accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
Q5BJJ6
|
MAT2B_DANRE
|
Methionine adenosyltransferase II beta
|
Danio
|
MPGFNYGGDQDEVYTPYRRVLVTGATGLLGRAVYKEFKNNDWDALGCGYNRARPFFLKCNLLDEDAVRGVIQSFQPHVIVHCAAERRPDVVERHTEAAMNLNVHACATLAKEAGGSFLIYISTDYVFDGRNPPYGENDAPNPLNLYGKSKLEGEREILRHCPGAAVLRVPILFGEVEKVEESAVTVLFERVQEGAESCTIDHCQQRFPTYTNDVARVCRNMAERALQDQSLRGIFHYSAKEQMTKYEMTCAIADAFNLPSSHLIPMTEQPAGAGAQRPQNAQLECSRLELLGLSVESTPFKNAIRDSLWPFQHDKRWRQTVFH
|
Regulatory subunit of S-adenosylmethionine synthetase 2, an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates MAT2A catalytic activity by changing its kinetic properties, increasing its affinity for L-methionine. Can bind NADP (in vitro).
|
Q5BJJ6
|
P75919
|
CLSC_ECOLI
|
Cardiolipin synthase C
|
Escherichia
|
MPRLASAVLPLCSQHPGQCGLFPLEKSLDAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGLDDILRLLDSHPRIEVRLFNPFSFRLLRPLGYITDFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGEEPLFSDLDVMAIGPVVEDVADDFARYWYCKSVSPLQQVLDVPEGEMADRIELPASWHNDAMTHRYLRKMESSPFINHLVDGTLPLIWAKTRLLSDDPAKGEGKAKRHSLLPQRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAANDVAVVHAGYARWRKKLLRYGVELYELKPTREQSSTLHDRGITGNSGASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKRFIQSQYDAAWQLRLDRWGRINWVDRHAKKEIILKKEPATSFWKRVMVRLASILPVEWLL
|
Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) from phosphatidylglycerol (PG) and phosphatidylethanolamine (PE).
|
P75919
|
P35654
|
HRPI_ERWAM
|
Harpin secretion protein HrpI
|
Erwinia
|
MSSLFVWLNRLAISAMQRSEVVGAAIVMSIVFMMIIPLPTGLIDVLIALNICISSLLIVLAMYLPKPLAFSTFPSVLLLTTMFRLALSISTTRQILLQQDAGHIVEAFGNFVVGGNLAVGLVIFLILTVVNFLVITKGSERVAEVAARFTLDAMPGKQMSIDSDLRAGLIEAHQARQRRENLAKESQLFGAMDGAMKFVKGDAIAGLVIVFINMIGGFAIGVLQNGMEAGAAMHIYSVLTIGDGLIAQIPALLISLTAGMIITRVSADGQQVDANIGREIAEQLTSQPKAWIMSAAGMLGFALLPGMPTAVFVIISAIALGSGLFQLWRIKQQDSQQQADELHAQQLAPEDNGYQDLRRFNPTRAYLLQFSQEHLNSEAAESLIQHIRRLRNRLVYHFGFTLPSFDIEFSPALAADEFRFCVYEIPLVTATFAVEQLAVRTSSIEIHLADGESDGQIQPGQAERDEHHWCWLPPQHPLLQQEDRRCWNAQQLIMLRMEQAIHQSGAQFIGLQESKSILNWLESEQPELAQELQRIMPLSRFAAVLQRLASERIPLRSVRTIAETLIEHGQHERDSAALTDFVRIALKEHICHQYQQPNGLNVWLLTPETEELLRDSLRQAQSETFFSLAQEYGINLLNQMRSAFPPYDNHHALILVAQDLRSPLRALLKDEFHAVPVLSFAELTSNVAINVLGRLDLQQSPPELQENDPCMNYAY
|
Involved in the secretion of harpin; a proteinaceous elicitor of the hypersensitivity response in plants.
|
P35654
|
C0QT74
|
SYDND_PERMH
|
Non-discriminating aspartyl-tRNA synthetase
|
Persephonella
|
MIDKLGDFKRDYFCGELTENNIGDEVRLLGWADSVRDHGGVIFINLRDKEGIIQVVIDPSKSPKEAYEKAKKVRSEYVLAVRGRVQRRPAGTENPKLPTGTIEIAVDELRILNTCDILPFPIEDGISAHEEVRLRYRFLDIRRPEMMKKLILRHEVYQATREYLAGHGFLEVETPMLTKSTPEGARDFLVPARLEKGKFYALPQSPQLFKQILMVSGIDRYFQIVKCFRDEDLRKDRQPEFTQIDFEMSFVDEEDVITVSEGLIHYIFKKVLGIELKLPFKRMSYTEAIERYGTDKPDLRYSLELKDITDIAKDVQFKVFKDTVEKGGIVKGINVKGGSKFSRKEIDDLTEEAKKYGAKGMAWIKINEDGSLQSPIVKFFTEEQINKIKEIMEGENGDLLIFIADSYEITHRVLGFLRKHLAEKLKLIPENVWEFVWVVDFPLVEWDEEEGRLVALHHPFTSPKEEDIDRLDEAIQDKKVALSFRSRAYDLVLNGEEIGGGSIRIHSSHIQKKVFELLGISDEEAEEKFGFLINALKYGAPPHGGLAFGLDRIVALMTGSESIRDVIAFPKTQKGICPLTDAPDFVQEDQLEELGIEVNIPEETV
|
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
|
C0QT74
|
B2HQI2
|
CLPS_MYCMM
|
ATP-dependent Clp protease adapter protein ClpS
|
Mycobacterium
|
MVVASAPAKPGSVGQQESASRDATASPWVTIVWDDPVNLMTYVTYVFQKLFGYSEPHATKLMLQVHNEGRAVVSAGSREAMEVDVSKLHAAGLWATMQQDR
|
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
|
B2HQI2
|
Q8RA32
|
DPO3_CALS4
|
DNA polymerase III PolC-type
|
Caldanaerobacter
|
MVPATFLENMQIKKVRVEKKSRKLTVVVSSFSSNAQKLSEFQSFLEESFPSLKEIKIVVESPSLSTVEEVLENWEKVVLELSEEYPSSLSFLKTCDVAKEGQNRITVKAPTYAIYEMAKSSKLDFAIREFLRNRYELNLDVELIFSEEGEEIAEKIIEEDIKAIEEVIQKDEKSKKEKSRSEENRVLLGKEMKAKPISIKDVSAETDEVVIEGEIFSIDFKELKSKVLMVFDITDYTSSILVKTFLTEEKYEILKDEIDVGTFVRLRGNVIYDKYEGDLVIDLKDLELIPPKKRMDLSEEKRVELHLHTQMSTLDAVPSATEVIKRAAEWGHKAVAITDHAVVQAFPEAMEASREYGVKVIYGMEGYMVDDGIPIVTGESEASLEGEFVVFDIETTGLSNINDEIIEIGAVKIKNKKIVDTFETFVNPQIPISSFITKLTGIDESMVKDAPLIEEVLPKFLEFAKGAVLVAHNANFDVSFIKSKAKKLGLTVENTVLDTLELSRHLYQDLKNYKLDTLAEFFEVKLLHHHRAVEDAKATAEIFIKMLEKLQEIGIKSVSEINSVLMEREVDVKKLPVYHVTILVKDQKGLRNLYEIISRSNLEFFHRTPRIPKSLLVKMREGLIIGSACEQGEVFRALVSNLEEKKLEDIINFYDYLEIQPVGNNEFLIERGEVRSVEELKEINRKIYELGKKYNKLVVATGDVHFLDPWDDVYRKILMAGKGYKDADRQPPLYFRTTEEMLMEFEYLGEEAAREVVIENPNKIAEIVEDVKPIPEGTFPPVIEGAEEELRRITLEKAHEIYGDPLPPIVQERLDRELNAIINNGYAVMYVIAQKLVSKSLQDGYLVGSRGSVGSSLVATMSGITEVNPLPPHYVCPKCKHSEFVTDGSFGCGVDMPDKYCPNCGTLMKKDGFDIPFEVFMGFEGDKEPDIDLNFSGEYQPIAHRYTEELFGKGHVFRAGTIGTLADKTAYGYVKKYFEERNLTVHKSEIKRLTMGCTGIKRTTGQHPGGVMVVPKDKSIYDFTPIQRPADAEDTDVITTHFDYHSLSGKLLKLDILGHDDPTVIRMLEDLTGVNARKIPLDDKKTMSLFTSVEALGIDPEELGTPVGTLGLPEFGTKFVRQMLIETRPTTFDELVRISGLSHGTDVWLNNAQDIIREGIATLKEVIAARDDIMLYLISKGMDKKLSFKIMENVRKGKGVTQEEIEEMKKHGVPDWFIQSCQKIKYMFPKAHAVAYVIMAFRIAYFKVYYPEAFYATYFTVRADDFNLDIVLGGKESIKRAIKEIEAKGNNATPKEKNLLTVLEVALEMYLRGIKFTNVDLYRSDAEKFLITEEGLLPPLNSLEGVGIQAAKAIAQERENGKFISIEDFRNRTRVSKTVIEILKQYGCLEDLPESNQLSLF
|
Required for replicative DNA synthesis. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
|
Q8RA32
|
Q7VD03
|
PSBY_PROMA
|
Photosystem II protein Y
|
Prochlorococcus
|
MLNLLVITLPILAAIGWVTLNIQKPAREQWDRQFGDNKPF
|
Manganese-binding polypeptide with L-arginine metabolizing enzyme activity. Component of the core of photosystem II.
|
Q7VD03
|
A7I5Q8
|
RL18_METB6
|
50S ribosomal protein L18
|
Methanoregula
|
MATGPRYLVAFRRRREGRTDYYQRTKLVVADAPRMVVRRTNRHIIVQLVTAEMEGDKTLVSANSAELEKYGYTGATANTPAAYLTGLLFAAKAKKAGQDSAILDIGLNRATPGARVFAALKGAVDGGLEIPYGESILPSEDRLKGEHIAAYNEKAGDIVKNVEQVAAAIKKELV
|
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
|
A7I5Q8
|
A6KYH6
|
RL15_PHOV8
|
50S ribosomal protein L15
|
Phocaeicola
|
MNLSNLKPAEGSTKTRKRIGRGPGSGLGGTSTRGHKGAKSRSGYSKKIGFEGGQMPLQRRVPKFGFKNINRVEYKAINLETIQKLAEAKNLTKVGMNDFIEAGFISSNQLVKVLGNGSLTTKLDVEANAFSKSAVAAIEAVGGNAVKL
|
Binds to the 23S rRNA.
|
A6KYH6
|
Q9GZK3
|
OR2B2_HUMAN
|
Olfactory receptor 6-1
|
Homo
|
MNWVNKSVPQEFILLVFSDQPWLEIPPFVMFLFSYILTIFGNLTIILVSHVDFKLHTPMYFFLSNLSLLDLCYTTSTVPQMLVNICNTRKVISYGGCVAQLFIFLALGSTECLLLAVMCFDRFVAICRPLHYSIIMHQRLCFQLAAASWISGFSNSVLQSTWTLKMPLCGHKEVDHFFCEVPALLKLSCVDTTANEAELFFISVLFLLIPVTLILISYAFIVQAVLRIQSAEGQRKAFGTCGSHLIVVSLFYGTAISMYLQPPSPSSKDRGKMVSLFCGIIAPMLNPLIYTLRNKEVKEAFKRLVAKSLLNQEIRNMQMISFAKDTVLTYLTNFSASCPIFVITIENYCNLPQRKFP
|
Odorant receptor.
|
Q9GZK3
|
B1XSQ3
|
RL23_POLNS
|
50S ribosomal protein L23
|
Polynucleobacter
|
MSQVRKNDHNLMKVLLGPVISEKATMVAEKNEQVVFQVARDANKSDVKQAVELLFKVQVDSVQIVNQKGKPKRYGRFEGRRDHTKKAYVNLKPGQEISFEAEAN
|
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.
