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2.75k
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5.51k
AlphaFoldDB
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E9RFT0
MIMB_MYCGD
Propane 2-monooxygenase, reductase component
Mycobacterium
MADSHKINFEPVDIEMDVREDENILDAAFRQGIHLMHGCREGRCSACKSYVLDGEIQMENYSTFACNDAEVDEGFVLLCRSHAFSDCTIELLNFDEDELLGGIPIQDVRTEVLAVEPKTRDIVSLRLKPVEPGKFDFKPGQYADLHIPGTEEHRSFSMATTPSCSDEVEFLIKKYPGGKFSALLDGHIQVGDEIALTGPYGSFTLKDGHVLPVVCIGGGAGMAPILSLLRHMNETGNGRPARFYYGARTAADLFYLDEILELGKGIKDFQFIACLSESAEGQVPGAVAVEEGMVTDVVARHESAIAKTEVYLCGPPPMVDAALGFLDANSVPKDQVFYDSFTSPIFDQ
Reductase component of the propane 2-monooxygenase multicomponent enzyme system which is involved in the degradation of propane via the O2-dependent hydroxylation of propane. Reductase catalyzes the transfer of electrons from NADH or NADPH to monooxygenase (Probable).
E9RFT0
Q06SD2
PSBA_STIHE
Photosystem II Q(B) protein
Stigeoclonium
MTAILEKTEVQSLWARFAAWIVSTENRLYIGWFGVLMIPCLLTATSVFIIAFVAAPPVDIDGIREPVSGSLLYGNNIISGAVVPTSNAIGLHFYPIWEAATVDEWLYNGGPYQLVVCHFFIGICCYMGREWELSYRLGMRPWIAVAYSAPVAAATAVFIIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTEAVSTNAGYRFGQEEETYNILAAHGYFGRLIFQYASFNNSRSLHFFLAIWPVVGIWFTALGLSTMAFNLNGLNFNQSIVDSQGRVVNTWADIINRANLGMEVMHERNAHNFPLDLASVEAPSING
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
Q06SD2
Q8U425
SYA_PYRFU
Alanyl-tRNA synthetase
Pyrococcus
MEFVMKTRMFEEEGWIRKTCKVCGKPFWTLDPDRETCGDPPCDEYQFIGKPGIPKKYTLDEMREKFLSFFEKHEVYPHGRVKRYPVLPRWRDDVLLVGASIMDFQPWVISGEADPPANPLTISQPSIRFTDIDNVGITGRHFTIFEMMAHHAFNYPGKHIYWIDETVELAFEFFTKELKMKPEDITFKENPWAGGGNAGPAFEVLYKGLEVATLVFMQYKKAPANADPSQVVIIKGEKYVPMETKVVDTGYGLERLVWMSQGTPTAYDAVLGYVIEPLKRMAGVEKIDERILMENSRLAGMFDIEDMGDLRYLREQVAKRVGISVEELERLIRPYELIYAIADHTKALTFMLADGVVPSNVKAGYLARLLIRKSIRHLRELGLEVPLAEIVAMHIKELSPTFPEFKEMEDIILEMIELEEKKYAETLRRGSDLVKREIAKLKKKGANEIPLEKLITFYESHGLTPEIVKEIAEKEGVKVHIPDNFYSLVAKEAEKQVEEKEEEVVDFELVKDLPDTRTLYYEDPFMKEFDAKVLKVIEDWVVLDQTAFYPEGGGQPYDTGILVVDGEEVKVTNVQKVGKVILHKVERPELFKEGTIVHGRIDWERRIQHMRHHTGTHVLMGALVRVLGKHVWQAGSQLSTDWARLDITHYKRISDEEIKEIERLANRVVMENRRVRWEWLPRTEADEKYGFRLYQGGVVPGRIIRILNIEDWDVQACGGTHLPSTGLIGPIKILRTERIQDGVERIIFACGEAAVREWQKEREIIKRTSQILRVPPEKLPETAERFFNEWKEARKEVEKLRKELAKLLVYELESKVEKVGEIEFIGEIVEGSMDDLREAANKLRKENRVVVLVNKEGHFVVAVGDKLPYTAGEFAKLITSVAGGGGGGRKELAQGKIRDIEKAKEAIEKVKGSL
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Q8U425
Q9BUE6
ISCA1_HUMAN
Iron-sulfur assembly protein IscA
Homo
MSASLVRATVRAVSKRKLQPTRAALTLTPSAVNKIKQLLKDKPEHVGVKVGVRTRGCNGLSYTLEYTKTKGDSDEEVIQDGVRVFIEKKAQLTLLGTEMDYVEDKLSSEFVFNNPNIKGTCGCGESFNI
Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway. Probably involved in the binding of an intermediate of Fe/S cluster assembly.
Q9BUE6
A8FJH3
RNH2_CAMJ8
Ribonuclease HII
Campylobacter
MKTLFDTKELLNEFDINLIGIDEAGRGALAGPMMMAACKLNKKLDGLCDSKKLSEKKREELYEIIIKNSNYLILAFSSEQIDALGLSTCLKTGLKLIKKHFKTENNFLYDGNTNLGINGIKTQIKADASILQVSAASILAKVSKDRVMNFLAKDFPCYEFEKNKAYGTKAHKELIAKFGICKLHRKSFKLL
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
A8FJH3
Q9V0T9
GATD_PYRAB
Glutamyl-tRNA(Gln) amidotransferase subunit D
Pyrococcus
MRVDEFLKERNINVGDFVRITKEEDGEEVTYEGYIMPPYELSAGDTLVLKLENGYNIGIALEKIRRIEVLERAKVKPEVHFEALIEGKPGLPEVTIIGTGGTIASRIDYETGAVYPAFTAEELAKAVPEIFEVANVKPKLLFNIFSEDMKPKHWVKIAHEVAKALNSGDYGVVVAHGTDTMGYTAAALSFMLRNLGKPVVLVGAQRSSDRPSSDAAMNLICSVRMATSEVAEVMVVMHGETGDTYCLAHRGTKVRKMHTSRRDAFRSINDVPIAKIWPNGEIEFLRKDYRKRSDEEVEVDDKIEEKVALVKVYPGISSEIIDFLVDKGYKGIVIEGTGLGHTPNDIIPSIERAVEEGVAVCMTSQCIYGRVNLNVYSTGRKLLKAGVIPCEDMLPETAYVKLMWVLGHTQNLEEVRKMMLTNYAGEITPYTRFDTYLR
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate.
Q9V0T9
Q5Z1V6
RL16_NOCFA
50S ribosomal protein L16
Nocardia
MLMPRKVKHRKQHHPSRTGMAKGGTSVAFGDYGIQALEPAYVTNRQIESARIAMTRHIRRGGKIWINIYPDRPLTKKPAETRMGSGKGSPEWWVANVKPGRVMFEMSYPNEETAREALRRAMHKLPMKCRIVTREEQF
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
Q5Z1V6
B6H233
ECM14_PENRW
Inactive metallocarboxypeptidase ecm14
Penicillium chrysogenum species complex
MRLFSPILVASTLIPLISAVPAGSSITPPPPLQPSYFTHSSPRPWARLRDWIIGSIWDIDHKHRSSKHSSPPSNIHDRYGSDVVLRFHLRQPDEAEALASASQVLFLDIWAITSEFVDIRLADDMIPSLLDLLPLTLRTSYTPLMDNLADEIYASYPSRHRSDSDFKSGLASAELKTISNCDLFFQEYQPLSVITQWMRLMASMFSSHVRMTSVGVSYEGRDIPALRLGTSHNTETTSGPRKTILIVGGSHAREWISTSTVTYVAYSLITHYGYSPAVTRLLHEYDWVLIPTINPDGYVYSWESDRLWRKNRQPTGLPLCPGVDLDRAWDYEWDGESTRSNPCSENYAGAEPFEALESQRLAQWAQNQTAHGGAEIVGFLDLHSYSQQILYPYSYSCSSVPPTLESLEELALGLAKAIRQTSHESYDVTSACEGILTQGAAAGITSGGSALDWFYHKLHTRFSYQIKLRDRGSYGFLLPSEHIVPTGKEIFRALLTFGKFVWGEEASDISLEDMTGDQIPLN
Inactive carboxypeptidase that may play a role in cell wall organization and biogenesis.
B6H233
Q7ND21
SYY_GLOVI
Tyrosyl-tRNA synthetase
Gloeobacter
MDERQVERLSGHGVAEIFPGGAEALTRRLADAETARMPLRVKLGIDPTRPDLHLGHTVVLRKLREFQDLGHTAILLIGGFTAQIGDPTGKSEARPRLSAAEVEEYAETYLDQARLILNFDTLEVRNNTEWLSGLDLAAIIKLLASTSVAQMLAKEDFGQRYEAGTAIYLHEFLYPLMQGYDSVALDADIELGGTDQRFNLLMGRNLQELFGKKPQLALTVPLLVGLDGVKKMSKSLDNYVGVTEDPLTMYSKLEKTPDALVETYFELLTDLSVSALSANPRERQKRLALAVTGWLHSPEQALRAQEAAAAMVTGSGGTGADLEAVPEFSLTEIAFPVRLANLLKAAGLCPTVSEGMRQIKNGAVRLNQERITDPNCGFAEAAELTGAVLQVGKKHFRRLVPS
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Q7ND21
A7E5P6
ARGJ1_SCLS1
Arginine biosynthesis bifunctional protein ArgJ 1 beta chain
Sclerotinia
MVINAGAKLSIARLIRPTASYHPAIGGIRYYSAPPESTIPAAKLKYIPTSGTYPQGFLVSGTYVGVKPTNKSTPDLAFLASEIPCAAAAVFTKNKFQAAPVTVSRKMLQRRENAGIRSVIINSGCANAVTGKGGMEDAEKMVAEADRCYHAPKDGKGGSSIVMSTGVIGQRMAGMTKGAGMIHPNMATLLGMIATDAPIAPALLPSLLKNAVDKSFNSISIDGDTSTNDTVAVLANGVAGGKEVTSESSKDHAAFQKVLTEFAIDLAKLVVRDGEGATKFVTIRVTEAPSEIGARKIASTIARSPLVKTALYGKDANWGRILCATGYSQISEPGEPINKVPEIVPEKTSVSFIPSDGSPELKLLVNGEPESVDETRAAEILEHEDLEILINLGGGKEEAVYWTCDFSHEYVTINGDYRT
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
A7E5P6
Q6F9F7
TGNC_ACIAD
(Z)-2-((N-methylformamido)methylene)-5-hydroxybutyrolactone dehydrogenase
Acinetobacter
MQQFQLYINGKFEDGAAQFDSINPATGEIWAKMPEARTDQVNRAVDAAEQAFYDSSWSGLTASQRGKLLYKLADLVEKSAPRLAALETTDTGKIIRETSSQIAYVAEYYRYYAGLADKIEGSFIPVDKPDMQAWLVREPVGVVAAIVPWNSQLFLSAVKVGPALAAGCTVVLKASEEAPAPLLEFAKLIDEAGFPAGVVNVITGFGPECGAVLSAHPKVAHIAFTGGPETAKHIVRNSAENLAKVSLELGGKSPFIVFADTDINSALNAQIAAIFAATGQSCVAGSRLLIEESIKDEFLQRLAERVQSIKMGLPDDMQTEYGPLCTLKQREKIQQVVQRSVEQGAKLITGGQVCDGAGYYYPPTILDCSGVSDAQSIHTELFGPVLSVDTFSTEAEAIQKANSTPYGLASGVFTSNLTRAHRMTRAIRSGIVWLNTYRVVSPLAPFGGYGLSGHGREGGLSAALEYTTTKTVWLRMSDQPIDDPFVMR
Involved in the degradation of the pyridine ring of trigonelline (TG; N-methylnicotinate) into succinate and methylamine as carbon and nitrogen sources, respectively. Catalyzes the NAD(+)-dependent oxidation of (Z)-2-((N-methylformamido)methylene)-5-hydroxybutyrolactone (MFMB) to yield (E)-2-((N-methylformamido)methylene)succinate (MFMS).
