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
|
|---|---|---|---|---|---|---|
A2C4V4
|
PSAB_PROM1
|
PsaB
|
Prochlorococcus
|
MATKFPSFSQGLAQDPTTRRIWYGIATAHDFESHDGMTEEQLYQKLFSTHFGHLAIIGLWVAGNLFHIAWQGNFEQWVLDPLHTRPIAHAIWDPHFGQGLTDALTQAGATSPVNIAYSGLYHWWYTIGMRTNEQLFQGAIFINILVCWLLFAGWLHLQPKYRPSLAWFKNAESQLNHHLAVLFGFSSIAWTGHLIHVAIPESRGIHVGWENWLTVMPHPEGLTPFFSGNWGAYAQNPDSIDAVFGTSQGAGTAIFTFLGGLHPQSESLWLTDIAHHHLAIGVVFIIAGHMYRTNFGIGHSLKEIIEAHNTSHPKDPHRGYFGIKHNGLFETVNNSLHFQLGLALASLGVACSLVAQHMGALPSYAFIARDYTTQSALYTHHQYIAMFLMVGAFSHGAIFFVRDYDPELNKDNVLARILSTKEALISHLSWVTMLLGFHTLGIYVHNDVVVAFGTPEKQILIEPVFAQFAQAASGKMMYGFNALLANASSSASIAANSMPGNHYWMDMINRPDALTNFLPIGPADFLVHHAIALGLHTTALILIKGALDARGTKLIPDKKDLGFAFPCDGPGRGGTCDSSSWDATYLAMFWALNTIAWITFYWHWKHLAIWMGNTAQFNESGTYLMGWFRDYLWLNSSQLINGYNPFGVNALSPWAWMFLFGHLIWATGFMFLISWRGYWQELIETLVWAHQRTPIANLVGWRDKPVALSIVQARLVGLTHFTVGNFVTFGAFVIASTSGKFG
|
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.
|
A2C4V4
|
P09820
|
FIXC_RHIME
|
Protein FixC
|
Sinorhizobium
|
MTKEKFDAIVVGAGMSGNAAAYAMASRGLKVLQLERGEYPGSKNVQGAIMYANMLEAIIPDFRNDAPLERHLVEQRFWIMDDTSHTGMHYRSDDFNEVTPNRYTIIRAQFDKWLSRKVCEAGGTVLCETTATGLEWDSAGKAIGVRTDRAGDVVLADVVVLAEGVNGLLGTRAGLREMPKSKNVALAVKELHFLPEEVIAERFGLTGDEGCVIEAGGTISRGMAGLGFLYTNKESISLGIGCLISNFAETMERPYALLDAFKRHPSIQPLIAGSEVKEYAAHLIPEGGFNAIPRLCGNGWVVVGDAAQLNNAVHREGSNLAMASGRMAGEAISIIKSRGGVMDKASLSLYKTMLDKSFVVEDLSKQKDMPSLLHTNSPNFFTTYPQLISHAAQNFVRVDGTPKIEREIATTAAFLRARSRWGLVSDAVRLASAWR
|
Could be required for the formation of a functional nitrogenase Fe protein. Probably accepts electrons from FixA/FixB and reduces a quinone.
|
P09820
|
A3QEP9
|
CMOA_SHELP
|
Carboxy-S-adenosyl-L-methionine synthase
|
Shewanella
|
MNSTQDTIYAQACEHISDFQFDDRVAGVFSDMIRRSVPGYGQIINTLGDFADKCVTPNSKIYDLGCSLGAATLSVRRRIEGRGCEIIAVDNSESMIERCKQNLSAYVSETPVDLICADIRDIEIQDASMVILNFTMQFLAPEDRQTLIAKIYQGLKPGGILVLSEKLVFEDEPVQHLLDELHLDFKRANGYSELEISQKRSSLEHVMKPDTLPQHQQRLKAQGFSHFSVWFQCFNFASMVAIK
|
Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
|
A3QEP9
|
Q5E6U4
|
YBEY_ALIF1
|
Endoribonuclease YbeY
|
Aliivibrio
|
MSIELDLQIACENENGLPSEKELMTWLNAVIPQFQPQAELTIRIVDEKESHELNHEYRGKDKPTNVLSFPFEAPPGLELNLLGDLIICRQVVEEEAIEQNKPLLAHWAHMVVHGSLHLLGYDHIEDDEAEEMESLETELMQGMGFEDPYIAEK
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
Q5E6U4
|
O75509
|
TNR21_HUMAN
|
Death receptor 6
|
Homo
|
MGTSPSSSTALASCSRIARRATATMIAGSLLLLGFLSTTTAQPEQKASNLIGTYRHVDRATGQVLTCDKCPAGTYVSEHCTNTSLRVCSSCPVGTFTRHENGIEKCHDCSQPCPWPMIEKLPCAALTDRECTCPPGMFQSNATCAPHTVCPVGWGVRKKGTETEDVRCKQCARGTFSDVPSSVMKCKAYTDCLSQNLVVIKPGTKETDNVCGTLPSFSSSTSPSPGTAIFPRPEHMETHEVPSSTYVPKGMNSTESNSSASVRPKVLSSIQEGTVPDNTSSARGKEDVNKTLPNLQVVNHQQGPHHRHILKLLPSMEATGGEKSSTPIKGPKRGHPRQNLHKHFDINEHLPWMIVLFLLLVLVVIVVCSIRKSSRTLKKGPRQDPSAIVEKAGLKKSMTPTQNREKWIYYCNGHGIDILKLVAAQVGSQWKDIYQFLCNASEREVAAFSNGYTADHERAYAALQHWTIRGPEASLAQLISALRQHRRNDVVEKIRGLMEDTTQLETDKLALPMSPSPLSPSPIPSPNAKLENSALLTVEPSPQDKNKGFFVDESEPLLRCDSTSSGSSALSRNGSFITKEKKDTVLRQVRLDPCDLQPIFDDMLHFLNPEELRVIEEIPQAEDKLDRLFEIIGVKSQEASQTLLDSVYSHLPDLL
|
Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B. Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm. Plays a role in neuronal apoptosis, including apoptosis in response to amyloid peptides derived from APP, and is required for both normal cell body death and axonal pruning. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). N-APP binds TNFRSF21; this triggers caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Negatively regulates oligodendrocyte survival, maturation and myelination. Plays a role in signaling cascades triggered by stimulation of T-cell receptors, in the adaptive immune response and in the regulation of T-cell differentiation and proliferation. Negatively regulates T-cell responses and the release of cytokines such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells. Negatively regulates the production of IgG, IgM and IgM in response to antigens. May inhibit the activation of JNK in response to T-cell stimulation.
|
O75509
|
P80961
|
AFP4_MYOOC
|
Antifreeze protein LS-12
|
Myoxocephalus
|
MKFSLVATIVLLALAQGSFAQGAADLESLGQYFEEMKTKLIQDMTEIIRSQDLANQAQAFVEDKKTQLQPLVAQIQEQMKTVATNVEEQIRPLTANVQAHLQPQIDNFQKQMEAIIKKLTDQTMAIEN
|
Antifreeze proteins lower the blood freezing point.
|
P80961
|
A5D4K4
|
THIE_PELTS
|
Thiamine-phosphate pyrophosphorylase
|
Pelotomaculum
|
MVRRRGLSGLLEADIYGITAWEYSLGRSNIEVVAQMIEAGIKVIQYREKERPARQKYEECLKIREMTREAGVTFIVNDHVDLALLVDADGVHLGQDDLPADRVRELVGDKMIIGLSTHSPAQARAAEKMGVDYIGVGPIFATKTKKDVCDPVGLEYLEFVVKNISLPFVAIGGIKEHNIAEVSSRGAKCIALVTEIVGAEDIKAKVRALRAIISRKED
|
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
|
A5D4K4
|
P32552
|
RS7_HALMA
|
HmaS7
|
Haloarcula
|
MSAEDTPEADADAAEESEPETARAKLFGEWDITDIEYSDPSTERYITVTPIAHTMGRHADKQFKKSEISIVERLINRLMQTDENTGKKQLATSIVTEAFELVHERTDENPIQVLVSAVENSAPREETVRLKYGGISVPKAVDVAPQRRVDQALKFLAEGVYGGSFKTTTTAAEALAQQLIGAANDDVQTYAVNQKEEKERVAAAAR
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center.
|
P32552
|
A7NR50
|
RS14Z_ROSCS
|
30S ribosomal protein S14 type Z
|
Roseiflexus
|
MARKALMVKAQRPQKYTVRAYNRCKICGRSRAYMRKFGMCRICFREHALRGLIPGVTKSSW
|
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.
|
A7NR50
|
Q3AP13
|
ATPB_CHLCH
|
F-ATPase subunit beta
|
Chlorobium
|
MQEGKISQIIGPVVDVDFPEGRLPSILDALTVKREDGSKLVLETQQHLGEERVRTVAMESTDGLVRGMGVVNTGAAIQVPVGAEVLGRMLNVVGDPIDGRGPVNSKKTYSIHRSAPKFEDISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVLIMELINNIAKQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDEENRDVLLFVDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQAIYVPADDLTDPAPATAFTHLDATTVLSRSIAELGIYPAVDPLDSTSRILDPNVVGDDHYNTAQAVKQLLQRYKDLQDIIAILGMDELSDEDKLVVSRARKVQRFLSQPFFVAEAFTGLAGKYVKLEDTIKGFKEIIAGKHDKLPENAFYLVGTIEEAIEKAKTL
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
Q3AP13
|
A6UPJ0
|
RPIA_METVS
|
Phosphoriboisomerase A
|
Methanococcus
|
MAKPKKSDEEVSIDSDSLKIKVAKEAAKLIKDEMVVGLGSGSTANLFIQELGKRVIEEELYIYGVPTSFDSRMMANQSGIPLISLDQCGEIDIAIDGADEIDKKTFSLIKGGGGCHTMEKIVDYYAKEFVVLADESKMVDSLGENTPVPLEVIPFSYSTVLSKLLKINAAPAIRSGSGKMGPVITDNGNMIIDVFINIEDAEETETMLNSIPGVLENGIFTKCDKVLIGTSKKVEVLKK
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
A6UPJ0
|
B5RCZ3
|
RODZ_SALG2
|
Cytoskeleton protein RodZ
|
Salmonella
|
MNTEATHDQNEAQTTGVRLRNAREQLGLSQQAVAERLCLKVSTVRDIEEDKAPSDLASTFLRGYIRSYARLVHVPEEELLPGLEKQAPLRAAKVAPMQSFSLGKRRKKRDGWLMSFTWLVLFVVVGLTGAWWWQNHKAHQEEITTMADQSTAGLNADKDSGQSVPLDTGAVTSQDTTPAQTAPAPATPVDSTAATQTPAPTAAATQNTVVAPSQANVDTAATSAAPAATETPSALPTSQAGVAAPAADPNALVMNFTADCWLEVTDATGKRLFSGMQRKDGNLNLTGQAPYKLKIGAPAAVQIQYQGKPVDLSRFIRTNQVARLTLNAEPTPAQ
|
Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis.
|
B5RCZ3
|
P0A4H3
|
BVGA_BORBR
|
Virulence factors putative positive transcription regulator BvgA
|
Bordetella
|
MYNKVLIIDDHPVLRFAVRVLMEKEGFEVIGETDNGIDGLKIAREKIPNLVVLDIGIPKLDGLEVIARLQSLGLPLRVLVLTGQPPSLFARRCLNSGAAGFVCKHENLHEVINAAKAVMAGYTYFPSTTLSEMRMGDNAKSDSTLISVLSNRELTVLQLLAQGMSNKDIADSMFLSNKTVSTYKTRLLQKLNATSLVELIDLAKRNNLA
|
Member of the two-component regulatory system BvgS/BvgA. Activates the transcription of virulence genes.
|
P0A4H3
|
Q04VC9
|
GRPE_LEPBJ
|
HSP-70 cofactor
|
Leptospira
|
MAETSNSENKTSEEAKASEKNSRSITLEETKLENMNSEESTQTTESTQAQAAEAADSELSLQSELDAAKKEVESLKDSWARERAEFQNFKRRSAQEFVSIRKEAVKSLVSGFLNPIDNLERVGATQSPSEELKPFVEGVAMILKEFYAVLEKSNVIRFDPKGESFDPMSMEALSSEEGDQYSEETVIDVYQAGYYYKENEDKFTLRPARVRIGKPKS
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
|
Q04VC9
|
Q9PD94
|
HSLU_XYLFA
|
Unfoldase HslU
|
Xylella
|
MPSKTDFTSSTMTPREIVQELDRHIVGQQAAKRSVAIALRNRWRRMQLPEELRNEVMPKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEVGYVGKDVEQIGRDLVDTAVKMYREQAKVRVRTQAEEYAEERILDVLLPRRSVGIGFDVDADVIRQEPSAHESETRAKFRRMLRSGELEEREIELDVAVNVSMDIMTPPGMEEMGQQLRQMFSNIGGGKSQKRKLTIKAARPLLIEEEAAKLVNEDEIRAAAIEACEQNGIVFIDEIDKVVKRGDTVGGGDVSREGVQRDLLPLVEGSNVSTKYGTIRTNHILFIASGAFHLTKPSDLIPELQGRFPIRVELDALSKADFIRILTEPKAALTKQYQELLKTEGVSLDFTEDAIDRIAEIAYLVNERQENIGARRLHTVLERLLEMLSYESPDRDGESVTVDADYVNAHLGELVKDPDLSRYIL
|
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.
