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Full Name
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taxon
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sequence
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2.75k
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5.51k
AlphaFoldDB
stringlengths
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10
Q9L7R5
YIHP_SALTY
Putative 2,3-dihydroxypropane-1-sulfonate exporter
Salmonella
MSQTSSNPATLRLPFKEKLAYGLGDLGSNILLDIGTLYLLKFYTDVLGLPGTYGGIIFLIAKFFTAFTDMGTGIMLDSRRKIGPKGKFRPFVLYAAFPVTLLAIANFVGTPFEVTGKTVVATMLFMLYGLVFSMMNCSYGAMVPAITKNPDERASLAAWRQGGATLGLLLCTVGFVPVMNLIEGNAQLSYIFAATLFSLFGLLFMWLCYAGVKERYVEVKPVDSAQKPGLLQSFRAIAGNRPLFILCIANLCTLGAFNVKLAIQVYYTQYVLNDPILLSWMGFFSMGCIFIGVFLMPGAVRRFGKKKVYIGGLLIWVAGDLLNYFFGGGSVSFVAFSCLAFFGSAFVNSLNWALVSDTVEYGEWRTGVRSEGTVYTGFTFFRKVSQALAGFFPGWMLTQIGYIPNVVQSAGTVEGLRQLIFIYPCVLAVITIIAMGCFYNLNEKMYVRIVEEIEARKHTV
Could be involved in the export of 2,3-dihydroxypropane-1-sulfonate (DHPS).
Q9L7R5
Q86I22
FAHD1_DICDI
Fumarylacetoacetate hydrolase domain-containing protein 1
Dictyostelium
MNKFWETGRKIVAVGRNYAQHAKELGNEIPSEPFFFLKPTSSYLLQGTGPIEIPLESSDIHHEVELGIVIGKKGRDIDLKSAMDYVSGYTLALDMTSRDQQSIAKAKSLPWTVSKGYDTFCPISGFIPKDKIKDLNNVELWCSVDGQIKQKGNTNQMIFDVPHLIQYISSIMTLESGDLILTGTPSGVGPVKPGQVIKCGITGLDTDMQFDIILRKRN
Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro.
Q86I22
B1KG88
GCSH_SHEWM
Glycine cleavage system H protein
Shewanella
MSNIPAELKYASSHEWIRKEEDGSYTVGISEHAQELLGDMVFVELPEVGDTLSAGEDCAVAESVKAASDIYAPLSGEVLAVNEALEDSPELVNSDAFGDGWFFRVMPSDVAEIDNLLDAEGYQAVIDEE
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
B1KG88
Q0KEE2
PYRC_CUPNH
Dihydroorotase
Cupriavidus
MTQKLTITRPDDWHLHLRDGAALAAVLPDTARQFARAIIMPNLKPPVTTVAQAQAYRARILAALPAGLQFEPLMTLYLTDNTTAEEIAAAKASGFVHGVKLYPAGATTNSDAGVTDIRRCYPALEAMQRAGLPLLVHGEVTDPSIDIFDREAVFIDRVMTPLRRDMPELKVVFEHITTKDAAEYVRDASGPVGATITAHHLLYNRNAIFTGGIRPHYYCLPVLKRETHREALVAAAVSGSPRFFLGTDSAPHARGLKEHACGCAGCYTALHAMELYAEAFDAAGALDKLEAFASFNGPAFYGLPRNTGTLTLEREDWELPAELPYGDTTLVPLRGGETLRWKAR
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Q0KEE2
Q1DLM0
EFGM_COCIM
Elongation factor G1
Coccidioides
MSVHTVMRTQVRSLAGMPKAAMRPLGNSFCARRYLSAAPLRSIPAAPTRLPLNRRWEPKRHSSSATAAAVLEQAAAQPETLSQDAIIESMDPAEAARISKVRNIGIAAHIDSGKTTSTERVLFYTGRIQAIHEVRGRDSVGAKMDSMDLEREKGITIQSAATFCDWVKKENGKDEKYHINLIDTPGHIDFTIEVERALRVLDGAVLILCAVSGVQSQTITVDRQMRRYNVPRISFINKMDRMGSNPFRAIEQINQKLKMHAAAVQVPIGLEDEFKGVVDIIRMKAIYNEGPRGEMVVEKDEIPADVRPVAEERRRMLIETLADVDDDIAELFLEEKEPTVEQLKAAIRRATIARTFTPVFMGSALADKAVQPMLDGICDYLPNPAEIENLALDQKRNEASVKLVPYNSLPFVGLAFKLEESNFGQLTYIRVYQGTLRKGTNVFNARNNKRIKVPRIVRMHSNEMEEVSEIGAGEICAVFGVDCASGDTFTDGQLNYSMSSMFVPEPVISLSIKPKNSKDLANFSKAINRFQREDPTFRVHFDTESEETIISGMGELHLDIYVERMRREYRVDCETGKPQVAYRETIGKRVEFDHLLKKQTGGPGEYARVAGWMEPTGNLDGNNFEEQITGGSISEKFLFACEKGFGLACDKGPLIGHKVLGTRMVINDGATHMTDSSEMSFKNATQQAFRKAFMDSQPHILEPLMKTVITAPSEFQGDVIALLNKRNAIINDTETGVDEFTVYADCSLNGMFGFSTHLRAATQGKGEYTMEFSHYEKAPGHLQKELIAEYEKAQAARHKK
Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Q1DLM0
Q328K3
ULAB_SHIDS
Ascorbate-specific phosphotransferase enzyme IIB component
Shigella
MTVRILAVCGNGQGSSMIMKMKVDQFLTQSNIDHTVNSCAVGEYKSELSGADIIIASTHMAGEITVTGNKYVVGVRNMLSPADFGPKLLKVIKEHFPQDVK
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 UlaABC PTS system is involved in ascorbate transport.
Q328K3
Q9L3I7
YQGF_AERHY
Putative pre-16S rRNA nuclease
Aeromonas
MSSRSIMGFDYGTKSIGVAIGQELTGTGQPLRAIKANDGIPNWDDIDKLLKEWQPDLLVVGLPLNMDGTEQEITVRARKFGNRLHGRFWQAVEFKDERLTTTDARARLFERGGYRALEKGSVDGVSAQLILEAWMEEQYG
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Q9L3I7
Q0I2G0
CCMA_HAES1
Heme exporter protein A
Histophilus
MQNNHLQLEQLACQRGDKILFTDLNLDAKSGDFVQIEGHNGIGKTSLLRIIVGLSFPAKGKVRWNKIEINKNREEYQHNLLYLGHLAGIKPELSAWENLQFYQKIGNCRQSEELLWDILQKVGLLGREDLPAGQLSAGQQKRIALARLWLSNAALWILDEPFTAIDKQGVNVLTQLFEQHVENGGIVILTSHQEIPSNKLQKVRLDQYKFFDQGNMA
Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system.
