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2.75k
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5.51k
AlphaFoldDB
stringlengths
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P0C6B5
DIDLB_ECHCA
Disintegrin schistatin-like subunit B
Echis
NSVNPCCDPQTCKPIEGKHCISGPCCENCYFLRSGTICQRARGDGNNDYCTGITPDCPRNRYN
May bind to both alpha-IIb/beta-3 (ITGA2B/ITGB3) and alpha-V/beta-3 (ITGAV/ITGB3) integrins, and may inhibit platelet aggregation.
P0C6B5
Q9BXF6
RFIP5_HUMAN
Rab11-interacting protein Rip11
Homo
MALVRGAEPAAGPSRWLPTHVQVTVLRARGLRGKSSGAGSTSDAYTVIQVGREKYSTSVVEKTHGCPEWREECSFELPPGALDGLLRAQEADAGPAPWAASSAAACELVLTTMHRSLIGVDKFLGQATVALDEVFGAGRAQHTQWYKLHSKPGKKEKERGEIEVTIQFTRNNLSASMFDLSMKDKPRSPFSKIRDKMKGKKKYDLESASAILPSSAIEDPDLGSLGKMGKAKGFFLRNKLRKSSLTQSNTSLGSDSTLSSASGSLAYQGPGAELLTRSPSRSSWLSTEGGRDSAQSPKLFTHKRTYSDEANQMRVAPPRALLDLQGHLDAASRSSLCVNGSHIYNEEPQGPVRHRSSISGSLPSSGSLQAVSSRFSEEGPRSTDDTWPRGSRSNSSSEAVLGQEELSAQAKVLAPGASHPGEEEGARLPEGKPVQVATPIVASSEAVAEKEGARKEERKPRMGLFHHHHQGLSRSELGRRSSLGEKGGPILGASPHHSSSGEEKAKSSWFGLREAKDPTQKPSPHPVKPLSAAPVEGSPDRKQSRSSLSIALSSGLEKLKTVTSGSIQPVTQAPQAGQMVDTKRLKDSAVLDQSAKYYHLTHDELISLLLQRERELSQRDEHVQELESYIDRLLVRIMETSPTLLQIPPGPPK
Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis.
Q9BXF6
P13009
METH_ECOLI
Methionine synthase, vitamin-B12-dependent
Escherichia
MSSKVEQLRAQLNERILVLDGGMGTMIQSYRLNEADFRGERFADWPCDLKGNNDLLVLSKPEVIAAIHNAYFEAGADIIETNTFNSTTIAMADYQMESLSAEINFAAAKLARACADEWTARTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDGLVAAYRESTKALVEGGADLILIETVFDTLNAKAAVFAVKTEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHAEALTFGLNCALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMAKQIREWAQAGFLNIVGGCCGTTPQHIAAMSRAVEGLAPRKLPEIPVACRLSGLEPLNIGEDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVENGAQIIDINMDEGMLDAEAAMVRFLNLIAGEPDIARVPIMIDSSKWDVIEKGLKCIQGKGIVNSISMKEGVDAFIHHAKLLRRYGAAVVVMAFDEQGQADTRARKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFRGNDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPAELRDAVEDVILNRRDDGTERLLELAEKYRGSKTDDTANAQQAEWRSWEVNKRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFIEASKEQGKTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVAALLSDTQRDDFVARTRKEYETVRIQHGRKKPRTPPVTLEAARDNDFAFDWQAYTPPVAHRLGVQEVEASIETLRNYIDWTPFFMTWSLAGKYPRILEDEVVGVEAQRLFKDANDMLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRDETRTHVINVSHHLRQQTEKTGFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALADAFEAQHDDYNKIMVKALADRLAEAFAEYLHERVRKVYWGYAPNENLSNEELIRENYQGIRPAPGYPACPEHTEKATIWELLEVEKHTGMKLTESFAMWPGASVSGWYFSHPDSKYYAVAQIQRDQVEDYARRKGMSVTEVERWLAPNLGYDAD
Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
P13009
Q4I2M7
ERFB_GIBZE
Ras protein acyltransferase
Fusarium
MASKPDDDGFLAPYVSRSDAQRPLSIVSSRMTDIASEDGDGPEVQNNRLSIPQSTDMGSRPDTARTGASSSRGPWQSQSLRNKTYLAGVQAKRGSVESSTAGSTSQPPSLSSRSHVPSLQSHAFFRPMSSQKLQAQRGGSHRPSTMSQMSAAASPSSPTSPTSPTSPRSDEHGESSSSQMRQSIISNPIAQLQRQMSNEENMRPPPSRGTEMTEQETLDRITANTSPSHGHYPAGSLTDSVRPLQGMSSDTGHFQHSIIVDKSYKDLSNLPSPIKTPRSFRSSFLMPGRSNDGQLSQNRSTEGAEKLSSAASSPQFRPVDSHNEQQHPRVPYKPSQKSDLGRVHQYFDGNTVFCLGGRWQNTRGRPINIATGIFVVVPCALFFGFEAPWLWNNVSPAIPIVFAYLAYICFSSFIHASVTDPGILPRNLHQFPPVDDDDDPLQLSPPTTDWALIKSAESTTAAMEVPVKHCRTCNIWRPPRAHHCRLCDNCIETHDHHCVWLNNCVGKRNYRYFFTFVTSATVLAAYLIATSLTQILLYRNRQGISFGQAVDHFRVPFALVFLGFITFLYPAALMGYHIFLMARGETTREYMNSHKFAKKERFRAFSQASVFKNFIVVLCRPRQPTYYQFKAHYHEGDQRLGIRRDKRPRSSSQGLEMHDVNPGSSGFQGPVSLRNDTPH
Palmitoyltransferase specific for Ras proteins.
Q4I2M7
B0FWD1
COX3_AEDAE
Cytochrome c oxidase polypeptide III
Stegomyia
MSTHANHPFHLVDYSPWPLTGAIGAMTTVTGLVQWFHQYDNTLFLLGNIITMLTMYQWWRDISREGTFQGLHTIPVTLGLRWGMILFIISEVFFFISFFWAFFHSSLSPTIELGMVWPPIGIEPFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHTQTIQSLFFTVLLGIYFSILQAYEYIEAPFTIADNVYGSTFFVATGFHGLHVLIGTSFLLICLFRHMNCHFSSSHHFGFEAAAWYWHFVDVVWLFLYISIYWWGN
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.
B0FWD1
B6JCI3
DNAK_AFIC5
Heat shock protein 70
Afipia
MGKVIGIDLGTTNSCVAVMDGKSPRVIENAEGMRTTPSIVALTDDDERLVGQPAKRQAVTNPEKTIFAVKRLIGRRYDDPTVAKDKDLVPYKIVKASNGDAWVEADGKIYSPSQISAFILQKMKETAEAHLGQKVDQAVITVPAYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKAKQGTIAVYDLGGGTFDVSVLEIGDGVFEVKSTNGDTFLGGEDFDMRLVGYLADEFQKEQGINLRNDKLALQRLKEAAEKAKIELSSTTQTEINLPFITADASGPKHLTMKLTRAKFEALVDDLVQKTIEPCRKALKDAGLSAGEISEVVLVGGMTRMPKIQEVVKQFFGKEPHKGVNPDEVVAIGAAIQAGVLQGDVKDVLLLDVTPLSLGIETLGGVFTRIIERNTTIPTKKSQVFSTAEDNQNAVTIRVFQGEREMAADNKALGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATGKEQQIRIQASGGLSESEIEKMVKEAEANAAEDKKRREAVDAKNHADALVHSTEKALAEHGSKVGEGERKAIEDALADLKEALKGDDSEAIKAKSNTLAQASMKLGEAMYQQQAEGDAARDAAQDAAKDDVVDAEFTEVDDDKNDKKSA
Acts as a chaperone.
B6JCI3
Q2IX83
KGUA_RHOP2
GMP kinase
Rhodopseudomonas
MKDGAAGSLNGIERRGLMFVLSSPSGAGKTTLSRMLVDEAPGLRMSVSATTRPKRPGEVDGRDYYFVDRPKFDAMVEAGEFLEWANVFDNCYGTPRAPVEAALSAGNDVLFDIDWQGTQQLRSRASNDVVSVFILPPSVQDLEHRLHTRAQDSDEVIRGRMKKAGDEMSHFDAYDYIVVNDNIGVAFESVKAILRAEQLKRERQIGIDAFVREMRRELEK
Essential for recycling GMP and indirectly, cGMP.
Q2IX83
A0KU07
DEOC_SHESA
Phosphodeoxyriboaldolase
Shewanella
MTDLKKAAQRAIELMDLTTLNDDDTDQKVIDLCHKAVTPAGNTAAICIYPRFIPIARKTLDELGAEDIQIATVTNFPHGNDDIAIAVLETRAAVAYGADEVDVVFPYRALMEGNESVGYELVKACKEACGDVLLKVIIESGVLADPALIRRASELSIDAGADFIKTSTGKVPVNATLEAAEIMLTVISEKNTKVGFKPAGGVRDAAQAAEFLGVAERILGADWVSPRTFRFGASSLLNSLLHTLELADAPKPTQGY
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
A0KU07
A8W3I9
RR4_CUSOB
Plastid 30S ribosomal protein S4
Cuscuta sect. Cleistogrammica
MSRYRGPRFKKIRRLGALPGLTNKSPRAIRDLRNQSRSEYRIRLEEKQKLRFHYGLTEKQLINYVQIARKAKGSTGKVLLQLLEMRLDNILFRLGMASTIPAARQLVNHRHVLVNGRLVDRPSYRCKPRDIIMPKNTTKSGVLVQNSLELFTGKELANHLNLFSTPYKGLVNKIVDTNWIGLKINELLVVEYYSRQA
With S5 and S12 plays an important role in translational accuracy.
A8W3I9
B1XQH8
RLMN_SYNP2
tRNA m2A37 methyltransferase
unclassified Synechococcus
MPQDVLLGKSLPELTDWIETTGQPAYRGKQLYNWLYQKGIHDLSEITVFPKAWREQMGTYPVGRSQIHHQRTAPDGTRKYLLQLHDGLIIETVGIPTEKRLTVCVSSQVGCAMACDFCATGKSGFTRHLQAHEIIDQVLTVQTDFQQRVSHVVFMGMGEPLANLEQVLKSIQSLNQDIGIGQRSLTVSTVGVPDQIRALAQQNLQITLAVSLHAPNQALRESIIPTAVHYPIEALLDECREYVAITRRRLSFEYILLAGVNDLPDHAAELAKKLKGFQSHVNLIPYNPITEVPFQRPGKKRINVFKQILQDHKIAVSVRYSKGLEADAACGQLRSNLRRSAPATVK
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
B1XQH8
C6C1J9
RL13_MARSD
50S ribosomal protein L13
Maridesulfovibrio
MKTYIPKDEDINREWFVVDAENMVLGRLATQIANKLRGKDKAMFTPHVDTGDFVVVLNADKIKVTGNKMDQKTYYKHTNHPGGLKERTLKVMLEKKPEVVIETAVRGMLPKNRLGKQMIKKLKVYAGTEHPHTAQQPKVLEF
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
C6C1J9
Q3KMX6
AMPA_CHLTA
Leucyl aminopeptidase
Chlamydia
MVLLYSQASWDKRSKADALVLPFWMKNSKAQEAAVVDEDYKLVYQNALSNFSGKKGETAFLFGNDHTKEQKIVLLGLGKSEEVSGTTVLEAYAQATTVLRKAKCKTVNILLPTISQLRFSVEEFLTNLAAGVLSLNYNYPTYHKVDTSLPFLEKVTVVGIVSKVGDKIFRKEESLFEGVYLTRDLVNTNADEVTPEKLAAVAKGLAGEFASLDVKILDRKAILKEKMGLLAAVAKGAAVEPRFIVLDYQGNPKSKDRTVLIGKGVTFDSGGLDLKPGKAMITMKEDMAGAATVLGIFSALASLELPINVTGIIPATENAIGSAAYKMGDVYVGMTGLSVEIGSTDAEGRLILADAISYALKYCNPTRIIDFATLTGAMVVSLGESVAGFFANNDVLARDLAEASSETGEALWRMPLVEKYDPALHSDIADMKNIGSNRAGSITAALFLQRFLEDNPVAWAHLDIAGTAYHEKEELPYPKYATGFGVRCLIHYMEKFLSK
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Q3KMX6
B1XXH2
RL9_LEPCP
50S ribosomal protein L9
Leptothrix
MQVILLEKVANLGVLGDVVKVKDGYARNFLIPTGAARRATEKAVAEFQARRAELEKVQAEKLAAAKAQGDKLAGKTVSISQKAGVDGRLFGSVTNADIAESLKALGFDVVKAQIRLPNGPLKTVGEFPVSVALHTDAVVEITVAVVGEHV
Binds to the 23S rRNA.