|
B1XSQ3
|
A0E2L1
|
SEY12_PARTE
|
Protein SEY1 homolog 2
|
Paramecium
|
MIKNYGDRYHLIDKKALEDKKLDKDQLVEFVRTSGISDIGKNYNIVSIIGSQSTGKSTLLNQLFGTKFDVQNRQQSVGQTTVGIWLSKDVQNNVVVLDVEGSDSVERKSGENMVENQTALMALAMSHCFIINVFLNALGQHTSCQLSIIKIIMQQNLKLFQQDTVKHIIFVVRDWDEDANYEEASRRLNGYLLNIWNEIPKPDHYKETDFHQLFSVQVVTLVYYKMKKEFIEQTNDLHAKLSNQQDPNFIFKDFDYEKNVRWSDMPQYLSNIWEVISNNKDLNLPNEKILISNMRCQQIKLEALDGVKQLNEDLQNRVRTKLVDNFAQECQTIMNLAFKLYDKDARDYHIEVYKEKEKELKDELVNRFYTYFQKQTEQLKQHYMNTLTENLETLKRESIYNLPDKLNELDLFKLQFEEQLAKSVIQKGLWQEEDHIRYFRQQFDNQLKAFVEAQLATFKQQLDNIIKSECDKIVSSQVLNISSKFWQQIESDYYAMISEKYQKYEVLLTGLRVQQKQIEDYLNKFEEDSFHNLKQVIAVASGRFKDQLFQQFKAQFVRAPDGQPRNWQKLTEEEIFHCYTDARDKVFQLLDSLRIRKIKFIRQQVVLKKKAQTLIISSSQKVQYQISSDADSDDVVLNDVFYTQVKMQLAEDIDVQYQDAIQKHKQDFLQNIPKPFWFLLLFFMYDDVLRWMGNPLFLYPILIILCFVGFCIAIGLHSLPKLAFQWVFRTLNQAVIPIIFGGISKLKGS
|
Probable GTP-binding protein that may be involved in cell development.
|
A0E2L1
|
P19382
|
SNAI1_XENLA
|
Protein snail homolog Sna
|
Xenopus
|
MPRSFLVKKHFSASKKPNYSELESQTVYISPFIYDKFPVIPQPEILSTGAYYTPLVWDTGLLTTFFTSESDYKKSPISPSSSDDSSKPLDLTSFSSEDEGGKTSDPPSPASSATEAEKFQCNLCSKSYSTFAGLSKHKQLHCDSQTRKSFSCKYCEKEYVSLGALKMHIRSHTLPCVCKICGKAFSRPWLLQGHIRTHTGEKPFSCTHCNRAFADRSNLRAHLQTHSDVKKYQCKSCSRTFSRMSLLHKHEETGCTVAH
|
Transcriptional repressor. Acts upstream of snai2/slug, zic5 and other neural crest markers in the specification of the neural crest and neural crest migration. Involved in embryonic mesoderm formation.
|
P19382
|
Q8ECU9
|
TRPA_SHEON
|
Tryptophan synthase alpha chain
|
Shewanella
|
MNSISNQTIPHQASRYQAAFSRLKAEGRGAFVPFVTLGDPSPELSLKIIDTLVQNGADALELGFPFSDPLADGPVIQGANLRALAAGTTPTACFELLAKIRAKYPELPIGLLLYANLVFANGIDAFYAKAQQAGVDSVLIADVPVEEAAPFIQAAKAHGIAPIFIAPPNADSDTLAKVSQSGEGYTYLLSRAGVTGADTKAGTPVEEILAKLQEFNAPPPLLGFGIAEPAQVSAAIKAGAAGAISGSAVVKIIETHQQDEVKLLAALGEFTRTMKAAT
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
Q8ECU9
|
P0C2L2
|
GSID_SHIF8
|
Glutathione transport system permease protein GsiD
|
Shigella
|
MRLFNWRRQAVLNAMPLVKPDQVRTPWHEFWRRFRRQHMAMTAALFVILLIVVAIFARWIAPYDAENYFDYDNLNNGPSLQHWFGVDSLGRDIFSRVLVGAQISLAAGVFAVFIGVAIGTLLGLLAGYYEGWWDRLIMRICDVLFAFPGILLAIAVVAVLGSGIANVIIAVAIFSIPAFARLVRGNTLVLKQQTFIESARSIGASDMTILLRHILPGTVSSIVVFFTMRIGTSIISAASLSFLGLGAQPPTPEWGAMLNEARADMVIAPHVAVFPALAIFLTVLAFNLLGDGLRDALDPKIKG
|
Part of the ABC transporter complex GsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane.
|
P0C2L2
|
Q74GY0
|
ATPB_GEOSL
|
F-ATPase subunit beta
|
Geobacter
|
MSQNFGKISQVIGAVIDVEFEPGKLPPIYNALRVTNPAIDDKEYNLVLEVAQHLGENAVRTIAMDSTDGLVRGQAVLDTGKQISVPVGRKTLGRILNVIGEPVDEMGPVNAEKEYGIHREAPAFVDQSTKVEAFTTGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELINNIAKQHGGFSVFAGVGERTREGNDLWMEMKESGVLDKAALVYGQMNEPPGARARVALSALSIAEYFRDEEGQNVLLFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGELQERITSTTKGSITSVQAIYVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILDPQVIGEEHYSIARQVQYVLQKYKDLQDIIAILGMDELSEEDKLVVARARKIQRFLSQPFHVAEAFTGSPGKYVELKDTIKGFQEIVAGKHDDVPEQAFYMVGTIEEALEKAKKLAA
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
Q74GY0
|
A8QE76
|
EFTS_BRUMA
|
Elongation factor Ts, mitochondrial
|
Brugia
|
MIVSRQVIRSVVRKSFNRLCSANVVALPSGSTKEALKELRRKTGYSYVNCRKALNEFGPDNLDEAIKWLKKRAIEEGWEKAAKLGDRPTRQGIVSVMTKGNKAAIVELNCETDFVSRNEDFKRLVEDVTKAVLHAADRDGTSTHGFELLNSNINSLKTSENGMLVKDLITEAIGRLGENITLSRAQLILAPPNVQLFGYAHPKEGTDRVYMGRYVSVVGLKGSNKTDFPTEKLGFQLCQHVVGMRSLTLGTPLPVKKTSVKDEVSQDDEINAFYNGEVTHIDENETQLLRQSFMLNPSQTVHEYVTGHGASIVDFYRTELSSNVSEESFQS
|
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
|
A8QE76
|
B2S533
|
ARGC_BRUA1
|
N-acetyl-glutamate semialdehyde dehydrogenase
|
Brucella
|
MKPKIFIDGEHGTTGLQIRTRLAERDDLEVISIPEAERRNKDLRADYLRAADIAILCLPDDASKEAVSLLEGHNSTRIIDTSTAHRVHPDWAYGFAELAKGQRERIAEARLVANPGCYPTGAIALVRPLRDAGLLPADYPVSVNAVSGYTGGGKQLIAQMEDRNHPDYLAANNFLYGLPLKHKHVPELQLHGRLDRRPIFSPSVGRFPQGMIVQVPLFLSELEGSPSLAKVHAVLTEHYAGQDIVEVVPLEESAKLPRVDAEELAGKDGMKLFVFGTEDHGQVNLVALLDNLGKGASGAAVQNMNLMLGK
|
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
|
B2S533
|
Q8DYT2
|
MURE_STRA5
|
UDP-N-acetylmuramyl-tripeptide synthetase
|
Streptococcus
|
MITIDKILEILKNDHNFREILFHEHYYYNWTQNVTFNALSYDSRQISSDTLFFAKGATFKKEYLDSAITAGLSFYVSETDYGADIPVILVNDIKKAMSLISMSFYNNPQNKLKLLAFTGTKGKTTAAYFAYHMLKVNHRPAMLSTMNTTLDGKSFFKSHLTTPESLDLFRMMATAVENQMTHLIMEVSSQAYLTKRVYGLTFDVGVFLNISPDHIGPIEHPTFEDYFFHKRLLMENSNAVVVNSQMDHFNIVKEQVEYIPHDFYGDYSENVITESKAFSFHVKGKLENTYDIKLIGKFNQENAIAAGLACLRLGVSIEDIKNGIAQTTVPGRMEVLTQTNGAKIFVDYAHNGDSLKKLLAVVEEHQKGDIILVLGAPGNKGQSRRKDFGDVINQHPNLQVILTADDPNFEDPLVISQEIASHINRPVTIIIDREEAIANASTLTNCKLDAIIIAGKGADAYQIIKGNRDNYSGDLEVAKKYLKR
|
Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
|
Q8DYT2
|
Q5WES3
|
RL21_ALKCK
|
50S ribosomal protein L21
|
Alkalihalobacillus
|
MYAIIETGGKQIKVEEGQEIYVEKLDAEAGEEVSFDKVLFVGGESAKVGAPFVEGASVTGTVEKHGRNKKIIVYKMKAKKNYRRKQGHRQPYTKVVIGKING
|
This protein binds to 23S rRNA in the presence of protein L20.
|
Q5WES3
|
Q91XI1
|
DUS3L_MOUSE
|
tRNA-dihydrouridine synthase 3-like
|
Mus
|
MAETAAESGGGGDSGVGACERGVAPIKAQYRTTKERFHEYLDGDKQEGACQEVPTGDPAEPGAKRIRLEDGQENGKTEVAIESRERQVPKRARGQNKSRPHVKPAHYDKDRLCPSFLQEPATPCAFGDRCRFLHDVGRYLETKPADLGPRCVLFETFGRCPFSMTCRFAGAHLGPEGQNLVQEEVVARCAQLPSVRNGLDRALQQQLRKRQVCFERAEQALNRLTQSPMPTVVPETTVAMATPKQNSCHAQLDTVGGAGTPQSSPVPTCGPLTDEDVIRLRPCEKKRLDISGKLYLAPLTTCGNLPFRRICKRFGADVTCGEMAVCTNLLQGQMSEWALLKRHPCEDIFGVQLEGAFPDTMTKCAELLNRTIDVDFVDINVGCPIDLVYKKGGGCALMNRSAKFQQIVRGVNGVLDVPLTVKMRTGVQERVSLAHRLLPELRDWGVALVTLHGRSREQRYTRLADWPYIEQCAKVASPMPLFGNGDILSFEDANCAMQTGVAGIMVARGALLKPWLFTEIKEQRHWDISSSERLDILRDFTHYGLEHWGSDTQGVERTRRFLLEWLSFLCRYVPVGLLERPPQRINERPPYYLGRDYLETLMASQQAADWIRISEMLLGPVPPGFVFLPKHKANAYK
|
Catalyzes the synthesis of dihydrouridine, a modified base, in various RNAs, such as tRNAs, mRNAs and some long non-coding RNAs (lncRNAs). Mainly modifies the uridine in position 47 (U47) in the D-loop of most cytoplasmic tRNAs. Also able to mediate the formation of dihydrouridine in some mRNAs, thereby regulating their translation.
|
Q91XI1
|
P97738
|
NPTX2_RAT
|
Neuronal pentraxin II
|
Rattus
|
MLALLTAGVALAVAAGQAQDNPIPGSRFVCTALPPEAARAGCPLPAMPMQGGALSPEEELRAAVLHWRETVVQQKETLGAQREAIRELTSKLARCEGLAGGKARGTGATGKDTMGDLPRDPGHVVEQLSRSLQTLKDRLESLELQLHTNASNAGLPSDFREVLQRRLGELERQLLRKVAELEDEKSLLHNETSAHRQKTENTLNALLQRVTELERGNSAFKSPDAFKVSLPLRTNYLYGKIKKTLPELYAFTICLWLRSSASPGIGTPFSYAVPGQANEIVLIEWGNNPIELLINDKVAQLPLFVSDGKWHHICITWTTRDGMWEAFQDGEKLGTGENLAPWHPIKPGGVLILGQEQDTVGGRFDATQAFVGELSQFNIWDRVLRAQEIINIANCSTNMPGNIIPWVDNNVDVFGGASKWPVETCEERLLDL
|
Likely to play role in the modification of cellular properties that underlie long-term plasticity. Binds to agar matrix in a calcium-dependent manner.
