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Full Name
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147
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taxon
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sequence
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2.75k
function
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5.51k
AlphaFoldDB
stringlengths
6
10
P25278
YC2M_HERAU
ORFC
Herpetosiphon
MMIESVAISVKESMPPQVSVEINGMLNDGCTAFHEAKQSIDGNTIKIEVTTIRPKDAMCNQQISPFSTIIQIEGELKPGEYTILVNDVAEALKL
Could be a silencing control element for the regulation of the restriction system.
P25278
A5ERG8
TILS_BRASB
tRNA(Ile)-lysidine synthetase
unclassified Bradyrhizobium
MSTGQSEDHLPISAAEAERLFAPFADSGVLTLAVSGGPDSMALMWLAARWRATRAGGPRLLAVTVDHGLRPESRREALMVKQLARQLGLTHRTLRWSGEKPAAGIPEAARIARYRLLARAAEQAGASHVVTAHTRDDQAETVLMRLLRGSGIAGLAAMAPVSRRDGLLLARPLLSLSKARLLATLRSAGIAFADDPTNRDPAFTRPRLRALMPTLAAEGADPRTLATLANRARRANAAIELMADGAERYLALLAAGRSSKRRGGEGEMFDPRAFAALPAEIRLRLLMRAIDRVGTEGPVELGKAEALLERLDRTLAGITDGGTAERGTLKQTLAGALVSLAKDAIRISPAPPRRRRGE
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
A5ERG8
Q92564
DCNL4_HUMAN
Defective in cullin neddylation protein 1-like protein 4
Homo
MHSDAAAVNFQLNSHLSTLANIHKIYHTLNKLNLTEDIGQDDHQTGSLRSCSSSDCFNKVMPPRKKRRPASGDDLSAKKSRHDSMYRKYDSTRIKTEEEAFSSKRCLEWFYEYAGTDDVVGPEGMEKFCEDIGVEPENVVMLVLAWKLDAQNMGYFTLQEWLKGMTSLQCDTTEKLRNTLDYLRSFLNDSTNFKLIYRYAFDFAREKDQRSLDINTAKCMLGLLLGKIWPLFPVFHQFLEQSKYKVINKDQWCNVLEFSRTINLDLSNYDEDGAWPVLLDEFVEWYKDKQMS
Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes which are necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs).
Q92564
O74876
MU135_SCHPO
Meiotically up-regulated gene 135 protein
Schizosaccharomyces
MSEEDNRLNELFANDLGVQPPCERSLKEGRRFLNDFEIAAKKKLLELERKALEDKEKNLNFVVESERTLFNSKKRAFDNDECYNDRCKLFRGIVNEWGRSERTLDSLDEPPAWFRREMGEWKKAREEDKAEWKKAREEDKAEWKKAREEDKAEWKKAREEDKAEWKKAREEDKAEWKKAREEDKEWRNSMDEWRKSMDEWRKSMDEWRKSMDEWRKSTDEWRKSTDERLENLLNIVREILDVQRDMRNDLSNLTRKVDRMDMRLSRNNNMIMRSFAQPITEVPFFNGDIPDPNLPRITRIEDIDSLSEENCTRYLKGYGVSYDENDQSLWKRQLAKAVGLTAAYDESYTFSPFSSSE
Has a role in meiosis.
O74876
Q8DD27
EFTU1_VIBVU
Elongation factor Tu 1
Vibrio
MSKEKFERVKPHVNVGTIGHVDHGKTTLTAAICTTLAKVYGGAARDFASIDNAPEERERGITISTSHVEYDTPARHYAHVDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLGRQVGIPYIIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALGALNGEEQWEAKIIELAEALDTYIPEPERAIDLPFLMPIEDVFSIQGRGTVVTGRIERGILKVGDEVAIVGIKDTTTTTCTGVEMFRKLLDEGRAGENVGALLRGTKRDEVERGQVLAKPGSITPHTKFESEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDVTGDISLPEGVEMVMPGDNIQMVVELISPIAMDEGLRFAIREGGRTVGAGVVAKIFE
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Q8DD27
Q91V12
BACH_MOUSE
Long chain acyl-CoA thioester hydrolase
Mus
MKLLVGTLRLWEVGRQVAFSSLTPGQECSGLRKTFWAAMRAVRTRADHQKLGHCVTMGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVHVMSENILTGTKKLTNKATLWYVPLSLKNVDKVLEVPPIVYLRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDNSQKRYRAASAFFTYVSLNQEGKPMPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHTEPQP
Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (Probable). Preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain-lengths of C8-C18 (Probable). May play an important physiological function in brain (Probable).
Q91V12
P24709
INVO_CEBAL
Involucrin
Cebus
MSQQHTLPVTLPPALSQELLNTVPPPINTQQEQREQPVPLPPPCQKVPVELPVEGPSKHEEKHVTIVKGVPEHECEQQQQAQGQERQQQHWGQNKEHQKAGNPEQQLKQEEAQREKQQLQGQLEEEKKLLDQQLDQELAKRDDQLGTKKKQLLEFPEQQEGQLKHLEQQEKPLELPEQQSGQPKYLEQQEGQLKHLEEQKGQLKHLEQQEGQLELPEQVDQPKHLEQLEKQLEHPEQQEGKLKKLEEEEEQLKHLEQQEEQLKHLEQQEGQLEHLEQQEGELKHLEQCEGQLEHLEQQEGQLELPEQQVGQSKHLEQEEKQLEHPEQQEGQLKHLGKQEAQLELPEQVGQPKHLEQQEKQLEHPEQQEEQQEGQLKDLEQQERQLEQPVFAPAPGQAQDIQQALPSKGEVLLPVDQQQQKQEVQWQQK
Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia.
P24709
A1AR93
GLMM_PELPD
Phosphoglucosamine mutase
Pelobacter
MKKLFGTDGVRGVANVYPMTTEMAMQLGRAAAYIFKSSSKRRHRIVIGKDTRLSGYMLENAMVAGICSMGVDVLLVGPLPTPGIANITSSMRADAGVVISASHNPFQDNGIKFFSADGFKLPDQIELKIEKLIESNKIDSLRPTASEVGKAFRIDDAAGRYIVFLKNTFPTEMDLSGMKIVLDCANGAAYRVAPAVFEELGAEVICLGVSPNGTNINADCGSLYPQVISEAVKKHRADIGIALDGDADRVIVCDEFGHEVDGDHIMAICATDMLRRKLLKKKTLVTTVMSNMGLDIAMRAAGGKIVKTAVGDRYVVEEMRKGGYNLGGEQSGHMIFLDSNTTGDGILSALQLLAVMRRTEKPLSELSEVMIALPQVLVNTRVREKKDITTIPEIAARIRDVEEKLGNEGRVLIRYSGTEPLLRVMLEGKDTYEITAWANEIIDLVRKHLGEKQ
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
A1AR93
Q04KB0
EX7L_STRP2
Exodeoxyribonuclease VII large subunit
Streptococcus
MEKYLSVTTLTKYLKMKFDKDPYLERVYLTGQVSNFRKRPTHQYFSLKDDHAVIQATIWSGIYQKLGFDLEEGMKINVIGRVQVYEPSGSYSIIIEKVEPDGVGALAIQFEQLKKKLTEEGLFQERFKQALPQFSKRIGVVTSRSGAVIRDIITTVSRRFPGVDILLYPTKVQGEGAAEEIARNIARANQRDDLDLLIIGRGGGSIEDLWAFNEEIVVRAIFESRLPVISSVGHETDVTLADFVADRRAATPTAAAELATPVTKLDVLAHLQNQEKRMVTAVRNVLSKKQEALKKCSQSVIFRQPERLYDGYLQRLDQLQLRLKQSLRTRISDNKQLVQARTHQLVQLSPVTKIQRYQDRLGQLDKLLGSQMALVYDAKVAEAKRLSEALLMLDTSRIVARGYAIVKKEESVVDSVESLKKKDQVTLLMRDGQVELEVKDVKTKEI
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Q04KB0
Q9W6S8
SMN1_DANRE
Survival motor neuron protein 1
Danio
MANGAEDVVFCRGTGQSDDSDIWDDTALIKAYDKAVASFKNALKGEDGATPQENDNPGKKRKNNKKNKSRKRCNAAPDKEWQVGDSCYAFWSEDGNLYTATITSVDQEKGTCVVFYTDYGNEEEQNLSDLLTEPPDMDEDALKTANVKETESSTEESDRSFTPQKSGHAKHKSKSNFPMGPPSWFPSFPPGPPPPPPHFKKMDGRRGEGPGPSFPGWPPMIPLGPPMIPPPPPMSPDFGEDDEALGSMLISWYMSGYHTGYYMGLRQGRKEAAASKKSHRK
The SMN complex plays an essential role in spliceosomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing in the nucleus . It may also play a role in the metabolism of snoRNPs . Required in motor neurons and proprioceptive neurons to ensure correct U12 intron splicing and proper levels of tmem41b mRNA . Required for the maturation of motor neuron axonal branches and dendrites .
Q9W6S8
A7X2A2
MURG_STAA1
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
Staphylococcus
MTKIAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQLPEIKYYPISSGKLRRYISLENAKDVFKVLKGILDARKVLKKEKPDLLFSKGGFVSVPVVIAAKSLNIPTIIHESDLTPGLANKIALKFAKKIYTTFEETLNYLPKEKADFIGATIREDLKNGNAHNGYQLTGFNENKKVLLVMGGSLGSKKLNSIIRENLDALLQQYQVIHLTGKGLKDAQVKKSGYIQYEFVKEDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLVPLGLDQSRGDQIDNANHFADKGYAKTIDEEQLTAQILLQELNEMEQERTRIINNMKSYEQSYTKEALFDKMIKDALN
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
A7X2A2
A4T5Y1
GLPK_MYCGI
Glycerokinase
Mycolicibacterium
MADFVAAIDQGTTSTRCMIFDHDGAEVGRHQLEHEQILPKAGWVEHNPVEIWERTGSVLATALNATKLATTDLAALGITNQRETSLVWNRHTGRPYYNAIVWQDTRTDRIASALDRDGRGDVIRRKAGLPPATYFSGGKLQWLLENVDGLRADAANGDALFGTTDTWVLWNLTGGHRGGVHVTDVTNASRTMLMNLETLDWDDELLGFFDIPRQMLPEIRPSSSPQPYGVTVETGPADGEIPITGILGDQQAAMVGQVCLDVGEAKNTYGTGNFLLLNTGEKIVRSDNGLLTTVCYQFGDSKPVYALEGSIAVTGSAVQWLRDQLGIISGASQSESLARQVDDNGGVYFVPAFSGLFAPYWRSDARGAIVGLSRFNTNAHVARATLEAICYQSRDVVDAMAADSGVPLEVLKVDGGITANDLCMQIQADVLGVDVVKPVVAETTALGAAYAAGLAVGFWEGADDLRANWQEGRRWSPQWSDEQRAEGYAGWQKAVHRTLDWVDVE
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
A4T5Y1
Q978S3
AROA_THEVO
5-enolpyruvylshikimate-3-phosphate synthase
Thermoplasma
MIVKVSNLGGSGIAEMPSSKSFTQRYVLASAFLNKSVVLNGITITNDDDVAMRIAESVGSTITINNRSIKISSNFKCPEEIYVGESGTSYRLSIGLLAASGCVTRIKGEDSLAKRPIEPLLMALGENGVKFERNEAGFYNVDGRNSQKKHVEIEGSSSQFVSSLMLYYAKKGGGEFTARNIKSIGYVYITKRVLYDLGYFANIERTITINPTGVWKTAIDVEPDYSSMAFFMVLGLLSDSVDVRFRIKRISRIQPDSVILDLFKNNILINGEEIRVISGINEPVSVDADMNPDLCPPLSVIGIFSKYGVQIRNYERLKTKESNRYEGIIDLAERFGANVEDNGQDLFIKPGSVRFPDVISYKDHRMIMAASIASLIGGFPTVIENAEKTAKSFPGFFAELSKFANVEELA
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.