|
Q9PD94
|
O80507
|
CSK2E_ARATH
|
Putative casein kinase II subunit beta-4
|
Arabidopsis
|
MYKDRSGGGIMGGGGSSRSEILGGAIDRKRINDALDKHLKKSSPSTSRVFTSKDKDSVPSTSTAKSQLHSRSPDVESDTDSEGSDVSGSEGDDTSWISWFCNLRGNEFFCEVDEDYIQDDFNLCGLSGQVPYYDYALDLILDVESSNGDMFTEEQHEMVESAAEMLYGLIHVRYILTTKGMAAMMEKYKNYDFGRCPRVFCCGQSCLPVGQSDIPRSSTVKIYCPKCEDIYYPRSKYQGNIDGAYFGTTFPHLFLMAYGNMKPQKPAQNYVPKIFGFKVHNKQ
|
Plays a complex role in regulating the basal catalytic activity of the alpha subunit. The tetrameric holoenzyme CK2, composed of two alpha and two beta subunits, phosphorylates the transcription factor PIF1 after an exposure to light, resulting in a proteasome-dependent degradation of PIF1 and promotion of photomorphogenesis . CK2 phosphorylates translation initiation factors. May participate in the regulation of the initiation of translation .
|
O80507
|
Q57IX6
|
HSLO_SALCH
|
Heat shock protein 33 homolog
|
Salmonella
|
MPQHDQLHRYLFENFAVRGELVTVSETLQQILDNHTYPQPVKTVLAELLVATSLLTATLKFAGDITVQLQGDGPLSLAVINGNNQQQMRGVARVQGDIPDNADLKTLVGNGYLVITITPEEGERYQGVVGLEGDTLAACLEDYFLRSEQLPTRLFIRTGDVDGKPAAGGMLLQVMPAQNAQAEDFDHLAMLTETIKSEELLTLPANDVLWRLYHEEEVTLYDPQNVEFKCTCSRERCAGALKTLPDEEVDSILAEEGEIDMHCDYCGNHYLFNAMDIAEIRNNASPADPQVH
|
Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
|
Q57IX6
|
A8FKW6
|
SYP_CAMJ8
|
Prolyl-tRNA synthetase
|
Campylobacter
|
MRFTKFYAPSLKEAPKDASLPSHIFLTRAGFIEQIGSGLYNFLPLGKRVLDKIKNIVKEEMDKAGAQEVNLSFITPASLWQESGRYNVFGKELLRFKDRKENEFVLGPTHEEAMLSLVKNKITSYKQLPLHLYQIGLKFRDEARPRFGLLRCREFLMKDGYSFHANEEDLGCEFELMYKTYSQILQRMGLDFRAVEADSGAIGGSGSKEFMVLAKNGEDDILICENCDYAANVEAAKRAKKTCQDERPEANYASKFHTPNIKTIDSLAQFFKINAFYTIKAVVKKAIYENESKLVVFFIRGSDDLQEIKAQNACSALELVDASEEELEKAGLVAGFIGFVGLKDIDFYIDFELENEKQMIMGANEKDYHLIGIDVVNLNKDRFKDLIEVKEGDCCAKCGAKLKQSKGIEVGHIFKLGQKYSKAMNANFLDENGKSQPFYMGCYGIGVSRLLAVAIEASHDEKGCIWNKTLAPFVLEIIVSNLKDEKALEFANKLYEDLTNLGLEVLLDDRNERFGVKMNDFELMGFPYALVIGKGLENNEIELIQREGLVKELIKTDELMEILKKKVL
|
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
|
A8FKW6
|
Q3ZJ61
|
PSAI_TUPAK
|
Photosystem I reaction center subunit VIII
|
Tupiella
|
MAASFLPSILVPLVGLIFPAIAMTSLFIYIEKQEVN
|
May help in the organization of the PsaL subunit.
|
Q3ZJ61
|
Q7UZY1
|
LIPA1_PROMP
|
Sulfur insertion protein LipA 1
|
Prochlorococcus
|
MTNISKNAVTKPDWLRVKAPQVERIGNTANLLSDLKLNTVCQEASCPNIGECFASGTATFLIMGPGCTRACPYCDIDFDRSKRDLDPTEPDRLAEAVFRLKLKHVVITSVNRDDLDDGGASQFYKCVSEVRKKSPETTIELLIPDLCGNWSALEKILDSRPNVLNHNIETVSALYRKVRPQGNYQRTLELLKRTREYFPSVYTKSGFMLGLGEKDDEVLTLLMDLRKNDVDIVTIGQYLSPGPKHLQVQRFVTPSKFNYFKLFGENELGFMQVVSSPLTRSSYHAEEIQKLMKKFPR
|
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
|
Q7UZY1
|
Q0JB89
|
MYB58_ORYSJ
|
Probable transcription factor MYB58
|
Oryza sativa
|
MARAPGGVRRRSGRRGAGGGGAGGGGEALRKGPWMAEEDEVLLEHVRTHGPMDWSSIRSKGLLPRTGKSCRLRWVNKLRPNLKSGCKFTAEEERVVIELQAQFGNKWARIATYLQGRTDNDVKNFWSTRQKRLARLLRGPLPAARPNKHNSGKGKAPSSSSLDSQTATFHQSSASLDQASLEGNSLGWQCREAAPFMGYDQACSGFFAFEGPLPLQLLPPADGEASSSNAAQSAPPPLLFDQPPYPLINFPGWPERYVDVGHGFVDAGAMDGLAYQELLPMVQSVPMIMPFFGMECAHDAVKHGAFDDLPPNMFDDAVDQPPPPPPPPPPPSPSPSPSRDDVL
|
Probable transcription factor.
|
Q0JB89
|
A7FVM3
|
PDXA2_CLOB1
|
Putative D-threonate 4-phosphate dehydrogenase
|
Clostridium
|
MINNKPIIGIPIGDPAGVGPEIVVKSLTEAEVYEKCNPILIGDAKVIKQAMGFCNVNLNINSIKKADEGKFTLGTIDLIDLNNIDIDELKIGKVQGIAGKAAFEYIKKSVEMAKEGELDAIATTPINKESLREGNVNYIGHTEILADLTDTEDPLTMFEVRGMRVFFLTRHVSLRKACDLVTKERVLDYIIRCSEALEKLGVKDGKMAVAGLNPHSGEHGLFGDEEMKAVVPAIEEAQKMGYKVEGPIGADSVFHLALKGRYNSVLSLYHDQGHIATKTLDFERTIAVTNGMPILRTSVDHGTAFDIAGTGQASSVSMVEAIILAAKYSPKFKK
|
Catalyzes the NAD-dependent oxidation and subsequent decarboxylation of D-threonate 4-phosphate to produce dihydroxyacetone phosphate (DHAP).
|
A7FVM3
|
P39084
|
RLXN_LITCT
|
Ranalexin
|
Lithobates
|
MFTLKKSLLLLFFLGTINLSLCEEERNAEEERRDNPDERDVEVEKRFLGGLIKIVPAMICAVTKKC
|
Potent microbicidal activity, active against S.aureus and E.coli. It acts as well as a membrane-disruptive agent at higher concentrations.
|
P39084
|
A9M881
|
PROB_BRUC2
|
Gamma-glutamyl kinase
|
Brucella
|
MLKKLKDYRRIVVKIGSALLVDRATGLKREWLESLGQDIAALQHAGVEVLVVSSGAIALGRTVLGLPKKALKLEESQAAAAAGQIALAKAYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEIRYGDNDRLAARVATMMGADLLILLSDIDGLYTAPPHKNPDAQFLPFVETITPQIEAMAGAAASELSRGGMKTKLDAGKIANAAGTAMIITSGTRFGPLSAIDRGERATLFEAAHAPVNAWKTWISGNLEPAGRLTVDAGAVKALKSGKSLLPAGVKEVDGDFERGDTVAVMNEDGREIARGLIAYDAADARKVAGHKSDEISAILGYDARAAMIHRNDLVVRAASDAKAA
|
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
|
A9M881
|
Q4FNA8
|
RECR_PELUB
|
Recombination protein RecR
|
Candidatus Pelagibacter
|
MQNINEIEELIKLISKLPGLGPKSAKRIVLKLINNRDELVKPMANTLAQVYKNVIRCQSCGTLKSNSLGCNNCENSKEKYNKICVVEDIADQWSIENSNIYKGYFHILGGTISSAGQRKEDLLINSLVERVSRENIEEVILATSATVEGQTTAYYIEDSLKKTSTKVTKLAQGLPVGGEIESLDDGTLYSAFKNRTGIKTNSD
|
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.
|
Q4FNA8
|
P0AFF4
|
NUPG_ECOLI
|
Nucleoside-transport system protein NupG
|
Escherichia
|
MNLKLQLKILSFLQFCLWGSWLTTLGSYMFVTLKFDGASIGAVYSSLGIAAVFMPALLGIVADKWLSAKWVYAICHTIGAITLFMAAQVTTPEAMFLVILINSFAYMPTLGLINTISYYRLQNAGMDIVTDFPPIRIWGTIGFIMAMWVVSLSGFELSHMQLYIGAALSAILVLFTLTLPHIPVAKQQANQSWTTLLGLDAFALFKNKRMAIFFIFSMLLGAELQITNMFGNTFLHSFDKDPMFASSFIVQHASIIMSISQISETLFILTIPFFLSRYGIKNVMMISIVAWILRFALFAYGDPTPFGTVLLVLSMIVYGCAFDFFNISGSVFVEKEVSPAIRASAQGMFLMMTNGFGCILGGIVSGKVVEMYTQNGITDWQTVWLIFAGYSVVLAFAFMAMFKYKHVRVPTGTQTVSH
|
Broad-specificity transporter of purine and pyrimidine nucleosides . Can transport adenosine, uridine, thymidine, cytidine, deoxycytidine, guanosine and inosine . Can also transport xanthosine, but with a very low affinity . Transport is driven by a proton motive force .