Q0I2G0
Q2JV04
MINE_SYNJA
Cell division topological specificity factor
unclassified Synechococcus
MLLDFLDQLFSRHSGNSREQAKQRLKLILAHDRADLTPAALEAMRLEILGVVSRYVELDSEGMQFHLAAEGGTTALIANLPIRRVKPLAEARLNSCEGENPQQDPGAAPSEGGHLSSPSP
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
Q2JV04
D7PI17
GSFC_PENAE
Griseofulvin synthesis protein C
Penicillium
MTLDQISRIQALVAEIADLSQTFEGPSERFMVDGLPFLRKSEELVTLVQSPAEHATSLIIKTMETAVIRTLLSLNVLQTIPTTGSITLQSLAVATETQESLLERLLRVVTKTGFIIRENGGYSHSHTSLAYAGPLGALFAPCYDEGIRALVRLPEYLSVKDKEEAKNARYSLFTWNEGQEGKATFEILSTMPARTEGIHTLAMNVQHLRPYTGFFDYSKLVSEDRERPVFVDVGGGNGHVIKEILQAFPQIRPEQCVLEDRAETLELARTTGLLPAGVQLLEHDYLTRQPVSNAKAYHLRAVAYNLGDAELVQLLKQIVPVMGADSKVLIAENILFDDNSTVFSTVSDMIMLGIGGKERTEQNFREVLYEAGLTIEGIHRAPGLEYGIMEASLATS
O-methyltransferase; part of the gene cluster that mediates the biosynthesis of griseofulvin, an important antifungal drug that has been in use for a long time for treating dermatophyte infections . The first step of the pathway is the formation of the heptaketide backbone by gsfA which is initiated by priming with acetyl-CoA, followed by sequential condensations of 6 malonyl-CoA units . O-methylation at 3-OH by gsfB leads to griseophenone D which is further methylated at 9-OH by gsfC to yield griseophenone C . Griseophenone C is then substrate of halogenase gsfI which is responsible for the regio-specific chlorination at the C13 position to form griseophenone B . The cytochrome P450 gsfF catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A which is further methylated at 5-OH by gsfD to yield dehydrogriseofulvin . Finally, gsfE performs stereospecific reduction of enone 18 of dehydrogriseofulvin to afford the final product griseofulvin .
D7PI17
Q38W67
RRF_LATSS
Ribosome-releasing factor
Latilactobacillus
MANPILEQAKENMEKAEASLRRTLGQIRAGRANASLVNRVNVEYYGAMTPLNQIAAITIPEARVLLITPYDKGALEDIEKALYTADIGISPANDGSVIRLVIPQLTGERRKEIAKEVGKEAELAKVVVRNARRDAMDNLKKAEKASEISEDEMHDLEEQVQNLTNEATKKIDAISKDKEKEITEG
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
Q38W67
O75635
SPB7_HUMAN
TP55
Homo
MASLAAANAEFCFNLFREMDDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQSGLQSQLKRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYDAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLLPENDLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGGRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIRKDDIILFSGKVSCP
Might function as an inhibitor of Lys-specific proteases. Might influence the maturation of megakaryocytes via its action as a serpin.
O75635
Q5NNS2
IF1_ZYMMO
Translation initiation factor IF-1
Zymomonas
MAKEELLEMRGRVVELLPNAMFRVQLENDHEILGHTAGKMRKNRIRVLVGDEVLVELTPYDLTKGRITYRFK
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Q5NNS2
A5EPZ7
GLGB_BRASB
Glycogen branching enzyme
unclassified Bradyrhizobium
MTHLSPEAFAIIEGRHADPFRYLGQHDVDGRTVIRAFLPEASRVEAVGDNGEVAPLARIHDAGLFTGTMSGPQRYRLRATFGDHVTDLEDPYRFLPILTDFDLHLLGEGNHERLYDKLGAHPMVLDGVDGVGFVVLAPNARRVSVVGDFNFWNARRHPMRVRGNGYWELFIPRAKAGDHYKFDIIGPQGEHLPLKSDPMAFAAEMRPKTASIVVDETRLPRPRPAPSDINKLDRPVSIYEVHLGSWRRKDNNQWLTYRELAEQLPAYARDMGFTHIEFLPVSEHPFDGSWGYQPTGLFAPTSRFGSPEDFCALVDACHREGLAVWLDWVPGHFPDDPHGLGHFDGTALYEHANPMQGRHLDWGTLIYNYGRTEVANFLRSNALFWLERYGIDGLRVDAVASMLYLDYSRPSGGWIPNKYGGRENLEAIEFLRRTNIEVFGHFPQATTAAEESTAWPQVSRPVDIGGLGFGYKWNMGWMHDTLRYVGKDPIHRKYHHGEILFGLHYAFSENFILPLSHDEVVHGKRSILGRMPGDDWQRFANLRAYYSFMFGHPGKKLLFMGCEIAQEREWNHDSSLDWHLLGDAKYAGIQALIRDLNHLYRNQPALHERDCEPEGFDWLITEDADRNVFAWVRKGFDERARCVVVVNFSPNVYYNYRVRVPLGGTWREVFNSDSSHYGGSNVGNVGQVHASEDQQLNLILPPMAAVFLVPEA
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
A5EPZ7
Q7K755
GLT11_CAEEL
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11
Caenorhabditis
MLLLWRRKTVGLICLFSILLTIYLYVSMYPEDNERVWNSGNADIQRKHEKLNNGGQGRHDFDDDEGAEKDEEDAVEKQNIAAPPLPKSFTTFPDRSKEIEIDTDLLGKINGKAEDDLQVEGYKKYQFNGLLSDRIGSRRKIKDSRNARCSSLTYSDSLPAASIVVCYFNESPSVLIRMVNSIFDRTKPEHLHEILLVDDSSEWSNATDEAIKYREKHIIQWEKVKFLKTDKNEGLIRAKIFGARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVCPIIDIIDAITMKYVESPVCTGGVNWAMTFKWDYPHRSYFEDPMNYVNPLKSPTMAGGLFAIDKEYFFEIGSYDEGMDVWGAENVEISVRIWTCGGELLIMPCSRVGHIFRRQRPYGIKTDSMGKNSVRLARVWLDEYLENFFEARPNYRTFTDYGDLTSRISLRRNLQCKPFKWYLENIYPELLPDNTPNQLNNQILVAGKKYLIKMANGTHCLSAENSQGRIANGNRVEMRKCNHMERMQQWKYSSTNELRPMGSSRMCLDSLRGISVILCHNQGAHQMWQVSNAGKLYSRSVNKCATGSNDVSALSTLKFCSLANSFQFVEL
May catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.