Q6F9F7
Q924K1
AIPL1_MOUSE
Aryl-hydrocarbon-interacting protein-like 1
Mus
MDVSLLLNVEGVKKTILHGGTGELPSFITGSRVTFHFRTMKCDDERTVIDDSKQVGQPMSIIIGNMFKLEVWETLLTSMRLGEVAEFWCDTIHTGVYPMLSRSLRQVAEGKDPTSWHVHTCGLANMFAYHTLGYEDLDELQKEPQPLVFLIELLQVEAPNEYQRETWNLNNEERMQAVPLLHGEGNRLYKLGRYDQAATKYQEAIVCLRNLQTKEKPWEVEWLKLEKMINTLILNYCQCLLKKEEYYEVLEHTSDILRHHPGIVKAYYMRARAHAEVWNAEEAKADLEKVLELEPSMRKAVLRELRLLESRLADKQEEERQRCRSMLG
May be important in protein trafficking and/or protein folding and stabilization.
Q924K1
P01909
DQA1_HUMAN
MHC class II DQA1
Homo
MILNKALMLGALALTTVMSPCGGEDIVADHVASYGVNLYQSYGPSGQYTHEFDGDEQFYVDLGRKETVWCLPVLRQFRFDPQFALTNIAVLKHNLNSLIKRSNSTAATNEVPEVTVFSKSPVTLGQPNILICLVDNIFPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKISYLTLLPSAEESYDCKVEHWGLDKPLLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTVFIIRGLRSVGASRHQGPL
Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.
P01909
B9L5U7
SYT_NAUPA
Threonyl-tRNA synthetase
Nautilia
MQQDVIALKIDDKIIDLQTAEAQGIEGGEPVYFDNSPEALEVIRHSAAHLMAQAIKELYPEAKFYVGPTIENGFYYDLKTETPITDKDLKNIEKKMKALAKKKFDITRYEISMEEAREKFKNDELKQAVLDMIPGDTVSIYKQGDFEDLCRGPHVPNTKYLHNVKLQKVAGAYLGGDSKNEMLTRVYGTAFATKEALQEYLKMLEEAAKRDHRKLGTELELWMFDEEVGAGMPIWLPNGALLRGNLEKLLYSAHIRREYLPVRGPELLRSHMWKISGHYYNYKENMYFTEIENDDPEKPADEYGIKPMNCLAHVKIFGHKVRSYKELPLRLFEFGTVHRHEKSGVLHGLLRVREFTQDDAHIFCRPDQIEEEVIKVLEFVDSIMERFGFNYEMEISTRPEKSIGSDEIWEKATESLKKALNSLNREYGIDEGGGAFYGPKIDIKITDAIGRKWQCGTIQVDFNLPERFDITYVDENNERVRPVMIHRAIIGSFERFIAILTEHYAGEFPTFIAPIKAIFVPIAESHVEYAKKLQKELLEADINTEIFASNDSLNKRIRNAEKRRVGYVVIIGDEEVETGTVAIRDRKKREQYKMTKGEFVEMIKNLSEVKL
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
B9L5U7
O20213
RR4_FURFO
30S ribosomal protein S4, chloroplastic
Furcraea
RFKKIRRLGTLPGLTSKRPRSGSDLKNPLRSVKRSQYRIRLEEKQKLRFHYGLTERQLLRYVHIAGKAKGSTGQVLLQLLEMRLDNILFRLGMASTIPGARQLVTHRHILVNGRIVDIPSYRCKPRDIITTKDKQRSKALIQNYIASSPHEELPNHLTIDSFQYKGLVNQIIDSKWIGLKINELLVVEYYSRQT
With S5 and S12 plays an important role in translational accuracy.
O20213
B8J4E1
RL20_DESDA
50S ribosomal protein L20
Desulfovibrio
MRVKRGLSGHRRHKKYLTAAKGFRGGRSRLYRTAREAVERSLQYAYVGRKLRKRDFRTLWILRINAGARLSGLSYSRFMHGLKLAGIELNRKVLADLAVYKKDDFAKIVDMAKAALGK
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.
B8J4E1
Q21882
HIUH1_CAEEL
Transthyretin-like protein R09H10.3
Caenorhabditis
MNKFSLFFALTATLMTITESAVPTASISAHVLDISGGSPAGGVQILAYIQQNDDWTKIGSEFTQDNGRVDWVSPDFTLIPGTYRLVYITEPYYKAKNVESFYPYVEVVFNIRDATQHYHVPLTLSPWGYSTYRGS
Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Q21882
C1KVI5
GLPK_LISMC
Glycerokinase
Listeria
MEKKYILALDQGTTSSRAMIIDEEGEVIGVAQEEFDQIFPKPGWVEHNANEIWASILAVIAGVLLKTNISSKEIAGIGITNQRETTVIWDKESGNPIYNAIVWQSRQTEDICKQLRKDGYEDTIRSKTGLLIDPYFAGTKARWILDHVDGAQERAEKGELLFGTIDTWLVWKLTGGRAHITDYSNASRTLLYNIYDLEWDDELLKMLNIPKAMLPEVRPSSEVYADTVPYHFFGEEVPVAGIAGDQQAALFGQGCFEKGMAKNTYGTGCFLLMNTGEKAVRSENGLLTTLAWGIDGKVEYALEGSIFVAGSAIQWLRDGLRMVRQSSDSENYASRIESSDGVYVVPAFVGLGAPYWDSDVRGAVFGLTRGTEKEQFIRATLESLAYQTRDVLYAMEQDSGISLKTLRVDGGASANNFLMQFQSDILGVPVERPENKETTVLGAAFLAGLAVGVWKDKNEIKKHWKLDKRFEVEMKDEQREDLYEGWHKAVKAAQAFK
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
C1KVI5
A1WVX2
DCUP_HALHL
Uroporphyrinogen decarboxylase
Halorhodospira
MSSSELKNDRILRAFQRQPVDRTPVWMMRQAGRYLAEYREVRAQAGSFMGLCRSPELAARVTMQPLERYELDAAILFSDILTIPEAMGLGLNFVTGEGPVFEHRVKTAADIDRLPQPSAQKELRYVMDAVAACRKELNGQVPLIGFTGSPWTLATYMIEGGSSKTFAASKSLLFNEPEAAHRLMAKLADTVADYLNGQVEAGAQALMIFDTWGGALDPVRYREFSLAYMQRILEQLPREREGRRIPVTLFTKGGGQWLEDIADTGCDGVGLDWTTSLADARRRIGGRVALQGNLDPCMLHANPEVIRREVARCLEEFGHGPGHVFNLGHGIQPETPPENVDAMIRALHELSPAYHDATATSATS
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
A1WVX2
Q12S27
TATB_SHEDO
Sec-independent protein translocase protein TatB
Shewanella
MFDGIGFMELLLIGILGLVVLGPERLPVAVRSVTGWIRALKRMANSVKDELEQELKIEQLHADLKKAESKGLANLSPELQESIDQLKQAAQSVNRPYQLDESNEQEPKIAPPQANIAETPTQSGDTHSKNNG
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Q12S27
Q9STY3
PME33_ARATH
Pectin methylesterase 33
Arabidopsis
MLRGIFHICLLASFLLLPFSSAVHDSGFTGGTDAPPPWDHNVSPPPETAPSPTPTSSPSTTSPPSPGPVAAPSPINNGSVSGDMTWWCNKTPHAETCNYYFRKSSQNNINLRPPRFRSEFLRMLVKVALDQAVITHSQTVKFGPSCTNNQRKAAWSDCVNLFQNTVAQLNRTLKGLNPAASSDVKCTDFDAQTWLSTAQTNIETCRSGSEDLNVSDFVMPVISNKNLSDLIGNCLAVNGVLMKQHDHTTTANHKEYFPSWVSRHERRLLVSASLAKSSPHLVVAQDRSGHFRSIQAAINFAARRRFKSRFVIYVKKGVYRENIDVGNDNHNIMLVGDGERKTIITSGRSVQHGYTTYNSATGGFGGQRFVAKDMTFINTAGPLRGQAVAVRSSSDLSVFYRVGIHGFQDTLYIHSQRQFFRECYISGTIDFIFGNAAVVFQNCMILVRRPLHGQANIITAQGRGDPFQNTGITIHSSRIIAASDLKPVIRAYKTYLGRPWQAYSRVTIMKTYIDNSISPLGWSPWLRGSNFALNTVFYGEYKNFGPGSSTRWRVRWKGFHAITSTAVASRFTVGSLIAGGSWLPATGVPFKSGL
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Q9STY3
P54700
FLIP_SALTY
Flagellar biosynthetic protein FliP
Salmonella
MRRLLFLSLAGLWLFSPAAAAQLPGLISQPLAGGGQSWSLSVQTLVFITSLTFLPAILLMMTSFTRIIIVFGLLRNALGTPSAPPNQVLLGLALFLTFFIMSPVIDKIYVDAYQPFSEQKISMQEALDKGAQPLRAFMLRQTREADLALFARLANSGPLQGPEAVPMRILLPAYVTSELKTAFQIGFTIFIPFLIIDLVIASVLMALGMMMVPPATIALPFKLMLFVLVDGWQLLMGSLAQSFYS
Plays a role in the flagellum-specific transport system.
P54700
A5UBV9
CDD_HAEIE
Cytidine aminohydrolase
Haemophilus
MQELIKRTLPQDDALNQAIVNELRSQNWAGFLNYSQVQQLCHNFELTPLKLAMHLLPLAASYSHTAISHFNVGAIAIGEQGDFYFGANQEFANSAIQQTIHAEQSAISHAWLRNERRISDMVVNYTPCGHCRQFMNELHGAEKISIHLPHSQNNPLHSYLPDAFGPKDLDIAAHLLADENHDLIADHQDDLINQAILAANQSHCPYSNSPHGIAILFKNGDMVTGRYAENAAFNPSLPALQTALNFAYLNDKKLSDIERIVMAEKALKLSHKTMAETLLSTLTSVELEYYSL
This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
A5UBV9
Q14GU4
UBIE_FRAT1
Demethylmenaquinone methyltransferase
Francisella
MSKENKTTDFGFTQVPWEEKQKKVAGVFHSVAAKYDLMNDLMSFGIHRIWKKQTIAKSGVRKGDNVLDLAGGTGDLAYKFCQMVGQQGKVILSDINSSMLEVGKEKLTNKGCVGNIEYVQANAECLPFPDNYFDCITISFGLRNVTDKDKALASMCRVLKPGGRSLVLEFSKPIIPLLSKVYDEYSFKALPFLGKIITQDAESYKYLAESIRKHPDQQTLKQMMYDAGFDNVEYQNMTGGIVALHIGYKY
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Q14GU4
A1KLV4
PDXT_MYCBP
Pyridoxal 5'-phosphate synthase glutaminase subunit
Mycobacterium tuberculosis complex
MSVPRVGVLALQGDTREHLAALRECGAEPMTVRRRDELDAVDALVIPGGESTTMSHLLLDLDLLGPLRARLADGLPAYGSCAGMILLASEILDAGAAGRQALPLRAMNMTVRRNAFGSQVDSFEGDIEFAGLDDPVRAVFIRAPWVERVGDGVQVLARAAGHIVAVRQGAVLATAFHPEMTGDRRIHQLFVDIVTSAA
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
A1KLV4
A1BJA7
GCSPB_CHLPD
Glycine dehydrogenase (aminomethyl-transferring) subunit 2
Chlorobium
MREKLIFDLSRNGRKGYSLSKNDLPETSVAAVIPSKFLRTTPAELPEVPESEVVRHFIRLSNLNYHVDKNMYPLGSCTMKYNPKVNDYTCDLPGFSTLHPLQPSETTQGALRLMYELSSMLSEIAGMAAVSLQPAAGAHGELTGILLIKKYHEAQGKMRNKLLVVDSAHGTNPASAAIAGYEIISVRSNADGRTDLEDLKARLQSDVAALMLTNPNTIGLFEKDILAIERMVHENGSLLYMDGANMNALLGITRPGDMGFDVVHYNLHKTFSAPHGGGGPGSGPIGVSARLAGYLPVPVIEKEESATGTSYRLNYDRPESIGRMISFYGNFSVLVRAYTYIRMLGPEGLRRVSENAIINANYLLSLLLERYDLPYPKSVMHEFCLSGDRQKKANGVKTLDMAKRLLDYGFHAPTIYFPLIVSEALMIEPTETETKETLERFAEAMIAIADEAENNPALVKSAPETTPVKRLDEAQASRQLNICCSL
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
A1BJA7
A4X3X5
RNPH_SALTO
tRNA nucleotidyltransferase
Salinispora
MARPDGRLPDHLRPVTLTRGWSTHPEGSVLVEFGATRVLCTASVTEGVPRWRKGSGLGWVTAEYAMLPRATNTRSDRESVKGRVGGRTHEISRLIGRSLRASIDLKALGENSIVLDCDVLQADGGTRTAAITGAYVALHDAVTWLAARRSLAGRPETVMHRSVAAVSVGVVAGEPRLDLNYAEDASAEVDLNVVCTGAGDFVEVQGTGEAGVFSRGQLDALLDLAVAGCVELAEAQRKALS
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
A4X3X5
P68896
PCP_STRP1
Pyroglutamyl-peptidase I
Streptococcus
MKILVTGFDPFGGEAINPALEAIKKLPATIHGAEIKCIEVPTVFQKSADVLQQHIESFQPDAVLCIGQAGGRTGLTPERVAINQDDARIPDNEGNQPIDTPIRADGKAAYFSTLPIKAMVAAIHQAGLPASVSNTAGTFVCNHLMYQALYLVDKYCPNAKAGFMHIPFMMEQVVDKPNTAAMNLDDITRGIEAAIFAIVDFKDRSDLKRVGGATH
Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
P68896
A5VKT6
MIAA_LIMRD
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Limosilactobacillus
MNKVIAIVGPTAVGKTALSIKLAHEFDGEVISGDSMQVYRRLDIGTAKVTPEEMGDVPHHLIDICNIEERFSAARFKKLADQKIDEIAQRNHLPIIAGGTGFYLQTLTDNLALGSDQFDQQTLDIRNHWKEVAEEKGAEYVWEQLNKLDPVASARIPKSNTRRVIRALEVIKKTGQLFSNQPHFKATNDFLLIGLTTDRPVLYDRINKRVDLMIQNGLLEEAKWLFDQGGEDLPAGKGIGYHELFPYFRGEISLDEAVEKIKQDSRHYAKRQLTWFRNKADTHWFDILRHPDDINQIKQFINDWLKK
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
A5VKT6
C0QKM9
RPOZ_DESAH
Transcriptase subunit omega
Desulforapulum
MARVTIEDCLKNVPSRFALVHMAALRVRQLREGADLLIKPSKNEDAVIALREIAANRIVLKNKSDKKG
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
C0QKM9
Q6B8V5
RK23_GRATL
50S ribosomal protein L23, chloroplastic
Agarophyton tenuistipitatum
MTKTIKVKKSALIDIIKYPILTDKTTQMIEENKYSFAVEVKAKKPKIKEAIEQLFDVKVQQINTLIVKPQKKRVGKYIGYKSKYKKAVIKLYDPYKINLFADN
Binds to 23S rRNA.