|
P0AFF4
|
Q931U2
|
PT1_STAAM
|
Phosphotransferase system, enzyme I
|
Staphylococcus
|
MSKLIKGIAASDGVAIAKAYLLVEPDLTFDKNEKVTDVEGEVAKFNSAIEASKVELTKIRNNAEVQLGADKAAIFDAHLLVLDDPELIQPIQDKIKNENANAATALTDVTTQFVTIFESMDNEYMKERAADIRDVSKRVLSHILGVELPNPSMIDESVVIVGNDLTPSDTAQLNKEFVQGFATNIGGRTSHSAIMSRSLEIPAIVGTKSITQEVKQGDIIIVDGLNGDVIVNPTEDELIAYQDKRECYFADKKELQKLRDADTVTVDGVHAELAANIGTPNDLPGVIENGAQGIGLYRTEFLYMGRDQMPTEEEQFEAYKEVLEAMDGKRVVVRTLDIGGDKELSYLNLPEEMNPFLGYRAIRLCLAQQDIFRPQLRALLRASVYGKLNIMFPMVATINEFREAKAILLEEKENLKNEGHDISDDIELGIMVEIPATAALADVFAKEVDFFSIGTNDLIQYTLAADRMSERVSYLYQPYNPSILRLVKQVIEASHKEGKWTGMCGEMAGDETAIPLLLGLGLDEFSMSATSILKARRQINGLSKNEMTELANRAVDCATQEEVIELVNNYVK
|
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
|
Q931U2
|
A8ID68
|
TRMFO_AZOC5
|
Folate-dependent tRNA(M-5-U54)-methyltransferase
|
Azorhizobium
|
MSQTSLQPVHVVGGGLAGSEAAFQLAERGVPVVLHEMRPVRGTEAHHTDGLAELVCSNSFRSDDAQTNAVGVLHAEMRRAGSLILRCADANQVPAGGALAVDRDGFSQAVTAALAEHPLVEIRREEVTAIPPEEWDNVIIATGPLTSPALAQAVLELTGESALAFFDAIAPIVHLDSIDLSKAWFQSRYDKVGPGGTGADYINCPLDKEQYEAFVDALLASEKVPLRDFEAKTPYFDGCLPIEVMAERGRETLRFGPLKPVGLTNPHNPDVKPHAVIQLRQDNKLGTLYNLVGFQTKMRHGEQVRVFRTIPGLENAEFARLGGLHRNTYLNSPRLLDGTLRLKAAPRLRFAGQITGCEGYVESAAVGLMAGRFAAAERRGEALVPPPATTAHGALLAHITGGHIETVDAGPRSFQPMNVNFGLFPQLDVSPKGADGKRLRGSEKTLAKKRLLAERALSDMSAWLDTPAAAA
|
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
|
A8ID68
|
Q5WVN3
|
LPXK_LEGPL
|
Lipid A 4'-kinase
|
Legionella
|
MSFFVNRVWYGNHFLQWILVPFSWLYRIVIRTRRWYLQRFCQQLYPIPIIVVGNVTVGGVGKTPLVIEIAKKIQQKGLKVGIVSRGYKAAIKHFPYEVKLNDSAELVGDEPLMMARKINCPVVIAPKRNEAVRYLLDKHSVEIIISDDGLQHYKMGRSIEIVVIDGMRKLGNGFCLPAGPLREPDSRLKQVDFVIVNQGAAGGAYSMELIPKNIVRLSTQEEVSKDSFTSEVAAVAGIGNPQRFYSTLSQLGIKFNPYSYPDHHQFKPHDLNDIDLPVIMTEKDAVKCYSFSSDKLYYLPVEAKLNDSFWEAFWSHQQLQGYY
|
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
|
Q5WVN3
|
Q72DU3
|
TRMD_DESVH
|
tRNA [GM37] methyltransferase
|
Desulfovibrio
|
MRCTILTLFPEFFDSPLDAGLMGKARESGLIDVALVNPRAYTTDRHSTVDDRPYGGGPGMVMRVEPWEKALQGIEEPGRILMMAPKGRPFTQAMARELAQEESLTILCGRYEGFDARLEEIYPIEAVSMGDFVLNGGETAALAVLEAVSRLVPGFMGKEESGTEESFSAGLLEYPHYTRPEDYAGHVVPEVLRSGDHGRIAAWRKECSLRLTLSQRPDILPEAQLDEADMDFLRGLSRNRPGRNLYCALVHYPVVLKEKNSGATSLTNLDIHDIGRSSCTYGLGGFYVTTPLEDQRRLLDTLLRHWTLGPGSRSNPDRAEALGRIKGVDDVRAAIEDIARRTGQVPYVVGTSAKGAGNATPASVRAMLEERPVLLVFGTGHGLAPEVLEGCDAILRPLRWMDGYNHLSVRAAAAIIMDRLLGDCY
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q72DU3
|
Q4G360
|
RK22_EMIHU
|
50S ribosomal protein L22, chloroplastic
|
Emiliania
|
MSKTLLQENETMAVARYVRMGPNKVRRVLRQITGKSYSEALLLLEFLPYKSCDPIIKVLRSAVANAKNNLGYDTTKLVIKKAFADQGPVMKRFRPRAQGRAYRILKPTSHITIVVGS
|
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.
|
Q4G360
|
P17707
|
DCAM_HUMAN
|
S-adenosylmethionine decarboxylase beta chain
|
Homo
|
MEAAHFFEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQKIEGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS
|
Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels.
|
P17707
|
C0HJV4
|
CTX23_LACTA
|
Cytoinsectotoxin-2c
|
Lachesana
|
SWDSIWKSAKNKMDKIMRQKVAKWMAKKEGKSVEEVQAKVDAMSKKDIRMHVISHYGKKAFEQLSKSLEE
|
Insecticidal and antimicrobial peptide. Has insecticidal activity against larvae of flesh fly S.carnaria. Has antibacterial activity against Gram-positive bacterium B.subtilis B-501 (MIC=1.25 uM) and Gram-negative bacterium E.coli DH5alpha (MIC=2.5 uM).
|
C0HJV4
|
A3CPK9
|
UPP_STRSV
|
UPRTase
|
Streptococcus
|
MGKLEVIAHPLIQHKLSILRRTDTSTKAFRELVDEIAMLMGYEVLRDLPLEDVEIETPITKTVQKQIAGKKLAIVPILRAGIGMVDGLLSLVPAAKVGHIGMYRDEETLKPVEYLVKLPEDIDQRQIFVVDPMLATGGSAILAVDSLKKRGASHITFVCLVSAPEGVKALQEAHPDVDIFTAALDDHLNDHGYIVPGLGDAGDRLFGTK
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
A3CPK9
|
A8MHH1
|
PYRH_ALKOO
|
Uridine monophosphate kinase
|
Alkaliphilus
|
MLEPQYKRVLLKLSGEALAGEKGFGLDPNVVTNIATQVKDIVNMGVEVAIVVGGGNYWRGRTGEGMDRTTADYMGMLATVINALALQDSLENLDVLTRVQSAIEMRQIAEPYIRRRAVRHLEKNRVVIFAAGTGNPYFSTDTTAALRAAEIEADVILLAKNVDGVYSADPSIDKTATKFNELTYIDVLKMGLKVMDSTAISLCMDNSIPIKVFGLEDPENIKKVIYGDKIGTYIYS
|
Catalyzes the reversible phosphorylation of UMP to UDP.
|
A8MHH1
|
P53396
|
ACLY_HUMAN
|
Citrate cleavage enzyme
|
Homo
|
MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALGHRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVPSPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHMSM
|
Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate for de novo cholesterol and fatty acid synthesis.
|
P53396
|
Q46GC9
|
RS11_METBF
|
30S ribosomal protein S11
|
Methanosarcina
|
MADMKWAVAHIKSSFNNTIITVTDITGAETIAKSSGGMVVKAARDESSPYTAMQMAGQLADQLRDKGIHGIHIRVRAPGGNKQRSPGPGAQAAIRAFARAGIRIGRIEDVTPVPHDGTRPKGGRRV
|
Located on the platform of the 30S subunit.
|
Q46GC9
|
Q9PET2
|
GLYA_XYLFA
|
Serine hydroxymethyltransferase
|
Xylella
|
MFPRDARLDMYDPELAKAIAAEVMRQEDHVELIASENYCSTLVMQVQGSQLTNKYAEGYSGKRYYGGCECVDIAEQLAIERAKQLFGADYANVQPHSGSQANQAVYFALLQPGDTILGMSLAHGGHLTHGANVNVSGKLFNAVQYGVNGQGLIDYEAVESLALEHRPKMVVAGFSAYSQKIDWARFRAIADQVGAYLLVDMAHVAGLVAACVYPNPLPHAHVVTSTTHKTLRGPRGGIIVAQAPQEALVKKLQSIVFPGIQGGPLMHVIAAKAVAFKEALEPAFKVYQQQVVKNAKAMAETLMLRGYKIVSGGTENHLMLVDMIGRDVSGKDAEGALGQAHITVNKNAVPDDPRSPFVTSGLRLGTPAVTTRGYQEQDCVDLAHWIADVLDAPADATVIAAVREKVAAQCRKYPVYR
|
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
|
Q9PET2
|
Q7MUX4
|
PYRE_PORGI
|
Orotate phosphoribosyltransferase
|
Porphyromonas
|
MKTLGKLIASKLIEVKAIKLQPNNPFTWASGWKAPIYCDNRKTLSYPQIRSLIKLELARVISETFGDVEAIAGVATGAIAQGALVADLLGLPFVYVRSSPKDHGLENLVEGELKPNSKVVVIEDLISTGGSSLKAAEAIRNFGCEVLGMVAVYTHGFPMAEQNFEKAEVKLVTLTDYDQVIEEALRTGYISAENVELLREWRKSPETWGI
|
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
|
Q7MUX4
|
Q5F8I1
|
LIPB_NEIG1
|
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
|
Neisseria
|
MKIIHKGLVEYLPTFEAMKTFNAGRNADTEDELWVVEHPPVFTQGLAGKPEHLLIRDDIPVVQIDRGGQITYHGPGQLVVYTMIDFKRRKTSVRNIVSALENSIIATLAEYGIEAAADPKRPGIYVGERKIASLGLRIKNGSVYHGLALNVNMDLSPFTQINPCGYAGMEMTQIADFVQPCPAPDEVASKLTAHLETQLTPKADNNE
|
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
|
Q5F8I1
|
A9MB89
|
GLPK_BRUC2
|
Glycerokinase
|
Brucella
|
MSGYILAIDQGTTSTRSMLFDRNMRVVGLGQQEFTQHFPSSGWVEHDAEEIWKSVQSTIRIALAQAGISAADVAAIGITNQRETTVVWDRISGKPVHRAIVWQDRRTAQFCDELKRRNLEPLFTEKTGLLLDPYFSGTKLAWLLNHVPGLRERAQKGQVCFGTIDSWLIYKLTGGKAHVTDATNASRTLIYHIGENRWDDELLDILGIPAAMLPEVKDCAADFGMTDPALFGVSIPILGVAGDQQAAVIGNACFEPGMMKSTYGTGCFALLNTGTDRVTSSNRLLTTIAYRLDGVTTYALEGSIFIAGAAVQWLRDEMGFISVASEVSALAEKADPNQRIYLVPAFTGLGAPYWDAEARGAIFGLTRGTGRAEFARAALESVAYQTFDLLEAMQGDWKGATNHTVLRVDGGMVASDWTMQRLADILNAPVDRPVFLETTVLGAAWLAASRAGIWPDRKGFSERWQRDCRFEPAMPEKERESAIAGWRDSVSRCLTRPQ
|
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
|
A9MB89
|
A6W2I4
|
PANC_MARMS
|
Pantoate-activating enzyme
|
Marinomonas
|
MKTFHTVAELRTALKIERLKDKKIVFVPTMGNLHDGHMSLIRKAKEEGDIIVSSIFVNPMQFSDQSDLERYPKTLEEDKRVLEANGCNYLFAPDALEMYPDGKRSQTQIEVVGISDILCGASRPGHFVGVSTVVTKLFNIVQPDTAIFGNKDFQQLKVIQDMVRDLSSNVRIIGVDTARNEDGLAMSSRNGYLTEEERRIAPTIYQTLLWAKEALLENRASHEDICEQAQQKLEAAGFRRDYFEIRAQENLQTPSEEEKRLVILTAAYLGKARLIDNLRVEL
|
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
|
A6W2I4
|
Q63532
|
SPR1A_RAT
|
Small proline-rich protein 1A
|
Rattus
|
MSSQQQKQPCTVPPQLHQHEVKQPCQPPPQEPCAPKTKEPCHPIPEPCNPKVPEPCQPKVPEPCQPKVPEPCQPKVPEPCQPKVPEPCQPKVPEPCQPKVPEPCHPKAPEPCHPVVPEPCQPVAPEPCQPVVPEPCPPTVTPSPYQQKTKQK
|
Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane.
|
Q63532
|
Q2P377
|
PANB_XANOM
|
Ketopantoate hydroxymethyltransferase
|
Xanthomonas
|
MSSHADSNPWTVPALAQAKRAGRKLVMLTAYDASFARTFDANGVDLILVGDSLGMVMQGHDSTLAVTTADMVYHTAAVARALDRALLVADLSFQADATPERALDAATQLLQAGAEMVKIEGAGHKLEVIRYLVEREIPVCSHLGLTPQSVLRFGGYKVQGRGEAGEQLRRDAQAVVDAGASLVVLECVPTPIATQISAELSVPTIGIGAGPGCDGQVLVMHDMLGLDSGHRRPKFVKDFLAEGGSVAGAVRAYAQAVRDGSFPDAEHAYAA
|
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
|
Q2P377
|
Q9GMY2
|
PEPC_RABIT
|
Pepsinogen C
|
Oryctolagus
|
MKWLLVALVCLHLLEAAVIKVPLRKFKSIRETLKEKGLLKEFLNTHKYDPALKYRFGDFSVTYEPMDYLDAAYFGEISIGTPSQNFLVLFDTGSSNLWVPSVYCQSEACTTHNRFNPSKSSTFYTYDQTFSLEYGSGSLTGFFGYDTFTIQNIEVPNQEFGLSETEPGTNFLYAEFDGIMGLAYPSLSVGDATPALQGMVQDGTISSSVFSFYLSSQQGTDGGALVLGGVDSSLYTGDIYWAPVTRELYWQIGIDEFLISSEASGWCSQGCQAIVDTGTSLLTVPQEYMSDLLEATGAQENEYGEFLVDCDSTESLPTFTFVINGVEFPLSPSAYILNTDGQCMVGVEATYLSSQDGEPLWILGDVFLRAYYSVFDMANNRVGFAALA
|
Hydrolyzes a variety of proteins.