B1XXH2
Q99KF0
CAR14_MOUSE
Bcl10-interacting MAGUK protein 2
Mus
MAELCRMDSTLTALDEEMLWDMLESHRCRIVQSICPSRLTPYLRQAKVLGQLDEEEILHSSRFTNSAMRVGHLLDLLKARGKNGAIAFLESLKFHNPDVYTLVTGLQSDIDFSTFSGLMETSKLTECLAGAISSLQEELAQEKAQKEVLLRRCQQLKERLGLAEAHAEGLRQLEVDHSRMKREVSTHFHEVLKLKDEMLNLSLHYSNALREKELAATRCHSLQEELYLVKQELQRASLVSSCERESRERSLKMASNLEPQGEELNRLKEENEKLRSMTFSLVEKDILEQSLDEARESKQELVDRIHSLRERAVAAERQQKQYWEEKEQTLLQFRKTQVDCELYKEKMTMLQGQVAELQKERDQAYTARDRAQMEISQRLVEKDALRRRVFELTEQVCELRTQLRRLQAEAPGGPKQEAGARELCLRGKQRLVRMHAVCPPDDSDCSLLSSTESRLWWDLNSTSSREQMDSFRSSSPMPPSQQSLYKRVAEDFLEDPESLSFPEVLEMRLQGATVDDTDTDLEFEMIDGADLSQTEDSLQGSSRSLNVSESSVPVRRRPARKILSQVTVLAFQGDALLEQIGVIGGNLTGIFIHRVTPGSAADEMALRPGTQIMMVDYKPTKPSLRATLENTTLEQAVGLLRRVNGSCYLSVKINTEGYKNLIQDLDAKVVTSGDSFYIRVNLAMQRGGDGELQTHCNDILHVTDTMFQGRSCWHAHHVNPYTMKDMEPGTIPNYSQAQQQLLALIQDMTQRCTVPRKPPGGPQKLVRIVSVDKAAVSPLTSSFDQSQWDSGKEEGGPSVCFWSESCFTLAPYTLVHPHRPARPRPVLFVPRLVGRILGKKLCLLQGFKQCSAEYLSQEEYATWSQRGDIIQEGESIGDHHWITRHAVESLMNMSTHALLDVRLDSVRVLHRMDMFPIIIHVSVNEKTAKKLRKGLHRLGSSEEQFLEVARQEEGELDRVPCLYSSLAPDSWSDLDSLLSCVRLAIADEQKKVVWTESPC
Acts as a scaffolding protein that can activate the inflammatory transcription factor NF-kappa-B and p38/JNK MAP kinase signaling pathways. Forms a signaling complex with BCL10 and MALT1, and activates MALT1 proteolytic activity and inflammatory gene expression. MALT1 is indispensable for CARD14-induced activation of NF-kappa-B and p38/JNK MAP kinases. May play a role in signaling mediated by TRAF2, TRAF3 and TRAF6 and protects cells against apoptosis.
Q99KF0
P10168
IL7_MOUSE
Interleukin-7
Mus
MFHVSFRYIFGIPPLILVLLPVTSSECHIKDKEGKAYESVLMISIDELDKMTGTDSNCPNNEPNFFRKHVCDDTKEAAFLNRAARKLKQFLKMNISEEFNVHLLTVSQGTQTLVNCTSKEEKNVKEQKKNDACFLKRLLREIKTCWNKILKGSI
Hematopoietic cytokine that plays an essential role in the development, expansion, and survival of naive and memory T-cells and B-cells thereby regulating the number of mature lymphocytes and maintaining lymphoid homeostasis . Mechanistically, exerts its biological effects through a receptor composed of IL7RA subunit and the cytokine receptor common subunit gamma/CSF2RG. Binding to the receptor leads to activation of various kinases including JAK1 or JAK3 depending on the cell type and subsequently propagation of signals through activation of several downstream signaling pathways including the PI3K/Akt/mTOR or the JAK-STAT5.
P10168
Q9UZ78
TMCA_PYRAB
tRNA(Met) cytidine acetyltransferase TmcA
Pyrococcus
MTIKIRFPKDVREYARKEKVKESIIKLTETSLAEAITNFHRRMIILQGDTLEKAKLAGILAGGVARILSEYIPEFLDRKLRDEDKIEVLYATDALGEDTYGRKRFEEFRKHFSVLAPNAELTSVTFKYSRDILGRTFDILVLDLSYDYSPNDLGRIIETVRGGGLIFILTNPFEKWKDMWTGFHKSLVTPPYTIDDVKKRFNRRLIRKFTEHKGIYIVDADKKKIERRPRKNKSQAKLPEREKVEIPRDIKFPRELYELCLTRGQVEVLKALEDLIENPGMVVLTADRGRGKSVSVGIASIGLAITSKKKNFRIVVTAPELENVQSLLKFAERSLKVLGYKTKTVKESGLIKEVYAKGIGIRYYPPTKGYRQKADLYIVDEAAGIHVPILHRYLEKERVVFSSTIHGYEGAGRGFSVKFLKKAKEKREYKEIHLSVPIRYAEGDPIERWLFDVLLLDAEPVELTEEDYELIRKMEVYLEEPDLDDWFENDREDLRHFVGIYVLAHYRNRPSDVALLADAPHHEARVLRLKNGKIVTAIQIAKEGGIPKAVIDKMAKGYKPPGNIIPDMMVKHHYAKEFAKLRGYRIVRIATHPDAMDLGLGSKALELLVKEAQEKGLDWVGSGFGASEELIRFWVRNGFAVVHLSPTRNPVSGEYTAIVIKPISERAKEIVKKANDEFRLRLTEWLGDTHRDLEPEIARWLFETPFGEAVNYPIHLTKVQRKRLEMFIKRVLTYDTVVDAVKPLVKLYFLDGWMRPYLDDRQIALLIHRVLQAHDWKETAKLLNRTELYTMIELRDIVRGLWYYYKHMLKDEEKDIS
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Q9UZ78
Q0B5V4
ARAG2_BURCM
Arabinose import ATP-binding protein AraG 2
Burkholderia cepacia complex
MTMQTITAVSGNDDAATHGAAAPPGGALLSLDGITVTFPGVRALDAVSLSVRAGEVHGLMGENGAGKSTLLKVLSGVNQPQAGTLTLNGTVQRFASTRAALEAGIAIIYQELHLVPELTVAENLMLGQLPSRLGVVDERALAVRALDALERLGEHIDPDIPVKYLSIGQRQMIEIGKALMRDARVIAFDEPTSSLSARETTQLFRIIRSLRAEGRAIIYVTHRMEEVDALCDRVTVFRDGRRIETFESVAELDRDQLIGCMVGRSIEDVYGYRPRAAGDVMIEAKGLTGPGLSEPVSFAARRGEIVGFFGLVGAGRSELMKLLYGATRPSGGHVELGGKRVAFSSPRHAVRAGIALCPEDRKQEGIVAIASVADNLNISARRHFSPARVLLDARRERDLAQRYIERLAIKTPDGDTPIGALSGGNQQKVVLARWLAERIDVFLMDEPTRGIDVGARAEIYNLFYELAEAGRTVILVSSDLAEVIGVSDRIIVMKEGRIAGEVAKAQATPDALIKLALPR
Part of the ABC transporter complex AraFGH involved in arabinose import. Responsible for energy coupling to the transport system.
Q0B5V4
B4U501
RL4_STREM
50S ribosomal protein L4
Streptococcus
MANVKLFDQTGKEVSTVELNDAIFGIEPNESVVFDVVISQRASLRQGTHAVKNRSAVSGGGRKPWRQKGTGRARQGSIRSPQWRGGGVVFGPTPRSYGYKLPQKVRRLALKSVYSAKVAEDKFVAVESLSFAAPKTAEFAKVLSALSIDTKVLVLVEEGNEFAALSARNLPNVAVATAATASVLDIVSADKLLVTKEAISTIEEVLA
Forms part of the polypeptide exit tunnel.
B4U501
B7GV10
DAPB_ACIB3
4-hydroxy-tetrahydrodipicolinate reductase
Acinetobacter calcoaceticus/baumannii complex
MSAAPRIGILGAGGRMGRILIQAVQQAGYQLGAAVVRPESTLIGADAGELAGIGSIGVKLTGSLAEVLEDCDVVIDFSTPAATSEHLKLCREAGVAIVIGTTGMSDEQKAELDETAKHIPVVYAANYSVGVNVSIKLLELAAKVFGDTVDIEVIEAHHRHKVDAPSGTALMMGEAIADTLGRNLKEVAVYGREGHTGPRDRQTIGFETIRGGDIVGEHTVMFIGEGERVEVTHKATNRMNFAAGAVRAAAWVVGREARKYDMKDVLGLNDVQV
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
B7GV10
A0QP27
MMPL3_MYCS2
Mycobacterial membrane protein large 3
Mycolicibacterium
MFAWWGRTVYQFRYIVIGVMVALCLGGGVYGISLGNHVTQSGFYDEGSQSVAASLIGDEVYGRDRTSHVVAILTPPDDKKVTDKAWQKKVTEELDQVVKDHEDQIVGWVGWLKAPDTTDPTVSAMKTQDLRHTFISIPLQGDDDDEILKNYQVVEPELQQVNGGDIRLAGLNPLASELTGTIGEDQKRAEVAAIPLVAVVLFFVFGTVIAAALPAIIGGLAIAGALGIMRLVAEFTPVHFFAQPVVTLIGLGIAIDYGLFIVSRFREEIAEGYDTEAAVRRTVMTSGRTVVFSAVIIVASSVPLLLFPQGFLKSITYAIIASVMLAAILSITVLAAALAILGPRVDALGVTTLLKIPFLANWQFSRRIIDWFAEKTQKTKTREEVERGFWGRLVNVVMKRPIAFAAPILVVMVLLIIPLGQLSLGGISEKYLPPDNAVRQSQEQFDKLFPGFRTEPLTLVMKREDGEPITDAQIADMRAKALTVSGFTDPDNDPEKMWKERPANDSGSKDPSVRVIQNGLENRNDAAKKIDELRALQPPHGIEVFVGGTPALEQDSIHSLFDKLPLMALILIVTTTVLMFLAFGSVVLPIKAALMSALTLGSTMGILTWMFVDGHGSGLMNYTPQPLMAPMIGLIIAVIWGLSTDYEVFLVSRMVEARERGMSTAEAIRIGTATTGRLITGAALILAVVAGAFVFSDLVMMKYLAFGLLIALLLDATIIRMFLVPAVMKLLGDDCWWAPRWMKRVQEKLGLGETELPDERKRPTVRESETDQRALVGVGAPPPPPRPHDPTHPAPEPVRPMPPMRSNAPSAAGTARISTPPQPPQPPQAPAQQAGDEPATTRFAMARNAVRNAVNSAVHGGAGSAAAPTERAPRPGGPAQPPAPPQREEREIESWLGALRGPAPAKNVPQPPAQPQRPSTDTTRAMPPQGRPPAGPADRGNENAPTTAFSAQRPPNGGAPADATTAIPTPPQREQEPSTEKLNTREDAPEDPETKRRGGGMSAQDLLRREGRL
Transports trehalose monomycolate (TMM) to the cell wall . Flips TMM across the inner membrane. Membrane potential is not required for this function . Transports probably phosphatidylethanolamine (PE) as well. Binds specifically both TMM and PE, but not trehalose dimycolate (TDM). Binds also diacylglycerol (DAG) and other phospholipids, including phosphatidylglycerol (PG), phosphatidylinositol (PI), and cardiolipin (CDL) . Contributes to membrane potential, cell wall composition, antibiotic susceptibility and fitness .