Q7K755
B7XHU4
RSSA_ENTBH
40S ribosomal protein S0
Enterocytozoon
MSDSSIKMPPVFGKLLLATQAHLGGVKVTKPMKKYIYGERQDKVSVFDLKKTWDKFILAARAFCGLNYGDDVTVISCKTFGKKPVLKFAETTGAKSYTGRFIPGSFTNTTIRNSCEPRLIIVSDPIVDKQAIEEAAKVNCPTIAFCNTDCDLKYVDIAIPLNNRSPKAIGASFFILSRIIRYIKFGTPMDQDIKEVELFFYRDPIELEKLQEDQNEDNYNEIFNKFSNANEDEFGKIIYK
Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.
B7XHU4
Q8PDA2
HGD_XANCP
Homogentisicase
Xanthomonas
MIQLDPTLLLSWRAGQHPDAPMHNDQRYMTGFGNEFASEAVADTLPVGQNSPQRVAHGLYAEQLSGTAFTAPRGENRRSWLYRMRPAAVHGTFSLIEQSQFHNDFGHGPVPPDQLRWSPLPLPQTPTDFIDGLYTMAGNGSPEAMNGVAVHLYAANASMQDRFFYNADGELLLVPQLGRLRVHTELGMLELEPQQIGVIPRGVRFRVELRDGTARGYVCENFGGLLHLPDLGPIGSNGLANPRDFETPCAAFEQREGRFELVAKFQGHLWRADIGHSPLDVVAWHGNYAPYRYDLRRFNTIGSISFDHPDPSIFTVLTSPSDTHGTANMDFAIFPPRWLVAQHTFRPPWFHRNVASEFMGLVHGVYDAKADGFAPGGASLHNCMSGHGPDAATFDKASQADLSRPDVITETMAFMFETRAVLRPTAQALHAPHRQGDYQQCWAGLRKAFQAPPAS
Involved in the catabolism of homogentisate (2,5-dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring cleavage of the aromatic ring of homogentisate to yield maleylacetoacetate.
Q8PDA2
Q2KU87
GMHA_BORA1
Sedoheptulose 7-phosphate isomerase
Bordetella
MDMTSRMTSHFRDAMALCEQSMQALSEPLAGAVELLFAALANNGRILACGNGGSAADAQHFVAELVGRFERDRLPLAGIALNTDTSILTAVGNDYGFDEIYERQVNALGQPGDVLVAISTSGNSPNVVRAMEAARDREMHVIALTGKGGGVMGELITPHDVHLCVPHDRTMRIQEIHILLLHALCDGIDALLLGDTE
Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
Q2KU87
Q831A4
ATPG_ENTFA
F-ATPase gamma subunit
Enterococcus
MGASLNEIKQRIASTKKTSQITKAMQMVSAAKLTKSEGASKSFQEYSSKIRSVVTHLVAAQLSELRETEQSSLSEGNYHVMLAQRPVKKTGYIVITSDKGLVGGYNSSILKQTMSMIQEDHDSNKEYALIAIGGTGADFFKARGIDVSYELRGLTDQPTFEEVRKIVTTATTMYQNEVFDELYVCYNHHVNSLTSQFRVEKMLPITDLDPSEATSYEQEYLLEPSPEAILDQLLPQYAESLIYGAIIDAKTAEHAAGMTAMKTATDNAQNIISDLTISYNRARQGAITQEITEIVAGAAALE
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Q831A4
Q9FVV7
RD521_ARATH
Organellar DNA-binding protein 1
Arabidopsis
MAGLGLRLKAAKWTLRSGSGAVSREWSSEMGKGVRRFSTETENDVPTSGISRPLAEILKELNKKVPDSVIRTRVEDGCSIKYIPWHIVNRIMNMHAPEWSGEVRSVTYSPDGNTVTVAYRVTLYGTDAEIFRESTGTTSVDDKGYGDAVQKAEAMAFRRACARFGLGLHLYHEDAL
Plant-specific single-stranded DNA-binding protein required for efficient heterologous recombination-dependent DNA repair in nuclear and mitochondrial compartments. Forms large nucleo-protein complexes with WHY2 in mitochondria. Binds ssDNA with high affinity, but with little sequence specificity . Involved in double-stranded DNA break repair . Involved in the hydrolytic splicing pathway in mitochondrion. Facilitates the excision of two cis-spliced group II introns, NAD1 intron 2 and NAD2 intron 1 .