|
Q9GMY2
|
Q49Y40
|
MTNN_STAS1
|
S-adenosylhomocysteine nucleosidase
|
Staphylococcus
|
MIGIIGAMEEEVAILKDKIVNLEIINVAHVVFYKGRLHDKEVILTQSGIGKVNVAISTTLLINRFHPDLIINTGSAGALDKSLGVGDIIVSDMVAYHDADARAFGYQLGQIPQMPAQFVADSHLIELAKEAINDQKWVAKSGLIVSGDSFIGTAEQRADIKTNFPQAMAAEMEATAIAQTCYQFNLPFIITRAISDLADGDAGITFEAFLEKAAIASSQIVDRLIKTI
|
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine.
|
Q49Y40
|
Q7T1M3
|
BNP_BOTJR
|
Bradykinin-potentiating peptide Va
|
Bothrops
|
MVLSRLAASGLLLLALLALSVDGKPVQQWAQSWPGPNIPQLLVQQWAQGGWPRPGPEIPPLTVQQWAQNWPHPQIPPLTVQQWAQGRPPGPPIPPLTVQQWAQARPPHPPIPPAPLQKWAPVQKWAPVQKWAPVQKWAPLLQPT
|
Acts as indirect hypotensive agent. Potently induces vasodilation of arterioles, with only a small increase in leukocyte rolling flux.
|
Q7T1M3
|
Q01651
|
G3P_CORGL
|
NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
|
Corynebacterium
|
MTIRVGINGFGRIGRNFFRAVLERSDDLEVVAVNDLTDNKTLSTLLKFDSIMGRLGQEVEYDDDSITVGGKRIAVYAERDPKNLDWAAHNVDIVIESTGFFTDANAAKAHIEAGAKKVIISAPASNEDATFVYGVNHESYDPENHNVISGASCTTNCLAPMAKVLNDKFGIENGLMTTVHAYTGDQRLHDAPHRDLRRARAAAVNIVPTSTGAAKAVALVLPELKGKLDGYALRVPVITGSATDLTFNTKSEVTVESINAAIKEAAVGEFGETLAYSEEPLVSTDIVHDSHGSIFDAGLTKVSGNTVKVVSWYDNEWGYTCQLLRLTELVASKL
|
Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
|
Q01651
|
C1EXK2
|
RBSD_BACC3
|
D-ribose pyranase
|
Bacillus cereus group
|
MKKHGVLNSEIASVLASLGHTDTIVIADCGLPIPAGVKRIDLAVEIGKPSFLDVLQVVADDMAIEKVTLAEEVINNNAEVNKEIELKLIEPAFEYVCHEQFKEHTKKAKAIIRTGEATPYANVILHAGVIF
|
Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
|
C1EXK2
|
Q06GY8
|
ACCD_DRIGR
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic
|
Drimys
|
MEKWWFNSMLSNEELEHRCGLSKSMNSLGRAIGNTSGSEDLIINDTDKNIHSWSDSGSYSCNNVDDLFGIRDIWSFVSDDTFLVRDSNGDSYSVYFDIENQIFQIDNDSSFLSELESSFSNYLNFSYLNSGSKSDNRYYDRYMYDIKYSWNNHINSCIDSYLHSEISIESYISSSSDNYGDSYISSFICNESVSVSDNGSSSIRTSGNGSDFNIRGRSNDFDINQKYRHLWVQCENCYGLNYKKFFRSKMNICEQCGYHLKMSSSDRIELSIDPGTWDPMDEDMVSIDPIEFHSEEEPYRDRIDSYQRKTGLTEAVQTGIGQLNGIPIAIGVMDFQFMGGSMGSVVGEKITRLIEYATNGSLPIIMVCASGGARMQEGSLSLMQMAKISSASYNYQSNKKLFYVSILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKRVIEQTLNKTVPDGSQAAEYSFHKGLFDSIVPRNPLKGVLSELFQLHGFFPLNQN
|
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
|
Q06GY8
|
Q8XVC2
|
OPGH_RALSO
|
Glucans biosynthesis glucosyltransferase H
|
Ralstonia
|
MELPATSGLNAQPGNAEGTTASTRPATALSVAERYLEALPLPAEARAALRREAGIEPADKDAVALAKLHRALARLDAAQTASIEGSVPAYASIGSRLDAAYGTPHAGTATPEPAPPLEHDTAGRIHLDTGPEPARRSMVPWPWVLGPIWRARRAIGRLFSGGTAPVPYEQPDSPDPKGIWRFVGARRRLTLLALMIAQTVAATWAMSSVLPYHGHDWLEAIIIALFALLFCWVSAGFWTAITGFLLLAFHGDRFVISRRAAPNAPIPDDARTAIVMPICNEDVQRVFAGLRATYESLQRTGHLEHFDFFVLSDSGDPDIRTAEADAWLHVCRALDGFGRVFYRWRRHRVKRKSGNIDDFCRRWGGRYRYMIVLDADSVMSGDCLTRLVQLMEGAPSAGIIQTAPLAAGRDTLYARIQQFATRVYGPLFTAGLHYWQLGESHYWGHNAIIRLEPFIKHCALAPIPGKGSLSGEIMSHDFVEAALMRRAGWAVWIAYDLDGSYEEMPPNLLDELGRDRRWCHGNLMNFRLFGSPGFHPVHRAVFVTGVMAYLSAPLWFLFLLLSTALLAKHTLIAPEYFTQPRQLFPIWPEWHPEKAAALFSATATVLFLPKILSVLVLWAKGPRRFGGAVHLALSMVIEAVFSVLAAPVRMLFHTRFVTAAFLGWKVHWKSPPRDDAQTHWGDAVRRHGLHTLLGLGWAALVYWLNPSFLWWLSPVVGALIVSILLSVFSSRVTLGRGMRRWRLFMIPEEVRPPRELRAMRKHLRQAPPTPDFRLAVVDPVTNALMCAIGTARFPHDPKLLEVRDATVLQALAAGPDKLTSKQKLVLLSDPLALSALHLAVWSSDVHRAAWLPANALASKAAA
|
Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
|
Q8XVC2
|
Q03SK6
|
UNG_LEVBA
|
Uracil-DNA glycosylase
|
Levilactobacillus
|
MKPFIHNDWWPVLEPEFEKPYYQELRRFLVEEYQHYRIDPDMYHIFTAFEWTPFSQVKVVILGQDPYHNPGQAHGCSFSVLPGTEIPPSLVNIYKELQDDLGVQPVQHGYLKHWADQGVLLLNSVLTVRDGIKTANTHRGHGWEQLTDSAIEKLSARPEPVIFILWGSAARSKIKLIDTQTNIVLQSPHPSPLSAYRGFFGSKPFSKTNIALTSLGETPIDWQLPQQVTISDESTSDTH
|
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
|
Q03SK6
|
A8GDC2
|
PEPT_SERP5
|
Tripeptide aminopeptidase
|
Serratia
|
MDKLLDRFFNYVSFDTQSKANVKHVPSTDGQMKLARALQQEMIELGFERVSLSEHGCVMGTLPGNVAWSVPAIGFISHLDTSPDFTGKHVNPQIVESYRGGDIALGIGDEVLSPVMFPILHQMLGQTLITTDGKTLLGADDKAGIAEILTAMVRLQQRNIPHGDIRVAFTPDEEVGKGARFFDVAQFNAEWAYTVDGGGVGELECENFNAASVTVKIVGNNVHPGSAKGVMVNALSLATRIQQALPADETPETTADYQGFYHLSSLKGSVERAEMHYILRDFEREGFEARKRRMFEVAKQVGKGLPRDCYIEVTIEDSYYNMREQVAEHPHVIALAQQAMRDCDIEPVMKPIRGGTDGAQLSFRGLPCPNLFTGGYNYHCKHEFVSLEGMEQAVAVIMRIAALTAERAK
|
Cleaves the N-terminal amino acid of tripeptides.
|
A8GDC2
|
Q0CRW7
|
STTB_ASPTN
| null |
Aspergillus subgen. Circumdati
|
MSISNMTSTVWPDLQVPAIEHNHLPILTVALLTGIASAVYINVSSVQDPCKVGSIPTVKRPRLLDAYRSGVWWRIFVPRLVPYIEEGYHKYNKNDQPFRIWLGGFQAYAYVLPERYLDKIKNMPESEASFAAMANKYFHTGLPTGEVNNLVLQVASKLVNGNLATIKTLMQGEVQKALAREIGSPRQWTKINAWQVARKTTEAPGLRVVFGEELANDKTFVTGVSEFVSNITVYAFTLRYINLGPLRDFILYLVHWRHRRSLPAVLTPLNNVITERKKVRSNRHISDDEESFDCIQWALDQPVSDDCKTAEAIARRLVVISLGTIDTVAGVLVKQLTHLASHPECHEEIRAEIRECLAEDDNGWTLKSTGRMKKLESFIQESLRMSSGAISLSGMRIVTGSGFRLDDNTVLPRDSFIAIPTRNILYDPEVFPEPEKFDPFRFYKIKEDEKNAGSRSNRRDIRASWLAFGYGRQACPGRFYAINAMKTILGEILLKYDIRLAEKQAPRIDIDLDPMLAPVRSTDLEFRVRA
|
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aspterpenacids . Performs the C22-oxidative modification of the terpene synthase sttA product preaspterpenacid I to produce preaspterpenacid II . It has still to be determined how preaspterpenacid II is further modified to produce aspterpenacids (Probable).
|
Q0CRW7
|
Q9HB20
|
PKHA3_HUMAN
|
Phosphatidylinositol-four-phosphate adapter protein 1
|
Homo
|
MEGVLYKWTNYLTGWQPRWFVLDNGILSYYDSQDDVCKGSKGSIKMAVCEIKVHSADNTRMELIIPGEQHFYMKAVNAAERQRWLVALGSSKACLTDTRTKKEKEISETSESLKTKMSELRLYCDLLMQQVHTIQEFVHHDENHSSPSAENMNEASSLLSATCNTFITTLEECVKIANAKFKPEMFQLHHPDPLVSPVSPSPVQMMKRSVSHPGSCSSERSSHSIKEPVSTLHRLSQRRRRTYSDTDSCSDIPLEDPDRPVHCSKNTLNGDLASATIPEESRLMAKKQSESEDTLPSFSS
|
Plays a role in regulation of vesicular cargo transport from the trans-Golgi network (TGN) to the plasma membrane . Regulates Golgi phosphatidylinositol 4-phosphate (PtdIns(4)P) levels and activates the PtdIns(4)P phosphatase activity of SACM1L when it binds PtdIns(4)P in 'trans' configuration . Binds preferentially to PtdIns(4)P . Negatively regulates APOB secretion from hepatocytes .
|
Q9HB20
|
Q72PL0
|
RL20_LEPIC
|
50S ribosomal protein L20
|
Leptospira
|
MPRAVNGTIHKNRRRRILKDAKGFRGARSKLYRTAKSAVMKAGQWAYRDRRAKKRDFRKLWIIRINAAARENGLSYSVFMNSLKKLGIHMDRKSLAELAFNDREVFNSLVEKIKVAG
|
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.
|
Q72PL0
|
Q98C03
|
DHAA_RHILO
|
Haloalkane dehalogenase
|
Mesorhizobium
|
MSSKANPPQPVATAPKRSQIPILDSTMSYVEAGASGPTVLFLHGNPTSSHIWRNIIPHVAPFGRCIAPDLIGYGQSGKPDIDYRFFDHVRYLDAFLDALDIRDVLLVAQDWGTALAFHLAARRPQRVLGLAFMEFIRPFERWEDFHQRPQAREMFKALRTPGVGEKLVLEDNVFVEKVLPASVLRAMSDDEMDVYRAPFPTPQSRKPVLRLPREMPIEGQPADVAAISAHDHRALRLSTYPKLLFAGDPGALIGPQAAREFAAGLKNCSFINLGPGAHYLQEDHADAIGRAIASWLPEVVLANQTDELA
|
Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons.