Q6B8V5
B9LJC8
EFG_CHLSY
Elongation factor G
Chloroflexus
MPRQIELDKVRNIGIIAHIDAGKTTTTERILFYTGRTYKIGEVHEGTATMDWMPQEQERGITITAAATTAPWRLDGVEYRINIIDTPGHVDFTVEVERSLRVLDGGVVVFDGVAGVEPQSETVWRQADKYNVPRICFVNKMDRVGASFERCVQMIKDRLGAKPAIVQLPIGVEDSFRGTIDLFKMKATVYYDDLGKDIREEEIPAELRPAAEQARNELIEMIAETDDELTLLYLEGQELTVEELKRGLRKATIERKLVPVLCGAALRNKGVQKLLDAVVEYLPSPLDRPAITGTLPGQVMGDEGVEVITRPVSDDAPFTALVFKIVADPYVGKLAYFRVYAGKITKGSYVLNSTRNQRERLGRILRMHANHREDIEEVYAGEIAAMVGPKNSYTGDTICDPDHPIVLESIRFPEPVIELAVEPKTKADQDKMSIALSRLAEEDPTFRVYTDPETGQTIIKGMGELHLEVILDRMRREYKVEANQGKPQVSYRETITIPVDQETRFVRQTGGKGQYGHVKIKFEPLPPGSGFEFVNAIVGGVIPKEYIPAVEQGLREAMQTGVIAGYPVVDVKATLYDGSYHEVDSSEMAFKIAASMCLKDAVRRGKPQLLEPIMKVETVTPEEFLGTVIGDFNSRRGRIEGMEARGNAQVVRAFVPLANMFGYMTDLRSATQGRATSSMEFDHYEPLPEALAKEIIEKRSAN
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.
B9LJC8
A6UX64
RECF_PSEA7
DNA replication and repair protein RecF
Pseudomonas
MSLTRVSVTAVRNLHPVTLSPSPRINILYGDNGSGKTSVLEAIHLLGLARSFRSARLQPVIQYEEAACTVFGQVMLANGIASNLGISRERQGEFTIRIDGQNARSAAQLAETLPLQLINPDSFRLLEGAPKIRRQFLDWGVFHVEPRFLPVWQRLQKALRQRNSWLRHGKLDPASQAAWDRELSLASDEIDAYRRSYIQALKPVFEETLAELVSLDDLTLSYYRGWDKDRDLQDVLASSLLRDQQMGHTQAGPQRADLRIRLAGHNAAEILSRGQQKLVVCALRIAQGHLINRAKRGQCVYLVDDLPSELDEQHRMALCRLLEDLGCQVFITCVDPQLLKDGWRTDTPVAMFHVEHGKVSQTTTIGSEA
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
A6UX64
A1S9L6
PYRC_SHEAM
Dihydroorotase
Shewanella
MTHLTLTRPDDWHIHLRDGDSLADTVRDAGRYMGRAIVMPNLVPPVTTTEAAIAYYERIKAHSSTAFEPLMVLYLTDKTSPDEIRAAKASGKVVAAKLYPAGATTNSDSGVTDVNNIYGVLKAMEEEGLLLLVHGEVTDSAIDIFDRERIFIENILSKVVADFPGLKIVLEHITTKDAVDFVMSAGDNVAATITAHHLLYNRNHMLAGGIRPHFYCLPILKRNTHQQALLAAATSGSKKFFLGTDSAPHAKDKKEAACGCAGSYTAHAALELYAEAFEAEGALDKLEAFASFNGPDFYGLPRNADTVALVKSPWQVPESYPLGSTTVVPIRAGEIIGWKVED
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
A1S9L6
Q08120
BACA_RHIME
Bacteroid development protein BacA
Sinorhizobium
MFQSFFPKPKLFFISSAVWSLLAVLAWYAGGRDIGAYLGLPPLPPGQEPVIGVSVFWSTPFLWFYIYYAVVAGLFAAFWFAYSPHRWQYWSVLGTALIIFNTYFSVQVSVAINAWYGPFYDLIQQALARTAPVTAGQLYSGMIGFSGIAFVAVTVGVLNLFFVSHYIFRWRTAMNEFYVAHWPRLRHVEGASQRVQEDTMRFSSTVERLGVGLVSSIMTLIAFLPVLFKFSEQVNVLPIVGEIPHALVWAAVFWSVFGTVFLAAVGIKLPGLEFRNQRVEAAYRKELVYGEDHEDRADPITLAQLFDNVRRNYFRLYFHYMYFNIARIFYLQADNLFGTFVLVPAIVAGKLTLGVMNQVLNVFGQVRESFQYLVNSWTTIVELLSIYKRLKAFESVLVDEPLPEIDRQFIDAGGKEELAL
Functions in the transport of molecules, possibly peptides, across the inner membrane. Is essential for bacteroid development.
Q08120
B2ISI9
SYP_STRPS
Prolyl-tRNA synthetase
Streptococcus
MKQSKMPIPTLREMPSDAQVISHALMLRAGYVRQVSAGVYSYLPLANRVIEKAKNIMRQEFEKIGAVEMLAPALLSAELWRESGRYETYGEDLYKLKNREKSDFILGPTHEETFTAIVRDSVKSYKQLPLNLYQIQPKYRDEKRPRNGLLRTREFIMKDAYSFHANYDSLDSVYDEYKAAYERIFTRSGLDFKAIIGDGGAMGGKDSQEFMAITSARTALDRWVVLDKSVVSFDEIPAEVQEEIKAELLKWIVSGEDTIAYSSESSYAANLEMATNEYKPSNRVVAEEEVTRVATPDVKSIDEVAAFLNVPEEQTIKTLFYIADGELVAALLVGNDQLNEVKLKNHLGADFFDVASEEEVANVVQAGFGSLGPVGLPENIKIIADRKVQDVRNAVVGANEDGYHLTGVNPGRDFTAEYVDIREVREGEISPDGQGVLNFARGIEIGHIFKLGTRYSASMGADVLDENGRAVPIIMGCYGIGVSRLLSAVMEQHARLFVNKTPKGEYRYAWGINFPKELAPFDVHLITVNVKDEEAQALTEKLEASLMGAGYEVLTDDRNERVGVKFSDSDLIGLPIRITVGKKATDGIVEVKIKATGDTIEVHADNVLETLEILSKK
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
B2ISI9
Q7WG18
LPTD_BORBR
LPS-assembly protein LptD
Bordetella
MRMLRWLILSAFSVAGAVQAQGNQDSAAASAPSASIGAPVLRTSPGLRVHRLPDEKIPAFMEADQISGDPDSEVTLTGNAQVRRVDGIIKGDRINYRRDTGDVDVQGSARMLRDGTLITGPSARLNVDTYSGEIQEPNFWIGASGGTAQARHADIFSKSQMRLSQVTYSGCPCPKPSWYIKADTVDLDFDENEGVARNGVLYFKDVPILASPYLTFPVKKERKSGFLMPTYGTTSNSGFDISLPYYFNLAPNYDLTLVPRYLSKRGAQLGGEFRYLGSGYRGVAIGTYLPDDNETGRDRWMYRTYHRQLLGNGFYTDWDIAGASDDNYFRDISELGLNTASTTYLPRRGRVGWSSTYWQTYAQVYKYQTLQDPDAPLAPPYDKVPELWLKGARYDWGGFDAEWVSTAVRFQRPLLNGRRLGPDGDRLQTYPTVSYPIVRPGWFLVPKVGVHYTQYRTDWYNRDWNRIGLSNYKRTESRTVPIMSLDAGMIFERDASLFGKAATQTLEPRLYYLRVPYRDQSALPVYDTTLADFSFDQAFQENIYTGGWDRIANANQLTAALTTRWLDANTGFERLSLSAAQRIYFQDQEVTLPAEQPRKNVRSDFLVGATAALTDTLTTDVAAQYNPYDNKWSRGMVSARWSPQRLTTVAVAYRYQRDPLPGISYQPQGQNQVSLAVQWPIHRRWYGVGRVDYSLRSEPATAAAAEQSPRVTQAIAGLEYKGDCCWVGRVVYQRYAVSAADTNTALFFQLELTGLGALGTDPISLLNRSIPGYQSVVPPTPTGTTFERYE
Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.
Q7WG18
B0B874
NDK_CHLT2
Nucleoside-2-P kinase
Chlamydia
MEQTLSIIKPDSVGKAHIGEIIAIFEKSGLRIAAMKMVHLSVKEAEGFYVVHKERPFFQELVDFMISGPVVVMVLQGENAVARNRELMGATNPKEAAEGSIRALFGESIGVNAVHGSDSLENAAIEVSYFFAKTEVVNSVA
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
B0B874
C5D3G3
IDI2_GEOSW
Type 2 isopentenyl diphosphate isomerase
unclassified Geobacillus
MSRAKRKIEHIQHALSTADQGASGFDDITFVHQSLPDVRMNDIHLHTALGELSLSSPFFINAMTGGGGKQTFEINKGLAEAAKHCRIAMAVGSQTSALRDNKQRGTFEIVRKVNKNGIIFANIGSEATVDDAKRAVDMIEADGLQIHLNVVQELVMPEGDRDFTGVLLRIEQIVQAVQVPVIVKEVGFGMSKETASRLEEVGVKIIDVGGLGGTNFARIENKRRSNIITYFNDWGIPTAASIVEVAQTSPSLVVIGSGGVRTALDAAKAIALGASAVGMAGPLLRTLVEQGVEALVASIEELHHDLTLIMGALGAKTIDKLQRVPLVIRGDTHHWLTERGFDTKVYSCR
Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
C5D3G3
Q4UWA4
RIMP_XANC8
Ribosome maturation factor RimP
Xanthomonas
MSEKATEIANLLGPTVESLGLELLGVEYLPAPGGATLRLYIDVPLAEQPDRIINVDDCERVSREVSAQLDVEDPISGNYTLEVSSPGVDRPLFTLDQFARHVGESAKIVLKLAQDGRRRFQGQIVRIDTEAAAVVFSVDGKDVQIGFGNIDKARILPDWVALGLAPQKPNKPGPKKPGHDKKKPSNEPAAGKPRAE
Required for maturation of 30S ribosomal subunits.
