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2.75k
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5.51k
AlphaFoldDB
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Q8DSY4
MSRA_STRMU
Peptide-methionine (S)-S-oxide reductase
Streptococcus
MERAIFAGGCFWCMVQPFEEQDGILSVRSGYTGGHVVNPTYEQVCSKMTGHTEAVEIIFDESKISYADLVEIYWRQTDPTDSFGQFEDRGDNYRPVIFYFDEQQRKIAEQSKANLQASGHFNRPIVTTIEAAQPFYEAEKDHQAFYRKNPERYARSSAIRHHFLKENWS
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Q8DSY4
Q7VXJ6
PRMB_BORPE
N5-glutamine methyltransferase PrmB
Bordetella
MQNNNRQELQTLRDLIRYAVSRLNAARVALGHGSDNAWDEAVYLVLHGLHLPPDTLDPFLDARVLPSERSRVLDLIDRRVTERLPAAYLTGEAWLRGHRFHVDRRVIVPRSPIAELLDEGLAPWVRDPLQVERALDMCTGSGCLAILAALAFPVAQVDAVDVSSDALEVAARNVAEYGLQDRLTLRQGNLFEALPAAAYDVIVCNPPYVNQASMGALPQEYRHEPALALAGGADGMDLVRRILAAAPGYLSADGVLVLEIGHERDHFEAAFPDLQPVWLDTAESSDQILLLTREQLNT
Specifically methylates the 50S ribosomal protein L3 on a specific glutamine residue.
Q7VXJ6
Q14203
DCTN1_HUMAN
p150-glued
Homo
MAQSKRHVYSRTPSGSRMSAEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGTDTTAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGASSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPVLTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFELSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDCTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEATDIALLLRDLETSCSDIRQFCKKIRRRMPGTDAPGIPAALAFGPQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLLVAALEELAFKASEQIYGTPSSSPYECLRQSCNILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEQQRGAIPGQAPGSVPGPGLVKDSPLLLQQISAMRLHISQLQHENSILKGAQMKASLASLPPLHVAKLSHEGPGSELPAGALYRKTSQLLETLNQLSTHTHVVDITRTSPAAKSPSAQLMEQVAQLKSLSDTVEKLKDEVLKETVSQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGFGQRHRLVLTQEQLHQLHSRLIS
Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule . Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon . Plays a role in metaphase spindle orientation . Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole . Plays a role in primary cilia formation .
Q14203
Q2P3S1
IHFB_XANOM
Integration host factor subunit beta
Xanthomonas
MTKSELIEILARRQAHLKSDDVDLAVKSLLEMMGQALSDGDRIEIRGFGSFSLHYRPPRLGRNPKTGESVALPGKHVPHFKPGKELRERVSSVVPVDMSDTTD
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
Q2P3S1
P0DMF5
NDB4V_CHATC
Peptide Ctri9194
Chaerilus
MKTQNVLLSFGIVFLMISFSSETYIRDFITRRPPFGNIGKRSLKDVESLDFLFDPTFTAADLAVLENALEDY
Antimicrobial peptide.
P0DMF5
Q252N9
HEM1_CHLFF
Glutamyl-tRNA reductase
Chlamydia
MVLGVVGISYREAALKEREAVINILKTFEADTLLAQRFFGGDGSFVLLLTCHRAEIYYFSKSNANVQSKLLSWISSLGTRPYCYQGLACFTHLFTVTSGMDSLIFGETEIQGQVKRAYIKAKTDRELPFALHFLFQKALKEGKDFRSQVSLSYPVVTMESIVEETLDLHGKSTKDKLLFIGYSDVNRKIAKGLSAKGYRNLIFCSRKNIPIPYDTVARSQLSFGKPYDVIFFGSSESARDFPGLSLESLAGIPNRVVFDFNVPRTFTLVERPEGISYLDMDFISERVQKKLQISKQCTNKEKPFLALAARKQWEVYEKKSSNISLSQIRTSRPKLLIL
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Q252N9
Q03478
LAFU_VIBPA
Chemotaxis protein LafU
Vibrio
MQKQEHVVFKRAKAHGHDEPHGGAWKVAFADFMIALMALFLVLWVMQVVDKEERKAIVAHLHSSSVFDKSYGNPFDTSQSISPIDLAQDSSVPSKHNSNHVVSSYFQGDGDGPEINSLVPGTFDTQEQLAALAKVIEEMTAQINAQGNVNVTVTPQGLRIVLQDDYKQHMFSRGGAELTPFFEDLLLALAPLFEQVTNPLIISGHTDAIPFKKRFGRQSNWALSASRADVARKTLVEGGMPDDRVMQVTGMSDRALLNPDEPDSSENRRIELFILTTPAAKVLETLFGNQDDSELQKAKQKAEFNQPVIRQEVIRYSADAEKQEAKIQAL
Probable integral membrane protein required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall.
Q03478
Q05184
PHT4_PSEPU
Putative 4,5-dihydroxyphthalate dehydrogenase
Pseudomonas
MMASHAESTARLRLGVVGLGRAFTLMLPTFLADRRVQLVGACDPREQARRQFERDFDAPAYETIEDLAADSNVDALYIASPHQFHAEHTRIAAANRKHVLVEKPMALSLDECDRMIADCAEAGVKLIVGHCHSFDTPYLRTRELIGSGEFGAVKMIQALNYTDYLQRPRRPEELSTAEGGGAVFSQAAHQVDVVRLLAGSRATRVRAAVGNWDPARPTEGAYTATLWFENGAFASITYNGYGHFDSDEWMDWVGEMGKPKNPEAYGGARRLLQQVQTADEEARLKAEGTYGGTRYVSPSPTDDATAFQHFGPIIVSCEGGDLRPMADAVMIYRPHSRDRMMLERPTVPRSEVIDELYLAQFYGVTPLHDGEWARDTLEICLAMLRSSEEQRDITLGVNVEDTQWRENPSS
Transforms 4,5-dihydro-4,5-dihydroxyphthalate to 4,5-dihydroxyphthalate.
Q05184
P27054
CHI4_PHAVU
Endochitinase PR4
Phaseolus
MGNKLVLVLVAVALVMGPKNVSAQNCGCAEGLCCSQYGYCGTGEDYCGTGCQQGPCTTASPPPSNNVNADILTADFLNGIIDQADSGCAGKNFYTRDAFLSALNSYTDFGRVGSEDDSKREIAAAFAHFTHETGHFCYIEEIDGASKDYCDEESIAQYPCSSSKGYHGRGPIQLSWNFNYGPAGSANNFDGLGAPETVSNDVVVSFKTALWYWMQHVRPVINQGFGATIRAINGALECDGANPTTVQARVNYYTEYCRQLGVATGDNLTC
Defense against chitin-containing fungal pathogens.
P27054
Q1WTT7
MNMA_LIGS1
tRNA-specific 2-thiouridylase MnmA
Ligilactobacillus
MKDKSQIRVVVGMSGGVDSSVSAYLLKQQGYDVVGVFMKNWDDKNDSGVCTVTEDYQDVAKVASQIGIPYYSVNFEKEYWDRVFTYFLDEYKNGRTPNPDIMCNKEVKFKAFLDYAMSIDADYIAMGHYAQLRRDEDGRVHLLRGADDNKDQTYFLSQLSQEQLQKVMFPIGHLQKSEVRRIAEEAGLATAKKKDSTGICFIGERNFSKFLGEFLPAQPGEMVTLDGEVKGNHFGLMNYTIGQRKGLGIGGDGKSNEPWFVIGKDLKTNTLLVGQGYHNEHLYANSLDASKLSFVDDISDCGDEFHCTAKFRYRQKDTGVTVKFNEDRTKVEVIFDEPVRAITPGQEVVFYDGEECLGSGTIDHAYKESKLLQYV
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Q1WTT7
Q9TSZ2
HEY1_CANLF
null
Canis
MKRAHPDYSSSDSELDETVEVEKESADENGNLSSALGSMSPTTSSQILARKRRRGIIEKRRRDRINNSLSELRRLVPSAFEKQGSAKLEKAEILQMTVDHLKMLHTAGGKGYFDAHALAMDYRSLGFRECLAEVARYLSIIEGLDASDPLRVRLVSHLNNYASQREAASGAHAGLGHLPWGSAFGHHPHVAHPLLLPQSGHGNTGTSASPTDPHHQGRLAAAHPEAPALRAPPSGGLGPVLPVVTSASKLSPPLLSSVASLSAFPFSFGSFHLLSPNALSPSAPTQAANLGKPYRPWGTEIGAF
Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGTG-3'. Downstream effector of Notch signaling required for cardiovascular development. Specifically required for the Notch-induced endocardial epithelial to mesenchymal transition, which is itself criticial for cardiac valve and septum development. May be required in conjunction with HEY2 to specify arterial cell fate or identity. Promotes maintenance of neuronal precursor cells and glial versus neuronal fate specification. Represses transcription by the cardiac transcriptional activators GATA4 and GATA6 and by the neuronal bHLH factors ASCL1/MASH1 and NEUROD4/MATH3.
Q9TSZ2
Q48D49
RS14_PSE14
30S ribosomal protein S14
Pseudomonas
MAKKSMKNRELKRQLTVAKYAKKRAELKAIIVDLNASPEARWEATVALQKQPRDASAARMRNRCRITGRPHGVYRKFGLGRNKLREAAMRGDVPGLVKASW
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.
Q48D49
O51739
RIMP_BORBU
Ribosome maturation factor RimP
Borreliella
MIKYFDKNNEVFNLIKDLTGRLNVEILEINIFRNKNNGKIQIVLYSKNFSLDIDFLTDLHKMILLILEANLKYGFTLELSTPGIDRKIKSDREFKIFEGKKIKLMLDNEFEEGFILESKPKSFIFKTDSKEVNVFYSDVKKARLV
Required for maturation of 30S ribosomal subunits.
O51739
Q7VVR6
IHFA_BORPE
Integration host factor subunit alpha
Bordetella
MGTTMLAEPRTLTKAELAELLFERVGLNKREAKDIVDTFFEEIRDALARGDSVKLSGFGNFQVRDKPPRPGRNPKTGETIPIAARRVVTFHASQKLKSVVEQPNSPPDPASAE
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
Q7VVR6
Q0I6D8
MNMG_SYNS3
Glucose-inhibited division protein A
unclassified Synechococcus
MSFSPPPTEVFDVIVVGGGHAGCEAAITAARLGLSTALFTLNLDRIAWQPCNPAVGGPAKSQLVHEVDALGGVIGRLADATAIQKRVLNASRGPAVWALRAQTDKRHYSREMLQLLHHTPNLALREAMVTGLEVDGDPEPAGQARITGVRTYFGSVYGAQAVVLTAGTFLGGRIWVGHQSMSAGRAGEQAAEGLTDALKQLGFQTDRLKTGTPARVDRRSIALDQLEAQPSDAADRFFSFDPTAWASGEQMSCHITRTTAATHQLIKDNLHLTAIYGGIIDSKGPRYCPSIEDKIVRFADKDSHQIFLEPEGRDTPEIYVQGFSTGLPETIQLELLRTLPGLEQCVMLRPAYSVDYDYLPATQLKPSLETKRVRGLFSAGQLNGTTGYEEAAAQGLVAGLNAARLIGGQEPVHFPRENSYIGTMIDDLVSQDLREPYRVLTSRSEYRLVLRGDNADRRLTPLGRELGLIDDRRWQLFNDKLQAMEEEKQRLETVRLKVSDPVASTVEKESGAPIRGSITLADLLRRSGVHSSDLVRHRLADAELPLAVREGAEIDIKYSGYLQRQQQQIDQVKRQSLRKLPADLDYASIGTLSREAREKLTAIQPTTLGQATHIPGVSQADLTALLLWLELQKRRSQKSESLASSTNSR
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Q0I6D8
Q7ZYA7
DDI2_XENLA
Protein DDI1 homolog 2
Xenopus
MLITVYCVRRDLSEITFSLEVDGDFELENFRALCELESGIPASDTLIVYAERPLTDNQRSLASYGLKDGDVVILRQKEAPETRPAAPFPGLDFSTIAVPGASSQPDPSQPQAPPPPPDTSSFPQGLDNPALLRQMLLANPHELSLLKERNPPLAEALLSGDLEKFTKVLQEQQQERARREQERIRLYSADPFDLDAQAKIEEDIRQHNIEENMTIAMEEAPESFGQVVMLYINCKVNGYPVKAFVDSGAQMTIMSQACAERCHIMRLVDRRWAGIAKGVGTQKIIGRVHLAQVQIEGDFLPCSFSILEEQPMDMLLGLDMLKRHQCSIDLEKNVLVIGTTGTHTTFLPEGELPECARLAYGPGREEVPPEEIADRELAEVLQKSADEADQQKP
Aspartic protease that mediates the cleavage of NFE2L1/NRF1 at 'Leu-104', thereby promoting release of NFE2L1/NRF1 from the endoplasmic reticulum membrane. Ubiquitination of NFE2L1/NRF1 is a prerequisite for cleavage, suggesting that DDI2 specifically recognizes and binds ubiquitinated NFE2L1/NRF1. Seems to act as a proteasomal shuttle which links the proteasome and replication fork proteins like RTF2. Required for cellular survival following replication stress.