Q978S3
Q9RA35
PLSX_MORMI
Phosphate-acyl-ACP acyltransferase
Moritella
MPNLTIALDAMGGDFGPHVTIPAAINILKKYKYLSIYLVGNEAEINSLLQNTSTSIKSRFTIIPSLDDIPMDLAPALALRNFKQSSMRMALNLVREGKAQACVSAGNTGALMVLSRHLLKVLPFVDRPALVSTLPSMTTQPVYMLDLGVNVSCDADALLQFALMGSALAEHVGNIPIPRVALLNVGQEDIKGNDLVKHAAQLLSKNPNLNYIGFIEGNDIFSGKADVIVCDGFTGNVALKTSEGVVDLVISQLTSVSNNNIFTKLLSLLVKPLIMSSLKRLKPDQYNGATLLGLPGIVIKSHGNAKQVAFEFAIEQAVKEVESGLVNKISASLDIID
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Q9RA35
B0T824
DDL_CAUSK
D-alanylalanine synthetase
unclassified Caulobacter
MTPANPKPLANHHIAVLLGGPSAEREVSLVTGAAYAAALERLGARVSRVDPGKDVAQVLTALAPDLVFNGLHGRWGEDGCVQGVLETLGLAYTHSGVLASALAMDKAKSKAVLAAAGIPVPGGGLFDRHDVAQGHVMPPPYVVKPNAEGSSVGVSLVFEGANGPPRQLAAPDWAFGEQVMVEPYIPGLELAVAVVGESNGPRALAVTEIRSSTGFYDYDAKYSQGGSIHVLPAPIPDAVRDRALHLAKLGHTALGCQGVTRSDFRYDDINDLLVLLEVNTQPGMTPTSLVPEQADHAGVSFDRLVFWIVEDAYARRFAGGIA
Cell wall formation.
B0T824
P38904
SPP41_YEAST
Protein SPP41
Saccharomyces
MAYDEDDGEINFNELVGNLLSSHNQEGQEEGEVQGGEQEGDDFEKIYPTSENIEPKHPDDSQHMHNSPDQNIEIPHFVDEEDELVSVVANAVQNIDDEQAKPENHLENGSEHVTSDTADDNHEKEQQQEWAHILQQEILKSDGEPLRENTERRVSTSQHHPSQRTDDALDQDDENLRMAILESLQELNTNEEEEKEPEKHEHAAPNDKLSSKKSSKKKKKDKSKNRESSKDKSSKKSKSSSHSKKHAKDRNKEKQSKPTNNENTLDLSNILENLIHENDNAAIDTAKQTVDIQDNSHTDNTNNEDVEAQALVEATLKAFENELLSSAPTEEPSQEQSIGPVSSRKAVEPPRKPTADDIPLAMLQAFKPKKRPPQEKKKTKSKTSKAASTANKSPASESTSKKKKKKKTVKESNKSQEAYEDDEFSRILADMVNQVVNTSLKETSTHTATQDNKLESESDFTSPVQSQYTTEDASTANDDSLDLNQIMQNAMAMVFQNQNDDEFDENIVEDFNRGLGDLSVSDLLPHDNLSRMEKKSVPKSSSKSEKKTAISRRASKKASRDASSVELTEVPSKPKKPSKTEVSLEKKLRKKYVSIANEAASVARKKRWAKNKELKEKEKLERQTAREERRHKKKLEKQRLAEEQEELKKIVERGPPYPPDLRLTKSGKPKKPYRRWTPEELLKRSQEAEKPRKVKKERKKKEKKMKVPSSALKKIPLFNFVKGNVQPSARHRLNDIEGSLSTIGLHKSPDGVRRILSRPKSEDHEWPLSDSSASQNYDAHLKTVVHKEKIPFHPPWTIPSQPPFALPVARRKKIPNIKKYRKRTNNSFRVSKEGTASTRNRILPAILLPIINTLKAAAKSQTAAGATPEEARKRLATIIQHAKSTVIRAALQARKNSMQAAHSKGTTTELATTASRMKNPLKMIPIFNTSRVKQQLDKQLPARSAGTEISSSESPDKATPDPHSNSTIAGHTLKGVTTPIKIEDSDANVPPVSIAVSTIEPSQDKLELTKRAESVEPVENNVETAKETQSVQEIKENVGTKASEEVTLTEDKTNGDPKNEKRILIESPVEKTDKKKPGEKIATDLNEDASLSDKKDGDEKSTLHSDAAQLTGNEPDSVNTTTGKPKLIDVSLKPLNEAKPKIPIIFPLKRPQIKPEVSVINLVQNLVNTKIPEIKNESVDLGSNITDILSSTITNILPEITATDVKNYQYEDENVKYLKKTPRQVLNLDGLVPPSGRCITKAKRVRRIKKLSADATTAPEADGKANSESITYTFDIPSPEEVQSKRSVVLKFAKARLTEAELSCLKKEINNVRKRRWREMNSTKNWEYDVKSRLKKRANAFFGEGESETKSKWIEERFQEKVSQEKYKDRLETTETQANNTKIVIDDKEILNILAVNMNNLNKARCIEKDIQESFREEKLASLQPKKKRKKSILH
Negative regulator of PRP3 and PRP4 genes.
P38904
Q9QZ59
DMRT1_MOUSE
Doublesex- and mab-3-related transcription factor 1
Mus
MPNDDTFGKPSTPTEVPHAPGAPPQGKAGGYSKAAGAMAGAAGGSGAGGSGGASGSGPSGLGSGSKKSPRLPKCARCRNHGYASPLKGHKRFCMWRDCQCKKCSLIAERQRVMAAQVALRRQQAQEEELGISHPIPLPSAAELLVKRENNASNPCLMAENSSSAQPPPASTPTPAASEGRMVIQDIPAVTSRGHMENTSDLVSDPAYYSSFYQPSLFPYYNNLYNYPQYSMALSAESSSGEVGNSLGGSPVKNSLRSLPAPYVPAQTGNQWQMKTSESRHPVSSQYRMHSYYGPPSYLGQSMSQIFTFEEGPSYSEAKASVFSPPSSQDSGLVSLSSSSPMSNESSKGVLECESASSEPSSYAVNQVLEEDEDE
Transcription factor that plays a key role in male sex determination and differentiation by controlling testis development and male germ cell proliferation. Plays a central role in spermatogonia by inhibiting meiosis in undifferentiated spermatogonia and promoting mitosis, leading to spermatogonial development and allowing abundant and continuous production of sperm. Acts both as a transcription repressor and activator: prevents meiosis by restricting retinoic acid (RA)-dependent transcription and repressing STRA8 expression and promotes spermatogonial development by activating spermatogonial differentiation genes, such as SOHLH1. Also plays a key role in postnatal sex maintenance by maintaining testis determination and preventing feminization: represses transcription of female promoting genes such as FOXL2 and activates male-specific genes. May act as a tumor suppressor. May also play a minor role in oogenesis.
Q9QZ59
D2Y2A0
H13A1_CYRHA
Hainantoxin-XIII
Haplopelma
MKTAIFTVVLALAVFAVLSFGWEANEKALSEEFTELIHEKEAASETEARECRYFWGECHDHMPCCDWLVCRYKWPITYNICVWNRTFPEK
Ion channel inhibitor.
D2Y2A0
P40303
PSA4_YEAST
Proteinase YSCE subunit PRE6
Saccharomyces
MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYDRKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEKQEQQEQDKKKKSNH
The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
P40303
A5GRJ7
DDL_SYNR3
D-alanylalanine synthetase
unclassified Synechococcus
MSSQQSKVVGLIFGGASGEHDVSIRSAATVAEGLSSGANKERYRVQHVYIDRQGRWWGDATARQVLSSGQALADDGSRPGFSGFPDGCLEVEIWYPVLHGPNGEDGTIQGLFSLMQRPFVGSGVLGSAVGMDKLAMKAAFSAAGLPQGPYRPVLASELVSNSQLLEELETQLGYPCFIKPANLGSSVGISKATNRSELQAGLDLAASHDSRLLVEKGLQVRELECAVLGGQHLKASVLGEVSFDADWYDYETKYSSGLSSTQIPADLPEAISSRAQHLAIEAVQAVGASGLSRVDFFYEEASGNLLINEINTLPGFTSQSMYPMLWKASGVPLEELVHQLLELAQ
Cell wall formation.
A5GRJ7
Q03VF1
TMCAL_LEUMM
tRNA(Met) cytidine acetate ligase
Leuconostoc
MQAVGIITEYNPFHNGHIYHIQQAKKLTGADVVVAVMSGNFVQRGEPALFDKWQRTQMALENGVDLVIELPTFFAVQPSHIFADGAIQLLSALGVDNIVFGSEHPEVDFLSIAKQAPTIAEGQEFKNHTQTFASAYAKQLEAETSFKLEEPNDILALGYASAILNQQANIGIIPIQRAEANYHDANFTDEQSIASASSIRLALHKGKTEKIKNVVPEATKVALDTAANTIDFESKFWSMLKYRLTTDTVGQLGQIYQMAEGLEHRFAKTALNDSGPQSYQSFIKSTKSKRYTFTRIQRTLLYTLLNIKVDQMQAAMQDPYLRILGFTSTGQQYLNEIKKQVTLPLISKVDSSLAKSNLRLDYKAGKVWQLLANEGAPTQDVTRMPLYWEK
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Q03VF1
Q1RH84
DUS_RICBR
Probable tRNA-dihydrouridine synthase
belli group
MIKIGNIELSSNIILAPMSGVTDLEFRRLVKRFGAGLVVSEMIASRAMIVESRQSLQKCSIMQDDATSACVQLAGCEPNVIAEAAKMNEDMGAKIIDLNFGCPAKKVVNGYSGSALMRDEGLAAKIFEAAVKAVKIPVTVKMRMGWDDQTKNAPTLAKIAERSGIQMVTVHGRTRCQFYSGNADWEFIKNVKEAVKIPVIANGDITNFAKAKEALEKSSADGVMVGRGAYGKPWLISQIDHYLKTGEEKPAPSIESQLDIVLEHYQAIVDYYGESAGVPIARKHMGWYSSGLPNSAEFRGAVNLMNDPIAVKDKIVEFYTSVINRE
Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
Q1RH84
P44337
ASNC_HAEIN
Regulatory protein AsnC
Haemophilus
MHNIDSLDQKILRVLTKDARTPYAEMAKNFGVSPGTIHVRVEKMRQSGIIKGTKVIIDERKLGYDVCCFIGIILKSAKDYEKVIKKLESFDEVVEAYYTTGNYSIFLKVMTHTIAELHSVLATKIQLIDEIQSTETLISMQNPILRDIKP
Activator of asnA transcription.