A0QP27
Q47ZU7
AZOR2_COLP3
FMN-dependent NADH-azoreductase 2
Colwellia
MITLLHIDTSARRTDNDVKEYNSISKSLAAHFMDKWITLNSKDKVIYRDLGLNPPDFISQDWIAAVFTPDEKQSEEQKSLLTLSDTLIDEVDQADIIVISSPMYNYGMPAVLKAWFDQVVRINKTFTFDLARGDFPIEPIMSGKKLILISSSGEFGFEIGGIREKMNYLAPHVETASKYLGVEEFYEIKSEYQEFADARHEESLSNAYRGVEELVKQLV
Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
Q47ZU7
B8FET3
RL23_DESAL
50S ribosomal protein L23
Desulfatibacillum
MNVYEIIRRPVVTEKSTIQKEENNQLTFEVDKKANKVEIARAIERIFKVKVLDVRTSTVNGKFKRRGKVLGKRRDWKKAMVTLAPGARIDFFDGV
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
B8FET3
Q3E906
CD205_ARATH
Cell division cycle 20.5, cofactor of APC complex
Arabidopsis
MMNTSSHLKAQASCPLVEHFLRRKLSKENFDRFIPNRSAMDFDFANYALTQGRKRNVDEVTSASRKAYMTQLAEAMNQNRTRILAFRNKPKALLSSNHSDPPHQQPISVKPRRYIPQNSERVLDAPGIADDFYLNLLDWGSSNVLAIALGDTVYLWDASSGSTYKLVTIDEEEGPVTSINWTQDGLDLAIGLDNSEVQLWDCVSNRQVRTLRGGHESRVGSLAWNNHILTTGGMDGKIVNNDVRIRSSIVETYLGHTEEVCGLKWSESGKKLASGGNDNVVHIWDHRSVASSNPTRQWLHRFEEHTAAVRALAWCPFQASLLATGGGVGDGKIKFWNTHTGACLNSVETGSQVCSLLWSKSERELLSSHGFTQNQLTLWKYPSMVKMAELNGHTSRVLFMAQSPDGCTVASAAGDETLRLWNVFGEPPKTTKKAASKKYTDPFAHVNHIR
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Q3E906
Q4HZE0
ALG10_GIBZE
Dolichyl-phosphoglucose-dependent glucosyltransferase ALG10
Fusarium
MGSSSPAQTSNWYELFTGNWLSRPIRAVLVGALALPFVIWPRNQPQNSNPRLLAFFVYLLHLASIPWLYLVTKLVPEPYLDEIFHIPQAQKYCQGRFLEWDDKITTPPGLYLVSLITPGVVQRNGYLDYACSVQNLRAFNVFALAVLAYLALQCRREIEARLYEARFSTRLSNTSQYAVHTAFNIAFFPLLFFFSGLYYTDVASTAAVLVAFLNHLKRIGRDQNSVLSDLVTISLGVFTLFFRQTNVFWVVVFMGGLEAVHAVKTLRPERVDQPVILTLSEQLKHYAWRCSLGDVHDPPLHAMWPDDMIFCVLSLGIAALCNPIRVIRQIWPYITTLLLFGSFVAWNGGVVLVGDKSNHVATIHLPQMLYIWPFFAFFSLPLLIPYALPLANALRRLLYMKTSSWSISSSSNKSLSRKSSSKVSNSKGDVAVDAPGSEYPQPSKELQYFEVVFGSKIFLWPLYLLGTIIFSFGIVHYNTIIHPFTLADNRHYMFYVFRYTIRRAAWIRFALVIPYTVARWMTWGTMAGCSQWFMTMHGPACSAYSKGDGKSPFLNHPAFTNRGASPQQTDAAPPAEVKDLDANQQQELSQALKKDPLLASVEPATTSTGLIFLLATTLSLMTAPLVEPRYFIIPWVMWRLLVPAWKFHDHDSEGVAATLERHPKTKPLLLFLQRYDLRLILETFWFIVINAVTGYIFLTKPYVWKAEDGTVLDGGRLQRFMW
Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Q4HZE0
A6LP38
TMCAL_THEM4
tRNA(Met) cytidine acetate ligase
Thermosipho
MKVLGVIVEYNPFHNGHLYHLQQAKKIVSPDYVIAIMSGNFCQRGEPAIINKFARAEIALKNGIDVVFELPTVYALQDAGGFAFGAITLLDKLTVVTDVVFGSESADKNFITTVAKTLLENPDKFDNLLKIELKKGLSFPNARKFALKKFLNENEDFLKMIENSNDILGIEYVKSILKLKSKINYHLIKRIGAKYNDTELESKYSSATAIRNAIVRNNPFETYVPQTSYKVLKREFSYGRGPVSLENMEQFILTFLRLKHRKDFESIYSFTEGLDQRFIKAIKTSKKLSDFLEKVKTKRFTYSRIRRAIFHALFDFKKEYIEFSNKLGTQYARILGFTKKGQKLLSKIKKASKIPIISNPSLHEKVLKKVLTDKDRKWEVNKKLFIWQFEKDIVASNIYTMFYPQKNERKYGLDFRKPIIEGENE
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.
A6LP38
Q1CXC6
PAND_MYXXD
Aspartate 1-decarboxylase alpha chain
Myxococcus
MRRILFKSKIHRATVTQADLDYEGSVTIDRDLLRAADIVENEKVAVWNITQGTRLETYALEGEAGSGVICINGAAAHLNKPGDLVILATFAEVEEAEVANWKPTVVFVDKDNRVVPGQTKEIPGPQRRSA
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Q1CXC6
P46883
AMO_ECOLI
Tyramine oxidase
Escherichia
MGSPSLYSARKTTLALAVALSFAWQAPVFAHGGEAHMVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEIKQAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADVIMLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFAAAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNYWAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKPMQIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKRKVMYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMGTLTSPIARGKDAPSNAVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERRELVVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETAKDDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQIIPYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKYPNRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWVHTLLKPWNFFDETPTLGALKKDK
The enzyme prefers aromatic over aliphatic amines.
P46883
B7KQ65
NUOB_METC4
NDH-1 subunit B
Methylorubrum
MALTPTFSRAPDIAPAPKGIIDPATGRPIGANDPTFLSINDELADRGFLVTSADELINWARTGSLMWMTFGLACCAVEMMQMSMPRYDCERFGFAPRGSPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYSVVRGCDRVVPVDIYVPGCPPSAEALLYGVLLLQRKIRRIGTIER
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.
B7KQ65
Q2T9M9
JHY_BOVIN
Jhy protein homolog
Bos
MSHSKFIPTVSIQSPVHHTNIKVQSTEPSFKKEDLHLISKDSLESDSESPTQKIKSQSDLEDQIQDNDMEPDSLEEENLSETEEEASRKAAQRAKKENLHTQDAAAINSRQPTEDKYSHIRYDPNWKSKKEEGKLLPVEALPESVDSSTENLTLNPLYPSKEPSMDLSAGKGEQKSPRSTASLLGSEFVSPNYELSTHRTEPFSVLSDSDPEEKSSNLSRYLKSSSSRSEAFLPGSRGPRRRKSKQYFVEKNKLTLGLPTPRMDSYLQLHNKKRGEGHLEQISYPVRVTDKTSIQNARETGNVAIDPEDKWHQRAQQLKDYQEHWSQYEHEKSSSGPRGQSSETTNGQQPSRKPAKHKIRKQRRHRHGPKSLVTEELVVSQGNQNNTPRHQQNPNKPIDTEVTQETVVIMNATNDDLQYSSVLRSQDPTVTSNQYAPLHQISDKVLYKNPARYYPVTNANRERGHNDQEEKRFSYQQLHIDTLSDMHLNYLHELNKKHPSGSQKGSQSVSNINRQASTEKKKQPKLAYTETKYKNLEILWKFHSSSEEQPAKASPDSRLSQIMEQHQQALLQLTEVQPHEGASPGLTLPPILPRVESESQLSSERSQRNQVKISRSNSESYLFQLEKGKKHRKRSSIKSSKLKGYQNRDVKLGGLGPDLESIRDKMQKLIQQKEYAKQVKEYNMKALSIPSKPQTAITENKSAVPRQKALEYAKTIPKPKPSNLSDQASKEKKTPTHAGKEDTLPEISLLEVLQNRHEREKQAVAAFKVLHIV
Required for the normal development of cilia in brain ependymal cells lining the ventricular surfaces.
Q2T9M9
Q8DEB6
MURA_VIBVU
UDP-N-acetylglucosamine enolpyruvyl transferase
Vibrio
MEKFRVIGSTQPLVGEVTISGAKNAALPILFASILAEEPVEVANVPHLRDIDTTMELLKRLGAKVERNGSVHVDPSSIDEYCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHITGLEQLGATITLEDGYVKAHVDGRLQGAHIVMDKVSVGATITIMCAATLAEGTTVLDNAAREPEIVDTAKFLNTLGAKISGAGTDTITIEGVERLGGGKHAVVADRIETGTFLVAAAVSGGKVVCHNTQAHLLEAVLAKLEEAGALVETGEDWISVDMTGRELKAVNIRTAPHPGFPTDMQAQFTLLNMMAKGGGVITETIFENRFMHVPELKRMGAKAEIEGNTVICGDVERLSAAQVMATDLRASASLVIAGCIAKGETIVDRIYHIDRGYDKIENKLNALGAKIERFRESN
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Q8DEB6
Q8D2R2
ISPH_WIGBR
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
Wigglesworthia
MNIFLANPRGFCAGVDRAINIVKNAIEIYGPPIYVYNEVVHNKYVVNSLKKIGSIFVKKICDVPEKSILIFSAHGVSKSILKEANKRKLIIFDATCPLVSKVHHEIKRASKLRSEVIIIGHKNHPEIIGTIGQYNNPNKKVFVIQSIEEICKLKIKDPNNLFYFTQTTLSVDDTNKIIFAIKKKYPYIIEPRKKDICYATENRQKSIKKIIKLVDIIFIIGSKNSSNSNRLFEIANKSGKKSYLIDTYKEIKKSWLNGVNNIGITAGASAPEILVQQVVNYLKIFYKNSVNIYQVDGDIEKTKFMIPKKLILKIK
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Q8D2R2
B2FPI7
PYRD_STRMK
Dihydroorotate oxidase
Stenotrophomonas maltophilia group
MYSLARPFLFSLDAERAHGLGLSALDLAYRTGTTPLLAARIAPMPSTVFGLTFPNPVGLAAGLDKNGEHIDALFALGFGFVEIGTITPRPQAGNPQPRLFRLPEHNAIINRMGFNNAGVDALVRNVERARNRRGLLGINIGKNKDTPNEQAVDDYIACLDKVYPLADYITVNISSPNTAGLRELQEETALRQLVSQLRDRQEDLAARHGRRVPMLVKVAPDLSDRDIDAAARVLGELQVDGVIATNTTIDHSKVAGDPLANEAGGLSGAPVLEQSTLVLRRLRSRLPESVPLVGVGGILSGADAVAKMAAGAALVQCYSGLIFRGPALVSECVEAIRRRREAPSRGAVAPL
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
B2FPI7
O77469
FBLN1_CAEEL
Fibulin-1
Caenorhabditis
MRICFLLLAFLVAETFANELTRCCAGGTRHFKNSNTCSSIKSEGTSMTCQRAASICCLRSLLDNACDSGTDIAKEEESCPSNINILGGGLKKECCDCCLLAKDLLNRNEPCVAPVGFSAGCLRSFNKCCNGDIEITHASEIITGRPLNDPHVLHLGDRCASSHCEHLCHDRGGEKVECSCRSGFDLAPDGMACVDRNECLTRQSPCTQSEDCVNTIGGYICQRRISRLVPHRHRANRIGNAPRRMRDDPYSRAGEYREASQANTEFGCPMGWLFQHGHCVDVDECNLGSHDCGPLYQCRNTQGSYRCDAKKCGDGELQNPMTGECTSITCPNGYYPKNGMCNDIDECVTGHNCGAGEECVNTPGSFRCQQKGNLCAHGYEVNGATGFCEDVNECQQGVCGSMECINLPGTYKCKCGPGYEFNDAKKRCEDVDECIKFAGHVCDLSAECINTIGSFECKCKPGFQLASDGRRCEDVNECTTGIAACEQKCVNIPGSYQCICDRGFALGPDGTKCEDIDECSIWAGSGNDLCMGGCINTKGSYLCQCPPGYKIQPDGRTCVDVDECAMGECAGSDKVCVNTLGSFKCHSIDCPTNYIHDSLNKNQIADGYSCIKVCSTEDTECLGNHTREVLYQFRAVPSLKTIISPIEVSRIVTHMGVPFSVDYNLDYVGQRHFRIVQERNIGIVQLVKPISGPTVETIKVNIHTKSRTGVILAFNEAIIEISVSKYPF
Involved in the assembly of the flexible hemicentin-containing tracks found joining the pharynx and body-wall-muscle basement membranes.
O77469
O94330
NAGS_SCHPO
N-acetylglutamate synthase
Schizosaccharomyces
MQKPSLSQDLIWILKSVQSRRSTKGFLQKHSSLKDGSPNKKSFAQPISSSFLNRISITKIDDVDSLSDNTLYGIGRSINSLARLGIQSVIVPTSNPIGMTSPFKYLENGTVVAKKRKLSIFEELQQQQNRVIRVSEIFSKAGVLTRPSYSSVCQLGPEGPSVENVQGIFQALSSLYTVIVPSSILMPNVIEVPIDGNEVLAGLTYSLHKPNFGFWVDRIVILDKNGGMPCSKRQTGSSHVLINLAQEFDELAKTLPPYHRKNLILVRRCLKMLPDDASALITTPEDAMLTNPVLDKNPLIHNVLTDRSIISCSLPRDRSPITKTTVLRSGVPVYTFLGPKCLTDGSVSWERLWVLINDSFKRTLDMDAYLDRLKNSLAAVIIAGDYLGTAIVTYEQPDGTTNEKVPYLDKLAVSQGAQGSAAISDVMFNVMTDLFPKELIWRSRLTNPVNKWYFERSVGSLKSSKTPWKLFWTGDSHVRNLDRVNQYMSVIDKIQPTWLN
N-acetylglutamate synthase involved in arginine biosynthesis.