Q9FVV7
A1UR85
RUVA_BARBK
null
Bartonella
MIGKLTGILDSVFEDHIILDVQGVGYVVFLSNRLLSSLPERGQAVSLFIETHVREDAIRLFGFETKVEQDWFCLLQNVRGVGAKVALAILSTLPPPQLAQAITLSDIAMISRSPGVGKMVSERIINELKNKALPSNAPHQSMPHFVSYSSETSSQAGTQHTGHQHSMDALAALTKLGFERDQATHALQEAIKAFEGETPSSALLIRHSLKLLSSHLK
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
A1UR85
C1C5V9
PNP_STRP7
Polynucleotide phosphorylase
Streptococcus
MAKQVFQTTFAGRELIVETGQVAKQANGSVVVRYGESTVLTAAVMSKKMATGDFFPLQVNYEEKMYAAGKFPGGFMKREGRPSTDATLTARLIDRPIRPMFAEGFRNEVQVINTVLSYDENASAPMAAMFGSSLALSISDIPFDGPIAGVQVGYVDGQIIINPSQEQAEQSLLELTVAGTKHAINMVESGAKELSEEIMLEALLKGHEAVKELIAFQEEIVAAVGKEKAEVELLHVDAELQAEIIAAYNSDLQKAVQVEEKLAREAATQAVKDQVTAVYEEKYANHEEFDRIMRDVAEILEQMEHAEVRRLITEDKVRPDGRKVDEIRPLDAVVDFLPRVHGSGLFTRGQTQALSVLTLAPMGETQIIDGLDPEYKKRFMHHYNFPQYSVGETGRYGAPGRREIGHGALGERALAQVLPSLEEFPYAIRLVAEVLESNGSSSQASICAGTLALMAGGVPIKAPVAGIAMGLISDGNNYTVLTDIQGLEDHFGDMDFKVAGTRDGITALQMDIKIQGITAEILTEALAQAKKARFEILDVIEATIPEVRPELAPTAPKIDTIKIDVDKIKIVIGKGGETIDKIIAETGVKIDIDEEGNVSIYSSDQDAINRAKEIIAGLVREAKVDEVYRAKVVRIEKFGAFVNLFDKTDALVHISEMAWTRTNRVEDLVEIGDEVDVKVIKIDEKGRIDASMKALLPRPPKPEHDEKGEKSERPHRPRHHKDHKPKKEFTETPKDSE
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
C1C5V9
Q75N23
TNFA_CAMBA
Tumor necrosis factor, soluble form
Camelus
MSTESMIRDVELAEEALPKKAGGPQGSRRCLCLSLFSFLLVAGATTLFCLLHFGVIGPQKEELLTGLQLMNPLAQTLRSSSQASRDKPVAHVVADPAAQGQLQWEKRFANTLLANGVKLEDNQLVVPTDGLYLIYSQVLFSGQRCPSTPVFLTHTISRLAVSYPNKANLLSAIKSPCQGGTSEEAEAKPWYEPIYLGGVFQLEKDDRLSAEINMPNYLDFAESGQVYFGIIAL
The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells.
Q75N23
Q13YU3
MASZ_PARXL
Malate synthase G
Paraburkholderia
MTQMNPRGGLQVAANLDQFVETEALPGTGLDSAAFWSGFDALVHELAPKNRALLAERDRLQTELDNWHRANPGPVRDLRAYRAFLEGIGYIVPVPASVKATTDHVDTEIAEQAGPQLVVPLSNQRYALNAANARWGSLYDALYGTDAIPEANGAEKQKAFNPVRGAAVIAYARRFLDQAAPLANGSHADATRYGVEGGKLVVTLKNGTSELKTPAQFIGYQGEESAPSAVLLKHNGLHFEIQIDANDSIGKTDSAHVKDVVVEAAVSTIIDCEDSVAAVDADDKVQLYRNWLGLMNGDLTEEVTKNGKTFTRRLNADRVYTAANGTAPVVLHGRSLLFIRNVGHLMTNPAVLTKDGHEIPEGILDAVITSLCALHDRKHKLNSRTGSIYIVKPKMHGPAEVAFASELFARVEDLLKLPRNTIKMGIMDEERRTSVNLLACINEARERVAFINTGFLDRTGDEMHTAMEAGPMLRKGDMKSSAWIAAYERSNVLVGLSAGLRGRSQIGKGMWAMPDLMHAMLEQKIAHPKAGANTAWVPSPTAATLHALHYHQVDVQAVQQELERTDYAKVRDELLDGLLTIPVVAEAKWSDDEIRSEIDNNAQGILGYVVRWIDQGVGCSKVPDIHNVGLMEDRATLRISSQHIANWLYHGVVKRELVEETFRRMARVVDEQNAGDPLYKPMAPGFDTIAFKAAQALVFEGRQQPSGYTEPLLHKFRLEVKKEA
Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
Q13YU3
A1S1G6
YIDD_SHEAM
Putative membrane protein insertion efficiency factor
Shewanella
MAQTQSPFQWLATKLIRGYQIFISPILGPKCRFQPTCSHYAIEAIQLHGVIKGSWFAAKRILKCHPLHPGGNDPVPPKKDRCNK
Could be involved in insertion of integral membrane proteins into the membrane.
A1S1G6
Q8S3R1
MDAR1_ORYSJ
Monodehydroascorbate reductase 1, peroxisomal
Oryza sativa
MGRAFEYVILGGGVAAGYAALEFVRRNGGASSQELCIISDEHFAPYERPALSKGYLLPQDAPRLPAFHTCVGSKDELLTEEWYNEHGIVLVLGTRVISADVRQKTLLTSSGETISYKTLIVATGARAVKLEEFGVSGSDARNVCYLRNVEDADKLVGVMRSCPGGNAVVVGGGYIGMECAAALVTNNIKVTMVFPKKHCMGRLFTPKIAEFYESYYASRGVTFVKEAAVTSMQISAGKVTAVNLGNGRRLPADMVVVGVGARANTGLFDGQLVMENGGIKVNGRMQASDASVYAVGDVAAFPVKLFGGDVRRLEHVDCARRTARHAVAAMLEGTGSVGHIDYLPFFYSRVFSLSWQFYGDNAGEAVHFGDLAPPGDGDGAAPKFGAYWVRDGRVAGAFLEGGSRQEYEAVAAAVRRGAAVADVAELERRGLAFATQATGGGGKPTCAWHATVGVAAAVSIAAFACWYGWQAPYVLKRDF
Catalyzes the conversion of monodehydroascorbate to ascorbate, oxidizing NADH in the process. Ascorbate is a major antioxidant against reactive oxygen species (ROS) and nitric oxide (NO).
Q8S3R1
Q4JAK2
AGL16_SULAC
Archaeal glycosylation protein 16
Sulfolobus
MYKVWMLTPLFLPVRGGTEVHVFNLSRELVKMSIDVEVHTTRDTYTEREKLIPFEIMDGIKVVRHKRTWIYRDSPSVLHFHNLGRKFSTWNLYTFLFFSLPSVEAPLVMTPHHIFVSDQGRVINWLKRNIGKRVDKLIAVSEWEKEEMINLGYDGSKIVVIPNGVDDMAFNYPKSEGFEDYLLYIGRISPEKNQLFAIECIKNLNVKLILIGQVRDKDYLEKIMTRVSELGLEDKVRYLGVVTEEEKYSLMDKSLAVILTSDIEAEGIVIKEAMVRGVPVIVGNKAKVLSTIVKDGVNGFVISSCQDLKDAVEKLRDPKVRKEIGENNISISREWRWRNVSLKVLELYKSLS
Glycosyltransferase catalyzing the last biosynthesis step of the N-glycan biosynthesis.