P44337
Q0SHR9
MURD_RHOJR
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
Rhodococcus
MAEEHGGLDWLRGRSVLVAGAGVSGRATIEPLRDLGALVTVTDANVDALAECARLGAATVPIDDLLAERDRVAEFALVVTSPGFRPDAPLLSLAAGDGVPIWGDIEFSWHVDRAGLYGPPRRWLVVTGTNGKTTTTSMLQSILEAAELPSLACGNIGIPVLDALRQTEPRAEALAVELSSFQLHWAPSVRPTAGAILNIAEDHLDWHGGMQPYIDAKARALTGEVAVLGLDDEVASSLFSSSPAVRTVGFRLGVPAPGELGVEDGYLVDRAFADGERLAPAEGITPPGPAGLMDALAAAALARAIGVPPDAVAAGLAAHVVGPHRAALVAEVGGVTFVDDSKATNPHAARPSILAHERVVWIAGGLLKGARVDDLVREVASRLAGAVLLGRDAMQIAESLARHAPEVPVVTVETGDDAGVSAVPQTATHRVVLPADTDSDAVMGVVVREAAALATAGDSVVLAPAAASLDMFASYGHRGDSFTDAVGRLDASDISRTLR
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Q0SHR9
Q3B1H3
RL11_CHLL3
50S ribosomal protein L11
Pelodictyon
MAKKVIGFIKLQIPAGAANPAPPVGPALGQKGVNIMEFCKQFNAKTQSEAGMIIPVVITVFSDKSFTFITKTPPAAVLLLKEAKLQKGSGEPNRNKVGTVTREQVKKIAELKMPDLNAFDLRGAEEMIMGTARSMGIVVEG
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Q3B1H3
Q5FG91
KTHY_EHRRG
dTMP kinase
Ehrlichia
MFITFEGIDGSGKTTQSRLLTEYLSGVYGVDNVILTREPGGTFFNESVRNLLFSTKNLDKLSELLFFIAMRREHFMKVIKPALTQQKIVICDRFIDSTIAYQGYGHGIDCKLIEELNDLVVDIYPNITFVLDSDINQSVARSNKNGYEFLDLEFYARVRDGFRDIVKRNQYRCYLITNVDATKNINEISAIYLKTIKILHAL
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Q5FG91
C5P334
DAPB_COCP7
Probable dipeptidyl-aminopeptidase B
Coccidioides
MGVEKRINDEEMQPLAERDDKSRDSIDSTSTASISLALLGGANGSAHGSRAARTRKSENQEKYHDDEEEGDLEEGFVPPAGGWSAPRKVSVIFTLIVTLCIAGWLVAFFVLLGRHKDSSKDAAVSQGESNIIPGIYSGGRGGKKLDLDGVLFGNWSPKSHDISWFPGPNGADGLLLEQGGDRNKAYLRVEDIRSRNPGNKADDTIVLMRESSFMVGKRLVRPSKVWPSPDLKTVLVMSDQRKNWRHSYTGNYWIFDVETQTGEPLDPESLDGGIQLASWSPNSDAIVFTRKNNMFIRRLPSKNVKQITTDGGTNLFYGIPDWVYEEEVFSDSSATWWDGDGKFVAFLRTNESRVPEYPVQYFIPNTNKPSRPSEENYPDIRKIKYPKAGAPNPVVNIQFFDVEKEEVFSVDVKDDLPDDDRLVIGVTWASNGNVLVRETNRESDRLSVVLIDAAKRAGKVVRSRNFSSLDGGWVEPSQTTHFVPADPKNGRPHDGYIETIPHDGFEHLAYFTPMDNSEPTVLTSGDWEVVDAPSAVDLKRGLVYFVAAKENPTERHIYTVKLDGSDLQPIVDTKSAGYYSISLSAGAGYALLKYEGPDIPWQKVISTPANEEKYEESIEKNPGLADMARKYALPSLHYQTITISGYELQVVERRPANFNPDKKYPVLFHLYGGPGSQTVTKKFKVDFQSYVASNLGYIVVTVDGRGTGFIGRKARCAVRGNLGHYEAIDQIETAKAWGKRSYVDAGRMAIWGWSYGGFMTLKTLEQDAGQTFQYGMAVAPVTDWRFYDSIYTERYMHTPQNNPEGYDRSAISNVTALDQAVRFMIVHGSGDDNVHIQNTLTLLDKLDLGSVKNFDVHVYPDSDHSIYFHNANKMVYQRLSDWLVNAFNGEWVKTRDPIPHKSLARRALGLINILRNG
Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
C5P334
A6T752
SULA_KLEP7
Cell division inhibitor SulA
Klebsiella
MFTSAHANRSAQASAPAGHYAHRSGEQNTNGLISEIVYREDQPMMTQLLLLPLLQQLGQQSRWQLWLTPQQKLSREWVQSAGLPLSKVMQISQLSPSHTIDSMIRALRTGNYSVVICWLAEELTADEHERLVNAAQVGSAMGFIMRPVRNQGTLGRQLSGLKIHSNLYH
Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division.
A6T752
B2TW57
NUON_SHIB3
NDH-1 subunit N
Shigella
MTITPQNLIALLPLLIVGLTVVVVMLSIAWRRNHFLNATLSVIGLNAALVSLWFVGQAGAMDVTPLMRVDGFAMLYTGLVLLASLATCTFAYPWLEGYNDNKDEFYLLVLIAALGGILLANANHLASLFLGIELISLPLFGLVGYAFRQKRSLEASIKYTILSAAASSFLLFGMALVYAQSGDLSFVALGKNLGDGMLNEPLLLAGFGMMIVGLGFKLSLVPFHLWTPDVYQGAPAPVSTFLATASKIAIFGVVMRLFLYAPVGDSEAIRVVLAIIAFASIIFGNLMALSQTNIKRLLGYSSISHLGYLLVALIALQTGEMSMEAVGGYLAGYLFSSLGAFGVVSLMSSPYRGPDADSLFSYRGLFWHRPILAAVMTVMMLSLAGIPMTLGFIGKFYVLAVGVQAHLWWLVGAVVVGSAIGLYYYLRVAVSLYLHAPEQPGRDAPSNWQYSAGGIVVLISALLVLVLGVWPQPLISIVRLAMPLM
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
B2TW57
Q9KKY0
PPNP_VIBCH
Xanthosine phosphorylase
Vibrio
MIKENVYFDGNVKSLGFSQQDGESTVGVMAPGQYTFGTGAPERMTVVKGALTIKRVTDADWVTFTAGEAFEVAGNSSFDLQVEVATAYLCEFLPA
Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
Q9KKY0
Q2INI7
ISCS_ANADE
Cysteine desulfurase IscS
Anaeromyxobacter
MKIPIYMDYHATTPVDPRVLEAMLPYFTTEYGNAASKSHAFGWKAEEAVEAAREEVAKLIGASAKEIVWTSGATESDNLAVKGAAHFYQAKGKHLVTCKTEHKAVLDSMHALERQGFEVTFLEPERDGRLDPAKVKAALRPDTILVSVMHANNETGVVHPIAEIGRIAREAGVVFHCDAVQSIGKIPFDVEAMNVDLASISAHKMYGPKGVGALYVRRKPRVRLVAEMDGGGHERGFRSGTLNVPGIVGMGKAAELARLERDAEAVRVTALRERLRKGLEQELDLLTVNGSLEHRVPGNLNVSFAYVEGEALMMAVKDVAVSSGSACTSASLEPSYVLRAMGVSEDLAHSSIRFGLGRFSTEEEVDYAIRLFGEKVRKLREMSPLYEMVKDGVDLNQIEWANPH
Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
Q2INI7
C3NHA6
RL2_SULIN
50S ribosomal protein L2
Sulfolobus
MGKNLLQQRAGKGSPTFRSPSWLRIGKVRYPNIFGHLVGKVIDIVHNPGMNTPVAIIKLENGTKFLTQAIQGLVINQKIEFGKGSPIANGNVIEIGDAPEGTIVCNVEENFGDGGKYARSAGSYAVVVGKSGDKVLIKLPSDKIKAVSNKARATVGVVAGGGVVEKPLLKAGANYWKYKVKAKKWPIVRGVAMNVVDHPHGGGLHQSVSRPSTVSRNAPPGRKVGHIAARRTGRKEGK
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.
C3NHA6
C5DAR2
TYSY_GEOSW
Thymidylate synthase
unclassified Geobacillus
MRQYLQLLEDILENGVEKDDRTGVGTLSVFGRQLRFNLQEGFPLLTTKKLHIRSIIYELLWFLKGDTNVRYLQENGVTIWDEWADENGDLGPIYGAQWRSWKGADGKTVDQISWVIEEIKRNPNSRRLLVSAWNVAELDKMKLPPCHYAFQFYVADGKLSCMWQQRSVDTFLGLPFNIASYALLTHMIAQQCDLDVGELIFSGGDVHLYKNHLEQAKLQLTREPRPLPKLVIKRKPASIFEYEFEDFEIVDYDPHPHIKAPVAV
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
C5DAR2
A8RG82
DPES_ENTBW
D-psicose 3-epimerase
Enterocloster
MRYFKEEVAGMKYGIYFAYWTKEWFADYKKYMDKVSALGFDVLEISCAALRDVYTTKEQLIELREYAKEKGLVLTAGYGPTKAENLCSEDPEAVRRAMTFFKDLLPKLQLMDIHILGGGLYSYWPVDFTINNDKQGDRARAVRNLRELSKTAEECDVVLGMEVLNRYEGYILNTCEEAIDFVDEIGSSHVKIMLDTFHMNIEETNMADAIRKAGDRLGHLHLGEQNRLVPGKGSLPWAEIGQALRDINYQGAAVMEPFVMQGGTIGSEIKVWRDMVPDLSEEALDRDAKGALEFCRHVFGI
Involved in the biosynthesis of D-psicose. Catalyzes the reversible epimerization of D-fructose at the C3 position to yield D-psicose. The enzyme is highly specific for D-psicose and shows very low activity with D-tagatose.
A8RG82
Q47146
FADE_ECOLI
Acyl-coenzyme A dehydrogenase
Escherichia
MMILSILATVVLLGALFYHRVSLFISSLILLAWTAALGVAGLWSAWVLVPLAIILVPFNFAPMRKSMISAPVFRGFRKVMPPMSRTEKEAIDAGTTWWEGDLFQGKPDWKKLHNYPQPRLTAEEQAFLDGPVEEACRMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQSRVLQKLSGVSGILAITVGVPNSLGPGELLQHYGTDEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGIVCMGEWQGQQVLGMRLTWNKRYITLAPIATVLGLAFKLSDPEKLLGGAEDLGITCALIPTTTPGVEIGRRHFPLNVPFQNGPTRGKDVFVPIDYIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMLGQSNFLARAYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVLEEMEAAKNNDVNAFDKLLFKHIGHVGSNKVRSFWLGLTRGLTSSTPTGDATKRYYQHLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASAVLKRYDDEGRNEADLPLVHWGVQDALYQAEQAMDDLLQNFPNRVVAGLLNVVIFPTGRHYLAPSDKLDHKVAKILQVPNATRSRIGRGQYLTPSEHNPVGLLEEALVDVIAADPIHQRICKELGKNLPFTRLDELAHNALVKGLIDKDEAAILVKAEESRLRSINVDDFDPEELATKPVKLPEKVRKVEAA
Catalyzes the dehydrogenation of acyl-coenzymes A (acyl-CoAs) to 2-enoyl-CoAs, the first step of the beta-oxidation cycle of fatty acid degradation. Is required for E.coli to utilize dodecanoate or oleate as the sole carbon and energy source for growth.