O94330
P63959
DLTC_STRP1
D-alanine--poly(phosphoribitol) ligase subunit 2
Streptococcus
MSIEETVIELFDRLFMEDVSEMMDEDLFDAGVLDSLGTVELIVELESTFNIKVPISEFGRDDWNTVTKIVQGVEELQHA
Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
P63959
B0TAZ6
DDL_HELMI
D-alanylalanine synthetase
Heliomicrobium
MMKQTIAVICGGRSGEHEVSLTSAQSIVDALDRFRFNVLTIGIDRHGAWWLGSNVIDNLRKGQQPYGQRVYFIPDPTCPGLIEENPVTRKPVPVDVFFPVLHGPNGEDGTIQGLFEAANVPYVGCGVLASACGMDKAIMKALFAQSDLPQLPYLVVLRNRWESAREQVIDEVEDRLGYPCFVKPANMGSSVGISKATNRAELVAAFDDAVRYDRKLIVEKGINVREIEVSVLGNDEVVASVPGEIVPAHEFYDYDAKYAAADSRLLIPAPIAAADVATFQEMAIRAFRAIDGSGLSRVDFLLDKNSGEVYINEINTLPGFTSISMYPKLWEATGIPYGELLSRLVDLGLARYREKQRNATERLPRL
Cell wall formation.
B0TAZ6
Q30KJ5
DB134_PANTR
Defensin, beta 134
Pan
MKPLLVVFVFLFLWDPVLAEMHKKCYKNGICRLECYESEMLVAYCMFQLECCVKGNPAP
Has antibacterial activity.
Q30KJ5
Q927Q9
FDHD_LISIN
Sulfur carrier protein FdhD
Listeria
MDIVSRQKVRRFEAGTFQEIESSVATEYPLTIYVNDQELVTIVCTPEHLEDLVVGFLTSEGIVRGPGDIDSVDIIEATGHAKVSANFVNKFNAKYRGKRYITSCCGKSRENFYFQSDASLVNVKQNSNLKLTTDRIFRLMEKFEQNSATFHQTGGVHNAALCSSAEIIYSRMDIGRHNALDKIYGRALKDGTATDDKAIIFSGRISSEILVKTAKLGCGIILSRSAPTELAINMAEELNITTVGFIRGDRLNVYSGFERIT
Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH.
Q927Q9
Q23280
DAF41_CAEEL
p23/cytosolic prostaglandin E synthase 3 homolog
Caenorhabditis
MAKQPTVLWAQRESLVYLTIEVDEAKIEELKGEGNKLHFQGSSKTDKYEATLEFFDEIDPASVKHTGSSTRVVEITVQKKTPAWWPRLLQNKGKVHWLKVDFGKWKDEDEDDEAEDAGAGIGGGMANGFDLNQYMSQMGGAGGADFGGLEDDEEDDDMPDLEDNEEEEGKNGTRA
Co-chaperone for hsp90/daf-21 . Involved in regulation of longevity, larval entry and exit from the dauer stage of development and response to environmental cues, such as oxidative stress, in a temperature-dependent manner. Role in daf-16 and hsf-1 inhibition at elevated temperatures .
Q23280
Q01888
GDC_BOVIN
Mitochondrial solute carrier protein homolog
Bos
MAAAAAALAATEPPPAMPQAAGAGGPAARRDFYWLRSFLAGGIAGCCAKTTVAPLDRVKVLLQAHNHHYRHLGVFSTLRAVPKKEGYLGLYKGNGAMMIRIFPYGAIQFMAFEHYKTLITTKLGVSGHVHRLMAGSMAGMTAVICTYPLDMVRVRLAFQVKGEHTYTGIIHAFKTIYAKEGGFLGFYRGLMPTILGMAPYAGVSFFTFGTLKSVGLSYAPTLLGRPSSDNPNVLVLKTHINLLCGGVAGAIAQTISYPFDVTRRRMQLGAVLPEFEKCLTMRETMKYVYGHHGIRKGLYRGLSLNYIRCVPSQAVAFTTYELMKQFFHLN
Required for the accumulation of coenzyme A in the mitochondrial matrix.
Q01888
B7J9Q0
CRCB_ACIF2
Putative fluoride ion transporter CrcB
Acidithiobacillus
MFATFGFIALFAVLGAWARYGQTLLVQAAFGRGFPWATLSINVLGCFLMGFLFFETLERISVSPELRTGMLTGGLGAYTTFSTFSLETLVLFENGEAVKGLLYMFTSLFLCVGAAFAGAWISHST
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
B7J9Q0
Q04HX2
RL9_STRP2
50S ribosomal protein L9
Streptococcus
MKVIFLADVKGKGKKGEIKEVPTGYAQNFLIKKNLAKEATAQAVGELRGKQKSEEKAHAEMIAEGKAIKAQLEAEETVVEFVEKVGPDGRTFGSITNKKIAEELQKQFGIKIDKRHIQVQAPIRAVGLIDVPVKIYQDITSVINLRVKEG
Binds to the 23S rRNA.
Q04HX2
Q18953
SPCS_CAEEL
UGA suppressor tRNA-associated protein homolog
Caenorhabditis
MKANFGKKEGEYSRLVSKSSNKLLNSLWEKKQIPEEGWSEHTLDLFLSWLSSHDTNNRVDMIPVGAGEREGRVLTPLVQRLHSNLTHGIGRSGNLLEIQPKALGSSMLACLSNEFAKHALHLLGLHAVKSCIVVPLCTGMSLSLCMTSWRRRRPKAKYVVWLRIDQKSSLKSIYHAGFEPIIVEPIRDRDSLITDVETVNRIIEQRGEEILCVMTTTSCFAPRSPDNVEAISAICAAHDVPHLVNNAYGLQSEETIRKIAAAHECGRVDAVVQSLDKNFQVPVGGAVIAAFKQNHIQSIAQSYPGRASSVPSRDLVLTLLYQGQSAFLEPFGKQKQMFLKMRRKLISFAENIGECVYEVPENEISSAMTLSTIPPAKQTLFGSILFAKGITGARVVTSSQSKTTIEGCEFINFGSHTTEQHGGYLNIACSVGMTDHELEELFTRLTSSYAKFVRELAKEDERINSSGRRIPINESFDMEND
Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Q18953
Q0W4U3
AROE_METAR
Shikimate dehydrogenase (NADP(+))
Methanocella
MMTIYGVVGYPVEHSLSPVMHNAAFKALDMDCAYHKFEVKGEHLKDAILGARYLGFGGLNVTIPHKEAALRIMEPDRTALEIGAANTLDFKQMRAFNTDAAGAIDALRDGGVELENKGVLVLGAGGAARAVVYGLVKEGATVTIANRTTAKAADLAAYMRSFGSVFGTSLDSLGEKVRAVDIVINTTPIGMGWEDKPLVTRDMLDRSQAVFDLVYRPVETPLLREARAAGAKTIDGISMLARQGAKSFEIWTGVKPPVDVMERSARDAL
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).
Q0W4U3
Q6F0E5
FTSH_MESFL
ATP-dependent zinc metalloprotease FtsH
Mesoplasma
MKTKKSKSTLWFWLIILLAIIVTIIIIAVTVKGTTQVISDATFADWMSKSPQIDPNADKYWKNVIIYYGSNNTVVVKGSYFLESTGKYVNFVAYLTQKRFETIMADKPYPWPALVYQGSVGMALLVSLAPLLIYVLLFGGIIWFMMKSSSGAGAGAGNIFGMGKNRARAEKSDVKFANVAGIEEEKSELVELVDYLKFPAKYAEAGARAPKGVLMEGPPGTGKTLLAKAVAGEAGVSFFSIAGSEFEEMFVGVGASRVREMFNDAKKSAPAIIFIDEIDAVGRKRNNGMGSGGNEQTLNQLLVEMDGFGTNSGIIVMAATNRADVLDPALLRPGRFDRVIQVSLPDIKERKAILELHAKGKKIDGSVDWYRVAERTPGFSGAQLENVLNEAAILMVREKRDIITITEIDEAIDRVVGGPAKKSRAMTKQDKDIVSYHESGHALIGLKLDSASKVQKVTIIPRGNAGGYTIMTPKDETVFSSKKDLFATIAGYLGGRAAEEIMFGKENVTTGAHDDLDKATNIARRMVVQFGMSSLGMTKFLTMAEESYGKMEGTYSDETAARIDAEISKILEESYKIALKIIKENMETLELLAESLRVLETITAEQIEYINVNKKLPEEVLEQKNRMAKEDEKIKKGEIIDIKVEDLDID
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Q6F0E5
Q28074
CD3G_BOVIN
T-cell receptor T3 gamma chain
Bos
MEQGKHLAGLILAVFLLQGTMAHVKEVKVDDNREDGSVILICVTNDTTITWLKDVEQIGSGDTKKNTWNLGSSTKDPRGIYKCEGSNNQSKSLQIYYRMCQNCIELNPSTVAGFIFTEIVSIFLLAVGVYFIAGQEGVRQSRASDKQTLLNNDQLYQPLKEREDDQYSHLRKN
Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition to this role of signal transduction in T-cell activation, CD3G plays an essential role in the dynamic regulation of TCR expression at the cell surface. Indeed, constitutive TCR cycling is dependent on the di-leucine-based (diL) receptor-sorting motif present in CD3G.
Q28074
Q8HZN9
BKRB1_PIG
B1 bradykinin receptor
Sus
MASQTLVVFQASNQSQLPPPNATLCDGAQEAWHLLHKVLPTCVVAICSGGLLGNLFVLSVFLVPRRRLNAAEIYLAHLAASDLVFALGLPFWAETIRNGFHWPFGAPLCRVVNGVIKANLFISIFLVVAISRDRYRALVHPVASWRRRRRRHWAQATCVLIWTAGGLLSIPTFLLRSVQVVPELNVSACVLPFPHEAWAFVRTVELNVLGFLLPLAAILFFNYHILAALRGREQLSRTRCGGPRDGKTTALILTLVAVFLLCWTPYHVCAFLEFLLHVRAIRGCFWEDFTDLGLQYTNFFAFINSCLNPVIYVFWGQLFRTKIWELYHRCLPRKLTAVSSSRRKEIFQIFWRN
This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation.
Q8HZN9
Q9H343
O51I1_HUMAN
Olfactory receptor OR11-39
Homo
MLGLNGTPFQPATLQLTGIPGIQTGLTWVALIFCILYMISIVGNLSILTLVFWEPALHQPMYYFLSMLALNDLGVSFSTLPTVISTFCFNYNHVAFNACLVQMFFIHTFSFMESGILLAMSLDRFVAICYPLRYVTVLTHNRILAMGLGILTKSFTTLFPFPFVVKRLPFCKGNVLHHSYCLHPDLMKVACGDIHVNNIYGLLVIIFTYGMDSTFILLSYALILRAMLVIISQEQRLKALNTCMSHICAVLAFYVPIIAVSMIHRFWKSAPPVVHVMMSNVYLFVPPMLNPIIYSVKTKEIRKGILKFFHKSQA
Odorant receptor.