Q7ZYA7
Q5WFM5
ACP_ALKCK
Acyl carrier protein
Alkalihalobacillus
MADVMERVTKIIVDRLGVEESEVKLESSFKEDLKADSLDVVELVMELEDEFDMEIADEDAEKIATVKDVVDYINNNQ
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Q5WFM5
Q08A29
FMT_SHEFN
Methionyl-tRNA formyltransferase
Shewanella
MKPLKIIFAGTPDFAARHLQALIDSEHDVIATYTQPDRPAGRGKKLTASPVKALALEHAIPVFQPASLRNEEAQAELAALNADIMIVVAYGLILPKVVLDTPRLGCINVHGSILPRWRGAAPIQRALWAGDTETGVTIMQMDIGLDTGDMLLKTHLPIEATDTSASLYEKLAEQGPKALVQALIGLSDGSLKAQKQDETLANYAEKLSKEEARLDWNKSAKQLWQDIRAFNPWPVSYFEHQQSVIKVWQADYSAELCSQAPGTIIAATKQGIEIATAEGKLMIKTMQLPNKKPLDVADILNARGDWFTAGVCLNQEAN
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.
Q08A29
P04920
B3A2_HUMAN
Solute carrier family 4 member 2
Homo
MSSAPRRPAKGADSFCTPEPESLGPGTPGFPEQEEDELHRTLGVERFEEILQEAGSRGGEEPGRSYGEEDFEYHRQSSHHIHHPLSTHLPPDARRRKTPQGPGRKPRRRPGASPTGETPTIEEGEEDEDEASEAEGARALTQPSPVSTPSSVQFFLQEDDSADRKAERTSPSSPAPLPHQEATPRASKGAQAGTQVEEAEAEAVAVASGTAGGDDGGASGRPLPKAQPGHRSYNLQERRRIGSMTGAEQALLPRVPTDEIEAQTLATADLDLMKSHRFEDVPGVRRHLVRKNAKGSTQSGREGREPGPTPRARPRAPHKPHEVFVELNELLLDKNQEPQWRETARWIKFEEDVEEETERWGKPHVASLSFRSLLELRRTLAHGAVLLDLDQQTLPGVAHQVVEQMVISDQIKAEDRANVLRALLLKHSHPSDEKDFSFPRNISAGSLGSLLGHHHGQGAESDPHVTEPLMGGVPETRLEVERERELPPPAPPAGITRSKSKHELKLLEKIPENAEATVVLVGCVEFLSRPTMAFVRLREAVELDAVLEVPVPVRFLFLLLGPSSANMDYHEIGRSISTLMSDKQFHEAAYLADEREDLLTAINAFLDCSVVLPPSEVQGEELLRSVAHFQRQMLKKREEQGRLLPTGAGLEPKSAQDKALLQMVEAAGAAEDDPLRRTGRPFGGLIRDVRRRYPHYLSDFRDALDPQCLAAVIFIYFAALSPAITFGGLLGEKTQDLIGVSELIMSTALQGVVFCLLGAQPLLVIGFSGPLLVFEEAFFSFCSSNHLEYLVGRVWIGFWLVFLALLMVALEGSFLVRFVSRFTQEIFAFLISLIFIYETFYKLVKIFQEHPLHGCSASNSSEVDGGENMTWAGARPTLGPGNRSLAGQSGQGKPRGQPNTALLSLVLMAGTFFIAFFLRKFKNSRFFPGRIRRVIGDFGVPIAILIMVLVDYSIEDTYTQKLSVPSGFSVTAPEKRGWVINPLGEKSPFPVWMMVASLLPAILVFILIFMETQITTLIISKKERMLQKGSGFHLDLLLIVAMGGICALFGLPWLAAATVRSVTHANALTVMSKAVAPGDKPKIQEVKEQRVTGLLVALLVGLSIVIGDLLRQIPLAVLFGIFLYMGVTSLNGIQFYERLHLLLMPPKHHPDVTYVKKVRTLRMHLFTALQLLCLALLWAVMSTAASLAFPFILILTVPLRMVVLTRIFTDREMKCLDANEAEPVFDEREGVDEYNEMPMPV
Plasma membrane anion exchange protein of wide distribution.
P04920
B0BWC2
GATB_RICRO
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
spotted fever group
MAYIEGNTGKWEYVIGLEIHAQISSKSKLFSGSSTIFAANPNSQVSYVDAAMPGMLPVLNKHCVHQAIKTGLGLKAKINKYSVFDRKNYFYADLPQGYQISQFYYPIVQNGTMEIPTSTGDLKTIRINRLHLEQDAGKSMHDQSPHYSFIDLNRAGIGLMEIVTEPDISSPEEAAEFVKKLRNLLRYIGSCDGDMEKGSMRCDANISVRRSGEPLGTRCEIKNINSIRNIIKAIEFEAKRQVDLLESGEEIIQETRLFNADSGETRTMRLKEEALDYRYFPDPDLLPLVISDELINELKANLPELPDQKIEKYTKEFSLSKYDAEVIVADESVAEYFEKAANECNPKMLTNWLTSELFGQLNKASIGINECKITPSNFAKLVKLIENDTISGKIAKTVFEIMFETGKAPDKIIEEKGLVQVSDNNVLNTVIDEVIAENPESVEGYRSGKDKLFGFFVGQVMKKTDGKANPTLVNQLLKEKLSS
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).
B0BWC2
P39078
TCPD_YEAST
CCT-delta
Saccharomyces
MSAKVPSNATFKNKEKPQEVRKANIIAARSVADAIRTSLGPKGMDKMIKTSRGEIIISNDGHTILKQMAILHPVARMLVEVSAAQDSEAGDGTTSVVILTGALLGAAERLLNKGIHPTIIADSFQSAAKRSVDILLEMCHKVSLSDREQLVRAASTSLSSKIVSQYSSFLAPLAVDSVLKISDENSKNVDLNDIRLVKKVGGTIDDTEMIDGVVLTQTAIKSAGGPTRKEKAKIGLIQFQISPPKPDTENNIIVNDYRQMDKILKEERAYLLNICKKIKKAKCNVLLIQKSILRDAVNDLALHFLSKLNIMVVKDIEREEIEFLSKGLGCKPIADIELFTEDRLGSADLVEEIDSDGSKIVRVTGIRNNNARPTVSVVIRGANNMIIDETERSLHDALCVIRCLVKERGLIAGGGAPEIEISRRLSKEARSMEGVQAFIWQEFASALEVIPTTLAENAGLNSIKVVTELRSKHENGELNDGISVRRSGTTNTYEEHILQPVLVSTSAITLASECVKSILRIDDIAFSR
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.
P39078
Q732H0
SEPF_BACC1
Cell division protein SepF
Bacillus cereus group
MSWSKVKYFFFDTPEEKEAAQYSYEKEQTDMKKQQDPPEQQDVTFPKAQTKQNVVSIETAKQSSKVVLLEPRTYSEAQGIADHLKGRRAVVINLQRMSTDQAVRIVDFLSGTVYAIGGDIQKIGPKTFMCTPENVDIVGAISELFGEEEDTNIKRW
Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
Q732H0
Q2NIV9
RL22_AYWBP
50S ribosomal protein L22
Candidatus Phytoplasma asteris
METKNAKAIARKVSIAPRKARLVVDLIRGKNIAQAQAILTFTPKVAAPVILKLLNSAVSNAVNNLKLNREQLYVKEVFVNEGFRLKRMFPRAKGSGDMIKKRTSHITLVITSSTNLQTSKEEEQSGSKN
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.
Q2NIV9
P0CW75
RELB4_CAUVC
Antitoxin RelB4
Caulobacter
MAEPDPDIFDEDDEAILAADAEADADFEAGRTVPHERVGEWLKTLGTPHQTPPPYSWRK
Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the effect of cognate toxin RelE4, but no other RelE or ParE toxin.
P0CW75
Q88Y23
MURE_LACPL
UDP-N-acetylmuramyl-tripeptide synthetase
null
MQASQLINSLKFKQVQPALTTDFDVTMLTQDTREVQPGAMFIAVVGYHVDGHDLVDQAIEKGAKIIVASKPLDVNVPVIYVENTERAMAILADVFYGAPSQKMRMIGVTGTNGKTTVTHLIEQIYRDQQQATGLIGTMYRKIKDEKLPTANTTPDAITTQRTLAAMRDAGVETVAMEVSSIALVLGRVWGIDYDIAVFTNLTQDHLDFHKTMAKYTEAKAMLFAQLGNKYSADGTNKVAVLNTDDPVGREFEQYTAAHVLTFGLKPDAMINAQNVEIKSHGTEFDLSVFGHVTHVTMQLIGQFNVYNMLAAFAAAYASGIPEDQIIKSLEKVTGVKGRFQSVPSHTGVSVIVDYSHTPDGLLNALETIQDFATKDIYCVVGCGGDRDKTKRPKMAKIAVEHSTKPIFTSDNPRTEDPTMILNDMVAGVPNADVPVYEDRHVAIAKAIEAAQPGDVVLIAGKGHEDYQIIGRTKHHFDDSEEAAKALALKPTID
Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
Q88Y23
Q2ISY9
BCHL_RHOP2
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Rhodopseudomonas
MNILTDPLKLKTSGCADANASKCAEGDGEGSVQVQLDPNVKIGSAKVFSIYGKGGIGKSTTSSNLSVAFSKLGKRVLQIGCDPKHDSTFTLTKRLIPTVIDVLEEVNFHSEELRPEDFVFEGYNGVMCLEAGGPPAGTGCGGYVVGQTVKLLKEHHLLEDTDVVIFDVLGDVVCGGFAAPLQHSERAMIVAANDFDSIFAANRIAAAIQAKSKNYGVRLAGIIANRSRETDQIDKFGAATGIQRVAHLPDLDVIRKSRLKKMTLFEMDHTDEILAVQQEYLRLATEMWEAKTPPVQGKPLKDRDIFDLLGFD
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
Q2ISY9
Q9W2U9
OR9A_DROME
Odorant receptor 9a
Sophophora
MSDKVKGKKQEEKDQSLRVQILVYRCMGIDLWSPTMANDRPWLTFVTMGPLFLFMVPMFLAAHEYITQVSLLSDTLGSTFASMLTLVKFLLFCYHRKEFVGLIYHIRAILAKEIEVWPDAREIIEVENQSDQMLSLTYTRCFGLAGIFAALKPFVGIILSSIRGDEIHLELPHNGVYPYDLQVVMFYVPTYLWNVMASYSAVTMALCVDSLLFFFTYNVCAIFKIAKHRMIHLPAVGGKEELEGLVQVLLLHQKGLQIADHIADKYRPLIFLQFFLSALQICFIGFQVADLFPNPQSLYFIAFVGSLLIALFIYSKCGENIKSASLDFGNGLYETNWTDFSPPTKRALLIAAMRAQRPCQMKGYFFEASMATFSTIVRSAVSYIMMLRSFNA
Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability.