Q4JAK2
A8M449
FOLD2_SALAI
Methenyltetrahydrofolate cyclohydrolase
Salinispora
MTATLLDGKATAAEIKDELRVRVKALAERGVTPGLGTVLVGADPGSQAYVNGKHRDCAEVGVASLRRELPADASQEQVDAVLADLNADPACHGYIVQLPLPDHLDTQRVLELIDPEKDADGLHPVNLGRLVLGYPGPLPCTPRGIVELLRRHDVALRGARVAVVGRGNTVGRPLGLLLTRRSENATVTLCHTGTLDLSAHTRAADIVIVAAGVPGLLTPDMITPGAVVVDVGITRVIGPDGKGRYTGDVDPGVTEVAGALVPMPGGVGPMTRAMLLTNVVERAERG
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
A8M449
Q9NYB0
TE2IP_HUMAN
Repressor/activator protein 1 homolog
Homo
MAEAMDLGKDPNGPTHSSTLFVRDDGSSMSFYVRPSPAKRRLSTLILHGGGTVCRVQEPGAVLLAQPGEALAEASGDFISTQYILDCVERNERLELEAYRLGPASAADTGSEAKPGALAEGAAEPEPQRHAGRIAFTDADDVAILTYVKENARSPSSVTGNALWKAMEKSSLTQHSWQSLKDRYLKHLRGQEHKYLLGDAPVSPSSQKLKRKAEEDPEAADSGEPQNKRTPDLPEEEYVKEEIQENEEAVKKMLVEATREFEEVVVDESPPDFEIHITMCDDDPPTPEEDSETQPDEEEEEEEEKVSQPEVGAAIKIIRQLMEKFNLDLSTVTQAFLKNSGELEATSAFLASGQRADGYPIWSRQDDIDLQKDDEDTREALVKKFGAQNVARRIEFRKK
Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes.
Q9NYB0
B9JV52
MNMG_AGRVS
Glucose-inhibited division protein A
Agrobacterium
MPRRFDVIVIGGGHAGSEAAYASARLGARTCLVTHRRDTIGVMSCNPAIGGLGKGHLVREIDALGGLMGRCADAAGIQFRLLNRKKGPAVRGPRTQADRKLYRQAVQNVLFNHPQLEIIEGDVFDLNVENGTVKGVILADGQSLPSASVILTSGTFLRGLIHIGQTKIPAGRVGEAPSLGLSATLGRLGLRLGRLKTGTPARLDGRTIDWAQLEMQAADEQPVPFSFMTDRITNRQIECGITRTTAATHTIIRDNIHLSAMYSGQIEGVGPRYCPSIEDKISRFGDRDGHQVFLEPEGLDDHTVYPNGISTSLPESVQKEFMRTLPGLENVTILQSAYAIEYDHIDPRELSASLELKRLSGLYLAGQINGTTGYEEAAAQGLVAGLNAARTAGGQDVVHFSRAQSYIGVMIDDLISHGVTEPYRMFTSRAEFRLSLRADNADMRLTPIGIALGCIASDQEKRFKDYRHQIDDTINMLETRKLTPNEAAAVGIPVNQDGRRRTALELLAYPDISIADLSRLWPELDALDSKVAEAVEIHATYAVYMDRQNADIAATKRDEDRLIPKDFDYASLSGLSNELKQKLEKTRPENLSQAAKVEGMTPAAISLLIAFLNKGMLRHVG
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
B9JV52
Q7M7W9
GPMI_WOLSU
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Wolinella
MAQKTLLIITDGIGHKPSSPHNAFTQAKKPTYDSLFASAPHALLSTHGLSVGLPEGQMGNSEVGHMCIGAGRILYQDLVKISLALKDGSLEKNPTLLGFSSRAKRIHLAGLASDGGVHSHMEHLLGLAQIFSRLGHEVLLHLITDGRDVSPTSSKEFIAQALALESDLIKIATISGRYYAMDRDKRWDRIKRAFGVIARGDSPTSLTPQEYIQAQYQAGITDEFIEPAALGGYQGFEPSDGFVFANFRSDRAREIVSALGGASFEGFDRGAYQPPKTLAMTSYDDSFPFPILFPKEKVEPTLAQVISEAGLSQLHVAETEKYAHVTFFFNGGIETPWENESRVLIPSPSVATYDLKPEMSAPEVAEATLSGMRQGYDFIVVNFANGDMVGHTGNTEAAISAVESVDRELGRLLEEAKKSGYAVILTSDHGNCEEMRDERGSMLTNHTVGEVWCFILAQGVTEIREGGLNQVAPTVLKIMGLPTPKEMDSPLF
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Q7M7W9
Q2JRH8
PETG_SYNJA
Cytochrome b6-f complex subunit V
unclassified Synechococcus
MIEPILLGIVLGMVLVTLAGLFVAAYRQYQRGNKMGL
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex.
Q2JRH8
Q72JJ7
RNJ_THET2
Ribonuclease J
Thermus
MENQERKPRRRRRRRPQEGSQGGPQDHVEIIPLGGMGEIGKNITVFRFRDEIFVLDGGLAFPEEGMPGVDLLIPRVDYLIEHRHKIKAWVLTHGHEDHIGGLPFLLPMIFGKESPVPIYGARLTLGLLRGKLEEFGLRPGAFNLKEISPDDRIQVGRYFTLDLFRMTHSIPDNSGVVIRTPIGTIVHTGDFKLDPTPIDGKVSHLAKVAQAGAEGVLLLIADATNAERPGYTPSEMEIAKELDRVIGRAPGRVFVTTFASHIHRIQSVIWAAEKYGRKVAMEGRSMLKFSRIALELGYLKVKDRLYTLEEVKDLPDHQVLILATGSQGQPMSVLHRLAFEGHAKMAIKPGDTVILSSSPIPGNEEAVNRVINRLYALGAYVLYPPTYKVHASGHASQEELKLILNLTTPRFFLPWHGEVRHQMNFKWLAESMSRPPEKTLIGENGAVYRLTRETFEKVGEVPHGVLYVDGLGVGDITEEILADRRHMAEEGLVVITALAGEDPVVEVVSRGFVKAGERLLGEVRRMALEALKNGVREKKPLERIRDDIYYPVKKFLKKATGRDPMILPVVIEG
An RNase that has endonuclease and possibly 5'-3' exonuclease activity. Probably involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
Q72JJ7
P41056
RL33B_YEAST
YL37
Saccharomyces
MAESHRLYVKGKHLSYQRSKRVNNPNVSLIKIEGVATPQEAQFYLGKRIAYVYRASKEVRGSKIRVMWGKVTRTHGNSGVVRATFRNNLPAKTFGASVRIFLYPSNI
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
P41056
Q8BIJ7
RUFY1_MOUSE
Rab4-interacting protein
Mus
MAARGECRRAGQDSEPEPEREPESEPGPEPEPQAGLESGEAFEIVDRSQLPSPGELRSASRPRVADSWSAPILTLARRATGNLSASCGSALRAAAGLGDGGGGGERAASKGQMMEERANLMHMMKLSIKVLLQSALSLGRSLDADYAPLQQFFVVMEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANLCLKGEDLDSQVGVIDFSLCLKDAQDLDSGREHERITDVLDQKNYVEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEITKQDTKVELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKALKGHTWLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCSSTAS
Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in early endosomal trafficking.