Q4UWA4
P49544
RK1_TRICV
50S ribosomal protein L1, chloroplastic
Trieres
MRKLSRRQKENRAKTKDSIYSNLEDAITILQETATAKFTETVELHANLNIDPKYADQQLRTTVTLPHGIGKTINIAVLTNDSNFTEAREAGADRVGSDDLIEEISQGNISFDLLIATPDMMPKLAKLGRVLGPKGLMPSPKSGTVSTTLTATLSEFKKGKFEYKADKAGVVHVSFGKSNFTHSQLMENLTALYKSIEQNRPSGVKGKYFKSLFICTTMGPSIQLDLNIFL
Binds directly to 23S rRNA. Might be involved in E site tRNA release (Potential).
P49544
Q8L4H0
WEE1_ARATH
Wee1-At
Arabidopsis
MFEKNGRTLLAKRKTQGTIKTRASKKIRKMEGTLERHSLLQFGQLSKISFENRPSSNVASSAFQGLLDSDSSELRNQLGSADSDANCGEKDFILSQDFFCTPDYITPDNQNLMSGLDISKDHSPCPRSPVKLNTVKSKRCRQESFTGNHSNSTWSSKHRVDEQENDDIDTDEVMGDKLQANQTERTGYVSQAAVALRCRAMPPPCLKNPYVLNQSETATDPFGHQRSKCASFLPVSTSGDGLSRYLTDFHEIRQIGAGHFSRVFKVLKRMDGCLYAVKHSTRKLYLDSERRKAMMEVQALAALGFHENIVGYYSSWFENEQLYIQLELCDHSLSALPKKSSLKVSEREILVIMHQIAKALHFVHEKGIAHLDVKPDNIYIKNGVCKLGDFGCATRLDKSLPVEEGDARYMPQEILNEDYEHLDKVDIFSLGVTVYELIKGSPLTESRNQSLNIKEGKLPLLPGHSLQLQQLLKTMMDRDPKRRPSARELLDHPMFDRIRG
Cell cycle regulatory kinase that is not rate-limiting for cycle progression under normal growth conditions. Transcriptionally activated upon DNA stress or damage in an ATR- or ATM-dependent manner. Once activated, inhibits plant growth by arresting dividing cells in the G2 phase before proceeding into mitosis. Down-regulates CDKA-1 and CDKD-2 by tyrosine phosphorylation. May target principally CDKA-1.
Q8L4H0
Q9JIF3
GTR8_MOUSE
Glucose transporter type X1
Mus
MSPEDPQETQPLLRPPEARTPRGRRVFLASFAAALGPLSFGFALGYSSPAIPSLRRTAPPALRLGDNAASWFGAVVTLGAAAGGILGGWLLDRAGRKLSLLLCTVPFVTGFAVITAARDVWMLLGGRLLTGLACGVASLVAPVYISEIAYPAVRGLLGSCVQLMVVTGILLAYVAGWVLEWRWLAVLGCVPPTLMLLLMCYMPETPRFLLTQHQYQEAMAALRFLWGSEEGWEEPPVGAEHQGFQLALLRRPGIYKPLIIGISLMVFQQLSGVNAIMFYANSIFEEAKFKDSSLASVTVGIIQVLFTAVAALIMDRAGRRLLLALSGVIMVFSMSAFGTYFKLTQSLPSNSSHVGLVPIAAEPVDVQVGLAWLAVGSMCLFIAGFAVGWGPIPWLLMSEIFPLHVKGVATGICVLTNWFMAFLVTKEFSSVMEMLRPYGAFWLTAAFCALSVLFTLTVVPETKGRTLEQVTAHFEGR
Insulin-regulated facilitative hexose transporter that mediates the transport of glucose and fructose . Also able to mediate the transport of dehydroascorbate .
Q9JIF3
A8EXL6
DAPB_RICCK
4-hydroxy-tetrahydrodipicolinate reductase
belli group
MINIGLSGSTGKMGRAIAERIDEFENCKISAKFSSTNSLYDLDNFCKHSDVFIDFSTPEILETLVNYALKHNTKLVIGTTGLQPKHFKLLEKAAQTLPILYSANMSIGANLLSYLAKEAIKILDDYDVEILDIHHRNKKDSPSGTAIMLAETIANGKDLDIIFNRGNRPRKKEEIGISSLRGGNVHSIHEISFLDDNEIITLKHEALNNNSFANGAIKAAIWLQDKPSALYSMQDIYKIY
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
A8EXL6
A2C296
FMT_PROM1
Methionyl-tRNA formyltransferase
Prochlorococcus
MKIVFWGTPKYAAENLRTIVKAGYEVIAVVTQPDRKRGRGKKLSPSPVKEAAEELSIPVYATHSISKDQKTKELLLNLKADVYLVVAFGQILPKEILDQPNLGCWNSHASLLPAWRGAAPIQWSIINADTKTGICIMSMEEGLDTGPVIEQESTIIKDSDNLEILTNRLSRMSSKLLLKSLEKIKLTKGLNKSSRLKKLNAIDQTNLKGSPSYARQITKEDNLIDWNQDAKKIIKKIQGLYPNAYTFYNAKRIKILEAIISSDNNQSKESQDIKNQSKTNRIPGEIIMINKQIGIKLMTNDYPILIKYAQLEGKKATDSYTLSIQSNLSINDKLGS
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
A2C296
Q26457
LA_AEDAL
La ribonucleoprotein
Stegomyia
MTEVEAKATATEETTKEEEEAPETTAEQTEESAQETSENVSKLEASTIRQLEYYFGDANLARDKFLQEQISKDEGWVPVDVLLTFKRLKSLSEDKKVIVDAIEKSDEGLIEVSEDREKLRRHPERPLPEQNEETRKEIYGRTVYVKGFAPEEGTQMSELLEFFEPFEKITNIVMRKYHDKATKKYLFKGSVFVTFATKDHCAEFLKKEKLGYKGKELIRKMQDDYFEEKKAERRKKDKKKEEDRFNIDHLPKGASVHLSGFNKDTSRETIKETILKLDESLEVAFIDYAKTDTEGTVRFAADDAGKKFMEKLTDSKIQIDEEEITARLLEGDEEKEFLRKVVKDQQARRQASNARNKGRTPEGRQASRPPQEWRRKAKGGRGE
May be involved in transcription termination by RNA polymerase III. Binds RNA and DNA. Binds to the 3' end of the minus strand of Sindbis virus RNA. This may be significant for Sindbis virus RNA replication.
Q26457
O19899
PYG_CYACA
Phycobilisome rod-core linker polypeptide cpcG
Cyanidium
MAIPLLYYPYSSQNHRVNSFEIKGNDEQPRIFSTDSLPTSSEMDEIIWAAYRQIFSEHQILKFNRDTYLESQLRFNQITVREFIRGLLLSERFRILNYDVNNNYRFSEMCVQRVLGRDIYNDKEKIAWSIVLCTRGIKAFVDSLVNSKEYEENFGDNTVPYQKRRVIFQRSKGEVPFNLKTPRYGSDFKERLGMPQYAWQGAIRTFRPQEIKPRPGDPVLYLDMSRELLFSRFR
Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
O19899
Q01369
GBLP_NEUCR
Cross-pathway control WD-repeat protein cpc-2
Neurospora
MAEQLILKGTLEGHNGWVTSLATSLENPNMLLSGSRDKSLIIWNLTRDETSYGYPKRRLHGHSHIVSDCVISSDGAYALSASWDKTLRLWELSTGTTTRRFVGHTNDVLSVSFSADNRQIVSGSRDRTIKLWNTLGDCKFTITEKGHTEWVSCVRFSPNPQNPVIVSSGWDKLVKVWELSSCKLQTDHIGHTGYINAVTISPDGSLCASGGKDGTTMLWDLNESKHLYSLNANDEIHALVFSPNRYWLCAATSSSIIIFDLEKKSKVDELKPEFQNIGKKSREPECVSLAWSADGQTLFAGYTDNIIRAWGVMSRA
Required to activate general amino acid control under conditions of amino acid limitation in the vegetative growth phase, and for formation of protoperithecia in preparation for the sexual phase of the life cycle of N.crassa.
Q01369
Q87AE8
THIG_XYLFT
Thiazole synthase
Xylella
MNNFASNDPLVIAGTVYSSRLLTGTGKFKDLDETRLATEAAGSQIVTVAIRRVNIGQDPHQPNLLNVLSPDRYAILPNTAGCYTAEDAVRTCRLARELLDGHRLTKLEVLGDKKTLYPDVVQTLKAAEQLVAEDFQVMVYTSDDPILAKRLEEIGCVAVMPLAAPIGSGLGVQNRYNLLEIIENAQVPIIVDAGVGTASDAAIAMELGCDAVLMNTAIAGARDPVLMASAMRKAVEAGREAFLAGRIPRKRYAAASSPVEGLVG
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Q87AE8
Q96CQ1
S2536_HUMAN
Solute carrier family 25 member 36
Homo
MSQRDTLVHLFAGGCGGTVGAILTCPLEVVKTRLQSSSVTLYISEVQLNTMAGASVNRVVSPGPLHCLKVILEKEGPRSLFRGLGPNLVGVAPSRAIYFAAYSNCKEKLNDVFDPDSTQVHMISAAMAGFTAITATNPIWLIKTRLQLDARNRGERRMGAFECVRKVYQTDGLKGFYRGMSASYAGISETVIHFVIYESIKQKLLEYKTASTMENDEESVKEASDFVGMMLAAATSKTCATTIAYPHEVVRTRLREEGTKYRSFFQTLSLLVQEEGYGSLYRGLTTHLVRQIPNTAIMMATYELVVYLLNG
Mitochondrial transporter that imports/exports pyrimidine nucleotides into and from mitochondria. Transports preferentially cytosine and uracil (deoxy)nucleoside mono-, di-, and triphosphates by uniport and antiport mechanism. Also transports guanine but not adenine (deoxy)nucleotides. Is inhibited strongly by pyridoxal 5'-phosphate, 4,7-diphenyl-1,10-phenanthroline, tannic acid, and mercurials (mercury dichloride, Mersalyl acid, p-hydroxymercuribenzoate). Participates in mitochondrial genome maintenance, regulation of mitochondrial membrane potential and mitochondrial respiration.