|
P97738
|
C3KYH5
|
RF1_CLOB6
|
Peptide chain release factor 1
|
Clostridium
|
MLERLNFIENKYEELSNKISDPSVMANQKEWQKLCKEHADLEIIVNTYREYKKAQEDLESDKEMLKEESDKDLREMAQEEIKELTLKLEDLERELTILLLPKDPNDDKDVFIEIRAGAGGEEAALFASNLLRMYTRYAERKNWKVETMSLNATDIGGFKEVTVAIKGKGAYSRLKYESGVHRVQRVPDTESSGRIHTSTATVAVLPEVDDVDININANDLRIDVYRASGHGGQCVNTTDSAVRITHLPTGLVVTCQDEKSQLKNKEKAMKVLKARLFEAAEAERAASIAEDRKSQVGTGDRSERIRTYNYPQGRITDHRIGLTLYKLETFLDGDIDEVIEALVTEDQAEKMKDLGRVN
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
C3KYH5
|
B2HQH3
|
MURI_MYCMM
|
Glutamate racemase
|
Mycobacterium
|
MSSPLAPVGIFDSGVGGLTVARAIIDQLPDEDIVYVGDTGNGPYGPLTIPEVRAHALAIGDDLVGRGVKALVIACNTASAACLRDARERYDVPVVEVILPAVRRAVATTRNGRIGVIGTRATITSHAYQDAFAAARDTEITAVACPRFVDFVERGVTSGRQVLGLAEGYLEPLQRSGVDTLVLGCTHYPLLSGLIQLVMGDNVTLVSSAEETAKEVLRVLTERDILRPHDAPPATRLFEATGDPEAFMALAARFLGPALTGVQPVRPSGMH
|
Provides the (R)-glutamate required for cell wall biosynthesis.
|
B2HQH3
|
Q91W27
|
TIP39_MOUSE
|
Parathyroid hormone 2
|
Mus
|
METCQMSRSPRERLLLLLLLLLLVPWGTGPASGVALPLAGVFSLRAPGRAWAGLGSPLSRRSLALADDAAFRERARLLAALERRRWLDSYMQKLLLLDAP
|
Plays a role as a potent and selective agonist of PTH2R resulting in adenyl cyclase activation and intracellular calcium levels elevation. Induces protein kinase C beta activation, recruitment of beta-arrestin and PTH2R internalization. May inhibit cell proliferation via its action of PTH2R activation. Neuropeptide which may also have a role in spermatogenesis. May activate nociceptors and nociceptive circuits.
|
Q91W27
|
Q7MWS9
|
YBEY_PORGI
|
Endoribonuclease YbeY
|
Porphyromonas
|
MAKINFYAEGVSLPRIRRRIVGKWIAEVCSRYGKAVGEISYLFCDDEYILKANQEFLDHDYYTDIITFDSCEADTVNGDLLISLDTVRSNARALDLRYEDELHRVIIHGILHLCGLKDKSKKDEAQMRAAEEKALVMLRETIGSELSLLHT
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
Q7MWS9
|
B1P1D0
|
JZ13B_CHIGU
|
Peptide F5-18.88
|
Chilobrachys
|
MKTSVLFVIFGLALLLCLSFAAELEDTGRQCGEFMWKCGAGKPTCCSGYDCSPTWKWCVLKSPGRR
|
Probable ion channel inhibitor.
|
B1P1D0
|
B8AFR8
|
ORR11_ORYSI
|
OsRR11
|
Oryza sativa
|
MSSIGAGAGGAVVGAAVAAVAVGGGAPPHVLAVDDSSVDRAVIAGILRSSRFRVTAVDSGKRALELLGSEPNVSMIITDYWMPEMTGYELLKKVKESSKLKKIPVVIMSSENVPTRISRCLEEGAEDFLVKPVRPSDVSRLFSRVLP
|
Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling.
|
B8AFR8
|
J9VJ99
|
PFA4_CRYNH
|
Protein fatty acyltransferase 4
|
Cryptococcus neoformans species complex
|
MAARNWSRVWVGGTVILISFIAFSSQIFVIWPWYGREISLDLLMLLVPLNLAAFMIFWNYRLCVITSPGTVPEGWRPNIGAMDGMEVKKGTHTPRYCKNCAHYKPPRAHHCRQCKTCWLKLDHHCPWIGNCVGFYNQGHFIRFLLWVDIGTTFHLIIMVRRVLYIAEYYHEPTLADVLFLVFNFATCVPVWLCVGMFSIYHVYLACGNSTTIEGWEKDKVATLIRRGKIKEVKYPYNIGIYKNIKSVLGPNPLLWLWPQKMQGDGLSFPVNPSAGDHMTQYFWPPQDPSRLPNPPPIPAHASPFVYGNNGFNPNLRPTNSLRARRSSTPRIDEDEYSHEQGRHYSSGDERDNGSISASSSPEPYLSDYDHYDEGPMYPGERMTTLVPRVRRGSEGWEVAPGGGWNAYAGMMDEEVGWDDEAGYDEAPGEDPYVERPWEMRGRYNVYDPEEESGYTH
|
Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function. Responsible for the modification of a subset of proteins that are critical in cryptococcal pathogenesis, with substrates involved in cell wall synthesis, signal transduction, and membrane trafficking. Palmitoylates chitin synthase CHS3.
|
J9VJ99
|
B9L7E1
|
BIOB_NAUPA
|
Biotin synthase
|
Nautilia
|
MKKIYLCAISNIRSGACNEDCKFCTQSVKWGADINRYKQKDLKTIVNEAKLAKKNGATGFCLVTSGKGLDDKTLEYVCSAAKSVIKEVDISIIACNGTAGKDSLKELKKAGVKIYNHNLETSREYYPKICSTHTWDERFETCENIKSVGLQLCCGGIFGMGESNEDIESFIRSLKELKPNGIPLNFFIENEKLPLKATHNKDFALKTVKRFANEFKEAIIMLAGGREIVFGNEWTEALKVGANSIVIGDYLTTKGERPDRDLEILLNEGFEIANEC
|
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
|
B9L7E1
|
O24933
|
HRCA_HELPY
|
Heat-inducible transcription repressor HrcA
|
Helicobacter
|
MLRRIKVGSNLNKKESLLDAFVKTYLQILEPISSKRLKELADLKISCATIRNYFQILSKEGMLYQAHSSGARLPTFKAFENYWQKSLRFETLKVNEKRLKSASENFGLFTLLKKPSLERLERVIECEKRFLILDFLAFSCALGYSVKMEKFLLELVGRSVKEVRSIAASFNALSLARQLERLEYSNTQITRFNLMGLKTLLNSPLFFDILGGKVLERLSKGLHFIEPDCMLVTRPVEFQNKRMQLLCVGKLECDYEGFFQTISEEE
|
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
|
O24933
|
B2UBP3
|
DNAK_RALPJ
|
Heat shock protein 70
|
Ralstonia
|
MGKIIGIDLGTTNSCVAIMEGNTPKVIENAEGARTTPSIIAYMEDGEILVGAPAKRQAVTNPKNTLYAVKRLIGRKFEEKEVQKDIGLMPYSIVKADNGDAWVEVRGQKLAPPQISAETLRKMKKTAEDYLGEEVTEAVITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAFGLDKNEKGDRKIAVYDLGGGTFDISIIEIADVDGEKQFEVLSTNGDTFLGGEDFDQRIIDYIIGEFKKEQGVDLSKDVLALQRLKEAAEKAKIELSSTQQTEINLPYITADASGPKHLNLKITRAKLEALVEDLIARTIDPCRTAIKDAGVKVSDIHDVILVGGMTRMPKVQEKVKEFFGKEARKDVNPDEAVAVGAAIQGQVLGGDRTDVLLLDVTPLSLGIETLGGVMTKMIGKNTTIPTKFSQTFSTADDNQPAVTIKVYQGEREMASGNKMLGEFNLEGIPPAPRGTPQIEVSFDIDANGILHVGAKDKATGKENKITIKASSGLSEAEIERMVKDAEANAEEDKKLRELVDSRNQGEALVHSTKKALGEYGDKLEAGEKDKIEAAIKELEETLKGTDKAAIDAKTEALATASQKLGEKVYADMQAKGEAGGAEQAAGAQAGAQAGQGAPHDDNVVDAEFKEVNDKK
|
Acts as a chaperone.
|
B2UBP3
|
B1JUW8
|
MUTS_BURCC
|
DNA mismatch repair protein MutS
|
Burkholderia cepacia complex
|
MTTLSPEAFAGHTPMMQQYLRIKADHPDTLVFYRMGDFYELFFEDAEKAARLLDLTLTQRGASAGTPIKMAGVPHHAVEQYLAKLVKMGESVAICEQIGDPATSKGPVERKVVRVVTPGTLTDAALLSDKNDVYLLAMCTGHNKRGVAVNIGLAWLNLASGALRLAEIEPDQLAAALERIRPAEILTPDGATDAIPAGAGASKRVPAWHFDIASGTQRLCDQLDVASLDGFGAHSLTSACGAAGALLLYAAATQGQQLRHVRSLKVENETEYIGLDPATRRNLELTETLRGTESPTLYSLLDTCCTTMGSRLLRHWLHHPPRASVAAQSRQQAIGALLDAPANASLDALRSALRQIADVERITGRLALLSARPRDLSSLRDTFAALPALRERISAIVANADALARVDAALAPPAECLDLLTSAIAPEPAAMVRDGGVIARGYDAELDELRDISENCGQFLIDLEARERARTGIANLRVEYNKVHGFYIEVTRGQTDKVPDDYRRRQTLKNAERYITPELKTFEDKALSAQERALARERALYDSVLQALLPFIPECQRVASALAELDLLAAFAERARALDWVAPTFTDEIGIEIEQGRHPVVEAQVEQFIANDCRFGTERKLLLITGPNMGGKSTFMRQTALIALMAYVGSYVPAKSACFGPIDRIFTRIGAADDLAGGRSTFMVEMTEAAAILNDATPQSLVLMDEIGRGTSTFDGLALAWAIARHLLAHNACYTLFATHYFELTQLPAEFPQAANVHLSAVEHGHGIVFLHAVNEGPANQSYGLQVAQLAGVPAPVIRAARKHLAYLEQQSASQHTPQLDLFSAPPAAVDDLECADAPALPDTPHPALEKLRDIDPDDLKPREALDLLYELRTLVRSHDADGHA
|
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
|
B1JUW8
|
B8E003
|
RF1_DICTD
|
Peptide chain release factor 1
|
Dictyoglomus
|
MLQKLVIDKLEEIEKRFEEIEGLLAKEDVISDFNKYQSLLKERAKIEEIVDKFREYKRLLKEKEDLEEMVKEEQDEDLRSLAETELEDIQEKLEKVEFELKALLLPKDPNDEKNIIMEIRAGTGGEEAALFAADLFRMYLGYAQKKGWKVEIVSSNPTGLGGFKEIIFIVEGKGAYSRLKFESGVHRVQRVPITESSGRIHTSTATVAVLPEMEEIEVEIDPKDLRIETFRSGGAGGQHVNKTESGVRITHIPSGIVVQCQDERSQHQNREKAMKVLRARLYEYYQREKENEIASQRRQQVGTGERSEKIRTYNFPQRRVTDHRINYSSFQLEEVLSGELDEFIDRLILAEKEEQIKKLFEEVGATS
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
B8E003
|
C5A285
|
RL4_THEGJ
|
50S ribosomal protein L4
|
Thermococcus
|
MKVKVFNLEGEPVEEIELPKVFSTPFRPDLIRRAVIASWTHRIQPQGRDPLAGKRRVTENIGKGHGMARVERIKTPPRFAAFVPFARGGRRTHPPKVEKIIWEDINKKERRLAIMSAIAATANPDLVRARGHVVDNVPAFPLVVVDDLQKVFKTAQTREIFKKLGIWDDIERAKRNTKIRAGKGKMRGRRYKKAKGPLIVVAKNEGIVQGARNHPGVDVVTVDNLGVELLAPGTHPGRLTIWTKGAIERLKEIYG
|
Forms part of the polypeptide exit tunnel.