Q8BIJ7
D4GP40
XAD_HALVD
D-xylonate dehydratase
Haloferax
MVEQAKLSDPNAEYTMRDLSAETIDITNPRGGVRDAEITDVQTTMVDGNYPWILVRVYTDAGVVGTGEAYWGGGDTAIIERMKPFLVGENPLDIDRLYEHLVQKMSGEGSVSGKVISAISGIEIALHDVAGKLLDVPAYQLVGGKYRDEVRVYCDLHTEDEANPQACAEEGVRVVEELGYDAIKFDLDVPSGHEKDRANRHLRNPEIDHKVEIVEAVTEAVGDRADVAFDCHWSFTGGSAKRLASELEDYDVWWLEDPVPPENHDVQKLVTQSTTTPIAVGENVYRKFGQRTLLEPQAVDIIAPDLPRVGGMRETRKIADLADMYYIPVAMHNVSSPIGTMASAQVAAAIPNSLALEYHSYQLGWWEDLVEEDDLIQNGHMEIPEKPGLGLTLDLDAVEAHMVEGETLFDEE
NADP-dependent D-xylose dehydrogenase involved in the degradation of D-xylose, a major component of hemicelluloses such as xylan. Catalyzes the third reaction in the xylose utilization pathway through dehydratation of D-xylonate into 2-dehydro-3-deoxy-D-xylonate.
D4GP40
C1DJ52
CYAY_AZOVD
Iron-sulfur cluster assembly protein CyaY
Azotobacter
MSLTEARFHELIDDLQQNVEDVFEDSDLDVDLENSAGVLSVRFENGSQLILSRQEPLRQLWLAARSGGFHFDYDEAGGRWICDASGDSLGELLARVTLEQIGEELEFPEL
Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis.
C1DJ52
Q31IZ0
RL7_HYDCU
50S ribosomal protein L7/L12
Hydrogenovibrio
MAITKDDILEAVANMSVMEVVELVEAMEEKFGVSAAAVAVAGPAGDAGAAGEEQTEFDVVLTGAGDNKVAAIKAVRGATGLGLKEAKSAVESAPFTLKEGVSKEEAETLANELKEAGIEVEVK
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Q31IZ0
Q18G49
MOAA_HALWD
Molybdenum cofactor biosynthesis protein A
Haloquadratum
MLEDEFGREVSGVRVSLTDRCNFDCVYCHNEGLGDTRGPMDPQDDEMSTDDVVRFLEVVSQFDIGKVKFTGGEPMLRDDLTEIIRRTPSSMEVSMTTNGTFLPGRAGALREAGLERVNVSQDALDPDEFAEITKSGAYDRVLEGVEAAVDAGLAPVKLNMVVFEHTAEYVEDMVNHVSENAGLQLQLIEYMPELTGHPEWNIDIQRVHDWLADIADRVETREMHDRNRYFVGDGMVEIVDPVENPTFCANCHRVRVTHEGYLKGCLNRNDDLRSMGEMTREEIRETFRETVANRVPYYGEYLIKENDEWVLNDKYLDAPTTHS
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Q18G49
A7X1H4
FMT_STAA1
Methionyl-tRNA formyltransferase
Staphylococcus
MTKIIFMGTPDFSTTVLEMLIAEHDVIAVVTQPDRPVGRKRVMTPPPVKKVAMKYDLPVYQPEKLSGSEELEQLLQLDVDLIVTAAFGQLLPESLLALPKLGAINVHASLLPKYRGGAPIHQAIIDGEQETGITIMYMVKKLDAGNIISQQAIKIEENDNVGTMHDKLSVLGADLLKETLPSIIEGTNESVPQDDTQATFASNIRREDERISWNKPGRQVFNQIRGLSPWPVAYTTMDDTNLKIYDAELVETNKINEPGTIIETTKKAIIVATNDNEAVAIKDMQLAGKKRMLAANYLSGAQNTLVGKKLI
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
A7X1H4
P08977
RT13_MAIZE
Ribosomal protein S13, mitochondrial
Zea
MSYISGARSLPDEQVRIASTKMDGIGPKKAIQLRYRLGISGNIKIHELTKYQIDQIEQMIAQDHVVHWELKRGERADIERLISISRYRGIRHQDGSPLRGQRTHTNARTARKQIRKGNERRLPKEQATD
Located at the top of the head of the small subunit, it contacts several helices of the 18S rRNA.
P08977
Q87XG1
RNC_PSESM
Ribonuclease III
Pseudomonas
MSVSLSRLERQLGYTFKDQELMILALTHRSFAGRNNERLEFLGDAILNFVAGEALFERFPQAREGQLSRLRARLVKGETLALLARGFDLGEYLRLGSGELKSGGFRRESILADALEALIGAIYLDAGMEAARERVLAWLTTEFDSLTLVDTNKDPKTRLQEFLQSRACDLPRYEVVDIQGEPHCRTFFVECEINLLNEKSRGQGVSRRIAEQVAAAAALIALGVENGHE
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Q87XG1
Q9ZJN2
NADC_HELPJ
Quinolinate phosphoribosyltransferase [decarboxylating]
Helicobacter
MEIKTFLECALKEDLGHGDLFERVLEKDFKATAFVRAKQEGVFSGEKYALELLQMTGIECVQNIKDKERFKPKDTLMEIRGDFSMLLKIERTLLNLLQHSSGIATLTSRFVEALNSPKVRLLDTRKTRPLLRIFEKYSVLNGGASNHRLGLDDALMLKDTHLKHVKDLKSFLTHARKNLPFTAKIEIECESFEEAKNAMSAGADIVMCDNMSVGETKEIAAYREAHYPFVLLEASGNISLESINAYAKSGVDAISVGALIHQATFIDMHMKMA
Involved in the catabolism of quinolinic acid (QA).