Q96CQ1
B3ECI3
SYM_CHLL2
Methionyl-tRNA synthetase
Chlorobium
MQHVTRTLVTTALPYANGPVHLGHLAGVYLPADIYVRYKRMKGEDVIHIGGSDEHGVPITITAEKEGISPQDVVDRYHRMNSEAFRKCGISFDYYGRTSSQGHHDTAKEFFLEIERKGIFRRKTEKLFFDAKAERFLSDRYVTGTCPICNNPEANGDQCEQCGTHLSPTELLNPKSKLSDATPELRDTMHWYFPLGRFQEALEAYVASHEHDWRPNVVNYTRTWLKQGLNDRAITRDLSWGIQVPLDDPEACGKVLYVWFDAVLGYISFTRQWAAEAGDESLWRAYWQDPESRVVNFIGKDNVVFHTLMFPAILMAWNEGRQSGIYNLADNVPASEFMNFEGRKFSKSRNYAVYLGEFLEKFPADTLRYSIAMNYPENKDTDFSWQDFQNRTNGELADTLGNFIKRSVDFTNSRFDGVVPFSCTDDDWNVLGIDWSQTIEKLDQAYEQFHIRETASLGMDIARSANRFLTESEPWKVIKTDREAAAKTMALSLNLCYALAITLYPVIPETAGRIYAMLGFEGSIDARIKRGVSAIEELLAPQLHKGHRIRKESEILFTKIEDADIEPELKKIEKLLADAEKLEAAALSQEMTFKPEISFDDFLKVDLRVATVLGAEKVKKAGKLLKLQLKVGTEARQVLAGIAQFYSPEEMVGKQVVLVANLAERTIRGEISQGMILAVEGADGRLCVVEPVGDEINGQQIQ
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
B3ECI3
B6EHW3
SYY_ALISL
Tyrosyl-tRNA synthetase
Aliivibrio
MTATNELLQDLKARGLIAQCTADEELAEHLSTDCRTLYCGFDPTADSLHIGSLVPLLVLKRFQQAGHKPLALVGGATGLIGDPSFKAAERQLNTSDVVGDWVNKIRAQVSAFVDFNESKNGAEVVNNLDWIGEINVIEFMRDIGKHFSVNSMIQKESVKQRIDREGSGISFTEFSYMLLQSYDFAALNKAKECTLQIGGSDQWGNITGGIDLTRRMNRNKVFGLTLPLVTKSDGTKFGKTESGTIWLDPSKTSPYAFFQFWLGTADADVYDFLRFFTFLSVDEIAAFEESDKSVQGRPAGQGVLAKEVTRLVHGEEGLASSERITAALFSGDLASLTETDLAQLAQDGLPTTELEASEQTIVEVLTQSELAKSNKMAREFIGNGAVSVNGEKVADAEVILKKEDALFGKYSVIKRGKKLFNLYIWK
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
B6EHW3
A5ELP2
RL11_BRASB
50S ribosomal protein L11
unclassified Bradyrhizobium
MAKKVTGYLKLQVPAGAANPSPPIGPALGQRGLNIMEFCKAFNAQTQKEEKNTPIPVVITIYADRSFTFEMKTPPMSYFLKQAAKIQSGSKAPGRDKAGKVTKAQVREIAEKKMKDLNCDSIESAMKMVEGSARSMGLEVAG
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
A5ELP2
A0A0K0XCY8
MIMG_MYCGD
Chaperonin-like protein MimG
Mycobacterium
MAKELRFNSDARARLEQGVNALADAVKVTLGPKGRNAILEKLTGPPTITNDGVTIAREIQLRDPFANMGAQLVKEVAMKTNGVVGDGTTTATVLAQAMVREGLEAVDAGANPMRVRRGIERTVPVVVESLRSHSVEVGSSADLRRIAALAASDDEAIGDVIAAAVEHVGKSGVVTTEESDTLGMAVDVVDGIEFDHGYTSGYMVTDPERMEAVLDNPLILLTNKKISQVQEIMPTLEVAKRADRPLVVIAEDVDGPALQLLVGGNMHKTMRSVVVRAPGFGHRRVAELEDLAVALNGHVIAKDTGIELGEVTREHLGSCDRLTATENDTTIVGPHGLQNLVDARVAQLEAQRERARLDADRDILDLRIARLTGRVAVIRVGGATSVELKERMLRVEDALAATRAALEAGIVSGGGTALAQAHRALDTLELVGDEAIGRDVVRRALAEPLRWIAINAGFEGDDVVDVVADLPLGHGFNALTGEYGDMFEEGIIDPFKVTRAALESAASIAALLITTETAVVEEIVGQPGAIMAPGFGDLAEGMVRPSNIY
Plays an essential role in the productive folding of MimA and MimC, and thus in the formation of the active MimABCD complex.
A0A0K0XCY8
Q8Y510
ADDB_LISMO
ATP-dependent helicase/nuclease AddB
Listeria
MTLQIIAGRSGTGKTTHLMDEVGEKIKQNSKTYIFIVPDQMTFQMETSFLNKENLAGMLGTQIFSFSRLAWKILQETGGLSKTFLSQTGIEMVIRKAALDQKDKLKIFSRATSRKGFYSELANLFKEMKQEEVSIEDMVKSATNLSTSVNNKVHDISLIYQKYEELLADKFLENEDYLRLLAEKIADSDYLNQTEIVIDGFTSFSKQELTVIGELMRKCDKVTISLTLNVPEIQHGLDEYSMFKASTEAYYALLELAKLNGTQVEENKFFLENKRAKTESLAFLANTWGHNKFMSFKNEPQNLKIHQANNRRAEIEGIAREIRQQALNGYRYRDIAILTRNLGDYDVLCETVMEAYNIPTFIDKKRAMAKHPFIEFIRSSLDAILFNWKYEPIFQAVKTEFFFDITEKSSLNRRKADILENYVLENGIQNKWKWEKEGDWIYRKIRGLSTNVLPQTDEEIHMQSIINEMRNLIVNPLSTLELNLRKAKTGMEFALALYHYLEQVNAVERLESWRQRAEEQGYLELAREHEQAWSSISALLDEFVEVLGEETLDLDSFTEIIGTGLDALEFSLLPPSLDQVVLSDMENAKLLDMKVIFAIGMNDGVMPLRQKDKGIFSDQDRDALRAEDSKLKPSAKNNIGEEDLLAYKIISLPSDKLFLSYPAADEEGKVLSESNYLRKIKGQFNELNESVYLTDPSLLSDAEQSSYIRSKQATLGLLTSQLQMYKRGYTLSSVWWDAYNSYFENEKESIMAKQVLSSLYYENKTKPLQETTAKNLFGETIHASVSRMEKFFSCEFQHYAQYGLKLEERGHFQLQAVDMGEIFHGAMEWISAELKRNNLDWGNLTEEECKQMAKLAMTFLAPKIQHEILLSSKRMEYIQYKLLQIITRATTVLNEQAKSSAFRPVGLEVDFGLKGDIPPLKIPLQSDSELLLQGRIDRIDMAEQDDRTFLRIIDYKSSSHDLALTEVYYGLALQMLTYLDIVVTNAQKMIGKTAEPAGVLYFHMHNQYVQAEKELSDEAIAKELQKSSKMKGLILSDPVAVSLMDMTLEKGKASTIIPAEIKQNGELSARSRTATRAEFDKMRQFVRHKYQEAGNKILDGAVSINPYKLKERTPCQFCSFRSFCGFDPSLTSNQYRHLANEKAETILTKMDIEGGTQ
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddB nuclease domain is not required for chi fragment generation; this subunit has 5' -> 3' nuclease activity.
Q8Y510
B1XL12
RUVA_SYNP2
Holliday junction ATP-dependent DNA helicase RuvA
unclassified Synechococcus
MFSYLKGEAIAIHRNLQGRFFLILEVRDIGYEIQVPGRLAQELAAAIGQPQHIFVHSQQREDGTYLYGFASAAARDLFRQLISVSGIGAQGAIALLDTLTLPELVQAIVTADHRQLAKAPGIGKKTAERLALELRSKLSQWRDQFSLPDTAAQPNAAVHEDLELTLLALGYQETEIRGAIATLSQDSILLQNDNADEWIRRAITLLSQT
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
B1XL12
A6WLC0
RNH2_SHEB8
Ribonuclease HII
Shewanella
MATFKSLSEADLLAFSTGLIAGVDEVGRGPLVGDVVTAAVILDPSKPISGLNDSKKLSEKRREALFDEICDKALCYQVGRASPAEIDELNILHATMLAMQRAVAGLNIAPELVLVDGNRSPIFVAHNGAELTSHSIIKGDGLIASISAASIIAKVTRDREMDVLDAAYPQYGFAKHKGYPTKAHFEAIAEHGVFDQYRKSFKPVKALLGL
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
A6WLC0
A9WR62
HIS6_RENSM
ImGP synthase subunit HisF
Renibacterium
MSVAIRVIPCLDVDAGRVVKGVNFADLRDAGDPVELARRYDGAGADELTFLDVTATSGNRETTFEMVARAAEEVFIPLTVGGGVREVADVDRLLRAGADKASINSAAVARPEVIDEITRHFGSQVLVLSLDARRVADGSTPSGFEVTTHGGRRGTGIDAVLWAREAADRGVGEILLNSIDADGTKAGFDLEMIRAVRAAVRVPLIASGGAGKPEDFPPAVQAGADAVLAASIFHFGPVDAIAQVKAAIRAAGFPVR
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
A9WR62
Q819Z1
PNP_BACCR
Polynucleotide phosphorylase
Bacillus cereus group
MSQEKQVFSIDLAGRQLTVETGQLAKQANGAVLVRYGDTAVLSTATASKEAKNVDFFPLTVNYEERLYAVGKIPGGFIKREGRPSEKAILASRLIDRPIRPLFADGFRNEVQVVSIVMSVDQDCSSEMAAMLGSSLALSISDIPFEGPIAGATVGRINGEFVINPTVEQQEQSDIHLVVAGTKDAINMVEAGADQVPEETMLEAIMFGHDEIKRLIAFQEEIVQAVGKEKSEVKLYEVDADLNQAVREMAEEDMHSAIQVHEKHAREDAINEVKKRVIEHYEAQEADADTLGQVNEILYKIVKEEVRRLITVEKIRPDGRKGDEIRPLASEVGILSRTHGSGLFTRGQTQALSICTLGALGDVQILDGLGVEESKRFMHHYNFPSFSVGETRPMRGPGRREIGHGAIGERALEPVIPSEKDFPYTVRLVSEVLESNGSTSQASICGSTLAMMDAGVPLKAPVAGIAMGLVKTGEHYTILSDIQGMEDHLGDMDFKVAGTAQGVTALQMDIKIDGLSREILEEALQQAKVGRVHILNHMLSVIPEPRTELSAYAPKIITMTINPDKIRDVIGPSGKQINKIIEETGVKIDIEQDGTVFISSINQEMNDKAKKIIEDIVREVQVGEIYEAKVKRVEKFGAFVELFSGKDGLVHISELALERVGKVEDVVKIGDVITVKVIEIDKQGRVNLSRKVLLKEEQEKEAVKEENKQEQQ
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Q819Z1
P59555
RIBA_BUCBP
GTP cyclohydrolase II
Buchnera
MKLTKISEAKLPTSFGEFLMIVFEESKTDKNHIALVYGDIKDTNNSVLSRIHSECLTGDALFSIRCDCGFQLKSALMEIVKEGSGILIYHRQEGRNIGLSNKIRAYALQDIGLDTVEANHHLGFSADERDFSVCIDIFNTLNIKKIKLLTNNPSKVTVLNNAGIQITERISLIVGRNAKNSKYLNTKAHKMGHFLPIEY
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
P59555
Q56461
MAUD_PARVE
Methylamine utilization protein MauD
Paracoccus
MTFLIASNILLWIAFLGVTVVMLGLMRQVGLLHERSSPMGAMITDHGPDIGDMAPEFDLPDYFGRSVHIGGASERPTLLMFTAPTCPVCDKLFPIIKSIARAEKIGVVMISDGAPEEHARFLKNHELGQIRYVVSAEIGMAFQVGKIPYGVLVDGEGVIRAKGLTNTREHLESLLEADKTGFASLQQFMASRKKNAA
May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Q56461
A6UNT3
RIBL_METVS
Flavin adenine dinucleotide synthase
Methanococcus
MDRKKIAVTAGTFDLLHPGHFNTLNFAKKHADELIVIIARDETVKKIKGRRPVIPEEQRKIMIEALKPVDRAVLGSLNDKLEPIININPDIIIIGPDQTTYQINELKRQLLNHGLKPEIIKVEEYVNCQFHSSYDILKEIVRRWCNKELKV
Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme.
A6UNT3
Q9CQA3
SDHB_MOUSE
Iron-sulfur subunit of complex II
Mus
MAATVGVSLKRGFPAAVLGRVGLQFQACRGAQTAAAAAPRIKKFAIYRWDPDKTGDKPRMQTYEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLSKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEDREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSVYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMATYKEKRALA
Iron-sulfur protein (IP) subunit of the succinate dehydrogenase complex (mitochondrial respiratory chain complex II), responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Q9CQA3
P20152
VIME_MOUSE
Vimentin
Mus
MSTRSVSSSSYRRMFGGSGTSSRPSSNRSYVTTSTRTYSLGSALRPSTSRSLYSSSPGGAYVTRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPTFSSLNLRETNLESLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE
Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2.