Q47146
Q2KYS7
TRHO_BORA1
tRNA hydroxylation protein O
Bordetella
MSIVNIAAYKFVSLPDTVLLREALQERADALGLKGTILLAPEGINLFLAGSGEAIEAFLAGLRADARFADIEVKYSTSADVPFGKMRVRLKREIIRMNHPAIRPEAGRAPSVNAHTLARWLEQGRDDDGREVVMLDTRNAFEVDVGTFRNAIDWRIDRFTQFPDAVREHRAELEGKTVVSFCTGGIRCEKAAIFMEDIGIAHVYQLEGGILKYFEETGGPGYDGACFVFDERHALDPALKPV
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Q2KYS7
Q9XZ58
CSN5_DROME
JAB1 homolog
Sophophora
MDSDAAQKTWELENNIQTLPSCDEIFRYDAEQQRQIIDAKPWEKDPHFFKDIKISALALLKMVMHARSGGTLEVMGLMLGKVEDNTMIVMDAFALPVEGTETRVNAQAQAYEYMTAYMEAAKEVGRMEHAVGWYHSHPGYGCWLSGIDVSTQMLNQTYQEPFVAIVVDPVRTVSAGKVCLGAFRTYPKGYKPPNEEPSEYQTIPLNKIEDFGVHCKQYYPLEISYFKSALDRRLLDSLWNKYWVNTLGSSGLLTNTEYTTGQIMDLSEKLEQSENFLGRGTDVNEKRSEDKLSKATRDCSRSTIELIHGLMAQIVKDKLFNKVGLGK
Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. The CSN complex plays an essential role in oogenesis and embryogenesis and is required for proper photoreceptor R cell differentiation and promote lamina glial cell migration or axon targeting. It also promotes Ubl-dependent degradation of cyclin E (CycE) during early oogenesis. Also involved in regulation of axis formation by checkpoint-dependent, translational control of Gurken.
Q9XZ58
P61984
CBID_DESVH
Cobalt-precorrin-6A synthase
Desulfovibrio
MESRADHAVPADEGHGATEPPRGRDRAALREGFTTGTAMTAGAVAALRHVFGLPFLPVLSVPLPPQEGVGVPGRLGVPVAEVLTEGDGATGVVIKDGGDDPDATHGARIETHVRLLPDATATLLLEGGTGVGRVTLPGLPVAVGEVAVNPGPRAQLEFAVREVCAAQGYGGGVRVTVRVPEGEAIARHTLNGRLGIVGGISILGTRGTVRPYSHEAWKAAIAQELSVARALGHRRACLSTGRRSETLLMRRYPDLPEQAFVQAADFVAFALGAAAERGFEALAWGCFFGKLVKLAQGLPHTHARTAPLDLPLLAQWCREAGVDEARVEAVAGANTAGQALDIITPDAACHTALDAVTRRAKAHAERFAGPGVGVTIHLFHLNGTELTSA
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
P61984
Q1QSC8
ATPA_CHRSD
F-ATPase subunit alpha
Chromohalobacter
MQQLNPSEISDIIKQRIEKLDVASEARNEGTVVSVSDGIVKIHGLADAMFGEMIEFPGSIFGMVLNLERDSVGAVVLGDYLQLEEGMTAQCTGRILEVPVGPELIGRVVDPLGVPIDGKGELDTKLTDAVEKVAPGVITRQSVDEPIQTGLKSIDAMVPIGRGQRELIIGDRQIGKSAIAIDTIINQKGKGVTCVYVAIGQKQSTIANVVRKLEEHGAMEHTIVVAAGAADPAPMQFLAAYSGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQVSLLLRRPPGREAYPGDVFYLHSRLLERAARVNADHVEKLTNGEVKGKTGSLTALPIIETQGGDVSAFVPTNVISITDGQIFLETNLFNSGVRPAINAGLSVSRVGGSAQTKIIKKLGGSVRLALAQYRELAAFSQFASDLDEATRKQLEHGQRVTELMKQNQYSPLSVAEMAVSLYAANEGFLDDVEVSKVLDFERALHAYMKSEHAELLDKINQSGGYDDEIQQGLKSGLETFKSTQTW
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Q1QSC8
P48717
RBL_TROMA
Ribulose bisphosphate carboxylase large chain
Tropaeolum
SVGFKAGVKDYKLTYYTPDYETKDTDILAAFRMSPQPGVPAEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYQIEPVAGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMMKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFIEKDRSRGIFFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLASEGNAIIREASKWSPELAAACEVWKEIKFEFPAMDTL
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.
P48717
P23407
RK18_CYAPA
50S ribosomal protein L18, cyanelle
Cyanophora
MKLTRKQATQRRHRRVRRKVFGTSERPRLAVFRSHQHIYAQIIDDTQHRTLAASSTLEPSVKNSELSSTSTCAASAIVGQLIAKKALEKGITQVVFDRGGKIYHGRVRTLAEAAREAGLQF
Binds 5S rRNA, forms part of the central protuberance of the 50S subunit.
P23407
Q31D21
NU1C_PROM9
NDH-A
Prochlorococcus
MEYGLDLEYSFNEFFKGFGLSSEIAHIIWLPIPMLLVLVAAVVGVLVTVWLERKISAAAQQRIGPEYAGALGVLQPIADGLKLLVKEDIIPAKADGILFTAGPILVLVPVILSWLIVPFGQNLLISNVGIGIFLWIALSSIQPIGLLMSGYASNNKYSLLGGLRAAAQSISYEIPLALSVLAIVLMTNSLSTIDIVNQQSGAGILSWNIWRQPVGFIVFWICALAECERLPFDLPEAEEELVAGYQTEYAGMKFALFYLGSYINLILSALLVSILYLGGWGFPIPVELIAKFLHLPINAPVIQVFTASIGIVMTVLKAYLLVFIAILLRWTTPRVRIDQLLDLGWKFLLPISLANLLITAGLKLAFPQFFGG
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Q31D21
B0U5A0
ATPA_XYLFM
F-ATPase subunit alpha
Xylella
MATTLNPSEISELIKTRIEQVKLSAESRNEGTVTSVSDGIVRIFGLADAMQGEMIELPNKTYALALNLERDSVGAVILGDYKHLREGDVAKTTGRILEVPVGKSLLGRVVNALGEPIDGKGTLGPTQTAPVERVAPGVIWRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTAMAIDTVISQKDTGIKCVYVAIGQKASTIANIVRKLEENDALDHTIVVAATASESAALQYISAYAGCTMGEYFMDRGEDALIIYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAARVSEEYVEKFTQGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETDLFNAGIRPAVNAGISVSRVGGSAQTKIIKKLSGGIRISLAQYRELAAFAQFASDLDETTRKQLERGQRVTELMKQKQYTSMSVANQALSIYAVNEGYLDDIPVDKVLTFEEGLHAHFSNTQGALIDKINNSGDWDNNIEAAFKQHIEEFKTTGSW
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
B0U5A0
A3CKV4
MUTS2_STRSV
Endonuclease MutS2
Streptococcus
MNTKILETLEFSKIKELFAPYLLTEQGQLELGLLLPTSKKETVVSAFLEMTDMQQIFVQHPHFSLAATQDITALTKRLELESDLNIEEFLALKRVLAVTQELKSFYEDLENVHLEKLDRLFDNLAVFPKLQGSLQAVNDGGFIESFASESLSRIRRKIQENENQVREILQEILKNKGEMLADQVVASRNGRNVLPVKNTYRNRISGVVHDISASGNTVYIEPRAVVNLNEEIASSRADERYEIQRILQELSDLFRPHAAEIANNAWIIGHLDLVRAKVRFMQETGAVVPDLSEEQDIQLLSVRHPLIENAVANDLHFGLDLTEIVITGPNTGGKTIMLKTLGLAQIMAQSGLPILADKGSRVGIFSQIFADIGDEQSIEQSLSTFSSHMTNIVSILEQVDSESLVLLDELGAGTDPQEGAALAIAILEDLRLRQIKTMATTHYPELKAYGIETDWVENASMEFDTDSLRPTYRFMQGVPGRSNAFEIAQRLGLSEVIVGHAQEQTDTDSDVNRIIERLEEQTLESRKRLDNIREVEQENLKFNRALKKLYNEFNREKETELNKARLEAQEIVDLALSESESILKNLHDKSSLKPHEIIEAKAQLKKLAPETVDLSKNKVLKQAKKNRAPKVGDDILVTSYGQRGTLVKQLKDGRWEAQVGLIKMTLEEQEFNLLKAEKEQQPKRKQVNVVKRANTAGPKARLDLRGKRYEEAMEELDAFIDQALLNNMAQVDIIHGIGTGVIREGVTKYLRRNKHVKSFGYAPQNAGGSGATIVIFK
Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity.
A3CKV4
Q5ZJ37
RABEK_CHICK
Rab9 effector protein with kelch motifs
Gallus
MGPRVLPLLEPGCRPQAGKWYRMAPRGEWPRGRVGHGCLFVPGGSGRVLLLGGADPAGAFADAHFVELGAHLWAPAAWSGLRPRYEHATFLSACRPPRLWVFGGAHRAGNRSCVQVLDPEIGTWESPEVTGIPPLPRTFHTSSAAIGDCLYVFGGGDKGAEPVKDQQLHVFDTVALAWTQPDTHGDPPSPRHGHVVVAVGTKLFIHGGLAGDIFYNDLFCIDTTDMKWVKIAATGDVPGGRASHSSAVFKDHLYIFGGIGPDGTLDTTYKYHIEEQQWTLLQFDSPLPAGRLDHAMCVIPWRVGKNGDAAAVSKEDKAEPTASAGDRAGHLCRGQDKKACTEDTMMHLLLIFGGMDTQAEIYRDCIVSLIE
Rab9 effector required for endosome to trans-Golgi network (TGN) transport.
Q5ZJ37
A0AEN0
RL9_LISW6
50S ribosomal protein L9
Listeria
MKVIFLKDVKGKGKKGETKNVADGYANNFLIKNGYAVEASNAALSTLSAQKKKEDKLAAEELAEAKALKEKMEKLTVELKAKSGEGGRLFGSITSKQIAQTLEKTHGIKIDKRKMDLPEAIRALGHTKVPVKLHHEVTATLDVHVSEE
Binds to the 23S rRNA.
A0AEN0
B7HZG7
NOC_BACC7
Nucleoid occlusion protein
Bacillus cereus group
MKNTFSRLFGFGDKESEFELQDESHEEIDKKVYEEIQEIPIVNITPNRYQPRTVFDDARIEELALTIRTHGLIQPIVVRQYEDEKYEIIAGERRFRAATKLGWEKVPAIIKNLNDTETASVALIENLQREELTAIEEAVAYQKLIELHNLTQEALAQRLGKGQSTIANKLRLLKLPEEIKNALLEKSITERHARALIPLKNEELQLKVLQEIVEKQLNVKQTEERIAKLLEEAKPKRKAKQKAVSRDTRIAMNTIRQSLQMVADSGLNVNSEEEEFDEYYQITIQIPKKK
Effects nucleoid occlusion by binding relatively nonspecifically to DNA and preventing the assembly of the division machinery in the vicinity of the nucleoid, especially under conditions that disturb the cell cycle. It helps to coordinate cell division and chromosome segregation by preventing the formation of the Z ring through the nucleoid, which would cause chromosome breakage.