Q9W2U9
Q6LWM3
TRUB_METMP
tRNA-uridine isomerase
Methanococcus
MELIVKEESKTDYNYGSDPYNRDIKTLLNTGLVVIDKPSGPTSHEVAAWVRNMLNLVKAGHGGTLDPKVTGALPVALGNTTKCVPIWHIPPKEYVCLMHLHDDAELVDIENIFKEFTGRIHQRPPLKAAVKRSLRIRKIYEIEILEIDGRDILFRTKCQSGTYLRKLVDDMGEALGTSAHMQELRRTISGPFYENEAVYLQDLLDAYIFWKEDGNEEELRKIVKPLEYGLQHLKKIIIKDSAVDAVCHGATLYSSGISKIEKGLGTDEVVLIETLKGEAVAVGKPLMNTKDMLKTEEGEVVEITRVIMEPGIYPRIWKKRNKNDKSKPELKKK
Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Q6LWM3
Q0HPB7
FADB_SHESM
3-hydroxyacyl-CoA dehydrogenase
Shewanella
MIYQSPTIQVELLEDNIAKLCFNAPGSVNKFDRETLASLDAALDSIKQQSNIQALVLTSGKDTFIVGADITEFLGLFAQDDAVLLSWVEQANAVFNKLEDLPFPTASAIKGFALGGGCEAILATDFRIADTTAKIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITTGKDQRPEDALKVGAVDAVVAPEALEAAAIQMLKDAVAEKLDWQARRQRKMSPLTLPKLEAMMSFTTAKGMVFAVAGKHYPAPMAAVSVVEQAATKGRSDALQIEHQAFIKLAKTDVAKALIGIFLNDQLVKGKAKKAGKLAKDVKSAAVLGAGIMGGGIAYQSASKGTPIVMKDIAQPALDLGLGEAAKLLSAQVARGRSTPEKMAKVLNNITPALDYAPVKHADVVVEAVVEHPKVKAQVLAEVEQYVSEDAIIASNTSTISINLLAKSMKKPERFCGMHFFNPVHKMPLVEVIRGEHSSEETIASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFNGLLAEGGDFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMAEGFPDRMGKSGNDAIDVMFENKRLGQKNGKGFYAYSVDSRGKPKKDVDPTSYELLKAAFGEQKAFDADEIIARTMIPMIIETVRCLEEGIVASPAEADMGLVYGLGFPPFRGGVFRYLDTMGVANFVALADKYAHLGGLYQVTDAMRTLAANNGSYYQA
Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
Q0HPB7
Q4JVN6
UPPP2_CORJK
Undecaprenyl pyrophosphate phosphatase 2
Corynebacterium
MTTDMTWAQTIILSLIQGLTEFLPVSSSGHLRIFSTLLWGEDAGASFTAVIQLGTELAVLVFFAKDIWNIASAWCKGVWEWLTDLTGKHGRRVHRQSFDYRMGWMVIVGTLPVAVLGYLGKDLIRDNLRNLWITATMLVLFSFVFILAERMGRRERSFDELTMRDSVIMGFAQCLALIPGVSRSGGTVSAGLFLNLDREVATRYSFLLAIPAVLASGLFSLPDAFSPDAGQAASGAQLFVGTAIAFAVGYASIAWLLKFVANHSFAWFALWRIPLGLAVMGLLAFGVLQA
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Q4JVN6
D8QAM0
PFF1_SCHCM
FXNA-related family protease 1
Schizophyllum
MGIVDYLVAAVSFRTLPTTFVAVLVYLAIFISVLITDELPATPKDQRGLNLTQAYSDLRQIAARPHPYNSHANDVVHDFILTRLQDATAGYDYAHVFDDKVSNGSWSSRNNSVYFEGTNILVKVDGHDADKSGALFSAHYDSVSTAPGATDDGMGVATLLQLVEYYVKHRPQRTAVFNINNGEEDWLNGAHAFLEHPWSNLTDTFLNLEGASSGGRPLLFRATATAPVRAFREKYVTHPHGNVLSSDAFARGVVRSGTDYSVYVDGRGMDGADLAFYKGRSRYHTRYDAVQYTDGGVRSLWAMMEAAQGVSGALLSSEAVHGDKGGAPVYFDLFGQALIVFPLSAMITFNIVFLVVGPIMLALLVTFDIVARHRRQEMIGGGYEEQGFFARAWTSFKSFRWVGGFWKHAKFWVALAVTVGLQVLLCVGYLYINPLIAYSSSHIVLLSFLSLAYLSTYLVHNIPSPTDTYGSHLPEQQKQAALFQLYFFTWILLLAATVVGAKLSVGSFYILSLWNAVLFAACAIGSIAGLLSSHTVEGDASYGSRRRIRGVRYDREGEEEGVESETAPTEVTPLIAQPITVVAPGGKEGEEVSGAIGWWFVQFVLSVPAVVILVSQLALLMLAATEQTLADGSPAVTVYGGASLMSVLAILPLAPFACKLHRRVAYVALVVLIASTAYAWLVFPFSERAPLKVFFQQQVDLDANITETRITGHPAYLRQAIAALPSAGGAPLNCTADDAKAGLQTCGWTPPPALEPSVIALDFNVSRSEGQNQARFEIAETDTRACRVYFDQAVTRFQVHGGTEGVQKGFEIPEEGVRELRLWSRTWDRTWVVDVDREGSALTGRVACEWSEYASGSLGVETRTRIPAYEEVLTFLPSWAVASKFADGLVEGYKAFAV
May be involved in vacuolar sorting and osmoregulation.
D8QAM0
Q9HGZ9
TRMBR_PYRFU
HTH-type sugar sensing transcriptional regulator TrmB
Pyrococcus
MEIPPEISHALSEIGFTKYEILTYWTLLVYGPSTAKEISTKSGIPYNRVYDTISSLKLRGFVTEIEGTPKVYAAYSPRIAFFRFKKELEDIMKKLEIELNNVKKEEQRPAIWRSRSFDEAIEMFRESLYSAKNEVIVVTPSEFFETIREDLIKTLERGVTVSLYIDKIPDLSEFKGKGNFFVRQFYKLNHLIGMTDGKEVVTIQNATFDSIGPPSFKSTYPEIIFSQYSLIIEIFKESTLEKEIIGNPKDIRFFAMFHAVDFVKNHLKNRNIYAEITGKNLESGRLETLTGRVVGYTLSLREAVNNIHLETENGVVKVGGMFAVIEDYESTEIKFIMG
Inhibits transcription of the trehalose/maltose transport gene cluster (malE operon) and of the maltodextrin transport gene cluster (mdxE operon). Acts by binding to two different operator sequences in both promoters, preventing polymerase recruitment and transcription.
Q9HGZ9
Q0TA90
BTUB_ECOL5
Outer membrane cobalamin translocator
Escherichia
MIKKASLLTACSVTAFSAWAQDTSPDTLVVTANRFEQPRSTVLAPTTVVTRQDIDRWQSTSVNDVLRRLPGVDITQNGGSGQLSSIFIRGTNASHVLVLIDGVRLNLAGVSGSADLSQFPIALVQRVEYIRGPRSAVYGSDAIGGVVNIITTRDHPGTEISAGWGSNSYQNYDVSTQQQLGDKTRVTLLGDYAHTHGYDVVAYGNTGTQAQPDNDGFLSKTLYGALEHNFTDVWSGFVRGYGYDNRTNYDAYYSPGLPLVDTRKLYSQSWDAGLRYNGELIKSQLITSYSHSKDYNYDPHYGRYDSSATLDEMKQYTVQWANNIIIGHGNIGAGVDWQKQSTAPGTAYVEDGYDQRNTGIYLTGLQQVGDFTFEGAGRSDDNSQFGRHGTWQTSAGWEFIEGYRFIASYGTSYKAPNLGQLYGSYGNPNLNPEKSKQWEGAFEGLTAGVNWRISGYRNDVSDLIDYDDHTLKYYNEGKARIKGVEATANFDTGPLTHTVSYDYVDARNAITDTPLLRRAKQQVKYQLDWQLYDFDWGITYQYLGTRYDKDYSSYPYQTVKMGGVSLWDLAVAYPVTSHLTVRGKIANLFDKDYETVYGYQTAGREYTLSGSYTF
Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB.
Q0TA90
Q5BK82
TRI69_RAT
Tripartite motif-containing protein 69
Rattus
MEVSSRPPSNFDPGNYVEVSDPSTHLPSKVVIQDITTELHCPLCNDWFRDPLMLTCGHNFCQACIQNYWKMQAKETFCPECKMLCQYSNCTFNLVLEKLVEKIKRLPLLKGHPQCPEHGENLKLFSKPDGKMICFQCKDARLSMGQSKDFLQISEAVRFFTEELAIYQSQLQTTLKELQSLRTMQKDAIAAYKDNKIQLQQNLSLEFLKLHQFLHNKEKDILNDLRDEGKVLNEEMDANLNQIQEQCLLAKDMLANIQARMEQQNSFDFLTDITKLLENMEKGMKTLVPRQLISKKLSLGRFKGPIQYTIWREMQSILSPGPSQLTLDPKTAHPNLVLSNSRTSVCHGDVKQVMPDDPERFDSSVAVLGSKGFTSGKWYWEIEVAKKTKWTIGIVRESIIRKGSCPLTPEQGFWLLRLRNQTDLKALDLPSCSLNLGDLRRVGVYLDYEGGQVSFYNATNMTHLYTFTSVFLEKLFPYLCPCLNDGGENKEPLHIVHPQ
May have E3 ubiquitin-protein ligase activity. May play a role in apoptosis.
Q5BK82
Q11VC0
NUOI_CYTH3
NDH-1 subunit I
Cytophaga
MQLTNRSKVVVDKKMTFMERIYIPSIVSGMMITLSHLFKKKATIQYPEVQREFAFVYRGKHILKRDEQGRENCTACGLCAVSCPAEAITIIADERKKGEEHLYKEEKYASLYEINMLRCIFCGLCEEACPKDAVYLTEELVPAQYNRKDFIYGKDKLVQPLGTSAHPKTYKPYKK
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.
Q11VC0
B6HY16
DRS4_AGACL
DRP-AC4
Agalychnis
MAFLNKSLLLVLFLGLVSLSICEEERRENEDEEEQEDDEQSEMRRSLLSTLGNMAKAAGRAALNAITGLVNQGEQ
Has antibacterial activity against Gram-positive bacterium M.luteus NCT C2665 but not against Gram-negative bacterium E.coli K12D31.