P20152
A9B0A2
METE_HERA2
Methionine synthase, vitamin-B12 independent isozyme
Herpetosiphon
MNFQTTVVGYPRVGVGRPYKQALERFWSGKLDETGFRAAINELCHDRLATQAQRLDLVPVGDFSLYDHVLDTALMLGAVPARFGKVDAHNLQGYFALARGRDGLPALEMTKWFDTNYHYLVPEIPERWELQANLVLEQVRFAQNVVGAKARPVLLGPWTFLRLARLAGAELAQHLQQLTAMYAQIVRELNDCNVAFIQCDEPALVGDVTEEEWQAFAACYRELSKHGKIVVQTYYGDVTPWYRELCRLPIHGLGLDLVQGHANWAAIQYHGFPQDKILVAGVVNGRNVWRSDLADLYTKITGLSEFVAPERLILSSSCSLLHLPETVTAERNLPVAVSSGLAFAQERLAELELLANALRDGIASVQPTWDAALASRQQWLDGVGRIVPAVRERTAALGTETPARLAYAERVPLQQAKLNLPLLPTTTIGSFPQTAALRKARAEAKRNPTGYAETINAEIAHVIALQEQWGIDVLVHGEPERNDMVQFFAEHLAGYVATQEGWVQSYGSRCVRPPVIAGDVYRTAALSVAETAYAQSLTKRPVKGMLTGPVTMLQWSFVRDDLPRSAVAAQIGLALRDEVTDLEAAGINIIQIDEPAFREGLPLRRNDWQNYLDWAVRAFRIATSDAKPSTQIHTHMCYSDFNDIIAAIAALDADVISIEDARSAGSLLAGLEGRYTQQIGPGVYDIHSPNIPTVEQLVARMRQLLNYLPAEQLWINPDCGLKTRTYAEVAAALQAMVTATKQVRNQIS
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
A9B0A2
A5CU44
SUCC_CLAM3
Succinyl-CoA synthetase subunit beta
Clavibacter
MDLFEYQARDLFESYGVPVLPGIVADTAEEVRAAAEKLGGTVVVKAQVKTGGRGKAGGVKVAQSADAAFEAAEGILGLDIKGHTVHRVMVAAGARIAQEFYFSILLDRAERSYLCLASYEGGMEIEELAVTRPEALARIEIDPVAGIDAAKAEEIARAASFPEELIAKVAPVFERLWWVYRDEDATLVEVNPLVLTESGEIIALDGKVTLDENAGLRHEGHAALEDAAAADPLEAKAKESDLNYVKLDGQVGIIGNGAGLVMSTLDVVSYAGEQHGGVRPANFLDIGGGASAEVMAAGLDVILGDEQVTSVFVNVFGGITSCDAVANGIVGALDKLGDAATKPLVVRLDGNNVEEGRRILEERAHPLVTVVGTMDEAADKAAELAAA
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
A5CU44
B3R0X8
KDSB_CUPTR
CMP-2-keto-3-deoxyoctulosonic acid synthase
Cupriavidus
MTVPAFTVVIPARLASTRLPDKPLADIGGRPMVVRVAERAHASSAQRTVVATDAPAVAQACAAHGIEAVLTRADHPSGTDRLAEVAAQLGLADDAIVVNVQGDEPLIEPALIDEVALHLAHHADCAIATAAHPLHDSAEVFNPNVVKVVCDAAGRALYFSRAPIPWARDAWSGVPAMPAASARVPLPDMPVLRHIGLYAYRAGFLRRFPTLAAAPLEQTEALEQLRAMWHGERIAVMQTAAAPAPGVDTQADLDRVRTLWAQSMAQEGP
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
B3R0X8
A8AIQ7
RLMC_CITK8
23S rRNA(m5U747)-methyltransferase
Citrobacter
MQCALYDAGRCRSCQWIVQPIRDQLSAKTADLKGLLADFSVEQWCAPVSGPEQAFRNKAKMVVSGSVEKPLLGMLHRDGTPEDLSDCPLYPDTFAPVFATLKPFIARAGLTPYNVARKRGELKYILLTESQFDGGMMLRFVLRSETKLAQLRAALPWLQAQLPQLKVITANIQPVHMAIMEGETEIFLTEQQALAERFNDVPLWIRPQSFFQTNPVVASHLYATARDWVRQLPVHHMWDLFCGVGGFGLHCATPEMTLTGIEIAPEAIACAKQSAAELGLTNLHFQALDSTQFATGQGEVPELVLVNPPRRGIGKALCDYLSQMAPEYIIYSSCNAQTMAKDIANLPGYRIERVQLFDMFPHTAHYEVLTLLTKTR
Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA.
A8AIQ7
O07627
YLAC_BACSU
RNA polymerase sigma factor YlaC
Bacillus
MKHRDSIEDLYRQYYQEILNYLFRRTHHLETAKDLAQDTFVKALNGLASFRGHSSIRTWLYTIAHHTFINWYRRDVKYQFTEISKNEGLTQTTYDQPEQYLSRTVKSETLRQELLKLKDQHQSVLILREFQELSYEEIAEILGWSLSKVNTTLHRARLELKKNMTKSREEERI
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor contributes to oxidative stress resistance.
O07627
Q8TZC4
RFCS_METKA
Mkn RFC intein
Methanopyrus
MAEHELRVLEIPWVEKYRPKRLDDIVDQEHVVERLKAYVNRGDMPNLLFAGPPGTGKTTAALCLARELFGEHWRDNFLELNASVSADTPILVRRGGEVLRVTFEDLDSWYFGDRGGEYVDVSDLEVLTVDRNFRVTWARVSKLIRHRARKILRVHLEDGTIELTGNHAVMVLDEGGLRAVKASEIEEGSFLLSFVAELDEQPTDGGTVVTSVGSGSRVSDTTYELPVEVRVELLRELADDGVIEASEDVSVDLAWLARISGVESRVTDDGVELVWETRTGDLLPADPVLKLVERLESDLVDDLESWVFDGRVSKEAVRKVLSSVDAKNLRGDARRAYRMLRTLVRSDVHAVKVEDLDVMDYDGYVYDVSVPGNEMFFAGEVPVLLHNSDERGIDVIRTKVKNFARTRPMGGARFKIIFLDEADNLTRDSQQALRRIMEMYSDACRFILAANYSSAIIDPIQSRCVVFKFTKLPESAIKERLRKIAESEGVEITEDALDAIVYVSEGDMRRAINVLQAAAALGREIDEDTVFQIAATARPEEVREMIHHAWNGDFERARELLHELLTRYGMSGEDVVRQVHREIFDMDEIPEEAIPELVNAVGDFEYRLIRGSDERIQLEALLARIHALGNEYSGG
Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA.
Q8TZC4
Q8Z6X9
BIOD2_SALTI
Dethiobiotin synthase 2
Salmonella
MLKRFFITGTDTSVGKTVVSRALLQALSSGGKSVAGYKPVAKGSKETPEGMRNKDALVLQSVSSLELPYEAINPIALSEEESSVAHSCPINYTLLSNGLASLSDKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVLMVVGIQEGCINHALLTAQAVANDGLPLIGWVANRINPGLAHYAEIIDVLGKKLPAPLIGELPYLPRAEQRELGQYIRLSMLGSVLAVDRIMA
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Q8Z6X9
Q7TVA3
FOLD_PROMA
Methenyltetrahydrofolate cyclohydrolase
Prochlorococcus
MTNILDGKKLAKELELRLHEDITEFSPEVGRPPGLAVIRVGDDPASGIYVSNKEKACNRIGLDSFLYHLGTNTSEQEILEVIKALNNDQKVDGILLQLPLPKGLDAEPLLKAIDPEKDVDGLHTLNLGRLLKGEKGPRSCTPAGIMVLLRRNNISLVGKKVVVIGRSILVGKPMALMLQAANATVTVAHSKTINLPEITNQAEVLIVAAGIPQLIGLEHVRSNAVVVDVGIHRIPMEPLKLTGSNYKLCGDVRAEEIYSKIKAITPVPGGVGPMTVAMLMVNTVNRWQYHCGLSSTLSDLLP
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Q7TVA3
Q89A79
RS14_BUCBP
30S ribosomal protein S14
Buchnera
MAKQSMKAREVKRIKLAKKFYSRREHLKSIISDLSVLEQDRWKAVLKLQTFPRDSSPIRQRNRCSQTGRPHAFLRKFGLSRIKVREAAMRGEIPGLKKSSW
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
Q89A79
P71229
HYFR_ECOLI
Hydrogenase-4 transcriptional activator
Escherichia
MAMSDEAMFAPPQGITIEAVNGMLAERLAQKHGKASLLRAFIPLPPPFSPVQLIELHVLKSNFYYRYHDDGSDVTATTEYQGEMVDYSRHAVLLGSSGMAELRFIRTHGSRFTSQDCTLFNWLARIITPVLQSWLNDEEQQVALRLLEKDRDHHRVLVDITNAVLSHLDLDDLIADVAREIHHFFGLASVSMVLGDHRKNEKFSLWCSDLSASHCACLPRCMPGESVLLTQTLQTRQPTLTHRADDLFLWQRDPLLLLLASNGCESALLIPLTFGNHTPGALLLAHTSSTLFSEENCQLLQHIADRIAIAVGNADAWRSMTDLQESLQQENHQLSEQLLSNLGIGDIIYQSQAMEDLLQQVDIVAKSDSTVLICGETGTGKEVIARAIHQLSPRRDKPLVKINCAAIPASLLESELFGHDKGAFTGAINTHRGRFEIADGGTLFLDEIGDLPLELQPKLLRVLQEREIERLGGSRTIPVNVRVIAATNRDLWQMVEDRQFRSDLFYRLNVFPLELPPLRDRPEDIPLLAKHFTQKMARHMNRAIDAIPTEALRQLMSWDWPGNVRELENVIERAVLLTRGNSLNLHLNVRQSRLLPTLNEDSALRSSMAQLLHPTTPENDEEERQRIVQVLRETNGIVAGPRGAATRLGMKRTTLLSRMQRLGISVREVL
A transcriptional activator of its own operon; when overexpressed operon expression is strongly enhanced by low pH (under pH 6.0), strongly inhibited by O(2) but only weakly stimulated by fumarate . Expression in situ is very weak .
P71229
Q9UBL0
ARP21_HUMAN
Thymocyte cAMP-regulated phosphoprotein
Homo
MSEQGDLNQAIAEEGGTEQETATPENGIVKSESLDEEEKLELQRRLEAQNQERRKSKSGAGKGKLTRSLAVCEESSARPGGESLQDQESIHLQLSSFSSLQEEDKSRKDDSEREKEKDKNKDKTSEKPKIRMLSKDCSQEYTDSTGIDLHEFLINTLKNNSRDRMILLKMEQEIIDFIADNNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTGKSVIINKTSSTRIPEQRFCEHLKDEKGEESQKRFILKRDNSSIDKEDNQQNRMHPFRDDRRSKSIEEREEEYQRVRERIFAHDSVCSQESLFVENSRLLEDSNICNETYKKRQLFRGNRDGSGRTSGSRQSSSENELKWSDHQRAWSSTDSDSSNRNLKPAMTKTASFGGITVLTRGDSTSSTRSTGKLSKAGSESSSSAGSSGSLSRTHPPLQSTPLVSGVAAGSPGCVPYPENGIGGQVAPSSTSYILLPLEAATGIPPGSILLNPHTGQPFVNPDGTPAIYNPPTSQQPLRSAMVGQSQQQPPQQQPSPQPQQQVQPPQPQMAGPLVTQRDDVATQFGQMTLSRQSSGETPEPPSGPVYPSSLMPQPAQQPSYVIASTGQQLPTGGFSGSGPPISQQVLQPPPSPQGFVQQPPPAQMPVYYYPSGQYPTSTTQQYRPMAPVQYNAQRSQQMPQAAQQAGYQPVLSGQQGFQGLIGVQQPPQSQNVINNQQGTPVQSVMVSYPTMSSYQVPMTQGSQGLPQQSYQQPIMLPNQAGQGSLPATGMPVYCNVTPPTPQNNLRLIGPHCPSSTVPVMSASCRTNCASMSNAGWQVKF
Isoform 2 may act as a competitive inhibitor of calmodulin-dependent enzymes such as calcineurin in neurons.