|
Q98C03
|
Q9UHV7
|
MED13_HUMAN
|
Vitamin D3 receptor-interacting protein complex component DRIP250
|
Homo
|
MSASFVPNGASLEDCHCNLFCLADLTGIKWKKYVWQGPTSAPILFPVTEEDPILSSFSRCLKADVLGVWRRDQRPGRRELWIFWWGEDPSFADLIHHDLSEEEDGVWENGLSYECRTLLFKAVHNLLERCLMNRNFVRIGKWFVKPYEKDEKPINKSEHLSCSFTFFLHGDSNVCTSVEINQHQPVYLLSEEHITLAQQSNSPFQVILCPFGLNGTLTGQAFKMSDSATKKLIGEWKQFYPISCCLKEMSEEKQEDMDWEDDSLAAVEVLVAGVRMIYPACFVLVPQSDIPTPSPVGSTHCSSSCLGVHQVPASTRDPAMSSVTLTPPTSPEEVQTVDPQSVQKWVKFSSVSDGFNSDSTSHHGGKIPRKLANHVVDRVWQECNMNRAQNKRKYSASSGGLCEEATAAKVASWDFVEATQRTNCSCLRHKNLKSRNAGQQGQAPSLGQQQQILPKHKTNEKQEKSEKPQKRPLTPFHHRVSVSDDVGMDADSASQRLVISAPDSQVRFSNIRTNDVAKTPQMHGTEMANSPQPPPLSPHPCDVVDEGVTKTPSTPQSQHFYQMPTPDPLVPSKPMEDRIDSLSQSFPPQYQEAVEPTVYVGTAVNLEEDEANIAWKYYKFPKKKDVEFLPPQLPSDKFKDDPVGPFGQESVTSVTELMVQCKKPLKVSDELVQQYQIKNQCLSAIASDAEQEPKIDPYAFVEGDEEFLFPDKKDRQNSEREAGKKHKVEDGTSSVTVLSHEEDAMSLFSPSIKQDAPRPTSHARPPSTSLIYDSDLAVSYTDLDNLFNSDEDELTPGSKKSANGSDDKASCKESKTGNLDPLSCISTADLHKMYPTPPSLEQHIMGFSPMNMNNKEYGSMDTTPGGTVLEGNSSSIGAQFKIEVDEGFCSPKPSEIKDFSYVYKPENCQILVGCSMFAPLKTLPSQYLPPIKLPEECIYRQSWTVGKLELLSSGPSMPFIKEGDGSNMDQEYGTAYTPQTHTSFGMPPSSAPPSNSGAGILPSPSTPRFPTPRTPRTPRTPRGAGGPASAQGSVKYENSDLYSPASTPSTCRPLNSVEPATVPSIPEAHSLYVNLILSESVMNLFKDCNFDSCCICVCNMNIKGADVGVYIPDPTQEAQYRCTCGFSAVMNRKFGNNSGLFLEDELDIIGRNTDCGKEAEKRFEALRATSAEHVNGGLKESEKLSDDLILLLQDQCTNLFSPFGAADQDPFPKSGVISNWVRVEERDCCNDCYLALEHGRQFMDNMSGGKVDEALVKSSCLHPWSKRNDVSMQCSQDILRMLLSLQPVLQDAIQKKRTVRPWGVQGPLTWQQFHKMAGRGSYGTDESPEPLPIPTFLLGYDYDYLVLSPFALPYWERLMLEPYGSQRDIAYVVLCPENEALLNGAKSFFRDLTAIYESCRLGQHRPVSRLLTDGIMRVGSTASKKLSEKLVAEWFSQAADGNNEAFSKLKLYAQVCRYDLGPYLASLPLDSSLLSQPNLVAPTSQSLITPPQMTNTGNANTPSATLASAASSTMTVTSGVAISTSVATANSTLTTASTSSSSSSNLNSGVSSNKLPSFPPFGSMNSNAAGSMSTQANTVQSGQLGGQQTSALQTAGISGESSSLPTQPHPDVSESTMDRDKVGIPTDGDSHAVTYPPAIVVYIIDPFTYENTDESTNSSSVWTLGLLRCFLEMVQTLPPHIKSTVSVQIIPCQYLLQPVKHEDREIYPQHLKSLAFSAFTQCRRPLPTSTNVKTLTGFGPGLAMETALRSPDRPECIRLYAPPFILAPVKDKQTELGETFGEAGQKYNVLFVGYCLSHDQRWILASCTDLYGELLETCIINIDVPNRARRKKSSARKFGLQKLWEWCLGLVQMSSLPWRVVIGRLGRIGHGELKDWSCLLSRRNLQSLSKRLKDMCRMCGISAADSPSILSACLVAMEPQGSFVIMPDSVSTGSVFGRSTTLNMQTSQLNTPQDTSCTHILVFPTSASVQVASATYTTENLDLAFNPNNDGADGMGIFDLLDTGDDLDPDIINILPASPTGSPVHSPGSHYPHGGDAGKGQSTDRLLSTEPHEEVPNILQQPLALGYFVSTAKAGPLPDWFWSACPQAQYQCPLFLKASLHLHVPSVQSDELLHSKHSHPLDSNQTSDVLRFVLEQYNALSWLTCDPATQDRRSCLPIHFVVLNQLYNFIMNML
|
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
|
Q9UHV7
|
Q501F9
|
P2C67_ARATH
|
Probable protein phosphatase 2C 67
|
Arabidopsis
|
MVKPCWRIGAGMERSKINPTKVDGLTWYKDLGLHTFGEFSMAMIQANSVMEDQCQIESGPLTFNNPTVQGTFVGVYDGHGGPEASRFIADNIFPKLKKFASEGREISEQVISKAFAETDKDFLKTVTKQWPTNPQMASVGSCCLAGVICNGLVYIANTGDSRAVLGRSERGGVRAVQLSVEHNANLESARQELWSLHPNDPTILVMKHRLWRVKGVIQVTRSIGDAYLKRAEFNREPLLPKFRLPEHFTKPILSADPSVTITRLSPQDEFIILASDGLWEHLSNQEAVDIVHNSPRQGIARRLLKAALKEAAKKREMRYSDLTEIHPGVRRHFHDDITVIVVYLNPHPVKTNSWASPLSIRGGYPMHSTS
|
Dephosphorylates and represses plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), thus influencing negatively plant growth and fitness . Promotes the apical hook maintenance of etiolated seedlings .
|
Q501F9
|
Q8PGW9
|
RSGA_XANAC
|
Small ribosomal subunit biogenesis GTPase RsgA
|
Xanthomonas
|
MSDTSPDYPTLQSIGWPWLGPPEEAAWQAVFAAHPQALPARVVEQHRTGYVVADTPEASVKAESLPEWQRPRFPSHERAAVGDWVLMEGKRIVALLPRRTSIKRGAAGEHYHQQVIAANIDTVFIVCGLDADFNPRRIERYLLLVGGGGAQPVVVLTKADQTEYAEDALAVLEELEAQNIPLRAVNAKDPDSVAALRPWLGDGRTAVLVGSSGAGKSTLTNTLLGTQKMKTNAVRENDSRGRHTTTHRALIPLPSGACLIDTPGMRELKPTGEEDLAEGGFSDVEALAAQCRFNDCAHIAEPGCAVRAAIDAGELDPERVANYMKLRMEVASAAEKLATRVAQNNRGKGSGKRPASVDRPGRH
|
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
|
Q8PGW9
|
A9N2D8
|
CYSN_SALPB
|
Sulfate adenylate transferase
|
Salmonella
|
MNTILAQQIANEGGVEAWMIAQQHKSLLRFLTCGSVDDGKSTLIGRLLHDTLQIYEDQLSSLHNDSKRHGTQGEKLDLALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFISTLLGIKHLVVAINKMDLVDYREETFARIREDYLTFAEQLPGDLDIRFVPLSALEGDNVAAQSANMRWYSGPTLLEVLETVDIQRAVDRQPMRFPVQYVNRPNLDFRGYAGTLASGSVKVGERIKVLPSGVESSVARIVTFDGDKEEACAGEAITLVLNDDIDISRGDLLLAANETLAPARHAAIDVVWMAEQPLAPGQSYDVKLAGKKTRARIEAIRYQIDINNLTQRDVESLPLNGIGLVEMTFDEPLALDIYQQNPVTGGLIFIDRLSNVTVGAGMVRELDERGATPSVEYSAFELELNALVRRHFPHWDARDLLGDKHGAA
|
With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
|
A9N2D8
|
O60238
|
BNI3L_HUMAN
|
NIP3-like protein X
|
Homo
|
MSSHLVEPPPPLHNNNNNCEENEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRHPKRSVSLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY
|
Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor.
|
O60238
|
Q8CMP5
|
METE_STAES
|
Methionine synthase, vitamin-B12 independent isozyme
|
Staphylococcus
|
MTTIKTSNLGFPRLGRKREWKKAIENYWAHKIDKAELDQTLTDLHKENLLLQKNYHLDSIPVGDFSLYDHILDTSLLFNIIPERFQGREVNDDLLFDIARGNKEHVASALIKWFNTNYHYIVPEWDNVEPKVEKNTLLERFKYAQSINVNAHPVIVGPITFVKLSKGGHQSFEEKVETLLPLYKEVLQSLVDAGAEYIQIDEPILVTDDSESYEDITRKAYDYFANEGLGKYLVIQTYFERVHLKFLSSLPVGGLGLDLVHDNGYNLKQIEDGDFDQSKALYAGIIDGRNVWAADIEAKKQLIETLQQHTQQLVIQPSSSLLHVPVSLDDETLDESIAEGLSFATEKLDELDALRRLFNDNDLSKYEHYKARYERFQSQSFKNLEYDFESVPTHRKSPFAKRKQLQNQRLNLPDLPTTTIGSFPQTREVRKFRADWKNNRITDAEYQEFLQNEIARWIKIQEDIGLDVLVHGEFERNDMVEFFGEKLQGFLVTKFGWVQSYGSRAVKPPVIYGDVKWTAPLTVKETVYAQSLTDKPVKGMLTGPVTILNWSFERVDVPRKVVQDQIALAIDEEVLALEEAGIKVIQVDEPALREGLPLRSEYHEQYLEDAVHSFKLATSSVHDETQIHTHMCYSQFGQIIHAIHDLDADVISIETSRSHGDLIQDFEDINYDLGIGLGVYDIHSPRIPTEEEITTAINRSLQQIDRSLFWVNPDCGLKTRKENEVKDALTVLVNAVKKKRQESESTTA
|
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
|
Q8CMP5
|
Q60695
|
RGL1_MOUSE
|
Ral guanine nucleotide dissociation stimulator-like 1
|
Mus
|
MKLLWQAKMSSIQDWGEEVEEGAVYHVTLKRVQIQQAANKGARWLGVEGDQLPPGHTVSQYETCKIRTIKAGTLEKLVENLLTAFGDNDFTYISIFLSTYRGFASTKEVLELLLDRYGNLTGPNCEDDGSQSSPESKAVIRNAIASILRAWLDQCAEDFREPPHFPCLQKLLEYLKQMMPGSDPERRAQNLLEQFQKQDVDSDNGLLNTSSFSLEEEEELESGGSAEFTNFSEDLVAEQLTYMDAQLFKKVVPHHCLGCIWSQRDKKENKHLAPTIRATISQFNTLTKCVVSTVLGSKELKTQQRARVIEKWINIAHECRILKNFSSLRAIVSALQSNSIYRLKKAWAAVPKDRMLMFEELSDIFSDHNNHLTSRELLMKEGTSKFANLDSSVKENQKRTQRRLQLQKDMGVMQGTVPYLGTFLTDLTMLDTALQDYIEGGLINFEKRRREFEVIAQIKLLQSACNSYCMGPDQKFIQWFQRQQLLSEEESYALSCEIEAAADANTTSPKPRKSMVKRLSLLFLGSDIIPGSTPTKEQPKSAASGSSGESMDSVSVSSCESNHSEAEEGPVTPMDTPDEPQKKLSESSSSCSSIHSMDTNSSGMSSLINPLSSPPTCNNNPKIHKRSVSVTSITSTVLPPVYNQQNEDTCIIRISVEDNNGNMYKSIMLTSQDKTPAVIQRAMSKHNLESDPAEEYELVQVISEDKELVIPDSANVFYAMNSQVNFDFILRKKNSVEEQVKLRSRTSLTLPRTAKRGCWSNRHSKITL
|
Probable guanine nucleotide exchange factor.
|
Q60695
|
Q8EUW7
|
SYP_MALP2
|
Prolyl-tRNA synthetase
|
Malacoplasma
|
MSKIVKQEENFSKWYTSIIENANLVDYGLVKGTIMFKPYGFAIWKRIQEEFNKILVSLNTAEVCFPMLIPYSEFMKEKEHVEGFNPELFKVSHLGEKKLEDELVIRPTSEISFCNYFKKNIKSYNDLPCILNQWGSVFRVEKNTRPFLRTSEFLWQEQHAVFADKKEAFDFSITMVNEYKKFVNDYLSIAVLMGEKTENERFAGADNTFTIEALMPDGQVLQSATSHYLGTNFAKSYDLKYQTKNNNYDLMFQTSAGLSTRIIGAIIMSHSDNNGLVLPFKIAPIQFAIVTSNEVNKDSDELKAIYKNLFGYKYQTYFVEKSLGLQLQENEIKGIPFQLILGKKEIENNTITIYRRDTREKQNISFKEFNQNFIENLIKEYSSNLFNKTEKRLNSSIEFVNNIDEFKKALDNKKIISAYWSGNAEDEKKLKELTTATPRCFDWNQKIDKTKKCFFTNKPNAKLVYFARAY
|
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
|
Q8EUW7
|
P13613
|
LACB1_EQUAS
|
Beta-lactoglobulin I, major monomeric
|
Equus
|
TNIPQTMQDLDLQEVAGKWHSVAMAASDISLLDSEEAPLRVYIEKLRPTPEDNLEIILREGENKGCAEKKIFAEKTESPAEFKINYLDEDTVFALDSDYKNYLFLCMKNAATPGQSLVCQYLARTQMVDEEIMEKFRRALQPLPGRVQIVPDLTRMAERCRI
|
Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
|
P13613
|
Q5ZM36
|
IF4A3_CHICK
|
Eukaryotic translation initiation factor 4A isoform 3
|
Gallus
|
MSGSAGSGGTTGSARKRIMKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILAPTRELAVQIQKGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI
|
ATP-dependent RNA helicase. Involved in pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms; the function is different from the established EJC assembly. Involved in craniofacial development.