Q9ZJN2
Q6AWU6
HOL3_ARATH
Protein HARMLESS TO OZONE LAYER 3
Arabidopsis
MENAGKATSLQSSRDLFHRLMSENSSGGWEKSWEAGATPWDLGKPTPVIAHLVETGSLPNGRALVPGCGTGYDVVAMASPDRHVVGLDISKTAVERSTKKFSTLPNAKYFSFLSEDFFTWEPAEKFDLIFDYTFFCAFEPGVRPLWAQRMEKLLKPGGELITLMFPIDERSGGPPYEVSVSEYEKVLIPLGFEAISIVDNELAVGPRKGMEKLGRWKKSSTFHSTL
S-adenosyl-L-methionine-dependent methyltransferase.
Q6AWU6
O48711
PME12_ARATH
Pectin methylesterase 12
Arabidopsis
MALSSFNLSSLLFLLFFTPSVFSYSYQPSLNPHETSATSFCKNTPYPDACFTSLKLSISINISPNILSFLLQTLQTALSEAGKLTDLLSGAGVSNNLVEGQRGSLQDCKDLHHITSSFLKRSISKIQDGVNDSRKLADARAYLSAALTNKITCLEGLESASGPLKPKLVTSFTTTYKHISNSLSALPKQRRTTNPKTGGNTKNRRLLGLFPDWVYKKDHRFLEDSSDGYDEYDPSESLVVAADGTGNFSTINEAISFAPNMSNDRVLIYVKEGVYDENIDIPIYKTNIVLIGDGSDVTFITGNRSVGDGWTTFRSATLAVSGEGFLARDIMITNTAGPEKHQAVALRVNADFVALYRCVIDGYQDTLYTHSFRQFYRECDIYGTIDYIFGNAAVVFQGCNIVSKLPMPGQFTVITAQSRDTQDEDTGISMQNCSILASEDLFNSSNKVKSYLGRPWREFSRTVVMESYIDEFIDGSGWSKWNGGEALDTLYYGEYNNNGPGSETVKRVNWPGFHIMGYEDAFNFTATEFITGDGWLGSTSFPYDNGI
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
O48711
P03018
UVRD_ECOLI
DNA helicase II
Escherichia
MDVSYLLDSLNDKQREAVAAPRSNLLVLAGAGSGKTRVLVHRIAWLMSVENCSPYSIMAVTFTNKAAAEMRHRIGQLMGTSQGGMWVGTFHGLAHRLLRAHHMDANLPQDFQILDSEDQLRLLKRLIKAMNLDEKQWPPRQAMWYINSQKDEGLRPHHIQSYGNPVEQTWQKVYQAYQEACDRAGLVDFAELLLRAHELWLNKPHILQHYRERFTNILVDEFQDTNNIQYAWIRLLAGDTGKVMIVGDDDQSIYGWRGAQVENIQRFLNDFPGAETIRLEQNYRSTSNILSAANALIENNNGRLGKKLWTDGADGEPISLYCAFNELDEARFVVNRIKTWQDNGGALAECAILYRSNAQSRVLEEALLQASMPYRIYGGMRFFERQEIKDALSYLRLIANRNDDAAFERVVNTPTRGIGDRTLDVVRQTSRDRQLTLWQACRELLQEKALAGRAASALQRFMELIDALAQETADMPLHVQTDRVIKDSGLRTMYEQEKGEKGQTRIENLEELVTATRQFSYNEEDEDLMPLQAFLSHAALEAGEGQADTWQDAVQLMTLHSAKGLEFPQVFIVGMEEGMFPSQMSLDEGGRLEEERRLAYVGVTRAMQKLTLTYAETRRLYGKEVYHRPSRFIGELPEECVEEVRLRATVSRPVSHQRMGTPMVENDSGYKLGQRVRHAKFGEGTIVNMEGSGEHSRLQVAFQGQGIKWLVAAYARLESV
A helicase with DNA-dependent ATPase activity . Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand. Initiates unwinding more efficiently from a nicked substrate than ds duplex DNA . Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair, and probably also in repair of alkylated DNA (Probable).
P03018
Q03674
PLB2_YEAST
Phospholipase B 2
Saccharomyces
MQLRNILQASSLISGLSLAADSSSTTGDGYAPSIIPCPSDDTSLVRNASGLSTAETDWLKKRDAYTKEALHSFLSRATSNFSDTSLLSTLFSSNSSNVPKIGIACSGGGYRAMLGGAGMIAAMDNRTDGANEHGLGGLLQSSTYLSGLSGGNWLTGTLAWNNWTSVQEIVDHMSESDSIWNITKSIVNPGGSNLTYTIERWESIVQEVQAKSDAGFNISLSDLWARALSYNFFPSLPDAGSALTWSSLRDVDVFKNGEMPLPITVADGRYPGTTVINLNATLFEFTPFEMGSWDPSLNAFTDVKYLGTNVTNGKPVNKDQCVSGYDNAGFVIATSASLFNEFSLEASTSTYYKMINSFANKYVNNLSQDDDDIAIYAANPFKDTEFVDRNYTSSIVDADDLFLVDGGEDGQNLPLVPLIKKERDLDVVFALDISDNTDESWPSGVCMTNTYERQYSKQGKGMAFPYVPDVNTFLNLGLTNKPTFFGCDAKNLTDLEYIPPLVVYIPNTKHSFNGNQSTLKMNYNVTERLGMIRNGFEAATMGNFTDDSNFLGCIGCAIIRRKQESLNATLPPECTKCFADYCWNGTLSTSANPELSGNSTYQSGAIASAISEATDGIPITALLGSSTSGNTTSNSTTSTSSNVTSNSNSSSNTTLNSNSSSSSISSSTARSSSSTANKANAAAISYANTNTLMSLLGAITALFGLI
Sequentially removes both fatty acyl groups from diacylglycerophospholipids and therefore has both phospholipase A and lysophospholipase activities. However, it does not display transacylase activity. Substrate preference is phosphatidylserine > phosphatidylinositol > phosphatidylcholine > phosphatidylethanolamine . The substrate specificity is pH- and ion-dependent. In contrast with activities observed at optimum pH 3.5, the order of substrate preference at pH 5.5 is phosphatidylserine = phosphatidylethanolamine > phosphatidylcholine > phosphatidylinositol .