Q9H343
A7Z8B5
AMPA_BACVZ
Leucyl aminopeptidase
Bacillus amyloliquefaciens group
MFYASDQLRHPETLVIGLFQKSTLNGFTKELDDKLDGHLTQLLKDGDVSAKRNRVSKVYPPAATGMKRIYFIGLGREADYSFEDTKECFARVFQQVHQDKKQEVSVLLDTFVSGEVPAADAAHALSESCLLAVYEVQDYKHKSNEPDQELKSVCAVTEEDLREVQAGLNVGAAYGQGTNSARTLVNMPGNMLTATDLASYAAELAAKYDFECEILEKDEMEELGMGGLLAVNKGSSEPPKMIVLKYQGKDQWEDVIGLVGKGITFDTGGYSIKPKTGIVGMKSDMGGAASVLGAMEIIGELRPEQNVLAVIPSTDNMISSDAMKPDDVIVSLSGKTIEILNTDAEGRLVLADGITYAKQHGASVLVDVATLTGGVIVALGNEMTGAMTNHAAFYEQVAESAKESGEPIWQLPITEKDKKRVRNSQMADLNNSPGREGHAIMAGAFIGEFAENTPWVHLDIAGTATANKATCFGPAGATGVMARTLAVLTERFTPER
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
A7Z8B5
Q74ND7
RL13_NANEQ
50S ribosomal protein L13
Nanoarchaeum
MEFLGELIYDAEGLVLGRLASIVARNLKRGYRVKIVNAEKAIITGDPNMVKKEWLQKVKRGDYYKGPFYPKRPDNILKRVIRGMLPRKTARGRELLKNVKVYIGVPEELKDKPKLGLNLENAKGYPEALIKEVLKAKPKFERGNIKYIELGELSKYLGAKFT
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
Q74ND7
Q3M5D0
RPOB_TRIV2
Transcriptase subunit beta
Trichormus
MISENYIEPAFLLPDLIEIQRSSFRWFLEEGLIEELNSFSPITDYTGKLELHFLGHNYKLKEPKYSVEEAKRRDSTYAVQMYVPTRLLNKETGDIKEQEVFIGDLPLMTDRGTFIINGAERVIVNQIVRSPGVYYKSEIDKNGRRTYSASLIPNRGAWLKFETDRNDLVWVRIDKTRKLSAQVLLKALGLSDNEIFDALRHPEYFQKTIEKEGQFSEEEALMELYRKLRPGEPPTVLGGQQLLDSRFFDPKRYDLGRVGRYKLNKKLRLSVPDTVRVLTSGDILAAVDYLINLEYDIGSIDDIDHLGNRRVRSVGELLQNQVRVGLNRLERIIRERMTVSDAEVLTPASLVNPKPLVAAIKEFFGSSQLSQFMDQTNPLAELTHKRRLSALGPGGLTRERAGFAVRDIHPSHYGRICPIETPEGPNAGLIGSLATHARVNQYGFLETPFRPVENGRVRFDQPAVYMTADEEDDLRVAPGDIPVDENGHIIGPQVPVRYRQEFSTTTPEQVDYVAVSPVQIVSVATSMIPFLEHDDANRALMGSNMQRQAVPLLKPERPLVGTGLEAQGARDSGMVIVSRTDGDVVYVDATEIRVRVSGQLPAASGKSTDNGQLTSQKGQEIRYTVSKYQRSNQDTCLNQKPLVRIGERVVAGQVLADGSSTEGGELALGQNIVVAYMPWEGYNYEDAILISERLVQDDIYTSIHIEKYEIEARQTKLGPEEITREIPNVGEDALRQLDEQGIIRIGAWVEAGDILVGKVTPKGESDQPPEEKLLRAIFGEKARDVRDNSLRVPNGEKGRVVDVRLFTREQGDELPPGANMVVRVYVAQKRKIQVGDKMAGRHGNKGIISRILPIEDMPYLPDGSPVDIVLNPLGVPSRMNVGQVFECLLGWAGHTLGVRFKITPFDEMYGEESSRRIVHGKLQEARDETGKDWVYNPDDPGKIMVFDGRTGEPFDRPVTIGVAYMLKLVHLVDDKIHARSTGPYSLVTQQPLGGKAQQGGQRFGEMEVWALEAFGAAYTLQELLTVKSDDMQGRNEALNAIVKGKAIPRPGTPESFKVLMRELQSLGLDIAVHKVETQADGSSLDVEVDLMADQLARRTPPRPTYESLSRESLDDDE
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q3M5D0
Q59MD0
PGA50_CANAL
Predicted GPI-anchored protein 50
Candida
MKLNLLLLLFIVELVAAVTNYNLGSAPVSRYLSKTGTYSPVAASRVCNDNCYSFYEGELFCGKFDSNVSETDYLNCLCLNKQYRSNFEGCNCKSESEVNFFDWKSSCSDISSVKNYSLPTTQLGTCNSHCSAYQTIPAECLVYESGKYQEDQVCICQNAEFWYHYENCDCLDFGDVDHEYEDICYYATNSFVTSDDYYDSFFATYTEGSFESILEKGSFLAEQKGSITSGLASKTETSKVSTTTFSSNGTSSGTTNGDTRAETKSSNSTQTSSSDKNSSQINSISSTGVANFVASFGMGTLLLFVLSLC
Probable GPI-anchored cell wall protein that may be involved in cell wall organization, hyphal growth, as well as in virulence.
Q59MD0
P00295
PLAS_MERPE
Plastocyanin
Mercurialis
LDVLLGSDDGELAFVPNNFSVPSGEKITFKNNAGFPHNVVFDEDEIPSGVDASKISMDEADLLNAPGETYAVTLTEKGSYSFYCSPHQGAGMVGKVTVN
Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.
P00295
Q7LFX5
CHSTF_HUMAN
N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase
Homo
MRHCINCCIQLLPDGAHKQQVNCQGGPHHGHQACPTCKGENKILFRVDSKQMNLLAVLEVRTEGNENWGGFLRFKKGKRCSLVFGLIIMTLVMASYILSGAHQELLISSPFHYGGFPSNPSLMDSENPSDTKEHHHQSSVNNISYMKDYPSIKLIINSITTRIEFTTRQLPDLEDLKKQELHMFSVIPNKFLPNSKSPCWYEEFSGQNTTDPYLTNSYVLYSKRFRSTFDALRKAFWGHLAHAHGKHFRLRCLPHFYIIGQPKCGTTDLYDRLRLHPEVKFSAIKEPHWWTRKRFGIVRLRDGLRDRYPVEDYLDLFDLAAHQIHQGLQASSAKEQSKMNTIIIGEASASTMWDNNAWTFFYDNSTDGEPPFLTQDFIHAFQPNARLIVMLRDPVERLYSDYLYFASSNKSADDFHEKVTEALQLFENCMLDYSLRACVYNNTLNNAMPVRLQVGLYAVYLLDWLSVFDKQQFLILRLEDHASNVKYTMHKVFQFLNLGPLSEKQEALMTKSPASNARRPEDRNLGPMWPITQKILRDFYRPFNARLAQVLADEAFAWKTT
Sulfotransferase that transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating units. It also transfers sulfate to a unique non-reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. May also act as a B-cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and/or regulation of B-cell-specific RAG expression; however such results are unclear in vivo.
Q7LFX5
A0L0R3
PANC_SHESA
Pantoate-activating enzyme
Shewanella
MITSAHIDDIRTQVRAWHAKGETVAFVPTMGNLHQGHITLVKEAAKKCDHVVVSIFVNPMQFGQNEDLDAYPRTLEADSQALTAAGAELLFTPTPTVIYPKGLAQQTYVEVPGISDVLCGASRPGHFRGVATVVCKLFNIVQPDVAFFGNKDYQQLLVIRTMVEDLSLPIEIIGVDTIREASGLAMSSRNGYLTAEEKAAAPALKKAIDAMAQGIKQGVSIEQVTAEAKASLIAAGFTPDYLEVCHATTLANAETTDQALVILAAAYLGKARLIDNLRFDR
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
A0L0R3
D5IGG6
FDR_SPHSX
Carbazole 1,9a-dioxygenase, ferredoxin reductase component
Sphingomonas
MTDTHYDVVIVGAGHGGAQTAIALRQNGFAGTIAIIGAEPDLPYERPPLSKEYLAAEKGFERILIRPASFWNDRHIAMHLGCAVERVDPTQRLVFLADGRSMGYGDLVWCAGGSARRLDCTGHDLGGVHYVRTRADTDALAAELPGVSKVVIIGGGYIGLEAAAVMAKFGKNVTLIEALDRVLARVAGEPLSRFFEEKHRSRGVDVRLRTKVGCLLGQDGRVTHVELNDADPIPADLVIVGIGIIPAISPLVVAGAKASNGLLVDASGRTSIPHVYALGDCAAHVNSFAPNDIPIRLESVQNANDQAVVVARTICGTAAQYHAVPWFWSSQYDIRLQTVGLTAGYDQTFVRGDPATGSFTVVYGRDGRVIALDCVNATKDYVQGKRLVEAKALIEPGMTDPQYPLKNFMTPSPA
Part of the multicomponent carbazole 1,9a-dioxygenase (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol.
D5IGG6
Q57NN4
HEM1_SALCH
Glutamyl-tRNA reductase
Salmonella
MTLLALGINHKTAPVSLRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNLNEDDLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTETDIGASAVSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEVISLSDIDARLQDADIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLVQRQAAAVEAETIVEQEASEFMAWLRAQGASETIREYRSQSEQIRDELTTKALSALQQGGDAQAILQDLAWKLTNRLIHAPTKSLQQAARDGDDERLNILRDSLGLE
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Q57NN4
A0A140JWT0
PTMQ_PENSI
Penitrem biosynthesis cluster 1 protein Q
Penicillium
MDYVAQSPWIATLIVTATTYCTLRWVQYWRSWVNVPVVGRRGFLGSWISTILWTWEARGCIQKGYEKNKDFAFQVSTPNGWEVCICNDDMIKEYKNLMDDQMSALAVTSETFQAKYTLPGADWDAVHKLVPQPALAKSLMWLRNRAANDTDPYFPDFVRAFQRAFKEEIQVEQDGPFEWQSFPCFPRYSRVVAALTVKALLGSLANRPELIDLLCEYAEVIPLDGFFIALFPAILKPIVAFFCKAPRLSDRLVKVITEEIARRELENKHRIPEDMTDWMAQWVKDNPGYSIESAVVRVIATFFGGIHTTTQLTVHTLLEIATRPEYVDPLRQEITTALKAHGGWTKSAIESMTKLDSFIKEAQRFNPLDAASLARQATRDFQFSNGLKLPRGTWVFAPNGPMLFDESLYPAGSQFDGLRFWKLAEQTQRPHDYRLVTASSKYLQFGDGRHTCPGRFMAADEIRLIVAHTLFHFDIAIKNHGPRPRNTTFKKICFPDMSAEIMLRPRKLHGSEGN
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline . Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ . Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase ptmH which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase ptmD . A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase ptmV and ptmI leads to the production of the prenylated form of penijanthine . The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase ptmE . Five sequential oxidative transformations performed by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various penitrem compounds. PtmK, ptmU and ptmM are involved in the formation of the key bicyclic ring of penitrem C via the formation of the intermediates secopenitrem D and penitrem D. PtmL catalyzes the epoxidation of penitrem D and C to yield penitrem B and F, respectively. PtmJ catalyzes the last benzylic hydroxylation to convert penitrem B to prenitrem E and penitrem F to penitrem A .
A0A140JWT0
Q8X7P7
GNU_ECO57
GlcNAc-P-P-Und 4-epimerase
Escherichia
MNDNVLLIGASGFVGTRLLETAIADFNIKNLDKQQSHFYPEITQIGDVRDQQALDQALAGFDTVVLLAAEHRDDVSPTSLYYDVNVQGTRNVLAAMEKNGVKNIIFTSSVAVYGLNKHNPDENHPHDPFNHYGKSKWQAEEVLREWYNKAPTERSLTIIRPTVIFGERNRGNVYNLLKQIAGGKFMMVGAGTNYKSMAYVGNIVEFIKYKLKNVAAGYEVYNYVDKPDLNMNQLVAEVEQSLNKKIPSMHLPYPLGMLGGYCFDILSKITGKKYAVSSVRVKKFCATTQFDATKVHSSGFVAPYTLSQGLDRTLQYEFVHAKKDDITFVSE
Involved in biosynthesis of the repeating tetrasaccharide unit of the O-antigen. Catalyzes the reversible epimerization of the hydroxyl group at position C4 of undecaprenyl pyrophosphate-N-acetylglucosamine (UndPP-GlcNAc) to yield undecaprenyl pyrophosphate-N-acetylgalactosamine (UndPP-GalNAc).
Q8X7P7
B7LF90
GCSH_ECO55
Glycine cleavage system H protein
Escherichia
MSNVPAELKYSKEHEWLRKEADGTYTVGITEHAQELLGDMVFVDLPEVGATVSAGDDCAVAESVKAASDIYAPVSGEIVAVNDALSDSPELVNSEPYAGGWIFKIKASDESELESLLDATAYEALLEDE
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
B7LF90
B8DFY0
GCST_LISMH
Glycine cleavage system T protein
Listeria
MTELLKTPIHPLYAKYGAKTIDFGGWDLPVQFAGIKAEHEAVRTDAGLFDVSHMGEILVEGPDSTSYLQYLLTNDIEKIKIGKAQYNIMCYETGGTVDDLVVYKKSETEYILVVNAANTAKDFEWMVKNIQGDVSVTNVSSEYGQLALQGPNAEKILAKLTDVDLSSISFFGFVEDADVAGVKTIISRSGYTGEDGFEIYMPSADAGKVFEAILAEGVAPIGLGARDTLRLEAVLALYGQELSKDITPLEAGLNFAVKLKKEADFIGKEALIKQKEAGLNRKLVGIELIERGIPRHDYPVFLNDEEIGIVTSGTQSPTLGTNIGLALIDTAYTELGQEVEVGIRNKKIKAKIVPTPFYKRAK
The glycine cleavage system catalyzes the degradation of glycine.