B6HY16
B2HX89
PDXB_ACIBC
Erythronate-4-phosphate dehydrogenase
Acinetobacter calcoaceticus/baumannii complex
MKIVADENLAFTDYFFSEFGDIQYKAGRTLTHTDVQDAEALLVRSVTAVNESLIQNTALKYVGSATIGTDHLDIQALEKQGITWANAAGCNAQAVAEYVITALLHLDASLLEQQEKFTLGIVGLGNVGKRLAYMAQLLGWKVIGFDPYVQLDSIENVSFQTLLQQANAVSIHVPLTKKGEHATYHLFDEKAFAALQPNTILINSARGPVVKEAALIEDIQRTQRKVVLDVFEHEPVISEELLNMLALATPHIAGYSLEGKARGTQMIYEAFCQKFGYDINKRFETQLPACEDYFSGHDLKAVLKQKLSQIYDIAQDDANIRACVKEGKVEQKAFDLLRKNYPLRREWAAHGGPQA
Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
B2HX89
A7RV13
PSMG1_NEMVE
Proteasome assembly chaperone 1
Nematostella
MVDAFGLWELNFPCSRVDDDDDEEEQITKEQEEQLCPQFVFSPQFSKDVGKTEPIECSVLVLGVGEVASTFLEVHFLCGNNSSVAAVISDKKTEKNFEYLVKNLRNKRSSLLHQLTRNNDVMVCQISSHVEQDKGFYWTQKIFSHIRPAKVVILTSSPASEYNSDDPSEIKTDFVKMMKTNAWSNSCAGPDITDIQTPNTVKGLAASVLTHCQIYKLPAALFMCYTESMHVDAQAVEAFRCKAPYKQSSMGLESGKL
Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with psmg2.
A7RV13
Q47UV5
RL11_COLP3
50S ribosomal protein L11
Colwellia
MAKKVQALIKLQVAAGAANPSPPVGPALGQHGVNIMEFCKAFNAKTDSLEKGAPVPVVITVYSDRSFTFETKTPPASFLLKKAAGIKSGSGRPNTDKVGTVTTAQLEEIVKTKEPDLTAGSLEAAVRTIAGSARSMGLVVED
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Q47UV5
A8EVZ7
RL1_ALIB4
50S ribosomal protein L1
Aliarcobacter
MAKVSKRYKALAEKVEERKYSLAEACTTVRDLKSAKFDESVEIALNLNVDPRHADQMIRGAVVLPNGTGKTVRVAVFAKGVKLDEAKAAGADVVGNDDLAEAIQAGNINFDVLIATPDCMGIVGKVGRILGPKGLMPNPKTGTVTMDVTKAVNDAKGGQVTYRVDKKGNMQAAVGKVSFSAEAIKENVEAFVAAINKAKPSTAKGRYITNAAISLTMSPSIILDNMELMEIR
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
A8EVZ7
Q6NWC9
GKAP1_DANRE
G kinase-anchoring protein 1
Danio
MASAVISVPTTASRFALLQVDSDSDSDSDVGKPKAAGRGAGKPRSGKSPSGKNSQNNEKKKEKRRRKKEQQQSEANELRSLAFKKIPQKSTAPPSLTLQDLANDLINPANVQQGSKPQENWQEWKQRDEQLTSDLYEADLEKALMLSKLEFEEHKKDADKAETASPKTKTGGKKDRKKNQQGKDKRVTVSLKDFQQEDQLKNKPEREPVNPALRDDKFFNKLEDDVSKIVQRDKRREQYSNSAGQEVNTSSEHEQDVRTEQLKYELEKKDQEIAKLKKTISQWEERYKEVKARNSQLLKMLQQGEMKDKAEILLQVEELLNIKEELSSQVTQLHTALEQERSKVKGLQSEQPKHQGNRKGKKASEGDV
May play a role in the regulation of insulin-dependent IRS1 tyrosine phosphorylation in adipocytes.
Q6NWC9
P40855
PEX19_HUMAN
Peroxisomal farnesylated protein
Homo
MAAAEEGCSVGAEADRELEELLESALDDFDKAKPSPAPPSTTTAPDASGPQKRSPGDTAKDALFASQEKFFQELFDSELASQATAEFEKAMKELAEEEPHLVEQFQKLSEAAGRVGSDMTSQQEFTSCLKETLSGLAKNATDLQNSSMSEEELTKAMEGLGMDEGDGEGNILPIMQSIMQNLLSKDVLYPSLKEITEKYPEWLQSHRESLPPEQFEKYQEQHSVMCKICEQFEAETPTDSETTQKARFEMVLDLMQQLQDLGHPPKELAGEMPPGLNFDLDALNLSGPPGASGEQCLIM
Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome membrane by binding to the integral membrane protein PEX3. Excludes CDKN2A from the nucleus and prevents its interaction with MDM2, which results in active degradation of TP53.
P40855
P45106
PRMB_HAEIN
N5-glutamine methyltransferase PrmB
Haemophilus
METSHNQELVATILEDNVANELQTIQDFLRWTYSILNRSDIYFGQGHDNPWDESLQLVLSSLHLPIDLPTELFNSRLTPSEKETLVQLVLTRIEQRVPVAYLTNSAWFCGHEFYVDERTIIPRSPISALIQDRFEDLISQEPNHILDLCTGSGCIAIACAYAFPNAEVDAVDLSVDALNVAEINISRHQLEHRVFPIQSNLFENILGQKYDLIVTNPPYVDEEDLADMPEEFHFEPELALGSGSDGLNITKQILKQAPDYLTENGVLVCEVGNSMISLIEQYPDVPFEWVELKNGGLGVFAIQRKDLVKYHDLF
Specifically methylates the 50S ribosomal protein L3 on a specific glutamine residue.
P45106
Q1WSU5
RECR_LIGS1
Recombination protein RecR
Ligilactobacillus
MQYPEPISKLIDSYMKLPGIGSKTATRLAFYTIDMQEDDVTEFAQSLISAKRDLSYCSICGNITESDPCMICADKSRDNSKVVVVEQPKDVMSLERMNEYHGLYHVLHGVLSPIEGKGPEDINIASLLRRLQKNEAIKEVIIATNATPEGEATAMYIARLVKPANIKVTRLAHGLAVGSDIEYADEMTLFKAIEGRQEI
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Q1WSU5
Q83IC1
RS18_TROW8
30S ribosomal protein S18
Tropheryma
MGYRAKGRRQPKADSVVAPPKRVSIKGLDYKDLASLKRFLSDRGKIRARRVTGASIQQQRQIAKAIKNAREMGVIPFKSGVSR
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Q83IC1
P33487
ABP1_ARATH
Auxin-binding protein 1
Arabidopsis
MIVLSVGSASSSPIVVVFSVALLLFYFSETSLGAPCPINGLPIVRNISDLPQDNYGRPGLSHMTVAGSVLHGMKEVEIWLQTFAPGSETPIHRHSCEEVFVVLKGSGTLYLAETHGNFPGKPIEFPIFANSTIHIPINDAHQVKNTGHEDLQVLVIISRPPIKIFIYEDWFMPHTAARLKFPYYWDEQCIQESQKDEL
Auxin receptor that controls cell elongation and cell division . Involved in embryonic morphogenesis . Acts on the cell cycle, endocycle, cell plate formation, and cell expansion and contributes to the control of auxin-related gene expression . Controls root meristem size and mediates auxin responsiveness . Involved in activation of ROP GTPases in response to auxin and regulation of clathrin-mediated endocytosis in roots . Acts as a positive factor in clathrin recruitment to the plasma membrane, thereby promoting endocytosis . Upon auxin binding, restricts the internalization of PIN proteins by inhibiting clathrin-mediated endocytosis . Involved in the regulation of polar auxin transport . Behaves as a negative regulator of the SCF(TIR1/AFB) signaling pathway, protecting AUX/IAA repressors from degradation . Regulates the expression of cell wall remodeling genes via an SCF(TIR1/AFB)-dependent pathway . Involved in the modulation of hemicellulose xyloglucan structure . Required for rapid auxin-mediated re-orientation of microtubules to regulate cell elongation in roots and dark-grown hypocotyls as well as asymmetric growth during gravitropic responses . Involved in the shade avoidance response . Forms with TMK1 a cell surface auxin perception complex that activates ROP signaling pathways . ABP1 sensing of auxin is important for the ABP1-TMK1 complex formation . Interacts functionally with phytochrome to regulate growth .
P33487
Q4UQP3
SYV_XANC8
Valyl-tRNA synthetase
Xanthomonas
MTQLASSYDPSSFESRLYAQWESAGHFKPSGSGEPYTVLLPPPNVTGTLHMGHAFQQTLMDALVRYHRMRGYDTLWQVGTDHAGIATEMVVSRNLALEGKGETRDTLGREGFIAKVWEWKAQSGDTIERQMRRLGTSSDWSRSTFTMDPQPSAAVTEAFVRWYEQGLIYRGQRLVNWDPVLKTAISDLEVENVEEDGFLWSIRYPLADGVTYEHVEHDADGVETLRETRDYLVVATTRPETMLGDTAVMVHPDDARYATLHAAQIVLPLTGRLVPVITDDYVDRAFGTGVVKVTPAHDFNDYQVGVRHDLPLINLFTVTAAINDNAPERYRGLDRYDARKLVLSELEDLGLLVETKPHKLQVPRGDRTGQVIEPYLTDQWFVKMDALAKRGLELVESGQVKFVPPNWINTYRHWMENIQDWCISRQLWWGHRIPAWFDEAGKCYVGHDEAQVRATHGLGAEVALHQDSDVLETWFSSQLWPFSTLGWPDAQAMDERGFARYLPSSVLVTGFDIIFFWVARMIMATDSFTGQVPFRDVYITGLIRDAQGQKMSKSKGNVLDPLDIIDGISIEDLVAKRTSGLMQPRMAEKIEKATRKEFPDGIIAHGADALRFTIAALATHGRDIKFDLGRAEGYKNFCNKLWNATRFALMNTEGAQFSGVPQPQTETERWILARLDAVAAEAQAHYANYRFDLLAQTLYEFAWNAFCDWFVELAKPALNGAVQDAADSTRHTLLYVLEALLRLLHPLTPFVTEELWQQVAPRLGITGDTISLQAFPQRGDVDTSGYAGAEADIEWLKAMVSALRRVRSELNVPPSKQVRLWLQAGSSDDRARVARFASQLAFLLKLEAIDWLAAGQEAPPAAAAIVGELTLLVPLEGLVDMDAERTRLDKEIKRVENEIGKCNGKLGNATFVQNAPAAVVEQERARLNDWTTQLTGLREQRAKL
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Q4UQP3
A0LI67
DNLJ_SYNFM
Polydeoxyribonucleotide synthase [NAD(+)]
Syntrophobacter
MPDREKAHARIEALREEIRHHNYLYYVLDRPEISDEAYDGLFRELVRLEESYPALITPDSPTQRVGAAPAEKFLPFPHTIPMLSLENAMSEAEVFEFARRVRKILGDRGDVDFMAEPKMDGLAVELVYENGELTGAGTRGDGYVGEDVTRNAKTIRAIPLKLYAGAGGASPPARIAVRGEVYMDRKDFAALNRSREQAGEPLFANPRNAAAGSLRQLDPSVTAARSLKAFFYGVGEVSGYRFKTQAQTLEQLRRWGLPVNPLSRVCPSIEDAVSFYNEIAAGRDALPFEIDGVVVKVNSIEWQEMLGEKSRSPRWAIAYKFSPHQARTRVLDIKVQVGRTGVLTPVAELEPVTVGGVTVRRATLHNQDEVERKDIRVRDQVMVRRAGDVIPEVVEVIGEARTGGEEVFQMPGQCPSCGSEVVRLPEEAVHRCLNRNCPAQIKASLRHFASRDAMNIEGLGKNIVSMLVDRGIVESVSDLYRLSVETLEQLPGFAGKSSRNLVESIERSKKTNLADFLYALGIYHVGSHVARLLAERFGTLDAVRRASVEELMSVNGVGEVVARSVVHYFSLPANRTLVESLLSAGLEMAATEPEAGPVDAFWNGKTVVFTGALSSMTRSNAAALTASRGARVSDSVSRKTDIVVAGADPGSKVEKARQLGITILDEREFLERLGM
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.