|
Q5ZM36
|
Q86L99
|
GACHH_DICDI
|
GTPase activating factor for raC protein HH
|
Dictyostelium
|
MSWSSIKLSRLPDATISVWGHTATISGEKDIVIFGGFDFCIEKPTNTTYILHTSQTNGLTKPSVSGSLPPPIYGHSSTQVGRKMFVFGGSLQDNVQVNDMYQFNTSNYSWSKPRPMGEPPIPRYGHSASLIYDNYILIFGGNNTKSSKPLNDIHIFNTERNSWTKPSSNSSTGEIIFNPHDISPRSSTTTPTHQSVNGSNSNSSSSSRVRSATISSHNNSPIVMPLNNNNNNNNNSNNSNNSNNNGGGSPMTTPPTLQQLHLSQLMANGIGMGGSISNGNSDSPPLTPSMMALESSMLNGFKSPLSLSQRLLRSGFRSSPPSARYFHSCSVINGKAFIFGGYNGTTLLNDLYILNIESMEWICPHTKGDLPTPRAGHTSIAIGSRLFIFGGTIEGDPSSSNAHCDNDLYMFEPELNYWTLLKTSGTLPSPRTGHVCLPISSKILIIGGSDAILNNKLKLSNTYHSLETLKLDFSHYSRGGSGGGSNNNIIIHPITSSNSTSSNSIITNYLPHLKPRSSSNSGGGGGSITNTPTTSSLHIKDNSASPSPLTPRSIARNSPKSSIFHDNINNNSNNNLLNTLQEASKFELSPGTPKSIRGIDSLSSVSLTQSIDRNGGSGGGSGGGNGVVSNDRGEFLRHYTTQSILINKNNNNNNNNNSGGSNLSISSNSGSNNSINSNDGLVLQCSTPLCIKKYNSLKDSYLELKQKYQEEREKRLELEKELERYRLSSPITSASSLVDTLSSPNNLNINSNNSTTTTTTTTTTTTTPIPLSTSNNNNNNNNNSTLTVQDQVTTSKQILEIYEDIYNLWGYYEKRVKWKENTEKEANQQLEVIKSKIDLFTSMVGLENHFSFNDDTKSCCSENINGDHNQQQQQQQQQNPQFQIDDNISETNSQISEPALIHETLTPRKSRENSVHHSRSVSNPIPLLSQIVKQSKSGDSTLTVPQQLHSSHNNLIQLASISTPQKPPQQPQQQQQQQPPQENGKEPSKSTQKIFKLLISKKNRASGHFKLSSSNESSNSEETTPTFSNNPNLINDEDDDSQQHQQQTNIGSNSISNINTSNSTTSLSSSVSSTSLQTQEEFEASERSKQKKRLGKALKQMINKDRQLKETAAAALAVSNSNGNLGGGGGGGSINGTTNVSGNGANNLGGLVLTSDKEKEKLEKEREKSERIEREKQEKEREKLEKEREKSERIEREKLEKAEKERLEKEKIEKEKLEKKHKKIKGLFGAKSSNKESLPFRRDVIEKVINHLRENSLDTEGIFRLSGNMESVRGIVKSFAHGEPNLSFEVHNISNALKHYLRSLDPPLIPYEFFLMLLDARKNEDAETIRNIFWKIPSDNRVVLTLLVDLMVKISENSNVNKMNSKNLSIVFGPTILKPRTPTLDRMALMTETQLQCGIIQTFIEDFHYIFSEFPTSGPKSFLGDDDYDSSSFGSNNTPSSHSPHSSSPTLNPAVTTTTTTTTTTNTTTTTNTTTTPTSATISPNIIQTNNCDSALCTPTTLSSTAAIIQSNNNNRTDSNRNN
|
Rho GTPase-activating protein involved in the signal transduction pathway.
|
Q86L99
|
Q04865
|
TF65_XENLA
|
XRel1
|
Xenopus
|
MDGFHWTDIVSSMPPSIPPVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTSKTHPTIKINNYQGPARIRISLVTKDSPHKPHPHELVGKDCKDGYYEAELSPDRSIHSFQNLGIQCVKKREVEDAVAHRIRTNNNPFNVSPEELKADYDLNTVCLCFQVFIPDQAAGRMLPLPFVVSQPIYDNRAPNTAELKICRVNKNSGSCLGGDEIFLLCDKVQKEDIEVIFGLGNWEARGIFSQADVHRQVAIVFRTPAFQDTKIRQSVKVQMQLRRPSDKEVSEPMEFQYLPDEGDPHHIDEKRKRTLDNFKHYVKNNPFAGGETRPQRRIAVANRNVPTKSEPIRPSIPVPNPVVSCLPFSMPVLKAENVTSPSTLLSTVNISDFSNLGFSSQPPSQSDHDRLESMLNYPSFPGDANLDLVEMLPHENESRCTSLSSIDNSDFSQLLSESQSSGTLSAALQEPGTSQGTFMAYPESIARLMTNRPNEDEGGERIDSGLINGMFDISREEIHLTSLFELDFSSLLSNMK
|
NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. RELA shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex.
|
Q04865
|
Q9GYF0
|
CHUP1_CAEEL
|
Cholesterol uptake protein 1
|
Caenorhabditis
|
MRTSQAIFILIFLDSVRNQSPQVIPAKWDVVYEKETGHNMSLTVFRFQVKEQYSVARIIMSCNESTEHNPLLAVFREKLAILSLQVPLIVDNYEYSQVARTLCPFTEYKEGEAFTVEVTSSRPVHYNFRAELVQNFYLYNNSQRLVTASASEPVYLRYDIPGDVDSVAVHLDSNSTICMTVSVQKIGCPVFDLPDNVNSMGLHQTMTTSATIPVEKSRMSSFYVVFVVNTNDDLCSEILSIKPNKPTKFPLRMKSFNVTIESSMKIFDYTIPIVFWACILLLVTIVVFVYHYFDGIWERRFVSRAYTHLEDNAQEQRIRDFYDFQRMSEDDDLKDYDLLTDCQDMMVVRAKASLTVADLSMTPYEERELKYDVYKIALAIIGIFYNITVLQLIISKAGSLRQSGDLDECTFNFQCARPLWYFVAFNNVVSNGGYVYFGTLIIVMNYCRERSFRRLFAVQPTLAERYGLPQHSGLMTAIGLAVIMEGISSATYHVCPNNINYQFDTALMYVIGMLGKLKIWSLRHPDMVVSAYHAFGFLGVFLMAAIAGVYVHNMIFWALFSIIYIASMLLVSLEFYFKGIWTLNLRELRNSIRLSWVSSRHLSCVVPAYKARFFVILLLNIANTAVVVYGLEAHPKDFLSFLLIPFIGNLFIYIIYYILMKMIYREKIPKRAIALLFAAVISWTCAGILFNQRVSDWSKMPAISRELNKPCIFLNFYDNHDLWHLSSAFAIFFSFTAINVIDDDLMFVMRNTIRVF
|
Cholesterol-binding protein which is involved in dietary cholesterol uptake from the environment . Does not play a role in double-stranded RNA transport in contrast to other SID1 family members .
|
Q9GYF0
|
C0PYG5
|
LEPA_SALPC
|
Ribosomal back-translocase LepA
|
Salmonella
|
MKNIRNFSIIAHIDHGKSTLSDRIIQICGGLSDREMEAQVLDSMDLERERGITIKAQSVTLDFKASDGETYQLNFIDTPGHVDFSYEVSRSLAACEGALLVVDAGQGVEAQTLANCYTAMEMDLEVVPVLNKIDLPAADPERVAEEIEDIVGIDATDAVRCSAKTGVGVTDVLERLVRDIPPPQGDPDGPLQALIIDSWFDNYLGVVSLVRIKNGTMRKGDKIKVMSTGQTYNADRLGIFTPKQVDRSELKCGEVGWLVCAIKDILGAPVGDTLTSARNPAEKALPGFKKVKPQVYAGLFPVSSDDYESFRDALGKLSLNDASLFYEPESSSALGFGFRCGFLGLLHMEIIQERLEREYDLDLITTAPTVVYEVETTAKETIYVDSPSKLPPLNNIYELREPIAECHMLLPQAYLGNVITLCIEKRGVQTNMVYHGNQVALTYEIPMAEVVLDFFDRLKSTSRGYASLDYNFKRFQASDMVRVDVLINNERVDALALITHRDNSQSRGRELVEKMKDLIPRQQFDIAIQAAIGTHIIARSTVKQLRKNVLAKCYGGDISRKKKLLQKQKEGKKRMKQIGNVELPQEAFLAILHVGKDNK
|
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
|
C0PYG5
|
P32188
|
EPD_ESOLU
|
Ependymin
|
Esox
|
MQAFAVAALSIWLCLGATTLAESLAQSHGPQHCTSPNMTGVLTVMALNGGEIKATGHYHYDTTDKKLRFTESDMHLNKSEHLEDYLMLFEEGVFYDIDLKNQSCRKMSLQSHAHALELPAGAVHQVELFLGSDTVQEENIKVNIWMGSVPETKGQYSVSTTVGDCLPLSTFYSTDSITLLFSNSQVVTEVKEPEVFSLPSFCEGLELEDTHNDFFSIFNTV
|
May play a role in neural plasticity. May be involved during axon regeneration.
|
P32188
|
Q6P280
|
ZN529_HUMAN
|
Zinc finger protein 529
|
Homo
|
MANSSFIGDHVHGAPHAVMPEVEFPDQFFTVLTMDHELVTLRDVVINFSQEEWEYLDSAQRNLYWDVMMENYSNLLSLDLESRNETKHLSVGKDIIQNTGSQWEVMESSKLCGLEGSIFRNDWQSKSKIDLQGPEVGYFSQMKIISENVPSYKTHESLTLPRRTHDSEKPYEYKEYEKVFSCDLEFDEYQKIHTGGKNYECNQCWKTFGIDNSSMLQLNIHTGVKPCKYMEYGNTCSFYKDFNVYQKIHNEKFYKCKEYRRTFERVGKVTPLQRVHDGEKHFECSFCGKSFRVHAQLTRHQKIHTDEKTYKCMECGKDFRFHSQLTEHQRIHTGEKPYKCMHCEKVFRISSQLIEHQRIHTGEKPYACKECGKAFGVCRELARHQRIHTGKKPYECKACGKVFRNSSSLTRHQRIHTGEKPYKCKECEKAFGVGSELTRHERIHSGQKPYECKECGKFFRLTSALIQHQRIHSGEKPYECKVCGKAFRHSSALTEHQRIHTGEKPYECKACGKAFRHSSSFTKHQRIHTDDKPYECKECGNSFSVVGHLTCQPKIYTGEKSFD
|
May be involved in transcriptional regulation.
|
Q6P280
|
Q3MEE5
|
KAIB_TRIV2
|
Circadian clock protein KaiB
|
Trichormus
|
MNKARKTYVLKLYVAGNTPNSVRALKTLKNILEQEFQGIYALKVIDVLKNPQLAEEDKILATPTLSKILPPPVRKIIGDLSDRERVLIGLDLLYEELTEEDWEAQSSL
|
Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-non-specific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it decreases the phosphorylation status of KaiC. It has no effect on KaiC by itself, but instead needs the presence of both KaiA and KaiC, suggesting that it acts by antagonizing the interaction between KaiA and KaiC.