B8DFY0
P57946
RSMG_PASMU
16S rRNA 7-methylguanosine methyltransferase
Pasteurella
MTNLEQQLSQKLEILLKQTALSITDQQKEQLIKLVLLLNKWNKAYNLTSVRDPMEMLVKHILDSVVVSPHLQGKHFIDVGTGPGLPGLPLAIVNPNKHFVLLDSLGKRISFIRNAIRELGLDNVEAVLSRVEEYHPEQPFDGVLSRAFASLKDMTDWCQHLPKQDGYFYALKGLYHQEEVEELSEKFTIQQVIRLQVPELIGERHLVIVK
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
P57946
Q0ABF1
RS4_ALKEH
30S ribosomal protein S4
Alkalilimnicola
MARYIGPTCKLARREGTDLFLKSGVRPLDSKCKLDQPPGPKLQRRTRMSDYGLQLREKQKVRRMYGVLERQFRNYYKEAARQKGATGTVLLQLLESRLDNVVYRMGFATTRAEARQLVSHRGVQVNGRVVNVPSMQVSPGDLVGLKEKAQKQLRVQAALEMAQQNGWPAWVEVDPKKFEGTYKARPDRADLSAEINESLIVELYSK
With S5 and S12 plays an important role in translational accuracy.
Q0ABF1
Q8YDC8
DAPB_BRUME
4-hydroxy-tetrahydrodipicolinate reductase
Brucella
MGLVVVGAGGRMGQTLIRTIQSIEGAKLVGAIERSGSPFLGKDAGEVTGIGTLGVAITDDPLPVFAKAHGVLDFTSPAASVEFAGLAAQARIVHVIGTTGCSAEDDEKIRAAARHATIVKSGNMSLGVNLLSVLVQKAAEALGPEDFDIEILEMHHRHKVDAPSGTALLLGEAAARGRDIALADNSVRVRDGYTGPRETGTIGFATLRGGSVIGDHSVILADTGERVVLSHHAEDRSIFARGAIKAALWAHGKKPGLYSMLDVLGLNT
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Q8YDC8
Q6FMH9
ASA1_CANGA
ASTRA-associated protein 1
Nakaseomyces/Candida clade
MERAATHFLRLHKSGISALCSGVIDPDYGITSPVLFSGDIDGEVTIWNLITRRPIFTSKICNEQVVDIQFLEGKYLSLLCKDHKLRLYELLKLGAIVKQSDFGGGDKVDLKQIFEVPVNTLNFANYVLTYLGNNKFELVTCHTQDAHFIDIYEFETPELNSLKRFSKAIDFLPMLRDRFGDNLLPKMDGLGIIMKFYKVNEVVYCGFESGYVIAFRRYRNKPLYRKRVSGFIGKPINECASGISKLLQHENVETSSSVNDLELDNVIEIVLVDRAHYPDPVLDMAPNPKKNGIICSSTTNKLVLTSVDEQYLAGPNSAYIFKSDEYLLDKKNCLLMSTNLKIDGSAVKDMMCKNIGFVLSLGDYIITGNWSGKTYIGRIESDKAVLAAAKSRSLIEVNESPVGNIQQDKSIQKSSKHTKIGAMTGFEVKDKEPDKLMCKNKELTPGKLRRLNAFVQSKWYFIGYTDGTIGLYRAE
Component of the ASTRA complex involved in chromatin remodeling.
Q6FMH9
Q8ZLD6
DTPB_SALTY
Dipeptide and tripeptide permease B
Salmonella
MNTTAPTGLLQQPRPFFMIFFVELWERFGYYGVQGILAVFFVKQLGFSQEQAFITFGAFAALVYGLISIGGYVGDHLLGTKRTLVLGAIVLAIGYFMTGMSLLNPDLIFIALGTIAVGNGLFKANPASLLSKCYQPKDPRLDGAFTLFYMSINIGSLLSLSLAPVIADKFGYAVTYNLCGAGLIVALLVYFACRGMVKNIGSEPDHKPLRFRNLLLVLLGTVVMIFLCAWLMHNVKIANLVLIVLSIVVTIFFFREAFRLDKTGRNKMFVAFILMIEAVLFYILYAQMPTSLNFFAINNVHHEILGFAINPVSFQALNPFWVVVASPVLAAIYTRLGSKGKDLTMPMKFTLGMFLCALGFLTAAAGMWFADAQGLTSPWFIVLVYLFQSLGELLISALGLAMVAALVPQHLMGFILGMWFLTQAAAFLLGGYVATFTAVPENITDPLQTLPIYTGVFSKIGLVTLAVTVVMAIMVPWLNRMINTPGTEQ
Proton-dependent permease that transports di- and tripeptides.
Q8ZLD6
A6LPR2
RL4_CLOB8
50S ribosomal protein L4
Clostridium
MPTVGVFNKEGNKVADMELNENVFAAEINEYALHQVVVALLANKRQGTQSTKTRSEVRGGGIKPWRQKGTGRARQGSIRSPQWIKGGIVFAPKPRDYRVSVPKSMRKVAMKSALTSKVQDNQMIVLDSLNFEAPKTKSMIEMLKALEANKALIITAESNEVVYKSARNIQGISVIPANNINVYDLLKYEKLIITKDAVSKIEEVYA
Forms part of the polypeptide exit tunnel.
A6LPR2
Q89AT7
NUOK_BUCBP
NDH-1 subunit K
Buchnera
MIPLSHGLILAFFLFSLGFVSLVMHKNILFMLISLEIMINSAALALVVVGNYWNQVDGQIMYILILTLGASESSIGLALLIQCYRHFKTLNIDKLSEMNG
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.
Q89AT7
A6S950
CHO2_BOTFB
Phosphatidylethanolamine N-methyltransferase
Botrytis
MSTSSMKSQDSNGLRERINNGSATNDDNMTARCGSEPPSEDFELDKDKKTFGRTPDGTIPQTHDMVSQLLDPRQPKNLSDLIVLVILALHIFALYALPSSLKRPVFAVIFLFWRGCYNVGIGYLLHIQSHHKRIVAWAKKWNLFENPVTGKNPRPWLYQLIKTELETKIPEDYKFEQAPIEYNTWLVFRRVVDLILMCDFTSYCLFAIACGGAPSDEGLVMSTLRWGAGIILVLFNLWVKLDAHRVVKDYAWYWGDFFYLIDQELTFDGVFEMAPHPMYSVGYAGYYGISMMAASYSVLAISIVAHMAQFAFLLVVENPHIDKTYNPPPPRKHQDNPTPSDIDHANALASSKEGLEYSLDSSPTQTPPLNTTQPLAVHNLMGLGNIDLFRITDVSILLLLGYVFLITALTPSTPVYQALFVINAMFWRLWYSVGLGIILDRQSSKKMWTRHFVKYGDSTEEAWRQWKGMYHLSMTMCYASFIAATWKMYSIPSDWAYGLVLLRHVLGAGLVSLQLWTAISIYESLGEFGWFFGDFFFDHAPKLTYSGIYRYLNNPERIIGLAGIWGAVFITGSRAIFCLALLSHTLTLAFLQFVEKPHMQKLYGRNLRSEAGLSKSIKRSLPPQIKKWHGNVDRVLEETGHFVEEFLDAARPKLAAGVSTIFRDTSALFSQYPARLTLTRIAPDLAGYDPRDYSVTIEGTSSDSALHKRTTSKEGITARIPQERMDGFKPLVFEYGAPIKVKWTAPTKHSKADWIVTRIPSAGRWVATVPNEYESSPADQGILVSNRFVSGSKRIDGSTQDYVEGEMIFEGDKLFWTQGVFEFRYHHDGKHNVMAISLPFEIRIPRFDDENSNVNITLDSDNSQSQSLIRSAVEQALLPVVRNCFDRDPDIAPNSVDESFGVLVARDGKYPRRVVHAVHFMFGIEFAPEVVRADGNVRNLAWRICNAKQVLAPYSMSHSKGTNTPDVDGEKA
Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
A6S950
O32261
GANP_BACSU
Galactooligosaccharides transport system permease protein GanP
Bacillus
MQHRQVALLLSIIPGLGQFYNKQWIKGIVFLFLGASFFAVFGDLLNMGFWGIFTLGTEVPRDNSVFLLAEGIIAVIVTCFGLAVYYVNLRDAFQSGKQRDENKPLSSLKEQYQHIISEGYPYVVSGPSLFILIFAVIFPILFSFALAFTNYDLYHSPPAKLIDWVGFQTFANIFTVDIWRSTFFDVLAWTVVWTLAASTLQVTLGIFLAIIVNQKDLRFKRFFRTILILPWAVPGFVTILIFAGLFNDSFGAMNHDILAFFGIDPLPWMTDANWSRLALILMQGWLGFPYIFLVSTGVLQSIPDDLYEAATIDGASVFSKLRYITLPMVFIAMAPIIITQFTFNFNNFNIIYLFNGGGPAVTGSTAGGTDILVSWIYKLTMQSSQYSLAAALTILLSVFVISIALWQFRQTKSFKEEA
Involved in galactan degradation . Part of the ABC transporter complex GanPQS involved in the uptake of galactooligosaccharides . Responsible for the translocation of the substrate across the membrane (Probable).
O32261
B4S6E3
ATPD_PROA2
F-type ATPase subunit delta
Prosthecochloris
MSSAIASRRYAAALLDVAEDSGVVEQVDTDLEMISATIADSHDLVVMLKSPLIKGDTKAKALKAVFHGMLNEKTLLFIDLICRKKRADHLPQMVEEYKALRDERSGLINVDVNSAVKLEDEQARELINSLATYTGKKVRARLALDEKLLGGVTVKIGDTIIDGSVRHQLDMLRVALTADV
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
B4S6E3
B2VJK2
KDPC_ERWT9
Potassium-translocating ATPase C chain
Erwinia
MSQLRPAVFLVLLLTLITGLLYPLLTTTLAQWMFPQQANGSLLLEQGSVRGSAPIGQSFSRADYFQGRPSATSDRPYNPLASSGSNLAGSNPALDQAVSQRVAALRAANPQAGQQVPVDLVTASASGLDPQISPQAAYWQADRIAAARRLPREVVKRLIDENTTTPMPAFLGEPAVNVLALNLALDALQR
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
B2VJK2
Q9H5J4
ELOV6_HUMAN
Very long chain 3-oxoacyl-CoA synthase 6
Homo
MNMSVLTLQEYEFEKQFNENEAIQWMQENWKKSFLFSALYAAFIFGGRHLMNKRAKFELRKPLVLWSLTLAVFSIFGALRTGAYMVYILMTKGLKQSVCDQGFYNGPVSKFWAYAFVLSKAPELGDTIFIILRKQKLIFLHWYHHITVLLYSWYSYKDMVAGGGWFMTMNYGVHAVMYSYYALRAAGFRVSRKFAMFITLSQITQMLMGCVVNYLVFCWMQHDQCHSHFQNIFWSSLMYLSYLVLFCHFFFEAYIGKMRKTTKAE
Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that elongates fatty acids with 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs. Catalyzes the synthesis of unsaturated C16 long chain fatty acids and, to a lesser extent, C18:0 and those with low desaturation degree. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Q9H5J4
Q5EY89
RL5_EIMTE
60S ribosomal protein L5
Eimeria
MAFVKAIKNKAYFKRFQVKYRRRREGKTDYAARRRLILQDKNKYNAPKYRFVVRVTNSRVLCQVMYATLQGDRLVCSADSQELTRYGIKVGLTNYSAAYATGLLLARRLLKQKGLADEFKGLEKPSGEEYHIEEVSEERRPFKCVLDVGIVATTVGNRVFGAMKGACDGGLHIPHSNKRFPGFTKGEDGADDSYNPEVHRARIYGLHVAEYMRTLKEEDPERYQAQFSAYIRNKIDPDSIEKMYEEAFQKIRANPDPVKKEAREVKRVRQGAMIKTAKSQYVRNVKLDKETRKERVLKKIQMVADKMAEEE
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Q5EY89
Q13444
ADA15_HUMAN
Metargidin
Homo
MRLALLWALGLLGAGSPLPSWPLPNIGGTEEQQAESEKAPREPLEPQVLQDDLPISLKKVLQTSLPEPLRIKLELDGDSHILELLQNRELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVRGYAGSWVSICTCSGLRGLVVLTPERSYTLEQGPGDLQGPPIISRIQDLHLPGHTCALSWRESVHTQKPPEHPLGQRHIRRRRDVVTETKTVELVIVADHSEAQKYRDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAHLLPRLPHDSAQLVTGTSFSGPTVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDLPGNSCPCPGPAPAKTCIMEASTDFLPGLNFSNCSRRALEKALLDGMGSCLFERLPSLPPMAAFCGNMFVEPGEQCDCGFLDDCVDPCCDSLTCQLRPGAQCASDGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPDVSLGDGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNPSGSYVSCTPRDAICGQLQCQTGRTQPLLGSIRDLLWETIDVNGTELNCSWVHLDLGSDVAQPLLTLPGTACGPGLVCIDHRCQRVDLLGAQECRSKCHGHGVCDSNRHCYCEEGWAPPDCTTQLKATSSLTTGLLLSLLVLLVLVMLGASYWYRARLHQRLCQLKGPTCQYRAAQSGPSERPGPPQRALLARGTKQASALSFPAPPSRPLPPDPVSKRLQAELADRPNPPTRPLPADPVVRSPKSQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL
Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain.