A0LI67
A1JJS3
CYSI_YERE8
Sulfite reductase [NADPH] hemoprotein beta-component
Yersinia
MSEKHPGPLVVTGKLSDGERMKSQSNFLRGTIAEDLNDGLTGGFNGDNFLLIRFHGMYQQDDRDIRAERAEQKLEPRHAMMLRCRLPGGIITPQQWLGIDKFAADNTLYGSIRITNRQTFQFHGILKGNVKPAHQLLNQLGLDALATANDVNRNVLCTSNPVESVLHQEAYEWAKKISEHLLPRTRAYAEIWLDAEKVATTDEEPILGATYLPRKFKTTVVIPPQNDVDLHANDLNFVAVADKGKLVGFNVLVGGGLSIAHGDKNTYPRKASEFGYIPLQHTLAIAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVEVFKAEVEKRAGVSFGAIKPYQFTGRGDRIGWVKGIDKKWHLTLFIENGRLLDYPGRSLKTGVAEIAKIHQGDFRLTANQNLIVAGVPEKDKARIEALAREHGLMDDSVSPQRENSMACVSFPTCPLAMAEAERFLPEFVTRIEGILQQHGLPDEHIVMRVTGCPNGCGRALLAEMGLVGKAVGRYNLHLGGNREGTRIPRMYRENITEDEILAITDQLVGRWAKERHTDEGFGDFVIRVGVIAPVIDSARDFYDVQEAV
Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
A1JJS3
A0LDW8
ATPF_MAGMM
F-type ATPase subunit b
Magnetococcus
MISAAYAATHAAAEHAQSGMPQFDSSTFSSQMFWTVISFVALLLLLKKFVVPAISDVLEARASRIEEELKAAENERKEAAALLVDQRAEVKAEREKIAQLLESARKEADALREQEKAELEAELAKLKSQATQDIEQARRQAMSEVRGVVVEVALAVTEKLITKSIDKAEANKLADEAIRHLEANKDQLH
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
A0LDW8
Q1MPA2
NDK_LAWIP
Nucleoside-2-P kinase
Lawsonia
MQHTFALIKPDAVQRNLIGAIINMIEKNDFYISAMKMLQMNRQQAEGFYSVHRERPFFNELVDYMISGPIVSLILTGENAVTRYRELMGATNPQNAQEGTIRKSFAISLMENAVHGSDSDENAIIEINYFFNAFERIR
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.
Q1MPA2
Q74IM2
EX7S_LACJO
Exodeoxyribonuclease VII small subunit
Lactobacillus
MAIKKNNFEEQLNELQEIVNKLESGNVPLEDALSEFQAGVKLSRELEKKLNDAEQTVAKLVDKDGNEKALDPQNASAPEEE
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Q74IM2
B1MCU7
DXS_MYCA9
1-deoxyxylulose-5-phosphate synthase
Mycobacteroides abscessus
MLDDIRGPGDLQGLSKRELDLLADEIREFLIHKVAATGGHLGPNLGVVELSLALHRVFESPYDPIIFDTGHQAYVHKILTGRAGDFDTLRQKDGLSGYPSRAESEHDWVESSHASTALSYADGLAKAFELTGQRRRHVVAVVGDGAMTGGMCWEALNNIAAAEHRRIIIVVNDNGRSYAPTIGGLASHLAGLRLTPSYEKVLDESKKLLRGMPVVGPLAYALMHSLKVGVKDAVSPQVMFTDLGLKYVGPVDGHDEHAVEDALRRARGYGGPVIVHVITRKGMGYAPAEDDEAEQMHSTGIIDPKTGRAIKASAPGWTSVFSDALIDVASEHRNIVAITAAMPGPTGLSKFGERFPDRLFDVGIAEQHAVTSAAGLAMGGLHPVVAIYSTFLNRAFDQVMMDVALHRLPVTFVLDRAGITGSDGASHNGMWDLSILNVVPGMRVAAPRDASRLREELTEALAVDDGPTALRFPKGEVGEDIPAIERRDGVDILARPASGLHADVLLVAVGSFASTALATADRLGKQGIGVTVVDPRWVLPVPPHVVELAGQHRLVVTLEDSGVHGGAGSAVTAAMQDADVDIPSRDIGVPQQFLEHASRGQVLEELGLTDQHIARKITGWVAAMSREIGDSTVNPAAQQVD
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
B1MCU7
A7Z9A7
FLIW_BACVZ
Flagellar assembly factor FliW
Bacillus amyloliquefaciens group
MIIKTKYHGEIRIDEGQIISFENGLPGFNDETQFVVLPLSEDSPFLALQSVKQEHIAFIVASPFIFFKGYEFDIDHATLELLHIEDIEDVEVMAILTLEEPFENTTANLKAPIIVNKKEMKAKQIILHDASYETKHLIGGGSC
Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum.
A7Z9A7
F4K6X0
CHR42_ARATH
Protein CHLORORESPIRATORY REDUCTION 42, chloroplastic
Arabidopsis
MALSFVSSTRFSKMQYGIWHSGSFTQRVSVRCCEIANEAPRPKSKLQVGSPIIIVEAPKVIKTAASMPCLRANSGLVKPGDVGRIVSRKPKDLWAVRLSIGTYLLDGKYFKALELDEGDSD
Required for both formation and activity of the chloroplast NAD(P)H dehydrogenase (NDH) complex of the photosynthetic electron transport chain . Functions in assembly or stabilization of the NDH complex; probably involved, together with CRR1 and CRR6, in the incorporation of NdhJ, NdhM, NdhK and NdhI into the NDH subcomplex A assembly intermediate (NAI500) to produce the complex NAI400 .
F4K6X0
Q8NHA4
O2AE1_HUMAN
Olfactory receptor 2AE2
Homo
MWQKNQTSLADFILEGLFDDSLTHLFLFSLTMVVFLIAVSGNTLTILLICIDPQLHTPMYFLLSQLSLMDLMHVSTIILKMATNYLSGKKSISFVGCATQHFLYLCLGGAECFLLAVMSYDRYVAICHPLRYAVLMNKKVGLMMAVMSWLGASVNSLIHMAILMHFPFCGPRKVYHFYCEFPAVVKLVCGDITVYETTVYISSILLLLPIFLISTSYVFILQSVIQMRSSGSKRNAFATCGSHLTVVSLWFGACIFSYMRPRSQCTLLQNKVGSVFYSIITPTLNSLIYTLRNKDVAKALRRVLRRDVITQCIQRLQLWLPRV
Odorant receptor.
Q8NHA4
A1JJS4
CYSH_YERE8
PAdoPS reductase
Yersinia
MSQFNLNELNALPKAEQAAALALVNGQLEHLTAQERVSWALENLPGEFVLSSSFGIQAAVCLHLVTRQQPDIPVILTDTGYLFPETYQFIDSLTEKLQLNLQVFRAQQSPAWQEARYGKLWEQGVEGIERYNDLNKVEPMNRALETLGAQTWFAGLRREQSGSRAKLPVLAIARGVFKLLPIIDWDNRQVYQYLTQHGLSYHPLWEQGYLSVGDTHTTRKWEPGMSEEETRFFGLKRECGLHES
Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.
A1JJS4
A1AV35
NADD_PELPD
Nicotinate mononucleotide adenylyltransferase
Pelobacter
MKIGLMGGTFNPIHMAHLRIAEEARELCGLDRVLFIPVADPPHKPLAGEVPFHQRCQMVRLAIAGNRAFELSEIEGQRPGKSYSIDTIGTFREQHPQAELYFIIGSDSFLELGLWRRYADILRSCNLIVVERPGRQVNDPLSALPVDIRGELRYTPASRSLEHVGGTRVHFFAGCLLDISSSEIRRLAATGRSITYLVPPQVEAYIKEQRIYSECP
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
A1AV35
A4IM90
CODY_GEOTN
GTP-sensing transcriptional pleiotropic repressor CodY
Geobacillus
MNLLEKTRKINAMLQKAAGRPVNFKEMAETLCDVIEANVFVVSRRGKLLGFAIKQSIENERMKRMLEERQFPEEYTRNLFNITETSPNIDINSEYTAFPVENRDLFKTGLTTIVPINGGGERLGTLILSRLDREFDNDDLILAEYGATVVGMEILREKAEEIEEEARSKAVVQMAISSLSYSELEAIEHIFEELDGTEGLLVASKIADRVGITRSVIVNALRKLESAGVIESRSLGMKGTYIKVLNDKFLTELEKLKSN
DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor.
A4IM90
Q39219
AOX1A_ARATH
Alternative oxidase 1a
Arabidopsis
MMITRGGAKAAKSLLVAAGPRLFSTVRTVSSHEALSASHILKPGVTSAWIWTRAPTIGGMRFASTITLGEKTPMKEEDANQKKTENESTGGDAAGGNNKGDKGIASYWGVEPNKITKEDGSEWKWNCFRPWETYKADITIDLKKHHVPTTFLDRIAYWTVKSLRWPTDLFFQRRYGCRAMMLETVAAVPGMVGGMLLHCKSLRRFEQSGGWIKALLEEAENERMHLMTFMEVAKPKWYERALVITVQGVFFNAYFLGYLISPKFAHRMVGYLEEEAIHSYTEFLKELDKGNIENVPAPAIAIDYWRLPADATLRDVVMVVRADEAHHRDVNHFASDIHYQGRELKEAPAPIGYH
Catalyzes the cyanide-resistant oxidation of ubiquinol and the reduction of molecular oxygen to water, but does not translocate protons and consequently is not linked to oxidative phosphorylation. Increases respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures.
Q39219
B0JSC7
ANMK_MICAN
AnhMurNAc kinase
Microcystis
MLVIGLMSGTSVDGIDTALVEISGTVESPQVQLLAGETYPYSPRLRETILQVCGGEKLSIEALASLDDNIAAEFAQAALNIQKEAPKAQLIGSHGQTVFHRPPANDRLGYTVQLGRGAAIAKITRIPTISNFRAADIAQAGHGAPLVPKIDAYLLSHPTKTRCVQNIGGIGNLTYLPPRQRENWQQKIFGWDTGPGNVLIDLAVQFLSQGQQTYDHNGQWSAQGQPCSELVHKWLQEPYFQQYPPKSTGRELFSPAYLAQLREDAQAYCLSDADWLASLTDLTAISIAHSYQTFLPEMPAEVLLCGGGARNAYLRQRLLAHLGSNVKLLTTDEVGLNSDFKEAIAFALLAYWRWHNFPGNLPQVTGAKAAVLLGEIYR
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
B0JSC7
Q6CIK2
HOT13_KLULA
Helper of Tim protein 13
Kluyveromyces
MEKAQIYGKLVDKESRCEHWHGPLDVIALRFKCCNGYYACYECHQELVPHVTERYNINDETVPLVICGVCKLEMSFAAYSDSLQCPNCRSQFNPGCKLHYDMYFMKDDEPENLR
Required for the assembly or recycling of the small Tim proteins in the mitochondrial intermembrane, thereby participating in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane.
Q6CIK2
P34715
EF1G_TRYCR
eEF-1B gamma
Schizotrypanum
MSLTLWSGVNPENARTHKLLAAAALANVAVTLKACEYGRENETAEYCRNCSPCGRYPVLQTEEGCVFESNAILRHIARLDRSGGFLYGRTPLEGSQVDMWLDFSATELDAASEPFVHHAFRGEPLPANAMDRVHEVLRALEAWLETRTFLVGERMTVADVAVAFALQWHYRLNGAEGEALTKKYRNAYRMYNTVMQQPKTVEVLRSQGATFGAREGGAKGQGRGCARPGREEAERAAAAADGAEEEDEAPREKKKPNPLDELPPSPFVLDAFKREYSNTDTRTVAAPYFFQHYDAAGYTTFWCRYKYNEDNKMQFMTANLIRGWFQRMEHVRKYAFGVALIIGEERRHDIVALWVFRGRGMPAIVEDVEDTELFDWEEVADVAAQRERITDYLSWEGPTIPRPVLEGRVFK
Probably plays a role in anchoring the complex to other cellular components.