Q9UBL0
Q65VB6
RECF_MANSM
DNA replication and repair protein RecF
Basfia
MAIARLIVENFRNISAVDLEFDHGFNFLVGNNGSGKTSLLEALFYLGHGRSFKSSVTTRVIRYDQPHFTLHGRIRELQHEWSVGLQKQRKDGNTIVKINGEDGNKISDLAHLLPMQIITPEGLTLLNGGPSYRRAFLDWGLFHHQPNFHSAWSALHRLLKQRNAALNQTYDYNMLKPWDMELAKLAHQVSQWRADYAEALSPEIEQTCRLFLPELDIHVSFHQGWEKDTDYAQLLTENFERDKAIGYTVSGPQKADFRFKSNGLPVEDVLSRGQLKLLMCALRLAQGEHLMAQKNRHCIFLIDDFASELDETKRALLAQRLQNSNSQVFVTAISPEQLKQMQPEKHRTFQVVNGQIEQLL
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
Q65VB6
Q6I5I8
CDPKG_ORYSJ
Calcium-dependent protein kinase 16
Oryza sativa
MGNCCRSPAAAAREDVKTSHFPASTGGGKKKPHQARNGGGGGGGGGGGGWEKKRLSVLGEEGSEVNGGIEEKYALDRELGRGEFGVTYLCMDRCSRELLACKSISKRKLRTPVDVEDVRREVAIMRHLPRSASIVSLREACEDDGAVHLVMELCEGGELFDRIVARGHYTERAAAAVTRTIVEVVQLCHRHGVIHRDLKPENFLFANKKENSPLKAIDFGLSIFFKPGEKFSEIVGSPYYMAPEVLKRNYGPEIDIWSAGVILYILLCGVPPFWAETEQGVAQAILRGNIDFKREPWPNVSDNAKDLVRQMLQPDPKLRLTAKQVLEHTWLQNAKKAPNVPLGDIVKSRLKQFSRMNRFKRRALRVIADHLSAEEVEDIKDMFKVMDTDNDGIVSYEELKSGIAKFGSHLAESEVQMLIEAVDTNGRGALDYGEFLAVSLHLQRMANGEHLRRAFLFFDKDGNGYIEPEELQEALVEDGATDIMEVVKDILQEVDTDKDGKISYEEFVAMMKTGTDWRKASRHYSRGRFNSLSIRLIKDGSVKLGNE
May play a role in signal transduction pathways that involve calcium as a second messenger.
Q6I5I8
Q12181
NDOR1_YEAST
NADPH-dependent FMN and FAD-containing oxidoreductase
Saccharomyces
MSSSKKIVILYGSETGNAHDFATILSHRLHRWHFSHTFCSIGDYDPQDILKCRYLFIICSTTGQGELPRNVNALKGERPVTFWSFLKRKNLPSNLLNHIQTAMLGLGDSSYPKFNYGIRKLHQRIVTQLGANELFDRLEADDQAMAGSNKGTGLGIESVYFEYEKKVLSFLLSKYPNRKVNGQIIKREELDPEVYLEPASYLQLSDEHANEKFTSTKVIFEGDESLKVGRVNINKRITSEGHFQDVRQFKFSNVDKIQENYEPGDTVTIYPCNTDEDVSRFLANQSHWLEIADKPLNFTSGVPNDLKDGGLVRPMTLRNLLKYHCDFMSIPRTSFFLKIWTFATDVTKMERGQEQLNDQREKLRQFATDQDMQDLYDYCNRPRRSILEVLEDFISVKLPWKYVLDYLPIIKPRYYSISSGPGDPNIELTVAIVKYKTILRKIRRGICTNYIARLQEGEQIRYKLQNNHIIKKEFLNKPMILVGPGVGLAPLLSVVKAEISKDIKLLFGCRYKDKDYIYKDMLEDWFRKGKIALHSSFSRDEENSPGVKYVQDYLWRLGEEITNLVVNKDAVFFLCGSSGKMPIQVRLTFIEMLKKWGNFSDEETAKKYLKEMEKSDRYIQETW
NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery . Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of DRE2, another key component of the CIA machinery . In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins . Positively controls H(2)O(2)-induced cell death .
Q12181
A9WQS5
YBEY_RENSM
Endoribonuclease YbeY
Renibacterium
MSVEVNNESGVELPEAELVRLSRFVFEKLYLHPQTELSIILADREAMEKLHVEWMYEPGATDVLSFPMDELRPGTVSRPAPAGLLGDIVICPQVAQEQAQAGGHSVEDELLLLTTHGLLHLLGYDHEDPEEKAEMFGLQRELLTSFLGRDAPAETTA
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
A9WQS5
Q5L5Z1
METN_CHLAB
Methionine import ATP-binding protein MetN
Chlamydia
MFNQNSPIISVEQLNKEIANHRILHRISFSVYPGEIVGIIGHSGSGKSTLLRCLDFLIEPTSGSISIAGFHTSSPIEKISRTAFAKRVAYVSQSCGLFLAKTVFENIAYPLKIRCPEMTKALIEEKVDDVLHFFNLYERKHAYPSRLSGGQKQKVAIAIAIVSDPRVLLCDEITSALDPRSTEDVVDKLSQLNEERGITQVFVSHEIEIVKKLCCQTLVMHQGSIEESGPTEQLFLNPQSAITEELFHMQSIAKGIYEHGENEEILRLGFPKGLAVQGMISQLIQSGGISINILSGDIHLFRKTPLGFLIVALSGGKEQRDWAKSSLREKGVIVKQFQKSR
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Q5L5Z1
P33025
PSUG_ECOLI
Pseudouridine-5'-phosphate glycosidase
Escherichia
MSELKISPELLQISPEVQDALKNKKPVVALESTIISHGMPFPQNAQTAIEVEETIRKQGAVPATIAIIGGVMKVGLSKEEIELLGREGHNVTKVSRRDLPFVVAAGKNGATTVASTMIIAALAGIKVFATGGIGGVHRGAEHTFDISADLQELANTNVTVVCAGAKSILDLGLTTEYLETFGVPLIGYQTKALPAFFCRTSPFDVSIRLDSASEIARAMVVKWQSGLNGGLVVANPIPEQFAMPEHTINAAIDQAVAEAEAQGVIGKESTPFLLARVAELTGGDSLKSNIQLVFNNAILASEIAKEYQRLAG
Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
P33025
P31424
GRM5_RAT
Metabotropic glutamate receptor 5
Rattus
MVLLLILSVLLLKEDVRGSAQSSERRVVAHMPGDIIIGALFSVHHQPTVDKVHERKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRDSLISSEEEEGLVRCVDGSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLRSHLPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKLRPETNLRNPWFQEFWQHRFQCRLEGFAQENSKYNKTCNSSLTLRTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAGLCDAMKPIDGRKLLDSLMKTNFTGVSGDMILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELKMDDDEVWSKKNNIIRSVCSEPCEKGQIKVIRKGEVSCCWTCTPCKENEYVFDEYTCKACQLGSWPTDDLTGCDLIPVQYLRWGDPEPIAAVVFACLGLLATLFVTVIFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCMFVPKVYIILAKPERNVRSAFTTSTVVRMHVGDGKSSSAASRSSSLVNLWKRRGSSGETLRYKDRRLAQHKSEIECFTPKGSMGNGGRATMSSSNGKSVTWAQNEKSTRGQHLWQRLSVHINKKENPNQTAVIKPFPKSTENRGPGAAAGGGSGPGVAGAGNAGCTATGGPEPPDAGPKALYDVAEAEESFPAAARPRSPSPISTLSHLAGSAGRTDDDAPSLHSETAARSSSSQGSLMEQISSVVTRFTANISELNSMMLSTAATPGPPGTPICSSYLIPKEIQLPTTMTTFAEIQPLPAIEVTGGAQGATGVSPAQETPTGAESAPGKPDLEELVALTPPSPFRDSVDSGSTTPNSPVSESALCIPSSPKYDTLIIRDYTQSSSSL
G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system and generates a calcium-activated chloride current. Plays an important role in the regulation of synaptic plasticity and the modulation of the neural network activity.
P31424
Q9C167
RIR2_NEUCR
Ribonucleotide reductase small subunit
Neurospora
MSVQTSPSKQVTSGIQNLNMDSPAKKLDFGATDKENKPFDEDLAKLEAEIDAEHNANKKAAEAKKMAPTLKPEEANEPLLTENPQRFVLFPIKYHEIWQMYKKAEASFWTAEEIDLSKDLHDWNNRLNDDEKFFISHILAFFAASDGIVNENLVERFSGEVQIPEARCFYGFQIMMENIHSETYSLLIDTYIKEPSQRTYLFNAIDTIPCIRKKADWALRWITDKSSTFAQRLVAFAAVEGIFFSGAFASIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLFSHLNNRPSKQLIQEIIVDAVRIEQEFLTEALPCALLGMNADLMKQYIEFVADRLLVALGNEKIYRSTNPFDFMENISLGGKTNFFEKRVGDYQKAGVMNSTKKADADAEVAKNENGGDFTFDEDF
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Q9C167
Q3B2W3
HYPA_CHLL3
Hydrogenase maturation factor HypA
Pelodictyon
MHEMSIAMSIVDAVDAKARAEGAVRISLIELKIGKLAGILPEALRFCFSAAATGSLAGQAQLVIDEPDGRGRCSDCGHEFSVDFYYARCPECGSLRIVIVSGEEFLIQSIIIDEEGE
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase.
Q3B2W3
Q12Z95
RL24E_METBU
50S ribosomal protein L24e
Methanococcoides
MEQRKCSFCGELLEPGTGLLFAKRDGSTYYFCSSKCKGNFDLGRLPRRTVWTEQGRIYLKKA
Binds to the 23S rRNA.
Q12Z95
A5V3U9
GATB_RHIWR
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Rhizorhabdus
MSSYRIQGATGEWEVVIGLEVHAQVVSNAKLFSGASAAFGAEPNQSVSLVDAAMPGMLPVPNEECIRQAVKTGMALGAEINRWSRFDRKNYFYADLPQGYQISQLYHPLVGEGTITIDADEKAGIAEARTIGVERLHVEQDAGKLMHDQHPTRSYVDLNRSGVALMEIVSKPDMRSPSEAGAYLRKLRSILRYVGSCDGNMEEGSMRADVNVSVRKAGDPFGTRTETKNVNSIRFVMAAIESEANRQVDVIEGGGKIVQETRLYDPDRNETRSMRSKEDAHDYRYFPDPDLLPLELSEEFVAQCRAELPELPDAKRARYEGELGLPAYNAAVLTSDVETARWFEALLDAAGKPGAEVARAASNWLISDLFGALNRLGKAIDESPVSPRQGAELLALVADGTLSGTLAKQVFEIMLETGDDPARIVEERGLKQTSDTGAIEAVIAEVMAANADKVAEYRGGKDKLFGFFVGQTMKAMGGKANPGVVNELLKKTLG
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
A5V3U9
A4WRM1
GLGC_CERS5
ADP-glucose synthase
Cereibacter
MKAQPPLRLTSQAMAFVLAGGRGSRLKELTDRRAKPAVYFGGKARIIDFALSNAMNSGIRKMAIATQYKAHSLIRHIQRGWNFFREERNEYLDILPASQRVDEHKWYLGTADAVTQNIDIVDSYDIKYVIILAGDHVYKMDYEIMLRQHCETGADVTIGCLTVPRMEATAFGVMHVDASLRITDFLEKPADPPGIPGDEGNALASMGIYVFDWAFLRDLLIRDAEDPNSSHDFGHDLIPAIVRNGKAMAHRFSDSCVMTGLETEPYWRDVGTIDAFWQANIDLTDFTPKLDLYDREWPIWTYSQIVPPAKFIHDSERRRGMAISSLVSGDCIVSGSEIRSSLLFTGCRTHSYSSLSHVVALPHVTVNRKADLTNCVLDRGVVIPEGLVIGQEPEEDARWFRRSEGGIVLVTQDMLDARARALG
Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
A4WRM1
Q1EBC4
NOP16_COCIM
Nucleolar protein 16
Coccidioides
MGRVLQKKKNRSSAPKIKIKSGKSKSGKKKINVLGNSIIAQNWDKKLTLAQNYRRLGLATRLNAPTGGVEKGVSAGALNNISSLATKGKTAAQIQPSEARVERDPETGKILRIIQPDQAGDDGTIEVAGHKRRRTNPLDDPLNELSDVEDSTLRDTGASTDVVSALERQAAAEEERVKKRKPRHQSKREEEWLQRLVDKYGDDVPAMVRDRKLNPMQQTEGDIRRRLRKWHGNKK
Involved in the biogenesis of the 60S ribosomal subunit.