Q13444
Q9M115
ZDH16_ARATH
Zinc finger DHHC domain-containing protein At4g01730
Arabidopsis
MTRRRHGWQRPLHPLQIVGAVIYSVLVAAFYVFLGFFLGNRIAVIALLSVFSSVAVSVIVLFVRCTAIDPTDKTSAKKKRKDKSKGVLMKLRVKVVLSQVVVRFFRRLERKILRNFLRRTYLDPWKSSVQLEPLLPFPLVMKDDDSVTPDPKEEDDISYCSLCDLEVKRSSKHCRTCNRCVEGFDHHCRWLNNCVGKKNYTTFILLMVFVLLMLIIEGGTALAVFVRCFVDKKGMEMELKRRLYVEFPQWALATISIILVLFTAYGSAAMGQLFLFHVVLIRKGMRTYDYILAMKEENQFTEVDPFDELDSSSDESSDFDSPERLRPTFISKFMCRKANENQQRLSIKIEGDEQSPSSTLINKKPGFHVSINPWKLITLSSEKALQAAEKAKERLRKTKPVSGTEENSLKPLPLETKFGLLLDPDNNNTVLQPSTTAAVKLQVSPGRFSSPRRRFSGSSSSTVPSPKQKYRTNFDLKLTEVSRELESYISRQVLCSVIKQDGSEASPR
S-acyltransferase involved in protein lipid modification.
Q9M115
Q49UU6
XPT_STAS1
Xanthine phosphoribosyltransferase
Staphylococcus
MDLLKQKVEADGVVIDEKILKVDGFLNHQIDARLMHDVGQTFYEQFKDEGITKILTIEASGIAPAIMAAMHFDVPCLFAKKAKPSTLKKGVYQAEIHSFTKNTTSTVVVSDEFLGENDRVLIIDDFLANGDASLGLNEIVKQAKATTVGIGIVVEKSFQPGRERLEEAGLTVSSLCKVASLSGNKVTFVGDEA
Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.
Q49UU6
B1LAF7
NFI_THESQ
Deoxyribonuclease V
unclassified Thermotoga
MDYRKLHGWDLSPEEAIKVQNELRKKIKLVPYEGEPEYVAGVDLSFPGKKEGLAVIVVLEYPSFRIVEIVSERGEITFPYIPGLLAFREGPLFLKAWEKLRTKPDVVVFDGQGLAHPRKLGIASHMGLFIEIPTIGVAKSRLYGTFKMPEDKRCSWSYLYDGEEIIGCVVRTKEGSAPVFVSPGHLMDVESSKRLVKAFTLPGRRIPEPTRLAHIYTQRLKKGLF
DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
B1LAF7
Q74BX0
PSD_GEOSL
Phosphatidylserine decarboxylase beta chain
Geobacter
MRNENTPIAVEGYPFIAIAGVLTLILAAVSWHAPVVWAGTAFFLTVTLFVAFFFRNPERITPGNENAVVAPADGVVIYLGPAREEHLGVETTKISIFMSVFNVHINRAPVSGTVLDTFYVKGKFLDVRDDRATFENEQAGLVIETARGLRLAVVQVAGLIARRIVCYAGKGDRLTRGGRYGLIRFGSRLDIYLPTTTEVKVALGEKTVAGETVLGILP
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Q74BX0
A8AJ40
GPMA_CITK8
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
Citrobacter
MAVTKLVLVRHGESQWNNENRFTGWYDVDLSEKGVGEAKAAGKLLKEEGYSFDFAYTSVLKRAIHTLWNVLDELDQAWLPVEKSWKLNERHYGALQGLNKAETAEKYGDEQVKQWRRGFAVTPPELTKDDERYPGHDPRYAQLTEKELPLTESLALTIDRVIPYWNETILPRMKSGERIIIAAHGNSLRALVKYLDNMSEEEILELNIPTGVPLVYEFDENFKPIKHYYLGNADEIAAKAAAVANQGKAK
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
A8AJ40
Q2YB06
RL7_NITMU
50S ribosomal protein L7/L12
Nitrosospira
MAIAKAEILDAIANMTVLELSQLIKEMEEKFGVSAAAAAVVAAAPAAGAAAAPAEEQTEFTVMLTAVGESKVNVIKVVRAVTGLGLKEAKDLVDGAPKPVKEGIAKADAEAIQKQLAEAGATAEIK
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Q2YB06
P52620
DPO3B_VIBHA
DNA polymerase III subunit beta
Vibrio
MKFTIERSHLIKPLQQVSGALGGRPTLPILGNLLLKVEDNVLSMTATDLEVELVSKVTLEGDFEAGSITVPSRKFLDICRGLPDDSIITFVLEGDRVQVRSGRSRFSLATLPANDFPNIEDWQSEVEVSLTQSDLRTLIEKTQFS
Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.
P52620
A7ZCK4
NAPA_CAMC1
Periplasmic nitrate reductase
Campylobacter
MNRRDFIKSAAASAACASAGIAVPSSLSAANEAEKGWRWDKAACRFCGTGCGIMVATKDGKIVAVKGDPEAPVNRGLNCIKGYFNAKIMYGEDRITHPLLRVNEKGEFDKKGKFKQVSWKQAFDVMEAQFRKTYDELGPHGVGVLGSGQYTIPEGYAAVKLMKGGFRSNSIDPNARHCMASAVLGFMQVFGIDEPSGCFDDIELTDTVIAWGANMAEMHPILWARVSDRKLSDPDRVKVVNLSTYSTRTSNLADIEIIFAPSSDLAIWNYIAREIVYNHPEMIDEEFVKKHCVFTAGPVDIGYGLRPDIHHKKYAPSELDTAATEKSKVLSEAEGVTLSYLGLKAGDTLENKNAAKADAHWQITFEEFKKALAPYTLDFTAKVAKGDPNEDINEFKKKLKALADLYIEKNRKVVSFWTMGFNQHQRGTWVNEQAYMVHFLLGKQALPGSGAFSLTGQPSACGTAREVGTFVHRLPADMVVGNPKHREITEKLWKLPAGTLSGTPGSHYVKMMRDLEDGKVKFIWVQVNNPWQNTANANHWIKAAREMDNFIVVSDPYPGISAKVADLILPTAMIYEKWGAYGNAERRTQHWRQQVLPVGEAMPDIWQMLEFSKRFKLKDVWGEKKVNDKVTLPSVLEAAKAMGYSEEDTLFDVLFANEDAKKFSANDPIMENYDNTEVFGDSRKVIGSDGKEFKGYGFFIHKYLWEEYRKFGVGHGHDLADFDTYHRVRGLRWPVVDGKETQWRFNTKFDPYAKKAAPNDKFAFYGNKNAALPTGDLKGVKNQEKTPLANKAKIFFRPYMDPCEMPSKDYPFWLCTGRVLEHWHTGTMTMRVPELYRAVPEALCYMHEDDAKKLGVLQNEIVWVESRRGKVKARVDLKGRNKPPVGLVYVPFFDENVFINKVCLDATCPISKETDYKKCAVKIYKA
Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.
A7ZCK4
Q3YRC1
DNLJ_EHRCJ
Polydeoxyribonucleotide synthase [NAD(+)]
Ehrlichia
MKQEEAKLELDKLNSQIQHHDFLYYTQDNPQITDAEYDVLCHKRNLILESFPELASNNNYQDNVGSTPDAKFAKVKHAEKMLSLDNAFNQQDIEKFITRTKKLLDMDNSQSIAISCELKIDGLSFSVIYKKGEISQASTRGNGYFGENITNNVKTIKNLPHTIQNAPDSLEVRGEIYIDRSDFIQLNKDGNNFANPRNAAAGSVRQLDINITAQRKLKYFMYTIVNTKCLTQEETLNQLKTLGFCVNEHTITTNNIEDALNFYNQFYNNRSNISYDIDGIIYKVNDIKSQHILGATNKSPRWAIAYKFPAAEAKTLVNKISIQIGRTGVLTPIAELSPINIGGVIVTRASLHNKSEIERKDIREGDYVIVKRAGDVIPQVVDVDKNLRAQELTKFIFPTTCPSCGSNLFQAEQEVSIYCTGELFCKNQILEKIKHFVSKDAFNIIGFGKKQLLFFYEQGLITNIVDIFTLEEKISNSDLKLESLHGWGEKSIHNLFSAINNSKTISLENFIFALGIRFVGKYIAKILAKHFLSYEKWYHEMLRLAQDENYLLNIQQIGHKTIHSLKMFFTEQHNLDTINNLVRHLTITDAKTTSHLSLLHGKTIVFTGELSNMSRHEAKTKSETAGAKVSSSLSKNTDFLIVGNNPGSKYKKAQSLNIQILTEDLWLQYISPNTNEN
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.
Q3YRC1
B3Q9V6
PANB_RHOPT
Ketopantoate hydroxymethyltransferase
Rhodopseudomonas
MSVQSTIRRKTAPDIRARKGGDPIVMLTSYHAHTASLVDRYCDAILVGDSLGNVMHGFETTVPVTLEMMILQGHAVMRGSQHALVVVDMPFGSYEASKEQAFHSAARILKETHCGAVKLEGGVRMAETIRFLTERGIPVMGHIGLTPQSINTLGSFRAQGREEGSWEPIEADAKAVAEAGAFSVVVEAVAEPLGRKITETIAIPTIGIGASAACDGQVLVLEDMLGLSPKPPKFVKRYGDLGPGIEAAIKGYAEEVRSRAFPGPEHVYGMKSKA
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
B3Q9V6
Q58P71
CHX8_ARATH
Protein CATION/H+ EXCHANGER 8
Arabidopsis
MGGGDISHMSPEVKWIFEMAWYGETVRYDGLICEEHPPKLSSDGIWEKLIIKSAGLYFWQYRLPKLEIVILLVFFLWQGFNILFKKLGLSIPKLSSMMLAGLLLNVLVTLSGENSIIADILVTKNRIDVAGCLGSFGFLIFWFLKGVRMDVKRIFKAEAKARVTGVAAVTFPIVVGFLLFNLKSAKNRPLTFQEYDVMLLMESITSFSGIARLLRDLGMNHSSIGRVALSSALVSDIVGLLLLIANVSRSSATLADGLAILTEITLFLVIAFAVVRPIMFKIIKRKGEGRPIEDKYIHGVLVLVCLSCMYWEDLSQFPPLGAFFLGLAIPNGPPIGSALVERLESFNFGIILPLFLTAVMLRTDTTAWKGALTFFSGDDKKFAVASLVLLIFLLKLSVSVIVPYLYKMPLRDSIILALIMSHKGIIELSFYLFSLSLKLVTKDTFSILVLSIVLNSLLIPMAIGFLYDPSKQFICYQKRNLASMKNMGELKTLVCIHRPDHISSMINLLEASYQSEDSPLTCYVLHLVELRGQDVPTLISHKVQKLGVGAGNKYSENVILSFEHFHRSVCSSISIDTFTCIANANHMQDDICWLALDKAVTLIILPFHRTWSLDRTSIVSDVEAIRFLNVNVLKQAPCSVGILIERHLVNKKQEPHESLKVCVIFVGGKDDREALAFAKRMARQENVTLTVLRLLASGKSKDATGWDQMLDTVELRELIKSNNAGMVKEETSTIYLEQEILDGADTSMLLRSMAFDYDLFVVGRTCGENHEATKGIENWCEFEELGVIGDFLASPDFPSKTSVLVVQQQRTVANNN
May operate as a cation/H(+) antiporter.
Q58P71
B1P1I2
TX32B_CHIGU
Peptide F5-9.19
Chilobrachys
MKLCVLTIATLLVTATSLETQKEIAEGNELTREETPSLVEHKEDEAAAASEKRSCIEEWKTCENSCECCGSSTICSSTWAEGKEIKLCKNEGGTFKKVLHFIQKGISKLKSCKEGN
Probable ion channel inhibitor.