B7HZG7
A1TAX0
MURD_MYCVP
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
Mycolicibacterium
MQPISPGAAVLVVGAGITGRAVLAALAPLGARATLTDDSPTALTASAQQRVEVLDPATAVDRIADFDLVVVSPGIPPTAPIPVAAAAAGIPVWGDVELAWHLDRSGRFGPPRQWLVVTGTNGKTTTTSMLYAMLQAGGRRAVLCGNIGDPVLSQLDRPADVLAVELSSFQLHWAPSLRPEAGAVLNVAEDHLDWHGSMAAYAGDKARALTGRVAVGGLDDAIAAGLLADAPAPVKVGFRLGDPGPGEFGVRDGVLIDNAFGRDLALADADTIPVAGPVGVLDALAAAALARAVDVPAAAIAEALATFHVGRHRAEVVAVADGITYVDDSKATNPHAAQASVSAFPRVVWVAGGLLKGASVDEMVEATKDRLVGVVLIGRDRAIVGNALSRHAPDVPVVELVTGEDSVVLEKDESGVTRVTRVIQTGDRTLADAVMTAAVDAARGLATSGDTVLLAPAGASFDQFTGYGHRGDAFAAAVRAAIR
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
A1TAX0
Q47NB8
WHIA_THEFY
Probable cell division protein WhiA
Thermobifida
MAMTGVVKDELSRLTVLKPCCRKAEVSTILRFTGGLHLVGGRIVIESELDTGVAARRLRKDIAEVFGHESEVLVLSPSGLRKGNRYVVRVIKEGESLARQTGLIDSNGRPVRGLPRHVVAGGVCDAESAWRGAFIAHGSLTEPGRSMSLEVTCPGPEAALALVGAARRLKVHAKAREVRGVDRVVVRDGDSISAMLTRLGAHQSVLAWEERRMRREVRATANRLANFDDANLRRSARAAVAAGARVQRALEILADDAPPHLVAAGKLRLKHKQASLEELGQLADPPLTKDAIAGRIRRLLAMADKRAADLGIPNTEASLTPDMLVP
Involved in cell division and chromosome segregation.
Q47NB8
P09445
EF2_CRIGR
Elongation factor 2
Cricetulus
MVNFTVDQIRAIMDKEANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGPAERAKKVEDMMKKLWGDRYFDPANGKFSKSANSPDGKKLPRTFCQLILDPIFKVFDPIMNFRKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGVVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKARARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRGSQVVAETRKRKGLKEGIPALDNFLDKL
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.
P09445
Q7IS11
MATK_TAXCU
Intron maturase
Taxus
MDEFQRYGNKHKSWQQCFLYPLFFREDLYTIAHDLYLDKSSSSEPTELSISNFFSFPTVKRLIRRIRQQNDSNSIGLFRNCDPNRFINRNRNSYSELVLEGLTVILEVSLAMQSKHFIEGMDGWKSIRSIHCIFTLMEDKFPYSNYVSDIRVPYSIHPEILVRTFRRWIRDAPSLHLLRSILHEWRNSFSAENLQKALVPPRENRRFSLFLWNSYVYECESFLVSLLKQFYHSRSLLYGSFPDRTHFDKKIKHIVIFPVKISTKRIWLLKYPFIYYVRYGERSLIALKGTHLQVKRCRYHLFNFWQYYFHLWSQPYRVCILELSKIYFYFLGHFLSFKMKTLVVRTKMLDDLLISDIIANEFNPIAPIRSILLYLTKERFCDISGQPISRLSWTNLSDDDILDRFDRMCRNIFHYYSGSINKDGLYYIKYILLLPCAKTLACKHKSTIRVVREESGSELFTKSFSKEREFIYSSFSKTCSQRERNWNSDIIQINILVNYWQKIHNKQIEK
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
Q7IS11
Q96N22
ZN681_HUMAN
Zinc finger protein 681
Homo
MEPLKFRDVAIEFSLEEWQCLDTIQQNLYRNVMLENYRNLVFLGIVVSKPDLITCLEQEKEPWTRKRHRMVAEPPVICSHFAQDFSPEQNIKDSFQKVTPRRYGKCEHENLQLSKSVDECKVQKGGYNGLNQCLPTTQSKIFQCDKYMKIFHKFSNLNGHKVRHTRKKPFKYKEFGKSFCIFSNLTQHKIICTRVNFYKCEDCGKAFNGSSIFTKHKRIHIGEKSYICEECGKACNQFTNLTTHKIIYTRDKLYKREECSKAFNLSSHITTHTIIHTGENPYKREECDKAFNQSLTLTTHKIIHTREKLNEYKECGKAFNQSSHLTRHKIIHTGEKPYKCEECGKAFNQSSHLTRHKIIHTGEKPYRCEECGKAFRQSSHLTTHKIIHTGEKPYKCEECGKAFNKSSHLTRHKSIHTGEKPYQCEKCGKASNQSSNLTEHKNIHTEEKPYKCEECGKAFNQFSNLTTHKRIHTGEKPYKCEECGKAFNQSSILTTHKRIHTGEKSYKCEECGKAFYRSSKLTEHKKIHTGEKPYTCEECGKAFNHSSHLATHKVIHTGEKPYQCEECGKAFNQSSHLTRHKRIHTGEKPYQCEKCGKAFNQSSNLTGHKKIHTGEKLYKPKRCNSDFENTSKFSKHKRNYAGEKS
May be involved in transcriptional regulation.
Q96N22
C0M7E5
CODY_STRE4
GTP-sensing transcriptional pleiotropic repressor CodY
Streptococcus
MPNLLEKTRKITSILQRSVDSLETELPYNTMASRLADIIDCNACIINGGGSLLGYAMKYKTNTDRVEEFFETRQFPDAYVKAASRVYDTEANLSVENELTIFPIESKDIYPDGLTTIAPIYGGGMRLGTLIIWRNDNEFSDDDLVLVEISSTVVGIQLLNLQTENLEETIRKQTVVNMAINTLSYSEMKAVAAILSELDGNEGRLTASVIADRIGITRSVIVNALRKLESAGIIESRSLGMKGTYLKVINEGIFDKLKEF
DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor.
C0M7E5
A7FJT1
MATP_YERP3
Macrodomain Ter protein
Yersinia
MKYQQLENLESGWKWAYLVKKHREGEAITRHIENSAAQDAVEQLMKLENEPVKVQEWIDAHMNVNLATRMKQTIRARRKRHFNAEHQHTRKKSIDLEFLVWQRLAVLARRRGNTLSDTVVQLIEDAERKEKYASQMSSLKQDLKDILDKEV
Required for spatial organization of the terminus region of the chromosome (Ter macrodomain) during the cell cycle. Prevents early segregation of duplicated Ter macrodomains during cell division. Binds specifically to matS, which is a 13 bp signature motif repeated within the Ter macrodomain.
A7FJT1
P50680
COX2_GAZSP
Cytochrome c oxidase polypeptide II
Gazella
MAYPMQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYVISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSELKPGELRLLEVDNRVVLPMEMTIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSARPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML
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.
P50680
Q5PF04
NRDI_SALPA
Protein NrdI
Salmonella
MSALVYFSSSSENTHRFMQRLGLPATRIPLNERERIRVDEPYILVVPSYGGGGMAGAVPRQVIRFLNDEHNRARIRGVIASGNRNFGDAWGCAGDVIAQKYGVPWLYRFELMGTQRDIDNVRRGVNEFWQQLPRSA
Probably involved in ribonucleotide reductase function.
Q5PF04
Q49V08
GLMU_STAS1
Glucosamine-1-phosphate N-acetyltransferase
Staphylococcus
MQRHAIVLAAGKGTRMKSKKYKVLHDVAGKTMIEHVADNVKQSGIDQLVTIVGHGADSVKETLGDTSLYSFQEEQLGTAHAVKMASEHLSESQGTTLVVCGDTPLITTATLKSLVEHHENNQAHATVLSATAENPFGYGRILRDSEGRLVSIVEQKDATDAEQQINEISSGIFAFDNQVLFEKLELVKNDNAQSEYYLPDVLSLILEDRGIVEVFHTNDFEEIMGVNDRVMLSEAEKAFRKRINEQHMKNGVTIIDPVTTYIGADVRIGEDTVVEPGVKLSGNSVIGEDTVIGQHTEITNSKIGSNVTIKQSVINEAIVDDYATIGPFAQLRPGADLGKKVKVGNFVEVKKSVVKAGAKLPHLSYIGDAEIGERTNVGCGSITVNYDGINKFKTVIGDDSFIGCNTNLVAPITLGNRSFIAAGSTITDNVPEDSLALARARQTTKEGYLKK
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Q49V08
Q9L6B6
ATPG_PASMU
F-ATPase gamma subunit
Pasteurella
MAGAKEIRTKIASVKSTQKITKAMEMVAASKMRKTQERMSSSRPYSETIRNVISHVSKATIGYKHPFLVDREVKKVGMIVVSTDRGLCGGLNVNLFKTVLNEMKEWKEKDVSVQLSLIGSKSINFFQSLGIKILTQDSGIGDTPSVEQLIGSVNSMIDAYKKGEVDVVYLVYNKFINTMSQKPVLEKLIPLPELDNDELGERKQVWDYIYEPDAKVLLDNLLVRYLESQVYQAAVENLASEQAARMVAMKAATDNAGNLINELQLVYNKARQASITNELNEIVAGAAAI
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Q9L6B6
Q8ESM5
PHNC1_OCEIH
Phosphonates import ATP-binding protein PhnC 1
Oceanobacillus
MIEFKDVGLVYPNGTEGLKNINVKINDGEFVVIVGLSGAGKSTFIRSINRLVTPTTGELIIDDENILNYSGNKLRMLRTKTGMIFQNYNLVKRSNVFKNVLAGRLGHTGTIRSIFNQYKKEDVALAYESLHRVNIAEKIYNRADELSGGQQQRVSIARVLTQQPKYILADEPVASLDPPTSHQVMTYLKKINREDKITTIVNLHFIDMAMEYADRIIGMRAGEVVFDGPVSEVSESTFEEIYGRSIREDDLRGGAKES
Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
Q8ESM5
B5YG20
RL20_THEYD
50S ribosomal protein L20
Thermodesulfovibrio
MPRAKGGFKTRRYHKKILSMAKGYYSGRRRCYKVAAKAVEKALEHSYRDRRLKKRDLRSLWITRINAAVRMFGLTYNQFIDGLKKANISLNRKALADIAYNDINVFGELVEKVKPFVKAA
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
B5YG20
A8W3B5
RPOC1_CUSEX
Plastid-encoded RNA polymerase subunit beta'
Cuscuta subgen. Monogynella