P34715
Q1EG28
OSTC1_SOLSE
Gamma-carboxyglutamic acid-containing protein
Solea
MKTLSVLVLCSLAVLCLTSDASFSSQPAVDTPAQEGLFVEQEQASSVVRQAPKELSLSQLESLREVCELNLACEDMMDTSGIIAAYTTYYGPIPF
Binds strongly to apatite and calcium.
Q1EG28
B2XTG4
PSAJ_HETA2
PSI-J
Heterosigma
MDNFKKYLSTAPVLLTVWLSITASGIMIINRLYPDPLIFPI
May help in the organization of the PsaE and PsaF subunits.
B2XTG4
B7V202
HISZ_PSEA8
ATP phosphoribosyltransferase regulatory subunit
Pseudomonas
MATVDRWLLPDGIEEVLPPEAARIEAARRQVLDLFHRWGYEFVVTPHIEYLESLLTGAGQDLDLRTFKVTDPASGRLMGFRADITPQVARMDAHSLRREGPSRLCYAGSVLHAQPRALSTSRSPIQLGAELYGDPSPASDVEVISLMLEMLEMAEVPDVHMDLGHVGIYRGLARAAGLSGEVEQQLFDALQRKAVDEVEALTADLPAELRGMLRALAELCGGRDALEQGRARLAAAPADVQVALNELIEIADSLAGRFPGLPLYFDLGELRGYHYHTGVVFAAFVPGVGQSIAQGGRYDDIGADFGRARPATGFSTDLKSLVTLGQARLDQAVSGIWAPAEGAGLWQAVQRLRRDGQRVVQALPGQDAASAREAGCDRQLALRDGNWQVAPLAS
Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
B7V202
A9NEF4
KAD_ACHLI
Adenylate monophosphate kinase
Acholeplasma
MKTRMIFVGPPGAGKGSQAKIISQTLNIPHISTGDMFRTHIKGSTPLGLEAKKYTDQGLLVPDDVTNQMVKDRLSQKDVEKGFIFDGYPRTPDQAIFLDNLLMVTNQKLDVVLNISSSDEVIVKRITGRRTCPVCGAIYHVDNYPPKVAGICDNDGATLVQRKDDQKETIIRRLSVYKEETFPLIKYYAHKNLLMDVDGNQPLEVITKHVLEILEQK
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
A9NEF4
A4Y398
CH60_SHEPC
Chaperonin-60
Shewanella
MAAKEVVFGNDARVKMLAGVNILANAVKVTLGPKGRNVVLDKSFGSPLITKDGVSVAKEIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIVTEGLKAVAAGMNPMDLKRGIDKAVIAAVAELKALSQPCADSKAIAQVATISANSDESIGEIIATAMEKVGKEGVITVEEGQALENELDVVEGMQFDRGYLSPYFINKPETGSVELDHPFVLLVDKKISNIRELLPILEGLAKTGKPLLIVAEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDVAILTGGTVIAEEIGLELEKATLEDLGTAKRVVITKDNTTIIDGNGEQAQIEARVSQIKQQIEESTSDYDKEKLQERMAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVPGGGVALVRVASKIAELEVLNEDQKHGVVIALRAMEAPLRQIATNAGEEASVVANTVKNGSGNFGYNAGNDTYGDMLEMGILDPTKVTRCALQFAASIAGLMITTEAMVAEIPQNSAPDMGGMGGMGGMGGMM
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
A4Y398
C1DIY3
TSAD_AZOVD
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
Azotobacter
MLVLGLETSCDETGVALYDSRRGLLADALFSQIDLHRIYGGVVPELASRDHVKRMLPLLRQVLDESGCRTGDIDGIAYTAGPGLVGALLVGASCAQALALAWGVPALGVHHMEGHLLAPMLEEQPPQFPFVALLVSGGHTQLVRVDGIGRYQVLGESLDDAAGEAFDKTAKLLGLGYPGGPEIARLAQDGRPGRFVFPRPMTDRPGLEFSFSGLKTFALNTWQHCRASGDDGEQSRRDIALAFQQAVVETLIIKCRRALKQTGLKRLVIAGGVSANQALRSALERMLGELDGQVFYARPRFCTDNGAMIAYAGCQRLLAGQRDGPAIQVHARWPMETLPAL
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
C1DIY3
B1XKB3
COXX_SYNP2
Heme O synthase
unclassified Synechococcus
MLGTSLSPHHENFWAVIKSYYQLTKPRIIPLLLITTAASMWIASHGHIDPVKLLITLLGGTLAAASAQTLNCIYDQDIDFSMQRTRKRPIPSGRVQPRHALIFALILGSLSFSLLMVFVNLLSACLALSGIVFYMLVYTHWLKRHHVQNIVIGGAAGSIPPLVGWAAVTGQLDWSAWILFALIFLWTPPHFWALALMIKEDYAEVEVPMLPVVKGEKITVDQIWIYTLIVVPFSLLLVFPFQASGLFYAIAALVLGAIFIQKAWELKQNPFDQSLAKSMFKYSILYMMLLCTAMVVDSLPAVHDVTALVTTTLASLT
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
B1XKB3
Q6V595
KLHL6_MOUSE
Kelch-like protein 6
Mus
MAGQRGACTMSDVVERSLEGPLALTTDKSSQKRGDLVEILTGEKVKFDDTRLSLILQNGLETLREENALTDVILCVDVQEFSCHRVVLAAASNYFRAMFCNDLKEKYEKRIIIKGVDAETMHTLLVYTYTSKALITKQNVQRVLEAANLFQFLQLVDACASFLTEALNPENCIGILRLADTHSLDSLKMQVQSYIIQNFVQILNSEEFLELPVDTLYHILRSDDLCVTEEAQVFETVMSWVRHKQSERLCLLPCVLENVRLPLLDPWYFVEMVEADPLIRQCPEVFPLLQEARMYHLSGNEIISERTKPRMHEFQSEVFMIIGGCTKDERFVAEVTCLDPLRRSRLEVAKLPLTEHELESENKKWVEFACVTLKNEVYISGGKETQHDVWKYNSSINKWIQIEYLNIGRWRHKMVVLGGKVYVLGGFDGLQRINNVETYDPFHNCWSEAAPLHVHVSSFAATSHKKKLYVIGGGPNGKLATDKTQCYDPSTNKWVLKSAMPVEAKCINAVSFQDHIYVVGGAMRALYAYSPLEDSWCLVTQLSHERASCGIAPCNNKLYITGGRDEKNEVIATVLCWDPEAQKLTEECVLPRGVSHHGSVTIRKSYTHIRRVVPGAVSV
Involved in B-lymphocyte antigen receptor signaling and germinal center formation.
Q6V595
C4L931
PAND_TOLAT
Aspartate 1-decarboxylase alpha chain
Tolumonas
MQRIMLRGKLHQARVTHAVLNYEGSCGIDQDFLDAAGIVEYEAIDIYNIENGERFSTYAISGERGSRMISLNGAAARKAAVGDRIIICAYGPMTEDEVAQHKPRLVYLDAQNNIVRTSKDIPLQLA
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
C4L931
Q3AUQ6
PSBH_SYNS9
Photosystem II reaction center protein H
unclassified Synechococcus
MAQRTRLGDLLRPLNSEYGKVVPGWGTTPVMGIFMVLFLVFLLVILQLYNKSLILEGINVNWNGLG
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. 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.
Q3AUQ6
Q8N6W0
CELF5_HUMAN
RNA-binding protein BRUNOL-5
Homo
MARLTESEARRQQQQLLQPRPSPVGSSGPEPPGGQPDGMKDLDAIKLFVGQIPRHLDEKDLKPLFEQFGRIYELTVLKDPYTGMHKGCAFLTYCARDSAIKAQTALHEQKTLPGMARPIQVKPADSESRGGRDRKLFVGMLNKQQSEEDVLRLFQPFGVIDECTVLRGPDGSSKGCAFVKFSSHTEAQAAIHALHGSQTMPGASSSLVVKFADTDKERTLRRMQQMVGQLGILTPSLTLPFSPYSAYAQALMQQQTTVLSTSGSYLSPGVAFSPCHIQQIGAVSLNGLPATPIAPASGLHSPPLLGTTAVPGLVAPITNGFAGVVPFPGGHPALETVYANGLVPYPAQSPTVAETLHPAFSGVQQYTAMYPTAAITPIAHSVPQPPPLLQQQQREGPEGCNLFIYHLPQEFGDTELTQMFLPFGNIISSKVFMDRATNQSKCFGFVSFDNPASAQAAIQAMNGFQIGMKRLKVQLKRPKDPGHPY
RNA-binding protein implicated in the regulation of pre-mRNA alternative splicing. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA.
Q8N6W0
Q1XDK3
PSAB_NEOYE
PsaB
Neopyropia
MATKFPKFSQALSQDPTTRRIWYGIATAHDFESHDGMTEENLYQKIFASHFGHLAIIFLWTSGNLFHVAWQGNFEQWVLNPLKVKPIAHAIWDPHFGQPALKAFSKGGSAYPVNIAYSGVYHWWYTIGMRSNQDLYSGALFLLVLSALLLFGGWLHLQPKFKPGLSWFKNNEPRLNHHLSGLFGVSSLARTGHLVHVAIPEARGQHVGWDNFTTVLPHPAGLQPFFSGNWSVYAQNPDTAQHLFGTNEGAGTAILTFLGGFHPQSQSLWLTDMAHHHLAIAVVFIVAGHMYRTNWGIGHNLKDILDAHRPPSGRLGAGHKGLFDTITNSLHIQLGLALASLGVITSLVAQHMYAMPPYAFMAKDFTTQASLYTHHQYIAGFLMVGAFAHGAIFFVRDYDPEQNKDNVLARMLEHKEAIISHLSWVTLFLGFHTLGLYVHNDTMIAFGTPEKQILIEPVFAQWIQASSGKALYGFDVLLSSSTNIATQAGSNIWLPGWLEAINSGKNSLFLTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAWDAFYLAVFWMLNTIGWVTFYWHWKHITIWQGNATQFNESSTYLMGWFRDYLWLNSSPLINGYNPYGMNNLSVWSWMFLFGHLVWATGFMFLISWRGYWQELIETLAWAHERTPLANLIRWKDKPVALSIVQARLVGLAHFSVGYVLTYAAFVLASTAGKFG
PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6.