|
Q3MEE5
|
Q8GUK1
|
DGS1_ARATH
|
Protein DGD1 SUPPRESSOR 1
|
Arabidopsis
|
MDSQPPVNESTPSTALSNFGELVPFYSSYLWNRLASLLPTSKPIFLGKISNLYRQTVSRKRSISFPLPLPSDFPSSSTITSNVSADTARIHGVLEEIMADVLSNLHDIQKSLDFWRSRAEGSNARKAYFMIFERGPTAFVNESTKFVSKSLSEDSAMQHLCQSSSSHMTERMRVLVELRSALASFIAQLYVELDKRGEDLVKIPEKALPSLLAVINGLFSNLEGSFSHLHAVRECDSSVDGSYPMPLVFDRLPEVNEEGSQWTDCELTDAINLVHKNLEKLNSYLSVMVGKHRKPRRMTLYWVRYTCGAVGLSVFSIWLLRHSSLMGSSDIENWVHDAKEATMSFFSDHVEQPLLSIRDELFDTFRKRHKGVMETEEVQLTQDSLHRMLRNFCEQATREKVPDNASDQEMLEVVMNRYEKELVHPIHNLLSGELARGLLIQVQKLKLDIETAMLELDQILRANEINFAILAALPAFFLSIVMLTVLRTWLKKDSKAQGRGRIARIHRRLLVVEIEKRIMQYQSYIEQGRDKDAETVFGLLIYSLERLYRVVEKPARATDEWDLVKQDLIELGRPQQQTSYKLTVTQRLVTVYDCLLPTLKRQ
|
Involved in galactoglycerolipid biosynthesis. May contribute to an intracellular signal that regulates an alternative DGD1-independent galactoglycerolipid biosynthesis pathway in chloroplasts.
|
Q8GUK1
|
Q253Y0
|
RSMH_CHLFF
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Chlamydia
|
MSEAPQHIPVLVNECLSLFADRNPKFFCDVTLGAGGHAEAFLSAYPSIVSYDGSDRDTMALSLAKERLEKFGNRVHLHHASFEDLAQNPRENVYDGILADLGVSSMQLDTLSRGFSFQGDDHDLDMRMDTSKGTTASEVLNTLREEDLGRIFREYGEEPQWKNAAKAIVQFRRHKKIITVRDLKEATTRVFPSYRLRKKIHPLTLIFQALRVYVNQEDVQLKVFLESAMRWLAPEGRLIIISFCSSEDRPVKWFFREAEAMGVGKILTKKVVMPTYEETRKNPRCRSAKLRCFEKKSS
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
Q253Y0
|
Q52955
|
ILVC_RHIME
|
Ketol-acid reductoisomerase type I
|
Sinorhizobium
|
MRVYYDRDADLNLIKSKKVAIIGYGSQGRAHALNLKDSGAQNVAIALKSGSATAKKAEADGFKVMTVAEAAAWADLMMMATPDELQADIYKADIAGNIRDGAAIAFAHGLNVHFGLIEPKASVDVVMIAPKGPGHTVRGEYQKGGGVPCLVAVHQDASGNALDLALSYACGVGGGRSGIIETNFKEECETDLFGEQVVLCGGLVELIRAGFETLVEAGYAPEMAYFECLHEVKLIVDLIYEGGIANMNYSISNTAEWGEYVTGPRIITEDTKAEMKRVLKDIQTGKFTSEWMQEYRSGAARFKGIRRVNDSHQIEEVGAKLRAMMPWIGKNKLVDKAKN
|
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
|
Q52955
|
Q5QY69
|
TMCA_IDILO
|
tRNA(Met) cytidine acetyltransferase TmcA
|
Idiomarina
|
MAERSGYRQLQLLQDASLWREYCEARSESSIYLSNLQTHADAVLSRYRDYLGHEFEQVWIDCHDGLHADAIAALCGTVTAGGLLSILLPAESNAMSHRMERFAAKHFAESNIKPYSSVNKTETRSANETLQLTNEQNSIFNALTQSTAKPYETHIITAERGRGKSTLLGQALAQAKEHRSIIVTAPRKANAKVLLQQAPEAHFVAWDKLLEQPGNSEVTLIIDEAAGLPLWATEQLCQKFNPWLLATTVAGYEGCGRGFAVHFTDWARKTLPQVSVHQLTQPLRWPANDPLEQWLTETFLLNEQPVTQFGNRESGTFIKHASELEEALLQQCFQLLLSAHYQSSPNDLNLLLTEPGHKLAYQSTNGEVTAVAWLMSEGPILSPLKEEVRQGQRRPKGNLLPQAIGYFLQQDWAMDLHWLRVARIAVPAAKRRRKAASELLAEIYRWALDNNYQMLGTSFAWSPGLDNFWKKNGYALWRLSSRIDSVSARPAAIYALPLTNEFTELYRVCQLLGQWGQNQLQWLSGGKETLQLTEERNKIRTSLIQAYRSKTIPFDAAHFALAQWFYWQHSNHPLTELLCNSSTTLKHLGEYWGGVSQRQANENLCKEVCLLH
|
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
|
Q5QY69
|
Q20351
|
TPSTB_CAEEL
|
Tyrosylprotein sulfotransferase
|
Caenorhabditis
|
MRAILDAHPDVRCGGETMLLPSFLTWQAGWRNDWVNNSGITQEVFDDAVSAFITEIVAKHSELAPRLCNKDPYTALWLPTIRRLYPNAKFILMIRDARAVVHSMIERKVPVAGYNTSDEISMFVQWNQELRKMTFQCNNAPGQCIKVYYERLIQKPAEEILRITNFLDLPFSQQMLRHQDLIGDEVDLNDQEFSASQVKNSINTKALTSWFDCFSEETLRKLDDVAPFLGILGYDTSISKPDYSTFADDDFYQFKNFYS
|
Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
|
Q20351
|
A1TJ16
|
RS17_ACIAC
|
30S ribosomal protein S17
|
Acidovorax
|
MTEAKKSLKRTLVGKVVSDKREKTVTVLVERRVKHPIYDKIVIKSSKYHAHDENSEYKLGDTIEITESRPLSKTKNWVATRLVQKAALV
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
|
A1TJ16
|
A5VWQ6
|
ENGB_PSEP1
|
Probable GTP-binding protein EngB
|
Pseudomonas
|
MQVKNPILGLCQKAKFALSAAKVEQCPDDQGYEVAFAGRSNAGKSSALNTLTHASLARTSKTPGRTQLLNFFSLDDERRLVDLPGYGYAKVPIPLKQHWQKHLEAYLGSRECLRGVILMMDVRHPMTDFDKMMLDWAKASSMPMHILLTKADKLTHGAGKNTLLKVQSEIRKGWGDGVTIQLFSAPKRLGVEDAYRVLADWMELEDKPVI
|
Necessary for normal cell division and for the maintenance of normal septation.
|
A5VWQ6
|
O00874
|
DPOLA_LEIDO
|
DNA polymerase alpha catalytic subunit
|
Leishmania
|
MSGGNDGASWRLSRKPNAPNFDETQEDQWRSLREEVLQSDEDENIPESGDLTIPQLPSAKKAAKKLRKPPSGAKPTPKPKQQTLAQSMSDMDMERLLKRYRIDEDIDIAEDIDMSHLLQLHSDSDDGGDAQEATLTADEFLARLARAEAAPAASIAKEKRESGENVTVVALKDELFNVERDQSAKPPRPRPTPGAGGGAGYRNEETPKQAIELTATLAPQMDAAQFVSPAVPYKSGEMTEGLFYWFDAREQPHTLSVDPGSLFLFGKMAVEKNGRTSYLSCCVRVRNMYRSVFVLPKAGSSQEDVVKEINDICRNQGIEQRRIKFVERYYAFEVPGVPHEKTQWAKLRYPGRYPPLNAKGPFRHILIIMGASSSLLELFLIKRKLKGPSFLRISGLVASANRISHCALEFSVESPKNLRAEDTKLPVPPFTLASIQIHTQLDSKGACNEILIASVAIYKDVNIENTIRYIPDNILTGVRPASMSTPLPIDLESYCSAKGLPGVRRFANERALLDWLAQQLGKIDADMMIGHNFLGFTLDILLRRYQELSISSWSTIGRLDLKRLPRFQGTATNVNQEKETCIGRLVVDSYSLSREHYKTVNYRLLSLADQMQLQGITKGSNNFEPGTSVLTPAMLSASRDIYDVLLQVCNCAVLSTAVVSHLDVIRLTKRLTTIAGNLWSRTLFGARSERIEYLLLHTFHDLKFITPDRYVQNFKRGRDDEEEEDGKRKAKYQGGMVLDPKCGLYSDYILLLDFNSLYPSLIQEFNICFTTVDRESGSEIDVPPPENLICASCAAAGLSAPCLHKCVLPKVIKSLVDSRREVKRLMKIEKDANNLALLEIRQKALKLTANSMYGCLGFEYSRFHAQPLAELVTRQGRLALQSTVDLIPQLNPSLRVIYGDTDSVMIQTGIKNDIKAVRDLGLDLKAKINKRYQSLEIDIDGVFRAILLLKKKKYAALTVTDWQGEGKTYKKEVKGLDMVRRDWCPLSKCVCDSVLSRVLNAEGSEDILDYVMNYMRDVSEKVRAGRYTLDNFVISKSLTKEPEAYRGNSFPHATVALRMKQRKELVRVGDLIPYVICTGDRLSDKAFHVEEVRQNSQLQIDSEWYLSVQIYPPVMRLCEHIQGFSNAQLSEAMGIACHTGAKLEEEEAETMNDFSHSSLFQSRNLEECFPAALSLQVACTHCRLMTPINPHTRVMEVLADQERQRDRFDLYVCVSCRKSLPVDYVANCFTQTCYGIIRQFYQCGSAAAVKAVRTQFTYYRALFDVPHAPGCPARVKDAHYYQARRCLGVDRRLYTLAEAADPAVQEVADPVDPLNAAAETIYKRIDHLFINLDSLFAGI
|
Polymerase alpha in a complex with DNA primase is a replicative polymerase.
|
O00874
|
B0VQB8
|
DXS_ACIBS
|
1-deoxyxylulose-5-phosphate synthase
|
Acinetobacter calcoaceticus/baumannii complex
|
MPHMLYTEIPTQRPVTPLLDAIDHPQQLRQLEHSQLLQVADELRQYILYAAGQSGGHFGANLGVVELTVALHYCFNTPNDRLVWDVGHQAYPHKILTGRREQITTIRAKNGLAAFPAREESVFDTFGVGHSSTAISAGLGMSLARRYQKDPCEVVCIVGDGAMTAGMAFEAMNDAVAHDADLIVVLNDNDMSISCSTGGFAKHLAAIWEKGHLVNVNEHGEAYIQPHPKWTYNSRLHQSATDAADNLFKAIGFDYFGPFDGHDVTQLVQVFNVLKKRKGPRLVHVYTKKGKGFAPAEADPITYHAIGKINAASGGKTPPKYSDVFGEWLCDEAAQDERLLAITPAMCEGSGMVKFAKQFPQRFFDVAIAEQHAVTLAAGMACEGLKPVVAIYSTFLQRGYDQLIHDVALQNLDVTFGIDRAGLVGEDGPTHAGAYDYAYMRTVPNMVIMAPKDENECRQMLHTAYAYNGPAAVRYPRGAGVGVEIQKEMTVLELGKAEIVAEIKANSDEQITVLAFGSRVMVALEAAEQFAQKHDVSVCVVNMRFVKPLDEQMIRDLAEHTHLFVTVEEHAIMGGAGSAVNEFMAQEQIVKPIINLGLPDSFLHQATHNQMLQDCGLDAKGILNSIERAWLKVNQVV
|
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).
|
B0VQB8
|
C4JUN6
|
CYNS_UNCRE
|
Cyanate lyase
|
Uncinocarpus
|
MANLATLDHPYLPQSASLLFDAKAKANLTFEDIARHIGRNEVATAAIFYGQAKASKEDVVKLAELLRLPAQALEMQMGGFPDRGRSVDMPPREPLIYRLYEIVQNYGYAYKAVLNEKFGDGIMSAISFSTNVEKETDDDGNNWAVITLRGKW
|
Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
|
C4JUN6
|
D4D449
|
DMAW_TRIVH
|
L-tryptophan dimethylallyl transferase
|
Trichophyton
|
MGSIEIPNCSGSIVYKTISDFIDFPDHEQKLWWHSTAPMFAEMLRVAGYDLHSQYKILGIFLNHVIPFLGVYPTRINNRWLSILTRYGTPFELSLNCSQSLVRYTYEPINSATGTVKDPFNTHSIWDALDRLMPLQKGIDLEFFKHLKQDLTVDDQDSAYLLENNLVGGQIRTQNKLALDLKGGNFVLKTYIYPALKALATGKSIKTLMFDSVYRLCRQNPSLEAPLRALEEYVDSKGPNSTASPRLLSCDLIDPSKSRVKIYILELNVTLEAMEDLWTMGGRLNDASTLAGLEMLRELWDLIKLPPGMREYPEPFLQLGTIPDEQLPLMANYTLHHDQAMPEPQVYFTTFGLNDGRVADGLVTFFERRGWNHMA
|
Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid . DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan . The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine . The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde . Chanoclavine-I aldehyde is the precursor of ergoamides and ergopeptines in Clavicipitaceae, and clavine-type alcaloids such as fumiclavine in Trichocomaceae . However, the metabolites downstream of chanoclavine-I aldehyde in Arthrodermataceae have not been identified yet .