|
C5A285
|
Q9QUT0
|
RHAG_MOUSE
|
Rhesus blood group family type A glycoprotein
|
Mus
|
MRFKFPLMAISLEVAMIVLFGLFVEYETPQNASQKNASHQNASQQGNTSSSAKKDQFFQLYPLFQDVHVMIFVGFGFLMTFLKKYGFSGVGFNLFLAALGLQWGTIMQGLLHSHGKEFHFGIYNMINADFSTATVLISFGAVLGKTSPIQMLIMTILEIAVFAGNEYLVTELFEASDTGASMTIHAFGAYFGLAVAGVLYRPGLRCEHPNDESVYHSDLFAMIGTLFLWIFWPSFNSAIADPGDHQYRAIVNTYMSLAACVITAYALSSLVERRGRLDMVHIQNATLAGGVAVGTCADMEIPLYAAMTIGSIAGIISVLGYKFFSPLLANKLMIHDTCGVHNLHGLPGVFGGLASIVAISWGMSTASMAMQAAALGSSIGSAIVGGLLTGLILKLPIWNQPPDEYCYDDSVSWKVPKFRELDNRFFQHANHNHVEHEV
|
May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. Involved in ammonia transport across the erythrocyte membrane. Seems to act in monovalent cation transport.
|
Q9QUT0
|
Q1QY21
|
PURA_CHRSD
|
IMP--aspartate ligase
|
Chromohalobacter
|
MGKNVVVLGTQWGDEGKGKVVDLLTESAATVVRFQGGHNAGHTLVIDGEKTVLHLIPSGVLRADKTCVIGNGVVLSPEALMDEIRELEAKGVPVRERLRLSPACPLILPYHVRLDQAREKARGIAKIGTTGRGIGPAYEDKVARRGLRLGDMLHRERFASKLGEVLDYHNFVLTQYHHEAPVDFQRVLDEAMEIAEELRPMVCDTVSLVHDTRKAGENILFEGAQGSLLDIDHGTYPYVTSSNTTAGGTATGSGVGPLYLDYVLGITKAYTTRVGSGPFPTELFDEFGRHLAEKGHEFGATTGRARRCGWFDAVALRHAVQINSVSGLCLTKLDVLDGLENIRVCIGYRSKDGETIDTPVDSEGYEVIEPLYQDLPGWSESTLGVKRIEDLPNNARAYISFLEEQTGVPIDIISTGPDRNETIVLRNPFLD
|
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
|
Q1QY21
|
A5GV87
|
CCS1_SYNR3
|
Cytochrome c biogenesis protein CcsB
|
unclassified Synechococcus
|
MKSLVLKAAAWLSDLRVAIVLLLLIAACSGLGTAIPQGEPAAFYHERYDAAPWLGVVNGNQLLSWELDHLYTSNWFLLLLAWLGLALLLCSLRRQWPALRASLRWLDYTKPRQLSKLAVATSLDTGDSAAALDQLERQLQQQGWAVRRQQNRLAARRGVIGRVGPLLVHTGLIVFMVGAVVGAFGGQRLERFLAPGRSLELLNPQGDTRLELQLDSFAIQRDPAGRPEQFSSQLLLRDGTGAPAQPAAVSVNHPLRHRGITVYQADWGLAAVTMQLGQSPLLQLPLQTFPELGEQVWGLVLPTRPDGSDPVLLALQSELGPVEVYGADSQQLGLLTVGGESQEILGLPLRIADVMPASGLLIKRDPGVPLVYAGFAITLLGGGLSLIATRQLWAISESGRLHIAGLCNRNLVAFADELPKLGSSAITGAPHDAR
|
Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
|
A5GV87
|
Q6ENW6
|
ATPA_SACOF
|
F-ATPase subunit alpha
|
Saccharum officinarum complex
|
MATLRVDEINKILRERIEQYNRKVGIENIGRVVQVGDGIARIIGLGEIMSGELVEFAEGTRGIALNLESKNVGIVLMGDGLMIQEGSFVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIVASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQDVICVYVAIGQRASSVAQVVTTFHEEGAMEYTIVVAEMADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNSLLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELQAFAQFASALDKTSQNQLARGRRLRELLKQSQSNPLPVEEQVATIYTGTRGYLDSLEIEQVKKFLDELRKHLKDTKPQFQEIISSSKTFTEQAETLLKEAIQEQLERFSLQEQT
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
Q6ENW6
|
Q9LRR9
|
GLO1_ARATH
|
Short chain alpha-hydroxy acid oxidase GLO1
|
Arabidopsis
|
MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLGKMDEANDSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHITTEWDTPRPSARL
|
Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2 . Is a key enzyme in photorespiration in green plants (Probable).
|
Q9LRR9
|
A8H1Q6
|
NUSB_SHEPA
|
Antitermination factor NusB
|
Shewanella
|
MKPSERRKARRLAVQAIYSWQLSGNNIADVEHEFLTEQDVAGVDIAYFRELLGGVATKKSQLDELITPFVTRPLDEVDPVEKAIVRIATYELTFRKDVPYKVAINEAIELAKAFGAEDGHKFVNGILDKLVARNK
|
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
|
A8H1Q6
|
Q1WU83
|
EFTU_LIGS1
|
Elongation factor Tu
|
Ligilactobacillus
|
MAKEHYERTKPHVNIGTIGHVDHGKTTLTAAITKVLAEKGLAEASDYASIDAAPEERERGITINTAHVEYETEKRHYAHIDAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVEYIVVFLNKCDLVDDDELLDLVEMEVRDLLSEYDFPGDDIPVIRGSALKALEGDKDAEAQIMELMDTVDEYIPTPQRPTDKPFLMPVEDVFTITGRGTVASGRIDRGTVKVGDEVEIVGLKDDVVKTTVTGVEMFRKTLDEGEAGDNIGALLRGVDRTQVERGQVLAKPGSIQTHKKFKGEVYVLTKDEGGRHTPFFSNYRPQFYFHTTDVTGVIELPEGVEMVMPGDNVTFTVELIAPVAIEKGLKFTVREGGRTVGAGVVSEIDD
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
Q1WU83
|
Q88DV3
|
GLMM_PSEPK
|
Phosphoglucosamine mutase
|
Pseudomonas
|
MSRKYFGTDGIRGRVGEYPITPDFMLKLGWAAGMAFRKQGHCRVLVGKDTRISGYMFESALEAGLSAAGADVMLLGPMPTPAIAYLTRTFHAEAGIVISASHNPHDDNGIKFFSGQGTKLPDEVELMIEELLDQPMTVVESGKLGKVSRINDAAGRYIEFCKSSVPSSTSFEGLKLVVDCAHGATYKVAPSVFRELGADVTVLHAQPDGLNINEGCGSTHIESLQAAVLVGHADLGIAFDGDGDRVLMVDHTGAIVDGDELLFIIARDLQEHGKLQGGVVGTLMSNLGLELALKDLDIPFVRAKVGDRYVMAELLEREWLVGGENSGHVVCCNHTTTGDAIIAALQVLMALKRRGETLAQARQALRKCPQVLINVRFGASKVDPLEHPAVKEASAKVTEALAGRGRVLLRKSGTEPLVRVMVEGEDESQVRAHAEALAKLVGEVCV
|
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
|
Q88DV3
|
B8G711
|
EFP_CHLAD
|
Elongation factor P
|
Chloroflexus
|
MAAGTTSDLRNGIVIRYNNDLYQVVEFQHVAPGNWRAFVRMKLKSLTTGKVIEDRVRAGAEIDIVRIERRPMQYLYREGDSFVFMDNDTFDQIPVSAELVGDAVKFMKENETVDLVYDAEKDQIIGVELPIFVNLKVVETTVAVRGDTATNVTKPATLETGAVIEVPAFINEGDVLKIDTRTGEYITRV
|
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
|
B8G711
|
B5Z7D2
|
MOBA_HELPG
|
Molybdopterin-guanine dinucleotide synthase
|
Helicobacter
|
MKNPIIDNIPCVLLAGGKSSRFITNNIQTNKALMPLKSYSSLLEYQYTRLLKLFKKVIISTKKSYELNAPYLLEKESDLFSPLFGIHNAFLTLQTPYIFFIPIDTPLVSFESIKALCGIKNFSVVYAKSPTKEHYLISLWHQSTLNALNYALKTQNYRLSDLIKNASSTAIHFDKEEEFLNLNTLKDYELAVQILKEGSNG
|
Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
|
B5Z7D2
|
Q0IE26
|
RL20_SYNS3
|
50S ribosomal protein L20
|
unclassified Synechococcus
|
MARVKRGNVARKRRNKILRLARGFRGSNGTLFRTANQRVMKALCNAYRDRRRRKRDFRRLWIARINAAARMNGVSYSRLIGGLKKADVRINRKMLAQMAVVDPASFANVVNATQG
|
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.
|
Q0IE26
|
Q12QI6
|
GLMM_SHEDO
|
Phosphoglucosamine mutase
|
Shewanella
|
MKQRQFFGTDGIRGKVGAGKMTPELALKLGWAAGRVLSRTGTKKVIIGKDTRISGYLFESALEAGLSAAGLNVLLVGPMPTPAVAYLTRTFRAEAGIVISASHNPYYDNGIKFFSTDGSKLDDAIELEIEAELEKPLTCVESHLLGKAKRIDDAAGRYIEYCKGNFPADQTLEGLKIVVDCAHGATYHIAPSVFSELGAEVIAIGDKPNGTNINHEVGATSMGKICETVLAEGADLGIALDGDGDRIMMVNRKGEVIDGDQILYILAADAQKRGQLKGGVVGTLMSNLGLDLALQALDIPFLRSNVGDRYVMEMLKKNDWRIGGENSGHILDLDHGTTGDGIVAGILVLAAMRRQNATLEQLVEPMKMLPQVLINVRFEGSNNPLDSDLVKSAQREVEQSLGARGRVLLRKSGTEPLIRVMVEGDDHDLVLAHANRIAAAVKLGC
|
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
|
Q12QI6
|
Q8XVE7
|
TRPD1_RALSO
|
Anthranilate phosphoribosyltransferase 1
|
Ralstonia
|
MTISPQDALTRCIEHREIFHDEMLHLMRLIMRGEMSPVIASALIMGLRVKKETIGEIAAAATVMREFATTVDVPAAILDHFVDIVGTGGDGANTFNISTASMFVAAAAGARIAKHGGRGVSSKSGSADVLEALGVNIMLTPEQVAQSIEAVGIGFMFAPNHHPAMKNVAPIRKELGVRTLFNILGPLTNPAGAPNILMGVFHPDLVGIQVRVMQRLGARHAVVVYGKDGMDEVSLGAATVVGELKDGEVREYEIHPEDYGLQMVSNRGLKVADAEESKAMLLGALENVPGTPREIVTLNAGAALYAANLAGSIGDGITLAREAIASGAARAKVDELVRVTNQFKK
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
Q8XVE7
|
C0ZL41
|
MTNX_BREBN
|
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase
|
Brevibacillus
|
MSKKLVLFCDFDGTITEKDNIVAIVRKFAPPEWEALTEQILSQKISVQEGVGKLFQLLPSSLRQDIIDFIVHEATIRPGFAEFVSYCREEGIELLITSGGIDFFLEPILAPFDLADVPIYCNGSDFSGERITITWPNACDEHCTNGCGMCKTTIIRRYDPATHFRIVIGDSITDLAGAKIADYVIARSFLADKAEELQLPHSTFATFHDVIRILQQVQQEVV
|
Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
|
C0ZL41
|
A4STA4
|
ZAPB_AERS4
|
Cell division protein ZapB
|
Aeromonas
|
MHMSLEVLEQLESKVQSAVDNISLLKMELDELKEQNSKLQDENHLLRNEHVAWQERLRALLGKMEQMGESI
|
Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA.