MNNNFSSMIDRYKHQQLQIGSVSPQQISAWATKILPNGEIVGEVKKPYTFLYKTNKPEKEGLFCERIFGPIKSGICACGNYRVIGDEKEEQKFCEQCGVEFVDSRIRRYRMGCIKLACPVTHVWYLKRLPSYIANILDKPLKELEGLVYCDFSFARPITNKPTFLRLRGLLKYEIQSWKSSIPLFFTTQGFDTFRNREISTGAGAIREQLADLDLRILLENSLLEWKDLGEEENTGNEWEDRKAGRRKGFLVRRMELVKHFIRTNIEPKWMVLCLLPVLPPELRPIIQIDGGKLMSSDINELYRRVIYRNNTLTDLLTTSRSTPGELVMCQEKLVQEAVDTLLDNGIRGQPMRDGHNKVYKSFSDIIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHQCGLPREIAIELFQPFVIRDLIKQHLASNIGVAKSKIREKEPIIWEILQDVMQGHPVLLNRAPTLHRLGIQAFQPVLVEGRVICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVPTQDMLIGLYVLTSEKHRGICTNRYTNCNIRTLQTKSSDYSNSKYKNPYNNGPFFCNSYDAIGAYRQKRINLESPLWLRWRLDRRVITSRETPIEVHYESRGTYFEIYGHFLIVRSLKKKILFIYLRTTVGHISLYREIEEAIQGFSRAWSSDT
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
A8W3B5
B9DY87
ISPD_CLOK1
MEP cytidylyltransferase
Clostridium
MKSNYAVIVAAGKGKRMKMPINKQFICIQGKPILYYSISVFSKNPLVDKIVLVCAEDEIEYCKQEIVKKYNFDKVVKIVSGGKERQHSVFNALKVLENCSVVLIHDGARPFVTDRIIEDGIKYSNMYGACACGVVPKDTIKIKGKEGFSYKTLVRKELFIVQTPQCFDYNLIYDCHKKLANNKVQVTDDTTVAEYFGNMVYLYEGSYDNIKITTPEDLIIAENIFKTHKYI
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
B9DY87
A8GWP2
SYE1_RICB8
Glutamyl-tRNA synthetase 1
belli group
MTKVITRFAPSPTGMLHVGNIRAALLNWLYAKKHDGQFILRFDDTDLERSKQEYKDAIRADLKFLNLNWDQTFNQLSRLSRYDEIKKLLLDKKRLYACYETPEELELKRKFQLSKGLPPIYDRAALNLTEDQIQKYIEQGRKPHYRFLVNHEPITWHDMIKGEVKYEGKALSDPIVIRADGSMTYMLCSVIDDVDYEITHIIRGEDHVSNTAIQIQMFEALDKYPPTFGHLSLIINKDEKISKRVGGFEIATLREEVGLEAMAIASFFSLLGSSAQIIPHKKMDELVKHFEISSFSKSPTIYQPEDLERLNHKLLISLEFNEVKDRLKEIDAEYIDENFWLSVRPNLKKLFDAKDWWEICHKTPNIQDLNLDKEYLKQAAELLPEEEITTETWGIWTKKLAAITNRKGKELFLPLRLALTGKESGPEISKVLPLIKREEIVKRLT
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
A8GWP2
Q8N6Y1
PCD20_HUMAN
Protocadherin-13
Homo
MRGRGNARSSQALGVSWCPATWHPRLDMGRLHRPRSSTSYRNLPHLFLFFLFVGPFSCLGSYSRATELLYSLNEGLPAGVLIGSLAEDLRLLPRSAGRPDPQSQLPERTGAEWNPPLSFSLASRGLSGQYVTLDNRSGELHTSAQEIDREALCVEGGGGTAWSGSVSISSSPSDSCLLLLDVLVLPQEYFRFVKVKIAIRDINDNAPQFPVSQISVWVPENAPVNTRLAIEHPAVDPDVGINGVQTYRLLDYHGMFTLDVEENENGERTPYLIVMGALDRETQDQYVSIIIAEDGGSPPLLGSATLTIGISDINDNCPLFTDSQINVTVYGNATVGTPIAAVQAVDKDLGTNAQITYSYSQKVPQASKDLFHLDENTGVIKLFSKIGGSVLESHKLTILANGPGCIPAVITALVSIIKVIFRPPEIVPRYIANEIDGVVYLKELEPVNTPIAFFTIRDPEGKYKVNCYLDGEGPFRLSPYKPYNNEYLLETTKPMDYELQQFYEVAVVAWNSEGFHVKRVIKVQLLDDNDNAPIFLQPLIELTIEENNSPNAFLTKLYATDADSEERGQVSYFLGPDAPSYFSLDSVTGILTVSTQLDREEKEKYRYTVRAVDCGKPPRESVATVALTVLDKNDNSPRFINKDFSFFVPENFPGYGEIGVISVTDADAGRNGWVALSVVNQSDIFVIDTGKGMLRAKVSLDREQQSSYTLWVEAVDGGEPALSSTAKITILLLDINDNPPLVLFPQSNMSYLLVLPSTLPGSPVTEVYAVDKDTGMNAVIAYSIIGRRGPRPESFRIDPKTGNITLEEALLQTDYGLHRLLVKVSDHGYPEPLHSTVMVNLFVNDTVSNESYIESLLRKEPEINIEEKEPQISIEPTHRKVESVSCMPTLVALSVISLGSITLVTGMGIYICLRKGEKHPREDENLEVQIPLKGKIDLHMRERKPMDISNI
Potential calcium-dependent cell-adhesion protein.
Q8N6Y1
Q47G67
NIFH_DECAR
Nitrogenase reductase
Dechloromonas
MAKLRQCAIYGKGGIGKSTTTQNLVAALAESGKKVMIVGCDPKADSTRLILHSKAQTTVMHLAAEAGSVEDLELEDVLSVGFGGIKCVESGGPEPGVGCAGRGVITAINFLEEEGAYDEDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAANNIAKGIVKYANSGGVRLAGLICNSRNTDREDELIMALAGRLGTTMIHFVPRDNAVQHAEIRRMTMVEYDPKHKQADEYRQLANKIVNNTNFVIPTPIEMEELEELLMEFGIMEAEDESIVGQTAAELAAAAA
The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
Q47G67
P63290
VIP_CAPHI
Vasoactive intestinal polypeptide
Capra
HSDAVFTDNYTRLRKQMAVKKYLNSILN
VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder.
P63290
B4IAD1
NUBP2_DROSE
Cytosolic Fe-S cluster assembly factor NUBP2 homolog
Sophophora
MLDKVKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQCDEGWVPVYTDESQTLAVMSIGFLLKNREDPVIWRGPKKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVMECLKEVGCHGAIIVTTPQEVALDDVRKEITFCKKTGINILGIVENMSGFVCPHCTSCTNIFSSNGGVSLATYAQVPHLGTLPIDPRVGVLAGTTTSVLDELPDSTTAEVLTHLVEKLKTMLVS
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.
B4IAD1
Q9ZD44
RS15_RICPR
30S ribosomal protein S15
typhus group
MSITTERKQQLIKEYAITENDTGSTAVQCAILTERINNLTEHFKSNHKDHTSRRGLLILVGRRRRLLNYIKKNNVSEYLDLISKLGIRKIK
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
Q9ZD44
Q5KVY7
YIDD_GEOKA
Putative membrane protein insertion efficiency factor
Geobacillus thermoleovorans group
MGQWLIWCIRFYQRFLSPLKPPTCRFYPTCSNYGIEAIRRFGAIKGGWLTAKRILKCHPFHPGGFDPVPESSEHAKRNKIT
Could be involved in insertion of integral membrane proteins into the membrane.
Q5KVY7
Q5E8M6
COABC_ALIF1
Phosphopantothenoylcysteine synthetase
Aliivibrio
MASLAGKRILLGISGGIAAYKCAELTRRLIERGAEVRVVMTKAAKEFITPLTMQAVSGHPVADSLLDPAAEASMGHIELAKWADIVLLAPATADLIARMAAGMGNDLLSTLVLATDSPVAVSPAMNQQMYSNIATQENIATLARRGMHIWGPAAGQQACGDVGMGRMLEPMELVHLCEDFFQANSCEQAEADEKPLKGQSLLITAGPTREAIDPVRYISNHSSGKMGFAIAEAAAQLGANVTLVSGPVNLATPENVKRIDIESAEQMHGAVMKNAQSHSIFIACAAVADFKLSQVATQKLKKTADEDGMTLHMVKNPDIVASVAALTNQRPFTVGFAAETQDVEKYARGKLERKNLDMICANDVSVQGQGFNSDNNALHLYWKEGDKALPLTTKSELGKAIMLEIVEKL
Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.
Q5E8M6
Q2JQN1
RL24_SYNJA
50S ribosomal protein L24
unclassified Synechococcus
MVRPLKPSQIRRLIRQTGVRKHRNSLRYKMRIKKGDTVQVISGDDKGKIGEVLQVFPERNMVLVEGVNIVTYHRKPQREGESGRIETKEAPIHACKVMLYSKKQEVASRIGYQITADGRKVRVLKKTGEILD
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
Q2JQN1
A0QVQ3
RS15_MYCS2
30S ribosomal protein S15
Mycolicibacterium
MALTAEQKKEILGQYGLHDTDTGSPEAQVALLTKRIQDLTEHLKVHKHDHHSRRGLLLLVGRRRRLLKYVAQVDVARYRSLIERLGLRR
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
A0QVQ3
Q89J89
RL22_BRADU
50S ribosomal protein L22
Bradyrhizobium
MSKPKRERSLAENEAKAVARMLRVSPQKLNLVAQLIRGRKAAAALADLQFSRKRIAVDVKKCLESAIANAENNHDLDVDDLVVAQAFVGNGLVMKRFAARGRGRSGRVYKPFSQLTIIVRQVEAEAAAA
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
Q89J89
B2A1G4
HEM1_NATTJ
Glutamyl-tRNA reductase
Natranaerobius
MILAVIGINHETASVETREQLAFSSKQVKELVQKLIEGQPIKEASVLSTCNRTEVHFTVNTGQIEAGKNHIMTYLSDFSDLDPREYVDHLYFITDQEAVSHIFKVTAGLNSLVTGETEILGQVKKAYQLSDEAGGVDSIFHGLYQQALRTGKRVHRETGINDNAASVSYASVELATKIFGSLQNRRALIIGAGKMSELAARHLYSNGVKDVIVINRTIERAKNLADKFGGLYASYDQLSEWLNEIDIVITSTGAPHFVIKEEQIKRAMKSRKYSPMFLIDIAVPRDVEPSVNNQDNAYLYTIDDLEAVVESNMQERQEEARNAELIISEEVAEFMVWYKTRDVVPLISALREKAEDVRKMELEKYHKKLKNLSPKEQEAVDKLTKSIVNKILKEPVLRIKEFAVEDKSELYMATLAQLFDLEDEVIPKDGEEHSSSKEVESVTQSSTERGHHESDFHN
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
B2A1G4
Q861W5
TNFL6_FELCA
SPPL2A-processed FasL form
Felis
MQQPLNYPYPQIYWVDSRASSPWGPPGSVLPCPSSVPGRPGQRRPPPPPPPTLPPPPPPPPLPPLPLPPLKTRRDHNTGLCLLVMFFMVLVALVGLGLGMFQLFHLQKELAELRESTSQKHVASSLEKQIGQLNPPSEKRELRKVAHLTGKPNSRSIPLEWEDTYGIALVSGVKYKKGGLVINDTGMYFVYSKVNFRGQSCNNQPLNHKVYMRNSKYPQDLVLMEGKMMNYCTTGQMWARSSYLGAVFNLTSADHLYVNVSELSLVSFEESKTFFGLYKL
Cytoplasmic form induces gene transcription inhibition.
Q861W5
P0DTY2
O1620_CONCL
O1_cal6.20
Californiconus
MKLTCVLIVAVLILTACQVIAADGWFGEESSCWWCTGQNKCCEEAQVCQSVNYACPPARR
Probable neurotoxin.