Q1EBC4
Q4QLG1
MRAY_HAEI8
UDP-MurNAc-pentapeptide phosphotransferase
Haemophilus
MLVWLAEYLVRYETAFNAISYITVRAILALLTALFISLWIGPKVIKRLQILKFGQEVRNDGPESHFAKKGTPTMGGVMILFSIGVSTLLWANLANSYIWVCLFVLFGYGAIGFVDDFRKITRKNTDGLIARWKYFWMSVVALVAILWLYWLGHDTDATRLVIPFFKDIMPQLGLFYIVLSYFVIVGTGNAVNLTDGLDGLAIMPTALVAGAFALIAWATGNVNFAEYLHIPYIKYSSEVVVFCTAIVGASLGFLWFNTYPAQVFMGDVGSLALGGALGVVAILVRQEFLLVIMGGVFVVEALSVILQVGSYKLRKQRIFRMAPIHHHFELKGWPEPRVIIRFWIISLMLVLMGLVTLKLR
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Q4QLG1
Q9SUT9
RTNLB_ARATH
VirB2-interacting protein 2
Arabidopsis
MADEHKHEESSPNLDPAVEVVERESLMEKLSEKIHHKGDSSSSSSSDDENEKKSSSSSPKSLKSKVYRLFGRERPVHKVLGGGKPADIFMWKDKKMSGGVFGGATVAWVLFELMEYHLLTLLCHVMIVALAVLFLWSNATMFIHKSPPKIPEVHIPEEPLLQLASGLRIEINRGISSLREIASGRDIKKFLSAIAGLWVLSILGGCYSFLTLAYIALVLLFTVPLFYDKYEDKVDSYGEKAMAELKKQYAVLDAKVFSKIPRGPLKDKKKD
Plays a role in the Agrobacterium-mediated plant transformation via its interaction with VirB2, the major component of the T-pilus.
Q9SUT9
Q5HQ07
FTSA_STAEQ
Cell division protein FtsA
Staphylococcus
MEEHYYVSIDIGSSSVKTIVGEKFHNGINVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKDVFLKLPIIGTEVYDESNEIEFYEDTEIDGTHIESVLEGIRDKNDVPETEVINVFPIRFVVDKDNEVSDPKELIARHSLKVDAGVIAIQKSILINMIKCVEACGVDVLDVYSDAYNYGSILTPTEKELGACVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQGLNTTYDTAEKVKHQYGHAFYDSASDQDVFSVDQVDSDEHVQYTQKDLSDFIEQRVEDIFFEVFDVLQELGLTKVNGGFVVTGGSANLLGVKELLQDMVSEKVRIHTPSQMGIRKPEFSSAISTISSSIAFDELLDYVTISYQDNEEFEEEVIESDKDSETKSSGFDWFKRKSNKKENDEVAPEAPREESYEDRENHLEDEQQTEGKAKEESKFKKLMKSLFE
Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Q5HQ07
A7Y3E3
NU3C_IPOPU
NADH-plastoquinone oxidoreductase subunit 3
Ipomoea
MFLLYEYDLFWAFLIISSLIPILAFFISGVLAPISKGPEKLSTYESGIEPMGDAWLQFRIRYYMFALVFVVFDVETVFLYPWAMSFDVLGVSVFIEAFIFVLILIGGLVYAWRKGALEWS
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory 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.
A7Y3E3
O02667
AA3R_RABIT
Adenosine receptor A3
Oryctolagus
MPDNSTTLFLAIRASYIVFEIVIGVCAVVGNVLVIWVIKLNPSLKTTTFYFIFSLALADIAVGFLVMPLAIVISLGITIGFYSCLVMSCLLLVFTHASIMSLLAIAVDRYLRVKLTVRYRRVTTQRRIWLALGLCWVVSLLVGFTPMFGWNMKPTLESARNYSDFQCKFDSVIPMEYMVFFSFFTWILIPLLLMCALYVYIFYIIRNKLVQSFSSFKETGAFYRREFKTAKSLFLVLALFAGCWLPLSIINCVTYFKCKVPDVVLLVGILLSHANSMMNPIVYACKIQKFKETYLLIFKARVTCQPSDSLDPSSEQNSE
Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase.
O02667
O19995
RR4_BABST
30S ribosomal protein S4, chloroplastic
Babiana
RFKKIRRLGALPGLTSKRPRSGSDLKNQLRSGKRSQYRIRLEEKQKLRFHYGLTERQLLKYVHIAGKAKGSTGQILLQLLEMRLDNILFRLGMASTIPGARQLVNHRHILVNGRIVDIPSYRCKPRDIITTKNKQRSKALIQNFIASSPHQEELPNHLTIDPFQYKGLVNKIIDSKWIGLKIN
With S5 and S12 plays an important role in translational accuracy.
O19995
Q8UA46
UXUA2_AGRFC
D-mannonate hydro-lyase 2
Agrobacterium tumefaciens complex
MKETWRWFGESDPITLEHVRQTGASGVVTALHQIPDGTAWPAEEIAKRKAMIEAAGLEWSVCESIPMEQSIKRGDADAPKAIARWKDTLSRLGRAGVPVVCYNFMPVVDWTRTNLRWQARNTGLALRFEMADFVAYDVFILKRIRAAENYDPALVARAEERFAQMSEDEQSLLERNIIAGLPGGALVQTRQSIAALIASFDGIDSATMQGNLLAFLKEVVPVAEEVGVHLGIHPDDPPFSLFGLPRVVSTPADIRAILSAVESPNNGITLCTGSYGARSDNDLVAMAKEFASRVNFAHLRNVTVEADGSFFEDDHLDGGADMIGVIEALLREERSTAKAGRRTNIPMRPDHGHLLGDDITKKTNPGYSYIGRMKGLGELRGVIRTIERQLRREEAAA
Catalyzes the dehydration of D-mannonate.
Q8UA46
A1CNV8
DRS1_ASPCL
ATP-dependent RNA helicase drs1
Aspergillus subgen. Fumigati
MAPSKKRTSVPDDDFVFTLSDDENDVLENGADEGDEQADEETASGSKKRKRETAEAPKGKNKKQKQLKQSKKGKGAAVAGSDGEEEEEGDEEEAADAGEDDGALDSEFEFDVGGHATAGVIEGFDGWETQNGDASANKNGDKKAVDIDDIISRRKEQKDAELKRKLKKEEKRKRMEESEDEAEAEDVESDGDMSVDFQDDELLAADGFGMGADGEDESGESDAGDGAGSDEENDSDDNGDDEGDADDDDAASDNDSVATPVGHPDDEVASDDESGAESEVDAEEAEKRKAFFAPEEKTTEEPTSKRSFQDFNLSRPILRGLASVNFTTPTPIQQKTIPVALLGKDIVGSAVTGSGKTAAFVVPILERLLFRPRKVPTSRVAILMPTRELAVQCYNVATKLATHTDVTFCQLVGGFSLREQENILKKRPDVIIATPGRFIDHMRNSPSFTVDTLEILVLDEADRMLEDGFADELNEILTTIPKSRQTMLFSATMTDSVDKLIRVGLNRPVRLMVDSKKNTSMNLTQEFVRLRPGREGKRLGYLLYLCSEIFTGRVIVFFRQKKEAHRVRIVFGLLGLKAAELHGSMSQEQRIKSVESFREGKVAFLLATDLASRGLDIKGVETVINYEAPQSHEIYLHRVGRTARAGRSGRACTIAADPDRKVVKAAVRAGKAQGAKIASRVVEPAVADQWAAKVEALEEEIEEVLKEEKLEKHMAQAEMQVTKGENLMKHGAEIMSRPKRTWFETERDKRASRKLGATELNGPSKKDKVKLSNKDKKRLDDSRQRHEGNQGWKKGKTEREAPKQAKTKGGKNQSDKKNKNKMKGKK
ATP-binding RNA helicase involved in ribosome assembly.
A1CNV8
B8GV56
RL23_THISH
50S ribosomal protein L23
Thioalkalivibrio
MNEERLLKVLVGPHVSEKATVLADAANQHVFKVAPDATRGEIKAAVEKFFEVQVSSVRVVNMKGKRKRFGRFEGRRNNWKKAYVTLAAGQDIALAGSE
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.
B8GV56
B0KTW1
MNMC_PSEPG
FAD-dependent cmnm(5)s(2)U34 oxidoreductase
Pseudomonas
MSTLLQHAQIDWDDQGRPHSRQYDDVYFAVNEGIEETKHVFLGQTRLAERFANLAPHTCGVIGETGFGTGMNFFCAWQLFDQHAHRDARLHFVSVEKYPLGHADMARAVSLWPELAAYTEPLLEQYVAVHPGFQQFTFANGRVTLTLLIGDVLEQLPQLDAQIDVWFLDGFAPAKNPDMWTPELFAQLARLSHPGTVLGTFTTTGWVRRSLVEAGFAMKKVPGIGKKWEVMSGAYVGPVPGPKAPWYARPAVAQGPREALVIGAGLAGSTTAASLARRGWQVTVLERHEAPAQEASGNPQGVLYLKLSAHGTALSQMILSGFGYTRRQLQRLQRGQDWDACGVLQLAFDAKEAERQGKLAAAFDHDLLHALERAEAEAIAGVALPAGGLFYPEGGWVHPPALCQQQLQHPGIRLLTHQDVIELRNIGQHWQAWAGDRLLASAPVVVLAGAADVRRFEPCAQLPLKRIRGQITRLPATASSRALRTVVCAEGYVAPPRGDEHTLGASFDFHSEDLAPTVAEHQGNLALLDEISVDLAQRLGVAELDAEQLQGRAAFRCTSPDYLPIVGPLADSQAFAEAYAVLGRDARQVPDVACPWLGGLYVNSGHGSRGLITAPLSGELVAAWVCGEPLPLPRAVAEACHPNRFALRRLIRGK
Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
B0KTW1
A7FKY8
LIPB_YERP3
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
Yersinia
MMPRLQQHKIILRQLGLQPYAPVSQAMHNFTEFRTDTTPDEIWLVEHQHVFTQGQAGKAEHVLMPGDIPVIQSDRGGQITYHGPGQQVMYVMVDLKRAKIGVRQLVTAIENTVIETLAHFNIDSHARPDAPGVYVEQQKICSLGLRIRRGCSFHGLALNIAMDLEPFQRINPCGYAGMQMTQVSALQPGVTVADVQPVLVREFTRQLGYPTAKLQPWSLSDYLLSSHSSSSVL
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
A7FKY8
A0SVK0
DOG1_ARATH
GLUCOSE SENSING QTL 5
Arabidopsis
MGSSSKNIEQAQDSYLEWMSLQSQRIPELKQLLAQRRSHGDEDNDNKLRKLTGKIIGDFKNYAAKRADLAHRCSSNYYAPTWNSPLENALIWMGGCRPSSFFRLVYALCGSQTEIRVTQFLRNIDGYESSGGGGGASLSDLSAEQLAKINVLHVKIIDEEEKMTKKVSSLQEDAADIPIATVAYEMENVGEPNVVVDQALDKQEEAMARLLVEADNLRVDTLAKILGILSPVQGADFLLAGKKLHLSMHEWGTMRDRRRRDCMVDTEVIFDACTTVNSGPRPTETTNNERN
Required for the induction of seed dormancy . The level of DOG1 protein in freshly harvested seeds determines the level of seed dormancy . Determines the temperature window for germination by regulating the expression of micropylar endosperm-weakening genes through temperature control of the gibberellins metabolism . Regulates seed dormancy and flowering time through an influence on levels of microRNAs miR156 and miR172 . Regulator of seed maturation interfering with abscisic acid signaling components and activating ABI5 . In cv. Cvi-1, enhances glucose induction of ABI4 .
A0SVK0