|
A4STA4
|
Q88S38
|
IOLG_LACPL
|
Myo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase
|
Lactiplantibacillus
|
MAEAHVTKVGIVGIGFIGSDHLHRLTKTVANVDVTAVCDIVPGKAQKALDQQGLTATTYEDYHDLVNDPNVEVVVCTANNEAHYEIVMAALKAGKFTFCEKPLALDAKQCMDIIDSEKKLGRRMLQVGFMRHYAPEYVQMKKMIDDGVIGKPLMMDQRHYNQTQPEEYDSSRSIIETAIHEIDIDHWLVNDDYANIRVFSPKQTRHVQNAKIQDPQIVMIETKSGINIINEVFVRCQYGYDIKCDVIGEEGVLELPTVPQVATRLNAQYSTAILTDWKARFESAYDIEFRDFINHVSQNESPVGPSAWDGYIAAVTADAALKSLAEDGAKQDLDFPSTPAFYTESEKVSE
|
Involved in the oxidation of myo-inositol (MI) and D-chiro-inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D-chiro-inositol (1KDCI), respectively.
|
Q88S38
|
Q28RK1
|
URED_JANSC
|
Urease accessory protein UreD
|
unclassified Jannaschia
|
MLDAATPTHQRVRGRAMARFTGRRLRDLHQSGSAKVLIPRVFGRAPEVVFLNTAGGITGGDRLDYALHVDDGTCVGTTQTAERAYRSHGPMGRVSTRLTIGQGATLHWVPQEMILFDGVALERDLSVEMAGDAELVMLETLVLGRAAMGEVLRDLHLRDRRRVTRGGKLAMVEAIGLGPDDFASSSPAGLNGAVATASLTLMAQDAEDRLNALRAVLPTDVRSAASAWDGRLTARFLAPQAYPLRRAVARAVEQVTCGALPRVWQI
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
Q28RK1
|
A1ALL1
|
ATPL1_PELPD
|
Lipid-binding protein 1
|
Pelobacter
|
MNFFTMCVFGAAIGMAIGTLGTAIGQGMAVKSAVEGVARNPGAASKIMTTMMIGLAMIESLAIYALVVCLIILFANPYKDIALKMVETVAK
|
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
|
A1ALL1
|
B8NI18
|
IMQA_ASPFN
|
Imizoquin biosynthesis cluster protein A
|
Aspergillus subgen. Circumdati
|
MVDSVFPAPSLVDETFLAPSSSETNDTAMAADGTLAKMNMFQFNSMLKEYSPPRFEDLFQDLDASKAGWEHYRPRLVSEVDLIDAEHYSLFSANTVSPL
|
Part of the gene cluster that mediates the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids that serve a protective role against oxidative stress that are essential for normal germination . ImqB is a canonical three-module NRPS that assembles the tripeptide backbone of the imizoquins via condensation of Trp, Tyr, and Leu-derived precursors . N-methylation by imqF and phenol oxidation by imqC, followed by cyclization via the FAD-dependent oxidase imqH carry out the three-step transformation of L-tyrosine into tetrahydroisoquinoline . Importantly, this sequence requires the presence of a free amine in the tyrosine moiety, indicating that isoquinoline formation occurs prior to peptide bond formation . The imidazolidin-4-one ring of imizoquins could form following additional oxidation of the methyl-derived bridgehead carbon by imqH . Lastly, O-methylation by imqG and leucine hydroxylation by imqE complete biosynthesis of the imizoquins .
|
B8NI18
|
Q9AET7
|
ASP3_STRGN
|
Orf3
|
Streptococcus
|
MKIQKHKEIYWGELRGASISKTRKDFTYLYGSTIIFHSPDQVYFENKLIASGQTIHEWSSSWNYQGDRQVPSLPLLKRGRSYSLTRDMTSYPSESVFLKLIFFDRYNREVSNHVERSDKMTFTYPEEAYSYKVQLLSAGVESFEFHCLRIEEILEESNG
|
Part of the accessory SecA2/SecY2 system specifically required to export GspB, a serine-rich repeat cell wall protein encoded upstream in the same operon.
|
Q9AET7
|
A8M4B3
|
ALR_SALAI
|
Alanine racemase
|
Salinispora
|
MWQAEVRVDLDAIRENVSWLRSGSAAELMAVVKGDGYGHGMVPAALAALDGGADWLGVCTLDEALTLRREGITAPILAWLLAPGLPLHEGVAAGIDLGAASVAQLDEMVQAGRTAGRPARLHLKIDTGLSRGGATVSDWPGLLTAAAKAQADGTVEVVGVWSHFVYADAPGHPTTDRQLAVFHEGLDMVEKAGLRPRYRHLANSAATLTRPDAHFDLVRPGLAVYGLSPVAGESFGLRPAMTARARVMLTKQVPAGAGVSYGHTYTTERDSTLAVIPLGYADGVPRSASNSGPVHLGGVRRTISGRVCMDQFVLDCGDDPVAPGDVAVLFGSGRNGEPTADDWAEAVGTINYEIVTRFGSTRVPRSYDGERP
|
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
|
A8M4B3
|
A2CBX2
|
PANCY_PROM3
|
Cytidine monophosphate kinase
|
Prochlorococcus
|
MGALHRAHGQLIKSVQGFGSLQPAAVLVSVFVNPLQFGPAEDFDSYPRDLEADCELASRSGASALWAPSVDQVFPGGASSQFRIQVPSHLQAHLCGAIRPGHFDGVVTVVARLLALVRPEVLVLGEKDWQQLVILRHLVAQLGLPVRVHGVATVRDDDGLACSSRNRYLMTQQRQQALALPQLLARAARESQDGRAVDLAGLRCAWEQLGLEVEYVETVDAFNLQPLHAGRKLCLLAAAVRCGETRLIDHTFLMSRQPIVAIDGPAGAGKSTVTRAFAERLGLLYLDTGAMYRAVTWLTQQHDVDPHDPVAVKTILENLELELEPSQSGPQKVRINGHDVTEAIRSPEVTSSVSVVAAHGCVRKALTAQQQRMGVRGGLVAEGRDIGTAVFPDAELKVFLTASPAERARRRALDLDNRGFPVPDLAELETQIEERDRMDSTREVAPLRQAEDATELISDGMSIEEVIETLIDLFRVQVPEEVWPTPGS
|
Catalyzes the transfer of a phosphate group from ATP to either CMP or dCMP to form CDP or dCDP and ADP, respectively.
|
A2CBX2
|
Q9DA32
|
SUN5_MOUSE
|
Sperm-associated antigen 4-like protein
|
Mus
|
MPRTRNIGALCTLPEDTTHSGRPRRGVQRSYISRMAEPAPANMNDPLLLPLRMNTPGLSLVQILLGYMSWLTYLACFLRTQTQQVFLNTCRCKLFCQKVMEKMGLLVLCVFGFWMFSMHLPSKVEVWQDDSINGPLQSLRMYQEKVRHHTGEIQDLRGSMNQLIAKLQKMEAISDEQKMAQKIMKMIQGDYIEKPDFALKSIGASIDFEHTSATYNHDKARSYWNWIRLWNYAQPPDVILEPNVTPGNCWAFASDRGQVTIRLAQKVYLSNITLQHIPKTISLSGSPDTAPKDIVIYGLESLPREEVFLGAFQFQPENVIQMFQLQNLPPRSFAAVKVKISSNWGNPRFTCMYRVRVHGSVTPPKDSHLEPLS
|
Plays an essential role in anchoring sperm head to the tail. Is responsible for the attachment of the coupling apparatus to the sperm nuclear envelope.
|
Q9DA32
|
P63239
|
NEC1_MOUSE
|
Proprotein convertase 1
|
Mus
|
MEQRGWTLQCTAFAFFCVWCALNSVKAKRQFVNEWAAEIPGGQEAASAIAEELGYDLLGQIGSLENHYLFKHKSHPRRSRRSALHITKRLSDDDRVTWAEQQYEKERSKRSVQKDSALDLFNDPMWNQQWYLQDTRMTAALPKLDLHVIPVWEKGITGKGVVITVLDDGLEWNHTDIYANYDPEASYDFNDNDHDPFPRYDLTNENKHGTRCAGEIAMQANNHKCGVGVAYNSKVGGIRMLDGIVTDAIEASSIGFNPGHVDIYSASWGPNDDGKTVEGPGRLAQKAFEYGVKQGRQGKGSIFVWASGNGGRQGDNCDCDGYTDSIYTISISSASQQGLSPWYAEKCSSTLATSYSSGDYTDQRITSADLHNDCTETHTGTSASAPLAAGIFALALEANPNLTWRDMQHLVVWTSEYDPLASNPGWKKNGAGLMVNSRFGFGLLNAKALVDLADPRTWRNVPEKKECVVKDNNFEPRALKANGEVIVEIPTRACEGQENAIKSLEHVQFEATIEYSRRGDLHVTLTSAVGTSTVLLAERERDTSPNGFKNWDFMSVHTWGENPVGTWTLKITDMSGRMQNEGRIVNWKLILHGTSSQPEHMKQPRVYTSYNTVQNDRRGVEKMVNVVEKRPTQKSLNGNLLVPKNSSSSNVEGRRDEQVQGTPSKAMLRLLQSAFSKNALSKQSPKKSPSAKLSIPYESFYEALEKLNKPSKLEGSEDSLYSDYVDVFYNTKPYKHRDDRLLQALMDILNEEN
|
Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Substrates include POMC, renin, enkephalin, dynorphin, somatostatin, insulin and AGRP.
|
P63239
|
O85735
|
CSRA_SERMA
|
Repressor of secondary metabolites
|
Serratia
|
MLILTRRVGETLMIGDEVTVTVLGVKGNQVRIGVNAPKEVSVHREEIYQRIQAEKSADDLLIPKQRLVA
|
Involved in the process of swarming and quorum-sensing signal production; overexpression strongly inhibits swarming motility, pigment and N-acylhomoserine lactone (quorum-sensing signal) production but not swimming motility or swarmer cell differentiation .
