1
A6U5Z0
IF1_SINMW
Translation initiation factor IF-1
Sinorhizobium
MAKEEVLEFPGVVTELLPNATFRVKLENEHEIIAHTAGRMRKNRIRVLAGDKVLVEMTPYDLTKGRITYRFK
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
A6U5Z0
Q04EL5
RPOZ_OENOB
Transcriptase subunit omega
Oenococcus
MSLMYPSVDELLNKVDSRYKLIALASKRAKELEELPRLKDELLKLKREEKPTDRDKKQIQEIAAQLETLVGPTLDNYKSVKPIGRALEEINAGNVQIDPVNKDKSED
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.
Q04EL5
A0A4D6QCQ2
MYB3_CROXC
Myb-related protein 3
Crocosmia
MVKRSQRVGKKAVEVNRGTWTAEEDEKLMNYVSAHGDKKWRMLPAKAGLKRCGKSCRLRWLNYLRPGIKRGNISEDEEDLIIRLHNLLGNRWSIIAGRIPGRTDNEIKNHWNTHLSKRSLTIDDLNNKQNPGLDNRDMLSPTKITQRSTPTHTNKNTNDELIDSWTDLPAPDFDLEQFLSLLPMSDLCPGSNGNDLELNDFGIPINDINQDSFRSDDYNVNYQEFLDSQVWSRAFEFDDIDQFLDCQAYGSLCSPIAGQ
Transcription activator involved in the spatiotemporal regulation of flavonoid biosynthesis specifically in the corms of Montbretia . Activates the promoters of enzymes involved in the biosynthesis of the flavonol myricetin and the flavonol-glycoside montbretin A (MbA) . MbA is a potent inhibitor of human pancreatic alpha-amylase and is being developed as drug candidate to treat type-2 diabetes .
A0A4D6QCQ2
O88969
CST8_RAT
Cystatin-related epididymal spermatogenic protein
Rattus
MTKPLLLSLIFFIIPAALAVDVDQSKNEVKAQRYFGSISISNANVKQCVWFAMKEYNKGSEDKYLFLLDKTLHATLQITDRMEYHIDVQISRSNCRKPLNNTENCIPQKNPKLEKKLSCSFLVGALPWNGEFDLLSKECKDV
Performs a specialized role during sperm development and maturation.
O88969
O60125
BAG1A_SCHPO
BAG family molecular chaperone regulator 1A
Schizosaccharomyces
MSEKTSTVTIHYGNQRFPVAVNLNETLSELIDDLLETTEISEKKVKLFYAGKRLKDKKASLSKLGLKNHSKILCIRPHKQQRGSKEKDTVEPAPKAEAENPVFSRISGEIKAIDQYVDKELSPMYDNYVNKPSNDPKQKNKQKLMISELLLQQLLKLDGVDVLGSEKLRFERKQLVSKIQKMLDHVDQTSQEVAA
Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release.
O60125
B0RYS0
RSMG_XANCB
16S rRNA 7-methylguanosine methyltransferase
Xanthomonas
MNDAALPPDVSAALANGLQAQSLDADFAAPLLRYLTLLVRWNKTYNLTAVRDPREMVTRHLLDSLAMQPYIVSGTLADLGTGPGLPGIPLAITRPQLQVTLVESNGKKARFMREALRHLALGNARVAEARAEAVDEPAAYDHLTARALDTLAGIIAVGGHLLRPGGSLLAMKGVYPREEIAALPAGWRVGDVHPLQVPGLEGERHLVVVHKD
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
B0RYS0
Q73I60
CLPX_WOLPM
ATP-dependent Clp protease ATP-binding subunit ClpX
unclassified Wolbachia
MDNNNDLHYCSFCNKAQDEVDKLITNSSDGLKVFICNECIELSHKAISQKKDRSFNSDRISDMKLLLKKPEDIKNFLSKHVVGQKHAQHVLSVAMYNHCQSMVQFHAISDIEIEKSNIMLIGPTGSGKTLLAKTLAKVSDVPFAMADATTLTEAGYVGDDVESVLSRLLQAANYDVVKAQRGIVFIDEIDKITRKSEGTSITRDVSGEGVQQALLKIMEGTVAYVPPQGGRKHPQQEFIQVDTSNILFICGGAFEGLDKIIEARKKGTSVGFGADISQSKEQKKKNALHDVQPEDLIKFGLIPEFVGRVPITAVLDELDHEDLIHVLTEPRNALIKQYKALLAFSKVNLEFSDEAISAIAKKAISYKTGARMLRAILESLLLDIMYTSGNGGFEGSTIVITKKMVELGKATVNHNNNGNVITVND
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
Q73I60
Q87EL4
AOTC_XYLFT
N-acetyl-L-ornithine transcarbamylase
Xylella
MALKHFLNTQDWTCSELNALLTQARAFKHNKLGNALKGKSIALVFFNPSMRTRSSFELGAFQLGGHAIVLQPGKDAWPIEFDTGTVMEAETEEHICEVARVLGHYVDLIGVRAFPKFLDWTYDRQDIVLNSFAKYSPVPVINMETITHPCQELAHIMALQEHFGTTDLRGKKYVLTWTYHPKPLNTAVANSALTIATRLGMDVTLLCPTPDYVLDERYIDWARQNIADTGSTFQVSHDIDNAYRGADVIYAKSWGALPFFGNWAMEKPIRDQYRHFIVDEAKMALTNNAVFSHCLPLRRNVKATDAVMDGSNCIAIHEAGNRLHVQKAIMAALASQ
Catalyzes the transfer of the carbamoyl group from carbamoyl phosphate to the delta-amino group of N(2)-acetyl-L-ornithine to produce N(2)-acetyl-L-citrulline. This is a step in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine.
Q87EL4
Q5LY70
ACPS_STRT1
4'-phosphopantetheinyl transferase AcpS
Streptococcus
MIFGHGIDLQEISAVKKAYDRNPRFAKKVLTPKEWERFESLSGERQMSFLAGRWAGKEAFSKAWGTGIGAVGFKDIEILNNDKGAPVVTQSPFEGNVFISISHSGDFVQASVILEKTKR
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Q5LY70
B8CJP6
ENO_SHEPW
2-phosphoglycerate dehydratase
Shewanella
MAKIINIIGREIMDSRGNPTVEAEVHLEGGFMGMAAAPSGASTGSREALELRDGDKARYLGKGVLKAVEAVNGTIADALIGKDATAQAELDQIMIDLDGTENKAKFGANAILAVSLAAAKAAAAFKGVPLYAHIADLNGTPGVYSMPLPMMNIINGGEHADNSVDIQEFMIQPVGAANFREGLRMGAEVFHSLAKVLKADGHSTAVGDEGGFAPNLPSNASALAAIKVAVANAGYELGKDITLAMDCAASEFYDKEANIYDLKGEGKKFTSEEFNFFLQDLTKEYPIVSIEDGLDESDWDGFAHQTKLMGDKIQLVGDDLFVTNTKILKRGIDNGIANSILIKFNQIGSLTETLAAIKMAKDAGFTVVISHRSGETEDATIADLAVGTAAGQIKTGSLSRSDRVAKYNQLLRIEEQLGEKAPYKGLKEVKGQA
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
B8CJP6