Q1XDK3
B4SUA7
PANC_SALNS
Pantoate-activating enzyme
Salmonella
MLIIETLPLLRQHIRRLRQEGKRVALVPTMGNLHDGHMKLVDEAKARADVVIVSIFVNPMQFDRPDDLVRYPRTLQEDCEKLNKRKVDYVFAPAVEEIYPHGLEGQTYVDVPGLSTMLEGASRPGHFRGVSTIVSKLFNLIQPDIACFGEKDFQQLALIRKMVADMSYDIEIVGVPIIRAKDGLALSSRNAYLTAEQRKIAPGLYNVMNRIAEKLIAGNRELQEIIAIAEQELNEKGFRADDIQIRDADTLLELTETSKRAVILAAAWLGQARLIDNQSVTLAQ
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
B4SUA7
P53971
FAP1_YEAST
FKBP12-associated protein 1
Saccharomyces
MTEHESLGLEQNQDGGDTYRHHNLSDGCISSVEDANEQPSSYEEESDDDMQYYERAIQEISSGDSYVCMICTVEMDYTCQMFACKRCYRVFDYGCIREWALKSTEKTVDRIWKCPNCYYVSKRVPVKNRPTCWCGKVVNPDPNPLDPNSCGQTCNASTCMHGCSKICHLGPHPECTRMVEIMCHCGKHSKSIFCYQSKVMKKNFNCQEVCGLPLSCSIHTCKKKCHPGLCGPCPEMIISKDSPKKQIKCYCGNHTRANIKCSETKFPKSGKSSKDENGNRWIGVFACADNRVVDYSCRKHSFIESCISPPTINGEKACPFLPSSLKTCPCGRTALEELTKPRKHCDDPIPTCDSRCGKPLKCGKHSCPFTCHDKACMEPCLQIDSVKCACEQSTFSVPCGFQGRPRCNIKCESLMSCRRHRCTDRCCSGRPSAIRRKKNLFRTQDLLDESLVEAKHICLKPCNLTLSCGIHKCQRKCHPGKCPPCLESDSNDLVCPCGNTVVPAPVRCGTKLPTCNHPCIKVVRGESTCGHKPMPHTCHSLDVSCPPCTETVFKPCKCGKKTKVRTVCFQTDVSCGIKCGIPLSYCYHTCQKTCHLPGNCQKVCKQTCGQKRLNCNHECPKPCHGKTECPDLPCATLVKIYCKCGRIKKSVTCGAKSDRVSVTESSVLDCNEECEALKRLKELKEAFGIKEETNNFTSNELDALKKLVSVATTFEELQLPFTEAALSVYSKQERWCSQIEAILNKLMDDKTRSSLHFKPMRPPQRHFIRELAKAYGLYSESQDREPMRSVFIKKEDNGASNKPVLSLAEAYPLYESFKQLQKERKAQEFQARTTAKLINFEVQDTEPKVEVAKKNGFLVQNLVAGNTAEDLRRFFEPHLKHTLVVNPQYLILDDGKTALVYPENYETASVNTERDMELLVGHFDFMAKEAFLADSISLCSTEEELERRLDTPVIQEDSPVMDNNT
May play a role in transcription regulation.
P53971
A0RR29
ATPD_CAMFF
F-type ATPase subunit delta
Campylobacter
MKEVVAKKYVKALILSLSSDEFDKLGNELKDISNAFLLPKLKVIIDSPDISSKQKADFLFSLLDNASNKIHNFLLLLAERKRLGLIPEISKEFEYQQAVRDCKFSGLISGNFELSAAQKTELEERFSKKFGAKIEFENIKNNYNGIKIELDDLGVEVSFSIDRLKAQMSEYILKAI
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.
A0RR29
P54036
RS17_METJA
30S ribosomal protein S17
Methanocaldococcus
MAARNIGIQVKAPEVECDDKNCPFHGNLPVRGQSFVGVVVSDKPHKTVIIKREVVKYIKKYERYERRTTKLAAHNPPCIHARVGDIVRVMECRPISKTKAFVVVEKLGRIDEVKGEE
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
P54036
Q9USY4
ABP2_SCHPO
ARS-binding protein 2
Schizosaccharomyces
MNFYSLLPSRHDVSADNITEKFCQFCLCCNPWYAGADTRQLANAFNMIPKSEGQKFEIWVLFLLVRQYHQKIINSWSKLVGFLGVERKDEQSTQKIQQYVVRLKRWMSQTHVDAFFDYLLNKPNPYYLEIPETQPQVRCNVNVTDDLVIKSLRAGLMSHPDVNSSSISTMRTSTSPSNWIHSASASLDDNTHNLGSFVTNPHADSQECPTPQSLLMRASHHMSERGSQQAHQTTPQNHSLPHPPNMFEPPDEDHQLPSAANNSHNHDHAFQTAEAVGVADSIDPDWHQWPDDLRDVSSPKESDGLNDSWSRQTNQVETENVENEAGVPRKRGRPPGARNKIKRLRSEPSVSLTLSISWYERFEKLMHAQNTMLRSAFSHVARLPMETVSQLLSHYTETISQYLPPSETSPIPKTPNFKFISSTLLALVSSHSEILEASTDRLIWTVHQGPLTATICHAFNLEKAPSMHSLAEAQMIPDVPISHSNSMEPLDTVSSLKLEIAKLNAALKEKNLELENLKRKIMNAVFD
Binds, preferentially, to the Maundrell ARS consensus sequence within ARS3002.
Q9USY4
B8DFG9
GATB_LISMH
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Listeria
MNFETVIGLEVHVELKTNSKIFSSAPAHFGAEPNTNTTVVDLGMPGVLPVLNKRAVEFGMKAAMAINCEIAEHTKFDRKNYFYPDNPKAYQISQFDKPIGEHGWIEIEVGGKKKKIGITRLHLEEDAGKNTHTSHGYSLVDINRQGTPLIEIVSEPDIRSAEEAYAYLEKLKSIIQYTGVSDVKMEEGSMRCDANISIRPIGQEEFGVKTELKNLNSFNNVRKGIEYEEKRQAEVLKSGGIIEQETRRFEEATGKTSLMRIKEGSDDYRYFPEPDLVDLFIDDAWKERIRAEIPELPDKRQIRYINDLGLPAYDAMVLTLTKEMSDFFEATLAAGADAKQASNWLMGEVSAYLNAEQKELHETGLTPENLAGMIKLIEAGTISSKIAKKVFRELAQNGGDAEQLVKDKGLVQISDEGALRTIISEILDNNEQSIVDFKNGKDRAVGFLVGQVMKATKGQANPPMVNKLLLEEMNKR
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).
B8DFG9
B2VBM9
RLMH_ERWT9
rRNA (pseudouridine-N3-)-methyltransferase RlmH
Erwinia
MKLQLVAVGTKMPDWVQTGFMEYLRRFPKDMPFELTEVPAGKRGKNADIKRILEKEGEMMLAATGKGNRIVTLDIPGQPWETPQLASQLERWKQDGRDVSLLIGGPEGLSPACKAAAEQSWSLSALTLPHPLVRVLVAESLYRAWSITANHPYHRE
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
B2VBM9
Q46J57
ATPA_PROMT
F-ATPase subunit alpha
Prochlorococcus
MVSIRPDEISSILKQQIADYDKSVSVSNVGTVLQIGDGIARVYGLEKVMAGELVEFEDGTEGIALNLEDDNVGVVLMGEALGVQEGSTVKATGKIASVPVGEAMLGRVVNPLGQQIDGKGEMATTDSRLIESIAPGIIKRKSVHEPMQTGITSIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGQDVICVYVAVGQKQASVANVVEVLKEKGALDYTIIVNAGASEAAALQYLAPYTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDAMGAGSMTSLPIIETQAGDVSAYIPTNVISITDGQIFLSSDLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDELAAFSQFASDLDEATQKQLGRGKRLRELLKQPQFDPLNLAEQVAIVYAGVKGLIDEVPEEEVVKFARELRDYLKTNKAEFLKNVLSEKVLSEASESMLKDAISEVKSSMLAA
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Q46J57
P14829
GYRA_KLEOX
DNA gyrase subunit A
Klebsiella
MSDLAREITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLYAMNVLGNDWNKAYKKSARVVGDVIGKYHPHGDTAVYDTIVRMAQPFSLRYMLVDGQGNFGSVDGDSAAAMRYTEIRMSKIAHELMADLEKETVDFVDNYDGTEKIPDVMPTKIPNLLVNGSFGIAVGMATNIPPHNLTEVINGRLAYVEDEEISIEGLMEHIPGPDFPTAAIINGRRGIEEAYRTGRGKVYICARAEVEADAKTGRETIIVHEIPYQVNKARLIEKIAELVKEKRVEGISALRDESDKDGMRIVIEVKRDAVGRVVLNNLYSQTQLQVSFGINMVALHHGQPKIMNLKEIIAAFVRHRREVVTRRTILALRKARDRADILEALSIALANIDPIIELIRRAPTPAEAKAGLIARSWDLGNVSAMLEAGDDAARPEWLEPEFGVRDGQYYLTEQQAQAILDLRLQKLTGLEHEKLLDEYKELLEQIAELLHILGSADRLMEVIREELELVREQFGDARRTDITANSVDINIEDLITQEDVVVTLSHEGYVKYQPVNDYEAQRRGGKGKSAPRIKEEDFIDRLLVANTHDTILCFSSRGRLYWMKVYQVPEASRGARGRPIVNLLPLEANERYTAILPVREYEEGVNVFMATASGTVKKTPADEFSRPRSAGIIAVNLNEGDELIGVDLTSGQDEVMLFSAAGKVVRFKEDDVRAMGRTATGVRGIKLAGEDKVVSLIVPRGEGRILTATENGYRKRTAVAEYPTKSRATQGVISIKVTERNGSVVGAVQVDDCDQIMMITDAGTLVRIRVSEVSIVGRNTQGVILIRTAEDENVVALQRVAEPVDDEELDAIDGSAAEGDEDIAPEADTDDDIAEDEE
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
P14829
E9ET41
ARP1_METRA
Scytalone dehydratase-like protein Arp1
Metarhizium
MNQSLTPSAGTDSKTGSSKAISFQDYLDLSTLDWARLRAILAPALYVDYTKIGKEKWDAMSADDFMAMVSNDDFLGDPCVKTQHLIGATYWERVSESKVIGHHQLRAAHQVYTSPDLKTVKLRGHSHATNEHYYVKSSGVWKFAGLKPEVRWNEYKFEEVFKGSYTQSEKHS
Scytalone dehydratase-like protein; part of the Pks2 gene cluster that mediates the formation of infectious structures (appressoria), enabling these fungi to kill insects faster . The product of the Pks2 gene cluster is different from the one of Pks1 and has still not been identified .
E9ET41
Q887L5
GCSP_PSESM
Glycine dehydrogenase (aminomethyl-transferring)
Pseudomonas
MTDRIELTTANEFIARHIGPRAADELAMLHTLGFDSIEALSDSVIPESIKGTSVLNLPAGQSEADALASIKAIASKNQLFKTYIGQGYYNTHTPAPILRNLLENPAWYTAYTPYQPEISQGRLESLLNFQTLISDLTGLPIANASLLDEATAAAEAMTFCKRLSKNKGSQQFFASSHCHPQTLDVLRTRAEPLGITVVVADETELGDVSDYFGALLQYPASNGDVFDYRELAERFHGANALVAVAADLLALTLLTPPGEFGADVAIGSAQRFGVPLGFGGPHAAYFSTRDAFKRDMPGRLVGVSVDRHGKQALRLAMQTREQHIRREKATSNICTAQVLLANIASMYAVYHGPRGLTQIANRVHHLTAILAEGLSQLGLNAEQAYFFDSLTLHTGGRTAALHAAARARHINLREIDDQRLGLSLDETTSQSAVEVLWDIFASTGQTLPDFTALAASVKSRLPAALLRQSAILSHPVFNRYHSETELMRYLRKLADKDLALDRTMIPLGSCTMKLNAASEMIPVTWAEFGNLHPFAPAEQSAGYQQLTDELEAMLCAATGYDAISLQPNAGSQGEYAGLLAIRAYHQSRGDEHRDICLIPSSAHGTNPATANMAGMRVVVTACDARGNVDIEDLRAKALQHREQLAAIMITYPSTHGVFEEGIREICGIVHDNGGQVYIDGANMNAMVGLCAPGKFGGDVSHLNLHKTFCIPHGGGGPGVGPIGVKSHLAPFMPGHARMQRKEGAVCAAPFGSASILPITWMYIRMMGGEGLKRASQLAILNANYISRRLEEHYPVLYTGTNGLVAHECILDLRPIKDSSGISVDDVAKRLIDFGFHAPTMSFPVAGTLMIEPTESESREELDRFCDAMIKIREEIRAVEDGTLDKDDNPLKNAPHTAAEIVGQWSHPYSREQAVYPVDSLIENKYWPPVGRVDNVFGDRNLVCACPSIESYQEA
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.