|
O85735
|
B2IA20
|
HSLU_XYLF2
|
Unfoldase HslU
|
Xylella
|
MPSKTDFTSSTMTPREIVQELDRHIVGQQAAKRSVAIALRNRWRRMQLPEELRNEVMPKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEVGYVGKDVEQIGRDLVDTAVKMYREQAKVRVRTQAEEYAEERILDALLPRRSVGIGFDADADAIRQEPSAHESETRAKFRRMLRSGELEEREIELDVAVNVSMDIMTPPGMEEMGQQLRQMFSNIGGGKSQKRKLAIKAARPLLIEEEAAKLVNEDEIRAAAIEACEQNGIVFIDEIDKVVKRGDTVGGGDVSREGVQRDLLPLVEGSNVSTKYGTIRTNHILFIASGAFHLTKPSDLIPELQGRFPIRVELDALSKADFIRILTEPKAALTKQYQELLKTEGVSLDFTEDAIDRIAEIAYLVNERQENIGARRLHTVLERLLETLSYESPDRDGESVTVDADYVNAHLGELVKDPDLSRYIL
|
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
|
B2IA20
|
Q2FLB5
|
ENO2_METHJ
|
2-phosphoglycerate dehydratase 2
|
Methanospirillum
|
MDTRIKRIIAREILDSRGNPTVEVDITLNNGIRGRAACPSGASTGIHEAVERRDGEKRFGGKGVQGAVQAVMDIISPKLLGRDALEQKSIDSVMIELDGTPNKAKLGANAILTVSMAVARAAANSEDVLLSEYLGPKSTLMPVPCMNIMNGGAHANWQGSDFQEYMIAPVGAPDYPEAVRWGCEVYHSLKSVLKKKGLSTGVGDEGGFAPIVPSNLEPASLIVHAIEEAGYIPGKDIALVLDPASSGFYKDGKYTLKTEKKVLTSEEMTDYYEDMIRTYPIISIEDGLAEDDWEGFAFMTKRLGNTIQIVGDDIFVTNPERIHRGLKEKTANAVLIKLNQIGTVTETIDAIRLAQKAGWGTMVSHRSGETCDSFIADLTVALGCGQLKTGAPCRGERVEKYNQLLRINEFLGDKARYAGRQAFNSA
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
Q2FLB5
|
Q9JJN5
|
CBPN_MOUSE
|
Carboxypeptidase N small subunit
|
Mus
|
MPDLPSAFLPLLLLSKFVTPVTFRHHRYDDLVRTLYKVHNQCPDITRLYNIGRSVKGRYLYVLEFSDYPGIHEPLEPEVKYVGNMHGNEVLGRELLLQLSEFLCEEFRNRNQRILRLIQDTRIHILPSMNPDGYEVAAAQGPNMSGYLVGRNNANGVDLNRNFPDLNTYFYYNSKNGGPNHHLPLPDNWKSQVEPETRAVIQWIRSLNFVLSANMHGGAVVANYPYDKSLEHRFRGPHRTSNSPTPDDELFQTLAKVYSYAHGWMHQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPRQEELQREWLGNREALIQFLEQVHQGIKGMVLDENSNNLTGAVISVTGINHDVTSGEHGDYFRLLLPGTYSVTAKAPGYDPKTVTVTVGPAGPTVVDFQLKRSSSQVYPVQRAPGRGQGGRAKQPRTSRKKDPATKRHRGPA
|
Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation.
|
Q9JJN5
|
Q43517
|
FER1_SOLLC
|
Ferredoxin I
|
Solanum subgen. Lycopersicon
|
MASISGTMISTSFLPRKPAVTSLKAISNVGEALFGLKSGRNGRITCMASYKVKLITPEGPIEFECPDDVYILDQAEEEGHDLPYSCRAGSCSSCAGKVTAGSVDQSDGNFLDEDQEAAGFVLTCVAYPKGDVTIETHKEEELTA
|
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
|
Q43517
|
B7IT40
|
KAD_BACC2
|
Adenylate monophosphate kinase
|
Bacillus cereus group
|
MNLILMGLPGAGKGTQAEQIVAKYNIPHISTGDMFRAAMKAETEMGLQAKSFIDKGALVPDEVTIGIVRERLSQEDCVRGFLLDGFPRTVAQASALEEIMKDLGKKIDYVLNINVDSGLLLKRLTGRRICKECGATYHLEFNPPAKADVCDKCGGELYQRSDDNEETVANRLDVNIKQTKPLLDFYDELGYLKSINGEQDINKVFADIDVLIGGLA
|
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.
|
B7IT40
|
Q5M5N0
|
PYRH_STRT2
|
Uridine monophosphate kinase
|
Streptococcus
|
MAEPKYKRVLIKLSGEALAGEKGVGIDLPTVQAIAKEIAEVADSGIQIALVIGGGNLWRGEPAAEAGMDRVQADYTGMLGTTMNALVMADSLKQLGVDTRVQTAIDMKSVAEPYIRGRALRHFEKGRIVIFAAGIGSPYFSTDTTAALRAAEIESDAILMAKNGVDGVYNDDPRKNADAVKFDKLTHVEVIKRGLKIIDATASTLSMDNDIDLVVFNMNEPGNIKRVIFGEQIGTTVSNKAELRK
|
Catalyzes the reversible phosphorylation of UMP to UDP.
|
Q5M5N0
|
Q8K9J0
|
PTGCB_BUCAP
|
PTS system glucose-specific EIIB component
|
Buchnera
|
MFKNVFSSLQKVGKSLMLPVSVLPIAGILLGIGSAHFTLIPEIISQIMAQTGGSIFSNMPLIFAIGVALGFSNNDGVAALAAVVAYSILIQTLSAVELNILNTDANTIKNKNFSDIGILGGIIAGAISAYMFNKFYKIQLPEYLGFFAGKRFVPIISGLFAIFVGLILSLIWPSIGNKIQIFSEWAAYQNPIIAFSLYGLVERALVPFGLHHIWNVPFQMQIGEYKNSIGQIFHGDIARYMAGDTTAGNLSGGFIFKMYGLPGAALAIWHTAKKENRKKIGSIMISAALTAFLTGITEPIEFSFILVAPILYIIHAILAGLSFPLCIFLNMRAGTSFSHGFIDFIVLSGHSHKIFLFPIVGICYGLLYYSIFYFLITTFNLKTPGREENKNTVFFRNNIEIAPYIVEALGGKNNIKNLDACITRLRITVSEISKVNEENLKNLGAAGVVISGSGVQAVFGTRSENIKTAIDEYINNI
|
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport.
|
Q8K9J0
|
Q5E2G9
|
ASTD_ALIF1
|
Succinylglutamic semialdehyde dehydrogenase
|
Aliivibrio
|
MTHWIAGDWVLGEGETIQSLSPYNSEVVWKGESATEAQVESAVNAARNAFIEWKKLPFENRQAIVERFAELVKENADSIAEVIAKETGKPFWETKTEAGAMVGKIAISIRAYHERTPYKEREAAGNKIVLRHRPLGVMAVFGPYNFPGHLPNGHIVPALLAGNTVVLKPSEQTPWTSEVIMKLWQKSGLPKGVINLVQGARATGEALANTKGIDGLLFTGSANTGHILHRQFAGDTGKMLALEMGGNNPMVISKAFGDLDATVYTIVQSAFISAGQRCTCARRLYVPEGKQGDALLARLVDVTKNIHVDQPFSETTPFMGPQISIAAAEFILNAQKKLQALGGESLLEARSLGHAFVSPGIIDATNVAELPDEEYFGPLLQVIRYTTLAQAVELANDTRYGLSAGLVSTDDSEWDYFVEHIRSGIVNRNRQLTGASGDAPFGGPGASGNLKPSAYYAADYCAYPMASMEGDACEIPEQLSPGLTL
|
Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
|
Q5E2G9
|
Q9CQ37
|
UBE2T_MOUSE
|
Ubiquitin-protein ligase T
|
Mus
|
MQRASRLKKELHMLAIEPPPGITCWQEKDQVADLRAQILGGANTPYEKGVFTLEVIIPERYPFEPPQVRFLTPIYHPNIDSSGRICLDILKLPPKGAWRPSLNIATVLTSIQLLMAEPNPDDPLMADISSEFKYNKIAFLKKAKQWTEAHARQKQKADEEELGTSSEVGDSEESHSTQKRKARPLGGMEKKFSPDVQRVYPGPS
|
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair: acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCL and FANCI. May contribute to ubiquitination and degradation of BRCA1. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination.
|
Q9CQ37
|
B7IWF0
|
MTNB_BACC2
|
Methylthioribulose-1-phosphate dehydratase
|
Bacillus cereus group
|
MKQLFRQWYDLSEIKKELTTRNWFPATSGNISIKVSHEPLTFLITASGKDKTKTTPDDFLLVDHVGVPVLETELRPSAETILHTHIYNNTNAGCVLHVHTTDNNVITNLYSDAVTLQNQEIIKALDIWEEGATIHIPIIENHAHIPTLGENFRKHIKGDSGAVLIRNHGITVWGRDSFDAKKRLEAYEFLFQFHIKLLSIQGGVSNGANSYS
|
Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
|
B7IWF0
|
B7NFY3
|
UBIC_ECOLU
|
Chorismate pyruvate-lyase
|
Escherichia
|
MSHPALTQLRALRYFKEIPALDTQLLDWLLLEDSMTKRFEQQGKTVSVTMIREGFVEQNEIPEELPLLPKESRYWLREILLCADGEPWLAGRTVVPVSTLSGPELALQKLGKTPLGRYLFTSSTLTRDFIEIGRDAGLWGRRSRLRLSGKPLLLTELFLPASPLY
|
Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
|
B7NFY3
|
Q02962
|
PAX2_HUMAN
|
Paired box protein Pax-2
|
Homo
|
MDMHCKADPFSAMHPGHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVDKIAEYKRQNPTMFAWEIRDRLLAEGICDNDTVPSVSSINRIIRTKVQQPFHPTPDGAGTGVTAPGHTIVPSTASPPVSSASNDPVGSYSINGILGIPRSNGEKRKRDEVEVYTDPAHIRGGGGLHLVWTLRDVSEGSVPNGDSQSGVDSLRKHLRADTFTQQQLEALDRVFERPSYPDVFQASEHIKSEQGNEYSLPALTPGLDEVKSSLSASTNPELGSNVSGTQTYPVVTGRDMASTTLPGYPPHVPPTGQGSYPTSTLAGMVPGSEFSGNPYSHPQYTAYNEAWRFSNPALLSSPYYYSAAPRGSAPAAAAAAYDRH
|
Transcription factor that may have a role in kidney cell differentiation . Has a critical role in the development of the urogenital tract, the eyes, and the CNS.
|
Q02962
|
P75569
|
PTG3C_MYCPN
|
PTS system glucose-specific EIIA component
|
Mycoplasma
|
MQIKAQDTGQQKKSCLLSNIRNKWKNRNRGSFRQWVGKLSNGLMIPIAVLPIAGIFLGVGDAIAGNAGDLTGLRYFGLFIKNGGDVVFANLPILFAIAIAITFSQDAGVAGFSAFVFWAAMNGFMSSLILPFDKAGKIITDTSTPIAGFKVLYNKSVPVHAIATTLGLRTLSTSVFGGIIVGALTSVLYKKFYAIRLPDVIGFFSGTRFVPIICFVVAIPVALILLMIWPAVSIGLNAIGTGLGFLGGKGYGANSLIFGYIERSLIPFGVHHAFYAPLWYTSAGGSLQEIVNQQVWIRPDFHLSDNYVARVIGWVDPNNSSMYIIPGALNGQNGSSTGNTMSKDLNGALSAYMSKESTAFLTWKDLVDGLTFKGNFDKMAENGLLDGSNKIWLGLNGSGILGKKLLLSDGNVYTITFKTFANTTPIAWSKGAQAVLPLNASSTIVNNPTALAAATQSNNNTNNIKLYPVNSFRVAVESLNPAQYSQGKFPFMLFGIPAAGVAMILAAPKDRRKEAASIVGSAAFTSFLTGITEPFEFTFLFLAPWLFYGVHAVLAAVSFWLMNILGANVGQTFSGSFIDFILYGALPDGRRWLANSYLVPIIGLFLAAIYFPTFYFLIKHFNLATPGRGGKLITKKEYLASKAAAKAEGVSGVAENFTQTQIEAGILLQAYGGKENIVELGACITKLRVTVKNPELVKEEPIKELGAAGVMRTTPTFFVAVFGTRAAVYKSAMQDIIQGKVNWEALQKVINTDQLAVEPKETTPPKEVMPVVQDEIVILSPVNGTLKSLNQVPDETFKQKLVGEGVAIVPSDGHFKAPGEAGVKTELAFPGGHAYIFDIDGIKVMLHIGIDTVQINAKKQPGEPLEVFDIKTKQGEYTKEKSESVVEVDLKKLSKKYNPITPFVVMKESLENFKLVPIRQRGEIKVGQPIFKLVYKKSQA
|
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport.