P0DTY2
B1ZES7
TRMFO_METPB
Folate-dependent tRNA(M-5-U54)-methyltransferase
Methylorubrum
MTNPIHIVGGGLAGSEAAWQIAQGGRRAVLHEMRPRRGTEAHQGEGLAELVCSNSFRSDDANGNAVGLLHQEMRSLNSLIMRAADANQVPAGGALAVDREGFSQAVTAALEEHPNVTILREEVAGLPPETWGSTILATGPLTSPALAEAVGALTGRDALAFFDAIAPIVHRDSIDMGKAWFQSRYDKAGPGGTGADYLNCPMDREQYEAFVAALIAGEKTTFKEWEATTPYFDGCLPIEVMAERGPETLRHGPMKPVGLTNPHNPTVKAYAIVQLRQDNALGTLFNMVGFQTKLRHAEQVRIFRTIPGLENAEFARLGGLHRNTYLDSPRLLDATLRLRARPQLRFAGQITGCEGYVESAAVGLMAGRYALAEAEGTTLAPLPPTTALGALIGHITGGHLEASEDAGANAPRSFQPMNVNFGLFPPLERMPRNETGKRLRGPEKAALKKRALTDRAREDLAAWIGGEDLPHAAE
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
B1ZES7
P33416
HSP78_YEAST
Heat shock protein 78, mitochondrial
Saccharomyces
MLRQATKAPIQKYLQRTQLLRRSTPRIYTIVQCKRSICSFNARPRVANKLLSDIKTNALNEVAISTCALKSSYGLPNFKRTYVQMRMDPNQQPEKPALEQFGTNLTKLARDGKLDPVIGRDEEIARAIQILSRRTKNNPCLIGRAGVGKTALIDGLAQRIVAGEVPDSLKDKDLVALDLGSLIAGAKYRGEFEERLKKVLEEIDKANGKVIVFIDEVHMLLGLGKTDGSMDASNILKPKLARGLRCISATTLDEFKIIEKDPALSRRFQPILLNEPSVSDTISILRGLKERYEVHHGVRITDTALVSAAVLSNRYITDRFLPDKAIDLVDEACAVLRLQHESKPDEIQKLDRAIMKIQIELESLKKETDPVSVERREALEKDLEMKNDELNRLTKIWDAERAEIESIKNAKANLEQARIELEKCQREGDYTKASELRYSRIPDLEKKVALSEKSKDGDKVNLLHDSVTSDDISKVVAKMTGIPTETVMKGDKDRLLYMENSLKERVVGQDEAIAAISDAVRLQRAGLTSEKRPIASFMFLGPTGTGKTELTKALAEFLFDDESNVIRFDMSEFQEKHTVSRLIGAPPGYVLSESGGQLTEAVRRKPYAVVLFDEFEKAHPDVSKLLLQVLDEGKLTDSLGHHVDFRNTIIVMTSNIGQDILLNDTKLGDDGKIDTATKNKVIEAMKRSYPPEFINRIDDILVFNRLSKKVLRSIVDIRIAEIQDRLAEKRMKIDLTDEAKDWLTDKGYDQLYGARPLNRLIHRQILNSMATFLLKGQIRNGETVRVVVKDTKLVVLPNHEEGEVVEEEAEK
Required, in concert with mitochondrial Hsp70 (SSC1), for the dissociation, resolubilization and refolding of aggregates of damaged proteins in the mitochondrial matrix after heat stress. May extract proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by the Hsp70 chaperone system. Required for resumption of mitochondrial respiratory function, DNA synthesis and morphology after heat stress. Its main role may be maintaining the molecular chaperone SSC1 in a soluble and functional state. Also required for the efficient degradation of proteins by matrix protease PIM1, independent on its protein remodeling activity.
P33416
P35168
CGGR_PRIM3
Central glycolytic genes regulator
Priestia
MRSLIEVQRKLLPELLSVMQKRYQILQYIRLMQPIGRRNLAVSLGLTERVLRSEVTFLKEQDLIDIYPSGMTLTNEGELLLAELEEVMKEVSGLRLLETTLKEAFSLSEVVVVSGDSDQSPWVKNEMGRASVSCIKERLVGKKNTVAVTGGTTLAAVAEMMTPDLKHPDVLFVPARGGLGENVQNQANTICAKMAEKSMSHYRLLHVPDQLSDEAYRSIIGEPSIKDMLHLIKSAGMVVHGIGDAMTMAERRKTPQADLEKVKNGHAVGEAFGYYFNHQGEVVHKVKTVGIQLDDLKNNKCVIAVAGGSSKAKAIKAFMQQAHDSILITDEGAAKELVRDFN
In the absence of glucose, represses the transcription of the gapA operon, which encodes five key glycolytic enzymes.
P35168
Q7NBX3
RF1_MYCGA
Peptide chain release factor 1
Mycoplasma
MEYNKQMYETLVAIRATAQKLNKELESLTNDFKRIHAINKELKQKKQLLEVFELYDKLVVSGLEAEKIINDNAMKEFHELAILDLDAAKEQIPDLEEKLKVLLLPADPNDDKEVIVEMRPAAGGDESSIFVGNMFDLYKEYCSKHNWKINVIEMLPTSVGYSFISFEINGEDVYSKMKFESGVHRVQRVPATEAKGRVHTSTITIAVLPQQDDVEIEINPADLRIDTYRASGAGGQHVNRTESAVRITHIPTGIVAACQEGKSQIANRETAMKMLRSKLWEAAEKEKNDALSALRKNQVGSGDRAEKIRTYNYPQNRVTDHRINMSLNSLDRFMMGEIDEMIDALRSKEQEEKMKLIMNE
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Q7NBX3
B7LW41
PANB_ESCF3
Ketopantoate hydroxymethyltransferase
Escherichia
MKPTTIASLQKCKQNKKRFATITAYDYSFAKLFAEEGLNVMLVGDSLGMTVQGHDSTLPVTVQDIAYHTAAVRRGAPNCLLLADLPFMAYSTPEQAFENAATVMRAGANMVKIEGGAWLVETVRMLTERAVPVCGHLGLTPQSVNIFGGYKVQGRGDEAGDQLLSDALALEAAGAQLLVLECVPVELAKRITEALAIPVIGIGAGNVTDGQILVMHDAFGITGGHIPKFAKNFLAETGDIRAAVRQYIAEVESGVYPGEEHSFH
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
B7LW41
Q72MV4
COAE_LEPIC
Dephosphocoenzyme A kinase
Leptospira
MQNSDSGKKTFLIGITGMIGGGKSTATKILEEMGCFGINADRLAKRYTEPDSPILIELVELLGSEILDEQGKPDRKKISEIVFNNPKKLSRLNQLIHPLVRKDFQKILETTAKGKMVIWEVPLLFETDAYTLCDATVTVDSDPEESILRTISRDKVKKEDVLARIKNQLPLTEKLKRADYILRNRGNIDSLREECKSLYSTLLGKML
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Q72MV4
B1XZN7
ACP_LEPCP
Acyl carrier protein
Leptothrix
MSDIEARVKKIIAEQLGVAEAEVTSEKAFVADLGADSLDTVELVMALEDEFGIEIPDEEAEKITTVQLAIDYAKNNVKA
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
B1XZN7
O35367
KERA_MOUSE
Keratan sulfate proteoglycan keratocan
Mus
MATPNCLILWVLLIADTVWTQSVRQAYEIQDPEDWDVHDDFYCPRECFCPPSFPTALYCENRGLTEIPPIPSRIWYLYLENNLIESIPEKPFENATQLRWINLNKNKITNYGIEKGALSQLKKLLFLFLEDNELEEVPSPLPRSLEQLQLARNKVSRIPQGTFSNLENLTLLDLQHNKLLDNAFQRDTFKGLKNLMQLNMAKNALRNMPPRLPANTMQLFLDNNSIEGIPENYFNVIPKVAFLRLNHNKLSDAGLPSRGFDVSSILDLQLSYNQLTNFPRINANLQHLHLDHNKIKNVNMSVICPTTLRAEQDAFIHGPQLSYLRLDGNEIKPPIPIDLVACFKLLQAFII
May be important in developing and maintaining corneal transparency and for the structure of the stromal matrix.
O35367
A1U7I4
RSMG_MARN8
16S rRNA 7-methylguanosine methyltransferase
Marinobacter
MSYPQWPGQLRDGLAAMNLSLSDSQQQQLLAFLALLNKWNKAYNLTAVRDERVMVSRQLLDSLSILPWVTTDHLLDVGAGGGLPGIPLAIVVPEKRFTLLDSNGKKTRFLNQCVLELGLDNVEVIHGRAEDCQPDQPFTQISSRAFTALENLVTWCGGLLANDGEFLAMKGQYPDDEVAALPAGWQVESSHSLTVPGADGERHLLIVARAERHR
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
A1U7I4
Q9P7R4
UBC8_SCHPO
Ubiquitin-protein ligase 8
Schizosaccharomyces
MSSPRRRIETDVMKLLMSDYEVTLVNDNMQEFYVRFHGPSETPYSGGIWKVHVELPSEYPWKSPSIGFVNRIFHPNIDELSGSVCLDVINQTWSPMFDMINIFEVFLPQLLRYPNASDPLNGEAAALLLREPNTYYAKVRDYIARYANKEDADITLNDSSDDDTMSSIDTESGDEIAGPMDSDF
Catalyzes the covalent attachment of ubiquitin to other proteins.
Q9P7R4
O69600
ALF_MYCLE
Fructose-1,6-bisphosphate aldolase
Mycobacterium
MPIATPEIYAEMLRRAKENSYAFPAINCTSSETVNAAIKGFADAGSDGIIQFSTGGAEFASGLGVKDMVTGAVALAKFTHTIAAKYPINVALHTDHCPKDKLDSYVRPLLAISARRVATGKDPLFGSHMWDGSAIPIDENLAIAQDLLKDAAAAKIILEVEIGVVGGEEDGVAGEINEKLYTTPKDFVKTIDALGAGEHGKYLLAATFGNVHGVYKPGNVKLRPDILAEGQKVAAAKLSQSEGSKPFDFVFHGGSGSEKSEIEEALRYGVVKMNVDTDTQYAFTRPVSGHMFTNYDGVLKVDGDVGNKKVYDPRSYLKKAEASMTERVLEACNDLRCAGKSVAAS
Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
O69600
Q5IZM4
CP51_MYCVP
Sterol 14-alpha demethylase
Mycolicibacterium
MTAVKEVPRVSGGEEEHGHLEEFRTDPIGLMKRVREECGDVGWFQLADKQVILLSGAEANEFFFRSSDSELNQAEAYPFMTPIFGEGVVFDADPERRAEMLHNTALRGEHMKGHATTIEAEVRKMIEGWGESGEIDLLEFFAELTIYTSTACLIGLKFRNQLDSRFANYYHLLERGTDPLCYVDPYLPIESFRIRDEARAGLVELVQDVMHGRIANPPKDKSDRDMLDVLVSIKDEDGNPRFTANEITGMFISLMFAGHHTSSGTSSWTLIELLRHPEFYAKVQQELDDLYADGQEVSFHALRQIPSLDNALKETLRLHPPLIILMRVAQDEFEVAGYPIHKGQMVAASPAISNRIPEDFPNPDDFDPDRYEKPRQEDLINRWTWIPFGAGKHRCVGAAFAQMQIKAIFSVLLREYEFEMAQPPESYQNDHSKMVVQLARPAKVRYRRRVRD
Its precise biological substrate is not known. Catalyzes C14-demethylation of lanosterol, 24,25-dihydrolanosterol and obtusifoliol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.