Q887L5
B1HU20
PANC_LYSSC
Pantoate-activating enzyme
Lysinibacillus
MKVMTTIQALTAEIQAAKQAHKTIGLVPTMGYLHEGHLTLAQTARAENDLVVMSIFVNPTQFGPNEDFESYPRDLPRDIALAESVGVDLVFAPSVEEMYPQDGGIRIHAGEQATILCGASRPGHFDGVLQVVAKLFHLTLPTRAYFGQKDAQQVAIITTMVRDFNFPLDMRVVPIVREEDGLAKSSRNIYLSESEREEAPAIHEALQLARDSFLATGDVREALAKAKAHIQIQTHGRIDYIELLAYPDLTPVTETTQQVLLAAAVYIGKTRLIDNSIFTVKEGL
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
B1HU20
A4QKJ6
NDHK_CAPBU
NADH-plastoquinone oxidoreductase subunit K
Capsella
MNSIKFPVLDRTTKNSVISTTLNDLSNWTRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDAITKLRKKIAREIYKDRIRPQQGNRCFTTNHKFFIVRSPHTGNYDQELLYPPSSTSEISTETFFKYKSPVSSHELVN
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.
A4QKJ6
P50377
EFTU_GRALE
Elongation factor Tu, chloroplastic
Gracilariopsis
KNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPNIVVFLNKQDQVDDEELLELVELEVRELLGQYGFPGDNIPFVAGSALRALENITQNNTIQRGENEWVDKIHSLMDAVDEYIPTPVRDVEKTFLMAVEDVFSITGRGTVTTGRIERGIIKVGDTIEIVGLRETTTTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYVLTK
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
P50377
A0L669
SYE_MAGMM
Glutamyl-tRNA synthetase
Magnetococcus
MRTRFAPSPTGFLHVGGARTALFCHLQARHVGGTTVLRIEDTDRERSNQALVDAILDGLHWLGLDPDEGPLFQSDHTQRHTDMALKLLEEGKAYKCYCTKQELDDMRAAQQARKEKPRYDGRCRHRSEPPSDQPYVIRFKTPLEGEVVWPDMVQGTIHIANKELDDLILLRSDGSPTYNLAVVVDDHDMEITHVIRGEDHTSNTPRQIHLFQALGWDVPSYAHIPLLHGEDGSKLSKRHGAVSVLQFREEGFLASALNNYLVRMGWSHGEKEEFTMDEMVALFDVNNVGRSAAIFNTSKLLWLNGVHIRQSGPEQLRGELMWHLQRLGVDNPNPNFIDQIIPGMQERVKTMLEMAQMAMFYFKAPTEYAETAVAKHLHADILPAYAALLEKLHTVTADEWDNGGLERAFKVVMAETGAKMGKIGQPVRIAISGSDIAPGIYDILQLVGRHESLRRLEVLLSFFQQRVHGANG
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
A0L669
Q9RRT8
SURE_DEIRA
Nucleoside 5'-monophosphate phosphohydrolase
Deinococcus
MTVPDPARPAASPSARPRVLVANDDGIFAPGIKALGLALSEWADVVVVAPDVEQSAVGHGITIRRPLRFKHTAAAGFGDIPAYRVDGTPADCVVLGVHLLGRPDLVVSGINIGPNLGEDLTHSGTVAAAIEGLTLGLPSIAFSQFANEAGEYDFGPSAAYASRLAREVCCRGLPPRVLLNVNFPRVSPRGVRVTEVGLHRWEDSVVTRQDPEGRDYHWVAGVSTAHDGHDEQTDYGAVQAGFISVSPVRLDLTARDLIGELTQALPPL
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Q9RRT8
B2T2S5
3HAO_PARPJ
3-hydroxyanthranilic acid dioxygenase
Paraburkholderia
MLTYGKPFNFQRWIDDHAHLLKPPVGNQQVWQDSDFIVTVVGGPNHRTDYHDDPLEEFFYQLRGNAYLHLWIDGKRERVDLKEGDVFLLPPHVRHSPQRPEAGSVCLVIERQRPAGVVDGFEWYCDACGHLVYRVEVQLKSIVSDLPPLFNAFYASEEKRRCGHCGHVHPGKAV
Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
B2T2S5
C6A2E8
PXPA_THESM
5-oxoprolinase (ATP-hydrolyzing) subunit A
Thermococcus
MKIDLNSDLGESFGRYKLGLDEEVMKYITSANIACGWHAGDPLIMRKTVKLAKDMNVEVGAHPGYPDLMGFGRRYMDLTKEEARNYILYQIGALYAFVKAEGLTLQHVKPHGALYNALVRDEELTIGVLEGIADFDKNIIFVGLSMSKPLEIAEEMGLKVAHEVFADRAYNPDGTLVSRRKPGAVIHNKEEIAERVISMVKDGGVKSINGEWVELRADTICVHGDNPKAVEITAYLRKRLEEEGIKIVSMRELIR
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
C6A2E8
P65725
Y187_MYCBO
Pirin-like protein Mb0187c
Mycobacterium tuberculosis complex
MTATVEIRRAADRAVTTTSWLKSRHSFSFGDHYDPDNTHHGLLLVNNDDQMEPASGFDPHPHRDMEIVTWVLRGALRHQDSAGNSGVIYPGLAQRMSAGTGILHSEMNDSATEPVHFVQMWVIPDATGITASYQQQEIDDELLRAGLVTIASGIPGQDAALTLHNSSASLHGARLRPGATVSLPCAPFLHLFVAYGRLTLEGGGELADGDAVRFTDADARGLTANEPSEVLIWEMHAKLGDSAT
Putative quercetin 2,3-dioxygenase.
P65725
Q8BMK4
CKAP4_MOUSE
63-kDa cytoskeleton-linking membrane protein
Mus
MPSAKQRGSKGGHGAASPSDKGAHPSGGADDVAKKPPAAPQQPQPPAPHPPQHPQNQAHRGGHRGRSSAATANASSASCSRRLGRVLNFLFYLSLVAAAAFSGWYVHHVLEEVQQVRRGHQDFSRQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEILKDLSDGIHVVKDARERDFTSLENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVGAHGSEEGAVFKDSKALEELQRQIEGLGARLQYVEDGVYSMQVASARHTESLESLLSKSQEYEQRLAMLQEHVGNLGSSSDLASTVRSLGETQLALSSDLKELKQSLGELPGTVESLQEQVLSLLSQDQAQAEGLPPQDFLDRLSSLDNLKSSVSQVESDLKMLRTAVDSLVAYSVKIETNENNLESAKGLLDDLRNDLDRLFLKVEKIHEKI
Mediates the anchoring of the endoplasmic reticulum to microtubules.
Q8BMK4
P43273
TGA2_ARATH
bZIP transcription factor 20
Arabidopsis
MADTSPRTDVSTDDDTDHPDLGSEGALVNTAASDSSDRSKGKMDQKTLRRLAQNREAARKSRLRKKAYVQQLENSRLKLTQLEQELQRARQQGVFISGTGDQAHSTGGNGALAFDAEHSRWLEEKNKQMNELRSALNAHAGDSELRIIVDGVMAHYEELFRIKSNAAKNDVFHLLSGMWKTPAERCFLWLGGFRSSELLKLLANQLEPMTERQLMGINNLQQTSQQAEDALSQGMESLQQSLADTLSSGTLGSSSSGNVASYMGQMAMAMGKLGTLEGFIRQADNLRLQTLQQMIRVLTTRQSARALLAIHDYFSRLRALSSLWLARPRE
Transcriptional activator that binds specifically to the DNA sequence 5'-TGACG-3'. Recognizes ocs elements like the as-1 motif of the cauliflower mosaic virus 35S promoter. Binding to the as-1-like cis elements mediate auxin- and salicylic acid-inducible transcription. Required to induce the systemic acquired resistance (SAR) via the regulation of pathogenesis-related genes expression. Binding to the as-1 element of PR-1 promoter is salicylic acid-inducible and mediated by NPR1. Could also bind to the C-boxes (5'-ATGACGTCAT-3') with high affinity.
P43273
P62496
ERF1_MESAU
Eukaryotic peptide chain release factor subunit 1
Mesocricetus
MADDPSAADRNVEIWKIKKLIKSLEAARGNGTSMISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTEEGKEKKVNIDFEPFKPINTSLYLCDNKFHTEALTALLSDDSKFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARLRMEKRHNYVRKVAETAVQLFISGDKVNVAGLVLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTEVLSNVKFIQEKKLIGRYFDEISQDTGKYCFGVEDTLKALEMGAVEILIVYENLDIMRYVLHCQGTEEEKILYLTPEQEKDKSHFTDKETGQEHELIESMPLLEWFANNYKKFGATLEIVTDKSQEGSQFVKGFGGIGGILRYRVDFQGMEYQGGDDEFFDLDDY
Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Required for SHFL-mediated translation termination which inhibits programmed ribosomal frameshifting (-1PRF) of mRNA from viruses and cellular genes.
P62496
A7IIE4
DER_XANP2
GTP-binding protein EngA
Xanthobacter
MTFSLAIVGRPNVGKSTLFNRLVGKKLALVDDRPGVTRDRREGDARLGDLSFRIVDTAGLEEADAASLEGRMRAQTEAAIGHADAILFMIDARIGLTPTDRAFADLVRKCGKPVILLANKSEGRGGEAGTLEAFALGLGTPLPFSAEHGEGLSDLYDAICDALPEQTRPEPEEDEDADTDFVEEEADDKPRRPIKVTVLGRPNAGKSTLINRLLGEDRLLTGPEAGITRDSISVEVTYAGAKLEVFDTAGLRKRARIEDKLEKLSAADALRAMKFAEVVVLLVDATHPFEEQDLRIADLVAREGRALVIGYNKSDLVARGGLITRLREDVDRLLPQVKGVPIVPVSGLMGHGLDKLVAAISSAHKVWNKRVATNPLNRFLQQVTDNHPPPAVSGRRIKLRYMTQPKARPPSFVLFCSRTDAVPESYIRYLVNGLRETFDLPGVPIRLTLREKGNPYAD
GTPase that plays an essential role in the late steps of ribosome biogenesis.
A7IIE4
A6MZM2
SUI1_ORYSI
Translation initiation factor 1
Oryza sativa
MSDLDIQIPTAFDPFAEANAGDSGAAAGSKDYVHVRIQQRNGRKSLTTVQGLKKEFSYNKILKDLKKEFCCNGTVVQDPELGQVIQLQGDQRKNVSNFLVQAGIVKKEHIKIHGF
Probably involved in translation.
A6MZM2
Q46AE4
GPMI2_METBF
2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2
Methanosarcina
MTQARRPLMLIIFDGWGYREAKEGNAVMTARTPNLDRLEKECPWCFLKASGEAVGLPKGMMGNSEVGHLTIGAGRIVNQDLTRINISIKNGDFFKNPVFLNAISNVKANASSLHLMGLASCGGIHSYMPHLHALLKLVQEKDLKKVYIHAFLDGRDEPPKAALGDIKKLDAFCKEHGNAKIATVSGRYYAMDRDKRWDRTKLAYDALTRGVAPYTAPNAETAVSNAYSRGETDEFVKPTIITEQVITEQVITEQAEKPVATVQDNDSVIFFNFRADRARQITWAFVKDDFDGFMREKRPEVYFVCMTQYDETLEVPIAFPPIKLENVLGEVLSKHGLIQLRIAETEKYAHVTYFLNGGEEKRYKDEDRCLIPSPKIATYDLKPEMSAYEITDEVIRRIQSGKYDVIVLNFANMDMVGHTGIFEAAVKAVEAVDKCIGRIVEVLKEKGGVALITADHGNAEEMIDLKTGEPHTAHTSNPVKCIYFGNSEIKALRNGKLCDVAPTILELLGIPKPQEMTGKSLLVKD
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Q46AE4