|
D4D449
|
Q8NSN2
|
METN_CORGL
|
Methionine import ATP-binding protein MetN
|
Corynebacterium
|
MSHTASTPTPEEYSAQQPSTQGTRVEFRGITKVFSNNKSAKTTALDNVTLTVEPGEVIGIIGYSGAGKSTLVRLINGLDSPTSGSLLLNGTDIVGMPESKLRKLRSNIGMIFQQFNLFQSRTAAGNVEYPLEVAKMDKAARKARVQEMLEFVGLGDKGKNYPEQLSGGQKQRVGIARALATNPTLLLADEATSALDPETTHEVLELLRKVNRELGITIVVITHEMEVVRSIADKVAVMESGKVVEYGSVYEVFSNPQTQVAQKFVATALRNTPDQVESEDLLSHEGRLFTIDLTETSGFFAATARAAEQGAFVNIVHGGVTTLQRQSFGKMTVRLTGNTAAIEEFYQTLTKTTTIKEITR
|
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
|
Q8NSN2
|
P11353
|
HEM6_YEAST
|
Oxygen-dependent coproporphyrinogen-III oxidase
|
Saccharomyces
|
MPAPQDPRNLPIRQQMEALIRRKQAEITQGLESIDTVKFHADTWTRGNDGGGGTSMVIQDGTTFEKGGVNVSVVYGQLSPAAVSAMKADHKNLRLPEDPKTGLPVTDGVKFFACGLSMVIHPVNPHAPTTHLNYRYFETWNQDGTPQTWWFGGGADLTPSYLYEEDGQLFHQLHKDALDKHDTALYPRFKKWCDEYFYITHRKETRGIGGIFFDDYDERDPQEILKMVEDCFDAFLPSYLTIVKRRKDMPYTKEEQQWQAIRRGRYVEFNLIYDRGTQFGLRTPGSRVESILMSLPEHASWLYNHHPAPGSREAKLLEVTTKPREWVK
|
Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
|
P11353
|
Q94361
|
GEI17_CAEEL
|
Gex-3-interacting protein 17
|
Caenorhabditis
|
MLPNNQWQIPINNGLTHQENMAAHAAVMKLRVHDLQSIISQLSLRKPRPQKSEHQKVVVESLRDPHHARQIYQMASNFPNGNYEMQKRPATTSQVRSHPYVLPSRSGASNHLVNHHYQQQQQQQPQPHNLLHQQMMASHHSHLQQQHHPSTVRWLTPELLEEQLRGSMRYGAPAAAAATNAPLHSSFPNHGRSSQQSLQKSEKSNRPKKMYADNFEPLPLPFYDVISVLLKPVELHSSDSPTLKQTKQLQFPFLLTAEHISKISYRADVTPLPRYELQLRFFNLTEPVQGPQKDDFPLNCYARVDDSVVQLPNVIPTNKTNAEPKRPSRPVNITSNMNRYKKEHTVAVEWLADKRVWAAGVYFVHRVNSDILFKRLNQNVSRHRSLEVTKQEVIKKLSGGEDDIAMDRLNISLLDPLCKTRMTTPSRCQDCTHLQCFDLLSYLMMNEKKPTWQCPVCSSNCPYDRLIVDDYFLDMLAKVDKNTTEVELKEDGSYDVIKEEAFCISDDDDDDVVPATVNGTASCSSTNGNGLANEAAKKKPADDDIITLSDDDDEELNRGIMNSLNDSFSPGRHTASAELAAQKTPPQQKKKTKDDDIEIITLDDTPPRPVAASANLPMRQMSQQNQMPVGSSPSGMASTQMGMNEGASKTIRDALNKIGEQSANSSTQSSPLVQLHHTTHPLNFAQSSYMNPSSGSQTPTSQYGYSPMINQAPHFQMQNGLIGRNNQMVHMQQHHLQQQQQQQQSPQIMSPSFYAQQQMSNGGAFAYYPPQYPQQQYRQN
|
Functions as an E3-type smo-1 ligase . Mediates smo-1 conjugation to air-2 in vitro and is required for proper chromosome alignment . In the early embryo, specifically suppresses checkpoint activation in response to DNA damage, maybe by promoting mus-101 sumoylation . In embryos, plays a role in determining telomere localization in the nucleus .
|
Q94361
|
A6X0B4
|
RS7_BRUA4
|
30S ribosomal protein S7
|
Brucella
|
MSRRHKAEKREINPDPKFGDLVITKFMNAVMLHGKKSVAESIVYGALDVIEAKAKSEPVALFHQALDNVAPHIEVRSRRVGGATYQVPVDVRPERRQALAIRWLINAARGRNETTMIDRLSGELLDAANNRGSAVKKREDTHRMAEANRAFSHYRW
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.
|
A6X0B4
|
Q8DEK2
|
RSMH_VIBVU
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Vibrio
|
MTDTFQHISVLLHESIDGLAIKPDGIYIDGTFGRGGHSRTILSKLGEHGRLYSIDRDPQAIAEAGKIDDPRFTIIHGPFSGMANYAEQYDLVGKVDGVLLDLGVSSPQLDDAERGFSFMKDGPLDMRMDPTSGIPVSQWLMEADLDDITWVIREFGEDKHARRIAKAIVAHREDETKEPLTRTSQLAKLISEAAPKSFKEKKHPATRAFQAFRIYINSELEEIDTALKGAASILAPEGRLSVISFHSLEDRMVKRFMRKESKGPEVPHGIPLTEAQIKALGSANMKTVGKAIMPTAQEIELNPRSRSSVLRIAEKL
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
Q8DEK2
|
Q4UMK4
|
PTH_RICFE
|
Peptidyl-tRNA hydrolase
|
spotted fever group
|
MILVIGLGNPGKEYQYTRHNIGFIAIEKIANQYNSSFSIKKKFNCEIAETISDGQKIIFIKPTTYMNLSGKSVISVKTYYNIQSAKIFVIHDDIDLETGRIKFKTGGGNGGHNGLKSIDGVIGNNYNRIRVGVGRPQNNQDVADYVLNNFLKSEYETALQAIDRIANNFDLILENKLEEFKNKIV
|
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
|
Q4UMK4
|
Q9N0C8
|
FBX27_MACFA
|
F-box only protein 27
|
Macaca
|
MGAWASRGRAARVPAPEPESEPEEALDLSQLPPELLLVVLSHVPPRTLLGRCRQVCRGWRALVDGQALWLLILARDHSATGRALLHLARSCQSPARNARPCPLGRFCARRPIGRNPCGQGLRKWMVQHGGDGWVVEENRTTVPGAPSQTCFVTSFSWCRKKQVLDLEEEGLWPELLDSGRIEICVSDWWGARHDSGCMYRLLVQLLDANQTVLDKFSAVPDPIPQWNNNACLHVTHVFSNIKMGVRFVSFEHWGQDTQFWAGHYGARVTNSSVIVRVHLS
|
Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Able to recognize and bind complex-type oligosaccharides.
|
Q9N0C8
|
B8G6P6
|
TRUA_CHLAD
|
tRNA-uridine isomerase I
|
Chloroflexus
|
MRTIALLLAYDGTDFAGSQWQTDIRTVQGAIEAAWEALTQEQRRIVLAGRTDAGVHASGQVAHVQTATRHSLATIWRGLNAHLPTDVTVQNVGEAVRDFHARYSAIEREYRYLIDCAPVPLPQLRHQALHYAGTLDVTAMATALKLLEGTHDFAAFTTATPSQRSTVRTMYWTRIVERVWFDRRLLAIELAANAFLQHMVRMIVGTLLLVGRGRMTVDQFGEVLAGRDRRLAGPTAPAHGLTLTAVRYPPGLIRWVEPLERQQGATKVEQPSSYVHEE
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
B8G6P6
|
C5BQG6
|
FABZ_TERTT
|
Beta-hydroxyacyl-ACP dehydratase
|
Teredinibacter
|
MLDILEIRKYLPHRYPFLMIDRVVELIEGESITAYKNVSINEEIFQGHFPHFPVFPGVLLIEAMAQACGVLGFKTANKTPEDGSIYLFAGIDGVRFKRQVVPGDRVYFECKVVSAKRGIWKFDCVAKVDGELVTSATIMCADRVVG
|
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
|
C5BQG6
|
Q46IT1
|
RS11_PROMT
|
30S ribosomal protein S11
|
Prochlorococcus
|
MATTSKKSGSKKSKRNVPNGVVHIQSTFNNTIVSITDTSGEVISWSSAGASGFKGARKGTPFAAQTAAELAARRALEQGMRQIEVLVRGPGSGRETAIRALQVAGLEITLIRDVTPLPHNGCRRPKRRRV
|
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
|
Q46IT1
|
B4TWF9
|
MURA_SALSV
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Salmonella
|
MDKFRVQGPTTLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNGSVHIDASQVNVFCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHITGLEQLGATIKLEEGYVKASVEGRLKGAHIVMDKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLVTLGAKIAGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAISRGKILCRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAQGTGFITETVFENRFMHVPELSRMGARAEIESNTVICHGVETLSGAQVMATDLRASASLVLAGCIAEGTTIVDRIYHIDRGYERIEDKLRALGANIERVKGE
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
B4TWF9
|
Q8DTM9
|
WHIA_STRMU
|
Probable cell division protein WhiA
|
Streptococcus
|
MSFTTQVKEEILNLDSADKNELSAIIKMSGSLGLADKKLSLSIITENAKIARHIYALLERLYRINPEIKYHHKTNLRKNRVYTVFLDDNVEQILADLQLSDSFFGIETGIEQQILSDDNAGRSYLKGAFLSTGSIRDPESGKYQLEIFSVYLDHAEDLAKLMQKFMLDTKVIEHKHGAVTYLQKAEDIMDFLIIIGSMEGMEAFENIKVMRETRNDVNRTSNAETANIAKTINASIKTINNINKIKETVGLESLPIELQRIAQIRAAHPDFSIQQIADSLAVPLTKSGVNHRLRKINKIAEDL
|
Involved in cell division and chromosome segregation.
|
Q8DTM9
|
Q84JK2
|
FD_ARATH
|
bZIP transcription factor 14
|
Arabidopsis
|
MLSSAKHQRNHRLSATNKNQTLTKVSSISSSSPSSSSSSSSTSSSSPLPSQDSQAQKRSLVTMEEVWNDINLASIHHLNRHSPHPQHNHEPRFRGQNHHNQNPNSIFQDFLKGSLNQEPAPTSQTTGSAPNGDSTTVTVLYSSPFPPPATVLSLNSGAGFEFLDNQDPLVTSNSNLHTHHHLSNAHAFNTSFEALVPSSSFGKKRGQDSNEGSGNRRHKRMIKNRESAARSRARKQAYTNELELEVAHLQAENARLKRQQDQLKMAAAIQQPKKNTLQRSSTAPF
|
Transcription factor required for the transition to flowering promoted by FT.
|
Q84JK2
|
Q9SNC0
|
MBD5_ARATH
|
Methyl-CpG-binding protein MBD5
|
Arabidopsis
|
MSNGTDQAQPPPENPATPVDSKSRKRATPGDDNWLPPDWRTEIRVRTSGTKAGTVDKFYYEPITGRKFRSKNEVLYYLEHGTPKKKSVKTAENGDSHSEHSEGRGSARRQTKSNKKVTEPPPKPLNFDFLNVPEKVTWTGINGSEEAWLPFIGDYKIQESVSQDWDRVFTLVTSQNAGKTMF
|
Transcriptional regulator that binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. In addition, binds specifically methylated m(5)CpNpN but not m(5)CpNpG (N is A, T or C). Plays probably a role in gene silencing.
|
Q9SNC0
|
B3E4X8
|
MURA_TRIL1
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Trichlorobacter
|
MDKLIINGGRKLKGEVTVSGSKNASLPICIAAVLAPGASTITNVPRLRDITTTAKLLESLGATIERHENTMRIDAGTINTVEATYDLVKTMRASVLVLGPLLARFGRSRVSLPGGCAIGARPIDQHLKGLKALGAEIRLEHGYVEAIAKKGLKGARINFDVSTVGGTEHLMMAAAIAKGESILENAAREPEIADLADYLNRMGAKVEGAGTDTIRIQGVSELTPAAYEVMPDRIEAGTFMCAAAITGGDIKINGMKLEHLDALTFKLMDAGVEITNRNGVVRVKGPKRPQAVNIKTRPYPGFATDMQAQFMALMCVAEGASVISENIFENRFMHVSELLRFGADITVEGNSATVKGVKKLSGAPVMATDLRASACLVLAGLAAEGTTEIQRIYHLDRGYEQIETKLAGLGADIQRVSEP
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
B3E4X8
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.