|
P75569
|
E7KI83
|
GEP3_YEASA
|
Found in mitochondrial proteome protein 38
|
Saccharomyces
|
MLNLCHALRGVRQFSCSVIVKVKCASCSIKLQDQDPSKPGYYTKPKSLPDSKLNPDLQDLKYLLFSQDIQLSKQAIQNDPDLKTKRDLLLRVICKRCSNALHHNNYNPEEFPESTLNDILNYVPRGSNVMHIVPFVEFPLHLDPNVLKRNDLETTLVLTKSDQVFKDKNAVSKKVPIFMKQFLKNTLRIDSNKTFAISALKNWNISMFYNYFKNYTYLLGNPNVGKSTLINTLLQKYLGYKVKIDSTGKINSPSEEVMQEAFTNPKNFFKIQAAGVSHIPNLTRSVQAYQVGGKILFDLPGYSTSTSRLRLEEPIDERWLQRLRKTDLFNRKHIKQKTYESMKGTSQGGCYTVGGIFYLVPPKGSINQIVKYIPGPSKTFKNIEKGIDVFNSCNSSSGTHPLSRYCGIKSVICEKSQYKRYAIPPFIGSIEIVLKDIGYILLRTTGRYEFKGLHEIWIPRGIQVGIREPLENLIESGYQRYIETNGKESSCPRDRPIISSLYEMAPDEADTLNAVKKSYLEKTEKDLSARRFVDDDPYDLVQHLRKKKESLLVLPMVRLAVHLVAPISSNAHVNMNVSKLKRKLGTKYIQKRIYRK
|
Interacts genetically with prohibitins and thus may be involved in the mitochondrial lipid metabolism.
|
E7KI83
|
B3E468
|
RUVB_TRIL1
|
Holliday junction ATP-dependent DNA helicase RuvB
|
Trichlorobacter
|
MERAITPEKRDDDLQFDATLRPRTLQDYIGQEKIRENLKLFIDAAKGRSEALDHVLLYGPPGLGKTTLANIIACEMGVNIKSTSGPVIERPGDLAAILTNLEPHDVLFIDEIHRLSHVVEEILYPAMEDFQLDIIIGQGPSARSIKLDLPRFTLVGATTRAGLLSSPLRDRFGVISRLEFYTHDELAFIVTRSARILGMAIDREGALELARRSRGTPRIANRLLRRVRDYAQVRADGAITLSVVQETLRLLEIDEMGFDQMDRMILLTIIDKFGGGPVGLDTIGAAIGEESDTIEDVYEPFLIQNGFLNRTPRGRVATPAAYQHFGRLTPERPQGSLF
|
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.
|
B3E468
|
O30298
|
BSUHB_ARCFU
|
Inositol-1-phosphatase
|
Archaeoglobus
|
MDERDALRISREIAGEVRKAIASMPLRERVKDVGMGKDGTPTKAADRVAEDAALEILRKERVTVVTEESGVLGEGDVFVALDPLDGTFNATRGIPVYSVSLCFSYSDKLKDAFFGYVYNLATGDEYYADSSGAYRNGERIEVSDAEELYCNAIIYYPDRKFPFKRMRIFGSAATELCFFADGSFDCFLDIRPGKMLRIYDAAAGVFIAEKAGGKVTELDGESLGNKKFDMQERLNIVAANEKLHPKLLELIK
|
Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate and fructose-6-phosphate. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.
|
O30298
|
Q76LV1
|
HS90B_BOVIN
|
Heat shock protein HSP 90-beta
|
Bos
|
MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVTAEEPSAAVPDEIPPLEGDEDASRMEEVD
|
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery. Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription. Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10.
|
Q76LV1
|
Q04L74
|
RS20_STRP2
|
30S ribosomal protein S20
|
Streptococcus
|
MANIKSAIKRAELNVKQNEKNSAQKSAMRTAIKAFEANPSEELFRAASSAIDKAETKGLIHKNKASRDKARLSAKLAK
|
Binds directly to 16S ribosomal RNA.
|
Q04L74
|
Q74N79
|
RL5_NANEQ
|
50S ribosomal protein L5
|
Nanoarchaeum
|
MEHPMRKIRIEKVTLNIGVGESGEKLDKAYELLKRLTGQKPVKTKAKVRVEQWHIRPGLPIGVKVTLRGEKAYKILKEKLLPAVDFKIKASSFTDRGFGFGIPEYIMIPGMKYDPELGLIGLEAYVTLERPGYRVERRRIKRSKVGSRHRLNKEEIIKWAQEELGVQII
|
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. May contact the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
|
Q74N79
|
Q9PLX1
|
RL3_CAMJE
|
50S ribosomal protein L3
|
Campylobacter
|
MEYIVEKIGMSRTITNPSIAVTLLRVVNAKVCEVEGGKALVAYPKGKASNKCVAGQQKKYNLSAEYNRFATLEVANTEAGDLDETPLNEAKILKVSFNTKGRGYSGVMKRHNFAGGPASHGSRFHRRHGSIGNREWPGRVQPGMKMAGHYGNTKVTIKNEVVSYDAENKILVVKGAVPGYNGAMGKIRIAK
|
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
|
Q9PLX1
|
B8CKR1
|
ISPG_SHEPW
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Shewanella
|
MYNESPIIRRKSSRIYVGDVPIGDGAPIAVQSMTNTRTTDVAATVAQIKALENVGADIVRVSVPTMDAAEAFKLIKQQTNVPLVADIHFDYRIALKVAEYGVDCLRINPGNIGNEERIRSVVECARDKNIPIRIGVNGGSLEKELMDKYKEPTPEALLESAMRHVDILDRLNFDQFKVSVKASDVFLAVESYRLLAKQIVQPLHLGITEAGGARAGSVKSAVGLGMLLADGIGDTLRISLAADPVEEIKVGFDILKSLRIRSRGINFIACPSCSRQEFDVISTVNELEQRLEDVVTPMDVSIIGCVVNGPGEALISDIGLTGGNRMSGYYKDGVRQKERFDNNNIVDQLEAKIRAKVAMSESRIPAQDVTK
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
B8CKR1
|
Q5HNH6
|
SYY_STAEQ
|
Tyrosyl-tRNA synthetase
|
Staphylococcus
|
MANALIEDLKWRGLIYQQTDEEGIEELLNKEQVTLYCGADPTADSLHIGHLLPFLTLRRFQEHGHRPIVLIGGGTGMIGDPSGKSEERVLQTESQVEANVKGLSNQMHRLFEFGSDKGAKLVNNKDWLGQISLISFLRDYGKHVGVNYMLGKDSIQTRLEHGISYTEFTYTILQAIDFGYLNRELNCKIQVGGSDQWGNITSGIELMRRMYGQTEAYGLTIPLVTKSDGKKFGKSESGAVWLDPEKTSPYEFYQFWINQSDEDVIKFLKYFTFLEKEEINRLEQSKNEAPHLREAQKALAENVTKFIHGEAALKDAIRISKALFSGDLKSLSAKELKEGFKDVPQVTLSTKTTNIVEALIETGIASSKRQAREDVNNGAIYINGERQQSVDYELSSKDLIEDEITIIRRGKKKYFMVNYQS
|
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).
|
Q5HNH6
|
A1R8A6
|
HEM1_PAEAT
|
Glutamyl-tRNA reductase
|
Paenarthrobacter
|
MVLFSLVATHADIDLETVAQLSNGSSELASAALTDSSVVSGAVVLATCNRYEVYGETANGADLEAARSALVSQISELSGLNEQLVSRSFATHTGPDVTRHLFAVSAGLDSAVVGEREIAGQVRRALITAQQEGTASSGLVRLFQAASKTAKDVGAQTALGSRGLSIVSVALDLATDLAENDDWTTKKVVVFGTGAYAGATMSLLRERGCTDISVYSSSGRAEGFVATRGGTALDADTLPAAVAAADVMIGCSGSDNRVEAADLARVRANSGKPLIAIDLALTHDFDPAVGELDGVELLTLESVRLAAPQEQAESLSQASAIVNGAATSFESEREARSVDTAIVALRRHTMNVLDAEMEKVRARHGCTAAAEEVEFALRRMVKQLLHIPTVRARELAANGQQDDYVAALEALYGIQVEQPQAAAPASECPVDHEQLRSESA
|
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
|
A1R8A6
|
Q33DR2
|
DPS1_MOUSE
|
Trans-prenyltransferase 1
|
Mus
|
MAMRWSCWRRGCSWRPTAVGSPRRERPGCVEPLGTRAASDTRAQIPYFSLMKILMSASPTMHSISQFHQRTPAMCSCRQTQSGEKYSDPFKLGWRDLKGLYEDIRKELHISTRELKDMSEYYFDGKGKAFRPIIVVLMARACNIHHNNAREMQASQRSIALVAEMIHTATLVHDDVIDDASSRRGKHTVNKIWGEKKAVLAGDLILSAASVALARIGNTAVVSMLAQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVSVLGCPDPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGIATGPVLFACQQFPEMNAMIMRRFSLPGDVDRARQYVLQSDGVQQTTYLAQQYCHKAVREIRKLRPSTERDALIQLSESVLTRDK
|
Heterotetrameric enzyme that catalyzes the condensation of farnesyl diphosphate (FPP), which acts as a primer, and isopentenyl diphosphate (IPP) to produce prenyl diphosphates of varying chain lengths and participates in the determination of the side chain of ubiquinone . Supplies nona and decaprenyl diphosphate, the precursors for the side chain of the isoprenoid quinones ubiquinone-9 (Q9)and ubiquinone-10 (Q10) respectively . The enzyme adds isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry .
|
Q33DR2
|
Q9HTC0
|
WBPZ_PSEAE
|
GDP-D-rhamnose:GlcNAc/GalNAc-diphosphate-lipid alpha-1,3-D-rhamnosyltransferase
|
Pseudomonas
|
MRVLHFYKTYLSETVGGIEQVIFQLCESSGSWGIDNHVLTLSSDPHPPVVPFGGHVVHRARLDLQLASTGFSLSVFKQFRELAAEADVVNYHFPWPFMDLVHFLTGMNKPSVVTYHSDIIRQRVLLKLYRPLMSRFLHSVDRIVAASPNYFSTSDVLRQYREKTRVITYGLDKDGYPKPATQRLEHWREKLGPRFFLFVGVMRYYKGLHILLDALQGTDYPVVIVGAGPLQAELYAQAAALGLRNVHFLGRVDDEDKVALLQLSYAMVFPSHLRSEAFGISLLEGAMYGKPMISSEIGTGTSYINIHGETGLVVPPSQPAAFRQAMRWLWEHPQQAEEMGRNAEARYRQLFTAEEMGRRWSELYRELLEEKASSRYVKAAR
|
Non-processive alpha-1,3-D-rhamnosyltransferase . Catalyzes the transfer of one D-rhamnose (D-Rha) residue from donor substrate GDP-D-Rha in alpha-1-3 linkage to both GlcNAc- and GalNAc-diphosphate-lipid acceptor substrates. Is also able to transfer D-mannose (D-Man) to these acceptors at a lower level. Nucleotide sugars GDP-D-Rha, GDP-Fuc, UDP-Gal, UDP-GalNAc, UDP-GlcNAc and CMP-sialic acid cannot act as donor substrates. Only compounds with a diphosphate as the aglycone group can act as acceptor substrates. No activity is detected with compounds containing a diphosphate mimic. Fluorescent undecyl-anthracenyl group-containing compounds, such as GlcNAc-PO(3)-PO(3)-AnthrU and GalNAc-PO(3)-PO(3)-AnthrU, are also good acceptor substrates . Involved in the biosynthesis of the common polysaccharide antigen (CPA), also called A band, which is one of the two major cell surface O-antigens of the P.aeruginosa lipopolysaccharide . Involved in susceptibility to antibiotic colistin .
|
Q9HTC0
|
Q5WLQ1
|
RL24_ALKCK
|
50S ribosomal protein L24
|
Alkalihalobacillus
|
MHVKKGDKVVVITGKDKGKQGTVLEAYPKKSRVLVEGVNMVKKHAKPSQDNPQGGILNQEAPIHSSNVMLVDPKTGERTRVGYKEENGKKVRVAKKSGEIIK
|
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
|
Q5WLQ1
|
G3XD30
|
PILN_PSEAE
|
Type IV pilus inner membrane component PilN
|
Pseudomonas
|
MARINLLPWREELREQRKQQFLVILGGVLVASAALVFLGDQYFTAAIENQNARNDFLRKEIVVLDARIKEISELKSRRQQLLERMKIIQDLQGNRPIIGRVFDQLVRTLPDGVYFTDLKMTGKNIAIAGAAESNNRVSNLMRNMDASEWLTAPTLNEVKAVTQGAVDQANVFQLTVQQTQPGEEDAKAKHGVAQGAKK
|
Inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus . In turn, associates with PilM and facilitates PilM functionally relevant structural changes .