B1P1I2
Q4A8H6
RL22_MESH7
50S ribosomal protein L22
Mesomycoplasma
MKLENHNLAVASLKTQRISAFKARLVAVLLKGKKVSDALAILAHTKKKASPIFTKLINSAVANAINNHGFEHSNLIIKAAIVNEGPTLKRFRPRAKGAASQILKRTSHFKVILVSQNGGESQNQEYQETEKNLVTKSPENTQSGALSQQSQAEQPQNDPENGVDSQLSAKTNSTTTAKKTDLADNSTKNDATNTVLAQEKEVK
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.
Q4A8H6
B2ISX1
YIDD_STRPS
Putative membrane protein insertion efficiency factor
Streptococcus
MKRILIALVRFYQRFISPVFPPSCRFELTCSNYMIQAIEKHGFKGVLMGLARILRCHPWSKTGKDPIPDHFSLKRNQEGE
Could be involved in insertion of integral membrane proteins into the membrane.
B2ISX1
Q8UCD5
MODC_AGRFC
Molybdenum import ATP-binding protein ModC
Agrobacterium tumefaciens complex
MTLSVSARHRLGTFELDASFTSEGGVTALFGRSGSGKTSMIRIIAGLLRPDEGQISLDGEVLADSGKRLFLPAHKRRFGYVFQEARLFPHLSVAQNLRYGRWFTTGKDTNANDDRIIDMLGISHLLQRRPNRLSGGEKQRVAIGRALLSSPRLLLMDEPLASLDEQRKAEIIPYLERLRDETKIPIVYVSHSIQEVARLADRVVVMKDGKVEAEGKAAEVLSRPDFSTYLERREAGSILSGNIESFDERHGLAAVRLNAALLQVPAKKATAGTPARVLIPARDVMLALVKPEGLSALNILEGHVTGISESEDGMVTIQMDCGGDIIQSRITDLSRERLHLEPGKPVHAIIKSAALDPY
Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Q8UCD5
P14698
UCRI_DESSP
Rieske iron-sulfur protein
Desmonostoc
MAQFSESADVPDMGRRQFMNLLTFGTVTGVALGALYPVVKYFIPPASGGAGGGTTAKDELGNDVSLSKFLENRNAGDRALVQGLKGDPTYIVVENKQAIKDYGINAICTHLGCVVPWNVAENKFKCPCHGSQYDETGKVVRGPAPLSLALAHANTVDDKIILSPWTETDFRTGDAPWWA
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
P14698
A9MKX9
DCD_SALAR
Deoxycytidine triphosphate deaminase
Salmonella
MRLCDRDIEAWLDEGRLSITPRPPVERINGATVDVRLGNKFRTFRGHTAAFIDLSGPKDEVSAALDRVMSDEIVLPDGEAFYLHPGELALAVTYESVTLPPDLVGWLDGRSSLARLGLMVHVTAHRIDPGWSGCIVLEFYNSGKLPLALRPGMLIGALSFEPLSGPAARPYNRRQDAKYRDQQGAVASRIDKD
Catalyzes the deamination of dCTP to dUTP.
A9MKX9
Q5X516
RLMN_LEGPA
tRNA m2A37 methyltransferase
Legionella
MDQQKVNLLNYNYSQLRELLIAWDEKPFRAQQLFQWIHQVGICDFAQMTNLGKVLRNKLSQLACIDLPEIVACQKSADGTHKWLLKLECGNCIETVFIPEANRGTLCVSSQVGCALNCSFCSTAKQGFNRNLSTAEIIGQVWLAARELSDNNGTHDKKITNVVMMGMGEPLLNFDNVVSAMNIMMDDLAYGLSKRRVTLSTSGVLPEMERLREVSPVALAVSLHAPTDELRNELVPINKKYPLSQLISLCKRYFKDEPRRKVTFEYVMLKGVNDQPEHASQLIKLLHNVPAKVNLIPFNPFPLTQYQRSSRETIDAFRDKLMKHGINTITRKTRGDDIDAACGQLAGEVKDKTSRSQRWQKLHFMSKTEKSTELTISSEEIA
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
Q5X516
Q5HPS6
RIMP_STAEQ
Ribosome maturation factor RimP
Staphylococcus
MSKITEQVEALIQPVLNDLNFELVDIEYVKEGKDHFLRISIDKEGGVDLNDCTIASEKISEVMDENDPIPEMYYLDVASPGAERPIKKEKDFYNAINQPIFVSLYAPIEGDKEWLGVLKSVNDESINMEVKEKAKTKEIEIPRNKIAKARHAVMI
Required for maturation of 30S ribosomal subunits.
Q5HPS6
Q8TXN4
AROA_METKA
5-enolpyruvylshikimate-3-phosphate synthase
Methanopyrus
MKRVELEGIPEVRGTVCPPPSKSGSHRALIAASLCDGSTELWNVLDAEDVRATLRLCRMLGAEVDVDGEERLEATVSGFGDSPRAPEDVVDCGNSGTTLRLGCGLAALVEGTTILTGDDSLRSRPVGDLLAALRSLGVDARGRVVRGEEYPPVVISGRPLRERVAVYGDVSSQFVSALLFLGAGLGALRVDVVGDLRSRPYVDMTVETLERFGVSVVREGSSFEVEGRPRSPGKLRVENDWSSAGYFVALGAIGGEMRIEGVDLDSSHPDRRIVEITREMGAEVRRIDGGIVVRSTGRLEGVEVDLSDSPDLVPTVAAMACFAEGVTRIENVGHLRYKEVDRLRALAAELPKFGVEVREGKDWLEIVGGEPVGARVDSRGDHRMAMALAVVGAFARGKTVVERADAVSISYPRFWEDLASVGVPVHSV
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.
Q8TXN4
Q24VQ6
CRCB1_DESHY
Putative fluoride ion transporter CrcB 1
Desulfitobacterium
MFGAMLRYLIGISFFADSRFPWATLTINLLGSFLLAWLTSYVFKKVRLSPHLSTAIGTGFVGSFTTFSTLSVETISLFQDGHNFLAMVYVLVSLLGGLTMSHLGFKVSKEVQKS
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Q24VQ6
Q9ZVH7
FAX3_ARATH
Protein FATTY ACID EXPORT 3, chloroplastic
Arabidopsis
MMSIPMELMSIRNPNSTLLYRAHSRPPVKLCAPPRSLLPSRRHFSAPRAVVSYPGIRFGFTSPEVLLNRSVVAFAASHEDSGESGVEVGKEKSDIDVEDDTSKEAWKQTLESFKEQVSKMQSVSSEAYSVNSQKAMTVLKETSEQLRIQAEKAKEELGTKAKVVSEEGREYILKAAEESPSDVKEIVEAFASTEDLKNVSRANDFHVGIPYGLLLLVGGFINFMVSGSIPAIRFGVILGGALFALSLASLKSHRKGESSTKFLKGQMAIVAIIFLRELRLLLSQKSTFLGFFTTLTSGGVLGFYLYKMVVKREKGPTLEDGGEDESSDGFVRSEG
May be involved in free fatty acids export from the plastids.
Q9ZVH7
Q9CIN4
METN_LACLA
Methionine import ATP-binding protein MetN
Lactococcus
MTAIIELNNLSVQFHQKGRLVTAVKDATLHIEKGDIYGVIGYSGAGKSTLVRTINLLQKPTKGQIVINGEKIFDSENPVKFTGAKLREFRQKIGMIFQHFNLLSEKTVFNNVAFALQHSQIEDKNGKKRYLTKKEKTDKVTELLKLVDLEELSDKYPAQLSGGQKQRVAIARALANDPEILISDEGTSALDPKTTNQILDLLKSLHEKLGITVVLITHEMQVVKEIANKVAVMQNGEIIEQNSLIDIFAQPKEALTKQFIETTSSVNRFIASLSRTELLAQLADDEELIHLDYSGSELEDPVVSDITKKFDVTTNIFYGNVELLQGQPFGSLVLTLKGSSEHRAAAKAYFVERHLKFEVLGKIERTVD
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Q9CIN4
C9D7C2
CAC1A_APIME
Cacophony protein
Apis
MLGGVGGRHMSTRRRGSSPLVRGGAGLTGYAGPGASGNSNDVAAIPPDMQRYAGRRRRAVTTSDHKSCALVQTRIKLGDIMLAAQEAAQRDPGYASQYRRRPRLAGLSFGDWTSFGGEVPGLVDMAPGRDQGGGAGGGGGGGKGTTSLFILSEDNCIRKHTRFIIEWPPFEYAVLLTIIANCVVLALEEHLPKQDKTILAQKLEATEIYFLGIFCVEASLKILALGFVLHRGSYLRNIWNIMDFFVVVTGFITAFSQGIELDMDLRTLRAIRVLRPLKLVSGIPSLQVVLKSIIKAMAPLLQIGLLVLFAIVIFAIIGLEFYSGTLHKTCYSIRDINVIVKEGEQASPCNTDNKSEAPFGAHVCDANISTCMDHWEGPNFGITSFDNIGFAMLTVFQCITMEGWTAILYWTNDALGSTYNWIYFIPLIVLGSFFMLNLVLGVLSGEFAKEREKVENRQSFLKLRRQQQLEHELYCYLNWICKAEEVILAEERTTEEEKKHILEGRKRAEAKKKKLGKSKSTDTEEEEGDDDQDDGELSSSTKEKGPCKQFWLAEKRFRYWIRKSVKSQKFYWFVIVLVFFNTVCVAVEHYGQPQWLTDFLYFAEFVFLALFMLEMFIKVYALGPRTYFDSSFNRFDCVVISGSIFEVIWSEVKSGSFGLSVLRALRLLRIFKVTKYWKSLRNLVISLLSSMRSIISLLFLLFLFILIFALLGMQLFGGQFNFDSGTPPTNFNTFPIALLTVFQILTGEDWNEVMYQGIESQGGHKKGMIYSLYFIVLVLFGNYTLLNVFLAIAVDNLANAQELSAAENEEEEEDKQKQAQEIEKEIQSLQNPKDGGAPKVEICPPNGKGGKQSSEEEKKQDEDDDTGPKPMLPYSSMFILSPTNPVRRAAHWVVNLRYFDFFIMVVISLSSIALAAEDPVWEDSPRNEVLNYFDYAFTGVFTVEMILKIIDLGIILHPGSYLREFWNIMDAVVVICAAVSFAFDMTGSSAGQNLSTIKSLRVLRVLRPLKTIKRVPKLKAVFDCVVNSLKNVINILIVYILFQFIFAVIAVQLFNGKFFYCSDESKYTQQDCQGQYFVFEDGALLPEPKKREWQSQFFHYDNVMAAMLTLFAVQTGEGWPQILQNSMAATYEDKGPIQNFRIEMSIFYIVYFIVFPFFFVNIFVALIIITFQEQGEAELQDGEIDKNQKSCIDFTIQARPLERYMPKERNSVKYKIWRIVVSTPFEYFIMGLIVLNTVLLMMKFHRQSDAYKNTLKYMNMCFTGMFTVECILKIAAFGVRNFFKDAWNTFDFITVIGSIVDALVIEFGENFINVGFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIALDADTSITKHNNFQSFIQGLMLLFRCATGEAWPNIMLSCVKGRPCDAKAGKQEGGCGSNIAYAYFVSFIFFCSFLMLNLFVAVIMDNFDYLTRDSSILGAHHLDEFVRIWAEYDPNATGKIHYTEMYDMLKNMDPPLGFGNKCPNRLAYKKLIRMNMPVDVDLKVNFTTTLFALIRENLNIKVRRASERNQANEELRDTIRSIWPLQAKKMLDLLIPRNEEIGRGKMTVGKIYVCLLILESWRTTRFGQIESAGQPIMELQDVVVSDSRAGSLESLTHTGKRLHPPVQPVRHPSRSPSLRHSPGRPGYDHHGHYYHEGPGFSDTVSNVVEIQRHTHHPHPSQYNHRHRMRGPWSASTSPARTPSPIHHIDRGRHYGTTSLEQRSRSPSPIGGRQPPHTHQHYHRHHPHQHSYPVLVTRRGRGRRLPPTPNKPSTLQLKPANINFPKLNASPTHGSHIHVPIPAGMQHPPPGQHLPPMQPSHCPLSFEQAVAMGRGGRLLPSPVPNGYKPQPQAKQRTPRHSDSDEDDWC
Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, neurotransmitter release, gene expression, cell motility, cell division and cell death.
C9D7C2
A4XS49
RNFG_PSEMY
Rnf electron transport complex subunit G
Pseudomonas
MLPEISRSMLKNALVLGLFAIGTVGSVALLQQGTATRIAAAEREAQVRALAEILPAGSYDNHLLDNRIELNAPELGHRSPQSAYLALKGEQPSALILPVTAPDGYSGAIHLLVGIFADGRLAGVRVLGHRETPGLGDKIELAKSDWIRSFEGKSLSDPNEDGWAVKKDRGEFDQFAGATITPRAVVKAVHGALRYFDKHRAQLLGLAEDEQ
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
A4XS49