Q5IZM4
Q54ER6
MTND_DICDI
Acireductone dioxygenase (Ni(2+)-requiring)
Dictyostelium
MKSYFYDNESDVISLDYLKEHNVLYFPMDREKENYKEPLETLCKERGYKNRDEVKLSKETPGLEDKLKIFFEEHLHDDEEIRFILDGCGFFDIRDKNDKWVKIKEKKGDLIIVPANMYHRFALDESRNIHAMRLFTDAPKWVPINRY
Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Q54ER6
Q14166
TTL12_HUMAN
Inactive tubulin--tyrosine ligase-like protein 12
Homo
MEAERGPERRPAERSSPGQTPEEGAQALAEFAALHGPALRASGVPERYWGRLLHKLEHEVFDAGEVFGIMQVEEVEEEEDEAAREVRKQQPNPGNELCYKVIVTRESGLQAAHPNSIFLIDHAWTCRVEHARQQLQQVPGLLHRMANLMGIEFHGELPSTEAVALVLEEMWKFNQTYQLAHGTAEEKMPVWYIMDEFGSRIQHADVPSFATAPFFYMPQQVAYTLLWPLRDLDTGEEVTRDFAYGETDPLIRKCMLLPWAPTDMLDLSSCTPEPPAEHYQAILEENKEKLPLDINPVVHPHGHIFKVYTDVQQVASSLTHPRFTLTQSEADADILFNFSHFKDYRKLSQERPGVLLNQFPCENLLTVKDCLASIARRAGGPEGPPWLPRTFNLRTELPQFVSYFQQRERWGEDNHWICKPWNLARSLDTHVTKSLHSIIRHRESTPKVVSKYIESPVLFLREDVGKVKFDIRYIVLLRSVRPLRLFVYDVFWLRFSNRAFALNDLDDYEKHFTVMNYDPDVVLKQVHCEEFIPEFEKQYPEFPWTDVQAEIFRAFTELFQVACAKPPPLGLCDYPSSRAMYAVDLMLKWDNGPDGRRVMQPQILEVNFNPDCERACRYHPTFFNDVFSTLFLDQPGGCHVTCLV
Negatively regulates post-translational modifications of tubulin, including detyrosination of the C-terminus and polyglutamylation of glutamate residues . Also, indirectly promotes histone H4 trimethylation at 'Lys-20' (H4K20me3) . Probably by controlling tubulin and/or histone H4 post-translational modifications, plays a role in mitosis and in maintaining chromosome number stability . During RNA virus-mediated infection, acts as a negative regulator of the DDX58/RIG-I pathway by preventing MAVS binding to TBK1 and IKBKE .
Q14166
A9M1A2
GPMA_NEIM0
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
Neisseria
MELVFIRHGQSEWNAKNLFTGWRDVKLSEQGLAEAAAAGKKLKENGYEFDIAFTSVLTRAIKTCNIVLEESDQLFVPQIKTWRLNERHYGQLQGLDKKQTAEKYGDEQVRIWRRSYDTLPPLLDKDDEFSAHKDRRYAHLPADVVPDGENLKVTLERVLPFWEDQIAPAILSGKRVLVAAHGNSLRALAKHIEGISDEDIMGLEIPTGQPLVYKLDDNLKVLEKFYL
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
A9M1A2
Q2RGY0
DNLJ_MOOTA
Polydeoxyribonucleotide synthase [NAD(+)]
Moorella
MDLAAARQRVEELRRLIEEHNYRYYVLDQPSISDREYDALMQELIALEEAYPELRTPDSPSQRVGGAPREEFNQVRHPQVLLSLNDAFNEGDLLEFDRRVRDLAGRPVEYVIEAKIDGLAVALTYRDGLFTLGATRGDGQVGEEVTANLKTIPALPLRLRRPLPFLVVRGEVYMPKVAFTALNAAREEAGEPLFANPRNAAAGSLRQLDPKITASRSLSLFVYQVISLTGAEVATQAGALDFLAELGFPVNPYRVVAPDIQAVLEEVKAWTPERRASLPYEIDGLVIKVNDLALHSVLGATAKAPRWAMAYKFPAEQATARVEGIILRVGRTGVLTPTAVLTPVRLAGTTVSRATLHNEDYIREKDIRIGDTVIVQKAGDIIPEVVAVIPERRTGSEEVFTMPERCPACGAAVVRPPGEAAHRCTGGLACPAQVLEGIIHFASRGAMDIQGLGPAIVAQLLEAGLIHDAADLYYLKEEDLLKLERFGQQSASNLLAAIAASKKQPLERLIFALGIRNVGQRAARVLADHFGSLDKLAAATVEELTALPDIGPRIAENIREFFGEPRNRAVLEKLKKAGVRLEALNAAAPAGPLTGKVFVLTGTLPGMTRQEAEELITRAGGKVSSSVSRKTDYVVAGEKPGSKLDRARELGVPVINADGLRQLLRQ
DNA ligase that 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. It is essential for DNA replication and repair of damaged DNA.
Q2RGY0
Q0RKH4
SSUB2_FRAAA
Aliphatic sulfonates import ATP-binding protein SsuB 2
Frankia
MGAVTVRGLRRAFGSHVVLDQLDLTIAESEFVALVGRSGGGKTTLLRTLAGLDPVAEGSVEVPALRSVVFQEPRLLPWRRVWQNVALGLPRSRGRDEATKALAEVGLADHARAWPLTLSGGEAQRVALARALVREPELLLLDEPFGALDALTRIHMHALVRQLHERHRPAVLLVTHDVDEALELADRVIVLRDGRLDEQIETRELFDDRRDPRFEQARARLLGLLGVTDTHVADPTATPSSAATAP
Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Q0RKH4
Q09158
NIFH_DESMC
Nitrogenase reductase
Desmonostoc
STRLMLHSKAQTSVLQLAAERGAVEDIELHEVMLTGFRDVRCVESGGPEPGVGCAGRGIITAINFLEENGAYTDVDFVSYDVLGDVVCGGFAMPIREGKAQEIYIVTS
The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
Q09158
A6L2M8
GLAB2_PHOV8
Exo-alpha-galactosidase B2
Phocaeicola
MKRIIFNFCFVWLAVSAFAGSKVVEMRNYGLVPDTHENLSPKLQKALQDIKSQVALGDKVTLLFESGRYDFHPEGAAVREYYISNHDQDNPKTVGFPLEDWKGLTVDGQGADFIFHGRMLPLSLLRSENCTLRNFSIDFETPHIAQVKILESGEEGITFEPAAWVKCRINEKGFFEAYGEGWSSAPQGGIAFEEKTKRLVYRTSDLWCPMEGVKEVSPRVYHAPQWKDARLKPGTVVALRTYYRPAPGIFLSNDKDTRLQNVKVHYAEGMGLLAQLCENITLDEFSVCLRGDKDPRYFTTQADATHFSSCRGKIDSRNGLYEGMMDDAINVHGTYLKIKQRLDDHTVIARYMHPQAYGFEWGVNGDEVQFVRSATMELTGGKNRVKEILPNDKDTVKGAKEYRITFAEPLDAEITDKEGFGIENLSWCPEVYFADNVIRNNRARGTLFSTPLKTVVERNLFDHTSGTAILLCGDCNGWFETGACRNVLIRNNRFINALTNMFQFTEAVISIYPEIPDLEHQKKYFHGGKGEKGVVIEDNYFETFDRPVLFAKSIDGLIFKNNVIRQNTDYPAFHHNKSRFRLLHTRNVKIEKNNFEDGDESIARE
Alpha-galactosidase. Removes both branched alpha-1,3-linked galactose residues of blood group B antigens and linear alpha-1,3-linked galactose structures.
A6L2M8
B8DF98
DCUP_LISMH
Uroporphyrinogen decarboxylase
Listeria
MTKITNDLFLKAARKEQVDRIPVWYMRQAGRSQPEYRKLKEKYSLFEITHQPEICAYVTKLPVDQYGVDAAILYKDIMTPLPGMGVDVEIKSGIGPVIHNPIRTFQDVEKLAIFKPEIEVPYVLDTIKLLADDMLDVPLIGFAGAPFTLASYMIEGGPSKNYHQTKSFMYREPEVWAILMEKLGRMTANYLIAQINAGASAVQLFDSWVGALSRADYAKYIRPVIEMIVSEVKAAHPTTPIIMQAVGASHLLAEWETMPLDVVGVDWRETITSAREKVPTKAIQGNLDPSTLLAPAKCLEEAERILQEGVLEPGYIFNLGHGVFPEVPPEMLKKLTNYIHERSEILLKKG
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
B8DF98
A8FHS1
PPAX_BACP2
Pyrophosphatase PpaX
Bacillus
MNESTINTVLFDLDGTLINTNELIIASFQHTLDHYYPGQYSREEILHFIGPSLFDTFSAMDPDLTDDMIQMYRTFNHEQHDLLVTEYETVLDTLKVLQDRGFKLGIVTTKIRDTVLMGLKLTGLEPFFEVIVTLDDVQNEKPHPEPVQLALSKLGSDPHEAVMVGDNYHDILSGQAAGTKTAGVAWSIKGEEALFKHRPDFMLKKMSDLLAIVGAD
Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool.
A8FHS1
A0QDL1
RNZ_MYCA1
tRNase Z
Mycobacterium avium complex (MAC)
MIEVTLLGTGSPIPDPNRAGPSTLVRAGGQVFLVDCGRGVLQRAAAVGVGAAGLSTLLLTHLHSDHVGDLGDVLITRWVSTFTPDPVPLPIIGPPGTAELVAATLNALRHDIGYRIAHHADLNAPPAVDVREHTDGPVWDRDGVSIRVAPTDHRPVAPTIGFRVDYQGASVVLAGDTVPCAGLDELAAGAGALVHTVIRKDIVATIPQQRLQDICDYHSSVEQAAATAARAGVGTLVMTHYVPALVAGQEEQWRALAAREFAGRVELGDDLHRVQVDAPS
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
A0QDL1
Q9KR19
ALAE_VIBCH
L-alanine exporter AlaE
Vibrio
MKARGPFCIRHAAADTFAMVVFCFVTGMIIEIFVSGMTFQQSLASRTLSIPVNIAIAWPYGVFRDYVLRQGRKISPTGWMKNLSDLVAYVLFQSPVYAAILFTVGASTDQIITAVATNALVSCGMGVLYGYFLDMCRRWFKVPGYTVSEG
Exports L-alanine.
Q9KR19
Q55075
RADA_SACS2
DNA repair and recombination protein RadA
Saccharolobus
MSNEVEQKKNIKTINDLPGISQTVINKLIEAGYSSLETLAVASPQDLSVAAGIPLSTAQKIIKEARDALDIRFKTALEVKKERMNVKKISTGSQALDGLLAGGIETRTMTEFFGEFGSGKTQLCHQLSVNVQLPPEKGGLSGKAVYIDTEGTFRWERIENMAKALGLDIDNVMNNIYYIRAINTDHQIAIVDDLQELVSKDPSIKLIVVDSVTSHFRAEYPGRENLAVRQQKLNKHLHQLTRLAEVYDIAVIITNQVMARPDMFYGDPTVAVGGHTLYHVPGIRIQLKKSRGNRRIARVVDAPHLPEGEVVFALTEEGIRDAEE
Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules.
Q55075