|
G3XD30
|
Q1EGL0
|
LGI3_PANTR
|
Leucine-rich glioma-inactivated protein 3
|
Pan
|
MAGLRARGGPGPGLLALSALGFCLMLQVSAKRPPKTPPCPPSCSCTRDTAFCVDSKAVPRNLPSEVISLTLVNAAFSEIQDGAFSHLPLLQFLLLNSNKFTLIGDNAFTGLSHLQYLFIENNDIWALSKFTFRGLKSLTHLSLANNNLQTLPRDIFRPLDILNDLDLRGNSLNCDCKVKWLVEWLAHTNTTVAPIYCASPPRFQEHKVQDLPLREFDCITTDFVLYQTLSFPAVSAEPFLYSSDLYLALAQPGVSACTILKWDYVERQLRDYDRIPAPSAVHCKPMVVDSQLYVVVAQLFGGSYIYHWDPNTTRFTRLQDIDPQRVRKPNDLEAFRIDGDWYFAVADSSKAGATSLYRWHQNGFYSHQALHPWHRDTDLEFVDGEGKPRLIVSSSSQAPVIYQWSRTQKQFVAQGEVTQVPDAQAVKHFRAGRDSYLCLSRYIGDSKILRWEGTRFSEVQALPSRGSLALQPFLVGGRRYLALGSDFSFTQIYQWDEGRQKFVRFQELAVQAPRAFCYMPAGDAQLLLAPSFKGQTLVYRHVVVDLSA
|
May participate in the regulation of neuronal exocytosis.
|
Q1EGL0
|
A8F3S3
|
RSMG_PSELT
|
16S rRNA 7-methylguanosine methyltransferase
|
Pseudothermotoga
|
MNKVAEIFREYGIKIDDSKTEKLDSYIDLLISAPINLTSLRDKEYAIHKHIVDIVFPVKMLTGKLLDVGTGGGIPGLILAILFPINATLVESVRKKVMWLEKILNMLNIGNVNLLCSRAEKLPADKKESFDIVTARAVSELRILLELCAPFCKVGGRLFFYKGPNWKQEYDAAHNAMKTLNVETIEIVSYTLKTGEKRVLLQFQKVGRTPDNYPRETKKILKNPL
|
Specifically methylates the N7 position of a guanine in 16S rRNA.
|
A8F3S3
|
Q8CWZ6
|
TIG_STRMU
|
PPIase
|
Streptococcus
|
MSTSFENKATNRGVVTFTISQDKIKPALDQAFNKVKKDLTAPGFRKGHMPRTVFNQKFGEEALYEEALNSILPAAYEEAVAELELDVVTQPKVDVKSMEKGKDWEITAEVVTKPEVKLGDYKNLEVSVEESKEVTDAEVDEKIERERNNLAELVLKEDAAVEGDTVVIDFVGSVDGVEFDGGKGDNFSLELGSGQFIPGFEDQLVGKKAGETVKVNVTFPEDYQSADLAGKDATFVTTIHEVKAKEVPELDDELAKDIDEEVETLDELKAKYRKELEATKETAYNDAVEAAAIDLAVANAEIVELPEEMIHDEVQRAMQEFMGNMQRQGISSEMYFQLTGTTEEDLRKQYEADADKRVKTNLVIEAVAKAEGFEATDEEIEKEISDLATEYKMEAEQVRSLLSPDMLKHDIAMKKAVNVITDSAKVK
|
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
|
Q8CWZ6
|
Q8ZL58
|
TAGAD_SALTY
|
StTGD
|
Salmonella
|
MALSANSDAVTYAKAANTRTAAETGDRIEWVKLSLAFLPLATPVSDAKVLTGRQKPLTEVAIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAHAKEIADNLLGEDPNDIDKIYTKLLWAGASVGRSGMAVQAISPIDIALWDMKAKRAGLPLAKLLGAHRDSVQCYNTSGGFLHTPLDQVLKNVVISRENGIGGIKLKVGQPNCAEDIRRLTAVREALGDEFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQLAAALDTPIATGEMLTSFREHEQLILGNASDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHFAMEVHLHLSAAYPLEPWLEHFEWLNPLFNEQLELRDGRMWISDRHGLGFTLSEQARRWTQLTCEFGKRP
|
Catalyzes the efficient dehydration of both L-talarate (also called L-altrarate) and galactarate to 5-keto-4-deoxy-D-glucarate (5-KDG) . Also catalyzes the epimerization of L-talarate to galactarate; epimerization occurs in competition with dehydration. Is required for the utilization of L-talarate as a carbon source. Also functions in galactarate utilization. Is not active on other acid sugars .
|
Q8ZL58
|
Q8N6L1
|
KTAP2_HUMAN
|
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2
|
Homo
|
MVVGTGTSLALSSLLSLLLFAGMQMYSRQLASTEWLTIQGGLLGSGLFVFSLTAFNNLENLVFGKGFQAKIFPEILLCLLLALFASGLIHRVCVTTCFIFSMVGLYYINKISSTLYQAAAPVLTPAKVTGKSKKRN
|
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity . May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1 .
|
Q8N6L1
|
A1B946
|
CCME_PARDP
|
Heme chaperone CcmE
|
Paracoccus
|
MKSLKKKRRIQILVAAAVALVLAVGLIGYGFRDGINLYRSPSQMAENPPEAGEVFRLGGLVEDGSLVRGASETVTFRVTDGGATVPVRFTGVLPDLFSEGQGMIGTGRMEGETFVASEILAKHDENYMPREVMDSLKEQGVYQEPNS
|
Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
|
A1B946
|
A7M969
|
PSBE_CUSRE
|
PSII reaction center subunit V
|
Cuscuta subgen. Monogynella
|
MSGNTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESRQGIPLITGRFDSLEQLNEFSRSF
|
This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). 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.
|
A7M969
|
O52377
|
AROQ_CORGL
|
Type II DHQase
|
Corynebacterium
|
MPGKILLLNGPNLNMLGKREPDIYGHDTLEDVVALATAEAAKHGLEVEALQSNHEGELIDALHNARGTHIGCVINPGGLTHTSVALLDAVKASELPTVEVHISNPHAREEFRHHSYISLAAVSVIAGAGIQGYRFAVDILANLKK
|
Catalyzes a trans-dehydration via an enolate intermediate.
|
O52377
|
A7H2P1
|
PRMA_CAMJD
|
Ribosomal protein L11 methyltransferase
|
Campylobacter
|
MQKKYYELFFIVEEQYKNLFLGFAFDLGIEAIEEKDNGIYIRSHESLEELSWALEIFAQKLTTTFNLNHKIISNLSLVEKENKDWIQEYKKGIKPILVDNVYIHTTWQEEKKNCINIKINPALAFGSGHHESTHSCVKFLQKFSKSKLRALDLGCGSGILGIIMAKFGCNVEICDTDELAIDSSLENARLNGVDFHKAWCGSIDKANGLYNLIVANIIADVILILEKDIKNHLEDNAILILSGILDKYSTRIKEKFQDLELIDEMQINEWCSFVYKNNKKDK
|
Methylates ribosomal protein L11.
|
A7H2P1
|
Q9SCY0
|
PGMP_ARATH
|
Glucose phosphomutase
|
Arabidopsis
|
MTSTYTRFDTVFLFSRFAGAKYSPLLPSPSFTLSTSGIHIRTKPNSRFHSIIASSSSSSVVAGTDSIEIKSLPTKPIEGQKTGTSGLRKKVKVFMEDNYLANWIQALFNSLPLEDYKNATLVLGGDGRYFNKEASQIIIKIAAGNGVGQILVGKEGILSTPAVSAVIRKRKANGGFIMSASHNPGGPEYDWGIKFNYSSGQPAPETITDKIYGNTLSISEIKVAEIPDIDLSQVGVTKYGNFSVEVIDPVSDYLELMEDVFDFDLIRGLLSRSDFGFMFDAMHAVTGAYAKPIFVDNLGAKPDSISNGVPLEDFGHGHPDPNLTYAKDLVDVMYRDNGPDFGAASDGDGDRNMVLGNKFFVTPSDSVAIIAANAQEAIPYFRAGPKGLARSMPTSGALDRVAEKLKLPFFEVPTGWKFFGNLMDAGKLSICGEESFGTGSDHIREKDGIWAVLAWLSILAHRNKDTKPGDKLVSVADVVKEYWATYGRNFFSRYDYEECESEGANKMIEYLREILSKSKAGDVYGNYVLQFADDFSYTDPVDGSVASKQGVRFVFTDGSRIIFRLSGTGSAGATVRIYIEQFEPDVSKHDVDAQIALKPLIDLALSVSKLKDFTGREKPTVIT
|
This enzyme participates in both the breakdown and synthesis of glucose (Probable). Factor that affects seed oil content . Accumulated starch in young embryos may play an important role in providing carbon resources for seed storage lipid biosynthesis in oilseed plants (Probable).
|
Q9SCY0
|
C1KYC4
|
YDJC_LISMC
|
Carbohydrate deacetylase
|
Listeria
|
MKIIFNADDFGISPGAVYGILESYKRGVVKSTTLLANSPAFDLAVEVAKENPGLDIGAHLTLTFGSPVLQGLETLTDDDGRFRRNYTSLENGLADVDMNEVERELTAQIEKILDAGITISHFDTHHSIEPLIYPVQHKLAEKYGVSIRRHSDVSDFGAIKTPDLFATEFYADGVSFETIKKLVQKHIGTNDVVEVMTHPAFIDETLREISSYVEPRIKEVSILTSRELQAYLGQQEVEIISFRDL
|
Probably catalyzes the deacetylation of acetylated carbohydrates an important step in the degradation of oligosaccharides.
|
C1KYC4
|
Q250M7
|
RL22_DESHY
|
50S ribosomal protein L22
|
Desulfitobacterium
|
MQQAKAIARYVRISPRKVRQVVDLIRGKNVSDALAILQFTPKGATEPVTKVLQSAVANAEHNYEMDTDALIVKEIYVDEGPTLKRIKPRAMGRADQIRKRTSHITVVVVEKKEG
|
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.
|
Q250M7
|
C9SEV5
|
AMPP3_VERA1
|
Prolidase
|
Verticillium
|
MASGDNVDYEAVMVDEFDALNIEVRVSAGPSSSVPGAALSAPRCPGMRALPLKAPVMSTPVPAAAPLPTPPAVDDGPSAVGVGNVPPAVDDVPSAVDDVVIQKETTKYSAKLHAAKVADELKASAGLVFLPGEPSRTYEYSDMGPAFSSNAATSSTSPASTSLTPRKVLYNGRVPSIKDVLAASDVDEVRHMQDLPAFLHAYAHQHDKATVYLLDASQSHPALVDNARVHIDTAALRPAMDEARVTKTAHEIALIREANAVSSAAHRAVMRHIRRFASERQVAALFTAECTVRGAPTQAYAPIAGSGPNAATLHYGANDEPLAGRHVLVLDAGCEVNCYASDVTRTLPLGPTGHFTPEARHIYDLVERMQEACVAAVAPGLLYYSLHLKASAIALRGLLRLGILKGDEKAIWAAGTVAAFFPHGLGHHIGLETHDVTGRDRLLLAAGEREPRAKRDAVSAEMLVGLAAAVATGPPYRGKQMLRPGMVVTVEPGIYFNKDYIEGYFLREDKHRAFIDRDVLARYYPVGGVRIEDCILVTDDGYENLTKAPKGEDMLRIIRGEAQ
|
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
|
C9SEV5
|
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