Q03674
A8LKV5
ISPDF_DINSH
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Dinoroseobacter
MSHRVLGTERISPREEHVLTPNVTAILVAAGRGTRAGGGLAKQWRPLGARRVIDWTLAAFDRATQVSELLVVLHPEDMDLAATLTAAKPLRCVSGGATRSASVACALAAVADPEAIVLIHDAARPVVSADLIARVVAGVIETGAAAPALPVVDALWTGAGDRVTGMQPRDGLYRAQTPQGFHAGAIRDAHAAATGAAADDVEIARAAGMPVAIVAGDEQNFKITYPQDFARAAALLKERDKMDIRTGNGYDVHRFGTGDAVILCGVEVPHDRALMGHSDADVGMHAVTDAIYGALGDGDIGQHFPPSDPQWKGAASEIFLRHAVALAAERGYTITHMDCTLVCERPKIGPYHAVMKAKMSELMGLQPDQVSVKATTSERLGFTGREEGIAALATVTLVRT
Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
A8LKV5
Q2YL58
LEU3_BRUA2
Beta-IPM dehydrogenase
Brucella
MASRKLLLLPGDGIGPEAMAEVRKVIAFLNSDLNLGFETEEGLVGGCAYDAHGQAISDADMEKALAADSVLFGAVGGPKWDSVPYEVRPEAGLLRLRKDMQLYANLRPAICYPALAHSSSLKPEVIEGLDILILRELTGGVYFGEPKEIIDLGNGQKRGIDTQVYDTYEIERIADVAFELARTRRNKVTSMEKRNVMKSGVLWNQGVTARHKEKHADVQLEHMLADAGGMQLVRWPKQFDVILTDNLFGDLLSDVAAMLTGSLGMLPSASLGAADSKTGKRKALYEPVHGSAPDIAGKGIANPIAMIASLAMCLRYSFGLVAEADRLEAAIAGVLDDGIRTADIWSEGNTKVGTTEMGDAILAKFKALSA
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Q2YL58
Q28UW0
RL23_JANSC
50S ribosomal protein L23
unclassified Jannaschia
MSADAKHYDVIRKPLITEKTTMASENGAVVFEVAIDSNKPQIKEAVEAVFGVKVKAVNTTITKGKVKRFRGQLGTRKDVKKAYVTLEEGNTIDVSTGL
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.
Q28UW0
P43556
RGD2_YEAST
Rho-GTPase-activating protein RGD2
Saccharomyces
MLSFCDYFWSEDLVSGLDVLFDRLYHGCEQCDLFIQLFASRMQFEVSHGRQLFGIEAGMDNLKAVQEDEDEGVTVSRALRGILQEMSQEGTHHLTIASNIESLVLQPFSKWCIEHRERIQYSEKTLLTNVNNFRKSKKYVGKLEKEYFNKCRQLEEFKRTHFNEDELANAMKSLKIQNKYEEDVAREKDHRFFNRIAGIDFDYKTMKETLQLLLTKLPKTDYKLPLISYSLSNTNNGGEITKFLLDHMSLKDIDQAETFGQDLLNLGFLKYCNGVGNTFVNSKKFQYQWKNTAYMFANVPMPGSEEPTTGESLISRFNNWDGSSAKEIIQSKIGNDQGAAKIQAPHISDNERTLFRMMDALAASDKKYYQECFKMDALRCSVEELLIDHLSFMEKCESDRLNAIKKATLDFCSTLGNKISSLRLCIDKMLTLENDIDPTADLLQLLVKYKTGSFKPQAIVYNNYYNPGSFQNFGVDLETRCRLDKKVVPLIISSIFSYMDKIYPDLPNDKVRTSIWTDSVKLSLTHQLRNLLNKQQFHNEGEIFDILSTSKLEPSTIASVVKIYLLELPDPLIPNDVSDILRVLYLDYPPLVETALQNSTSSPENQQDDDNEEGFDTKRIRGLYTTLSSLSKPHIATLDAITTHFYRLIKILKMGENGNEVADEFTVSISQEFANCIIQSKITDDNEIGFKIFYDLLTHKKQIFHELKRQNSKN
Acts in signal transduction. Activates CDC42 and RHO5.
P43556
C0MGJ9
PFKA_STRS7
Phosphohexokinase
Streptococcus
MKRIAVLTSGGDAPGMNAAIRAVVRKAISEGMEVYGINRGYAGMVDGDIFPLGSKEVGDKISRGGTFLYSARYPEFAQLEGQLAGIEQLKKHGIEGVVVIGGDGSYHGAMRLTEHGFPAVGIPGTIDNDIAGTDYTIGFDTAVNTAVEAIDKLRDTSSSHGRTFVVEVMGRNAGDIALWAGIASGADQIIVPEEEFDIHKVVSTIKDDFENRGKNHHIIVLAEGVMSGEAFAQQLKEAGDESDLRVTNLGHILRGGSPTARDRVIASWMGAHAVELLKEGKGGLAVGIRNEELVESPILGSAEDGALFSLTDEGNIVVNNPHKARLDYAALNRSLAQ
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
C0MGJ9
Q99880
H2B1L_HUMAN
Histone H2B.c
Homo
MPELAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Q99880
A0AJ41
THII_LISW6
tRNA 4-thiouridine synthase
Listeria
MEFDRILIRYGELSTKGKNRKQFVTRLAHNVKRAMKDLPEVRIHGERDRMYIILNGEDHKLAEERLKPIFGIQSFSPAVRVNLELDEVKNAALALVQDVHEQNGTFKVAARRSHREFPLDSNEINQEIGAYVLQNIEDLSVNVKNPDVKLTIDVRKEGVFLSCRTIIGAAGLPVGSSGRAMLMLSGGIDSPVAGYLAQKRGVEIEAVHFHSPPYTSEQAKQKAVDLAAKLAKYGGEVKMHIVPFTEIQEMIKQQIPESVIMTVTRRMMLKITDELRRKRNGLAIVNGESLGQVASQTLESMLAINAVTTTPIIRPVVSMDKNEIIQIAQKIDTYNLSVQPFEDCCTIFTPPSPKTKPKLDKIERYESFTDFDSLITKALDNIETITVNITENTQVKDEFADLF
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
A0AJ41
Q9GL50
STEA1_PIG
Six-transmembrane epithelial antigen of prostate 1
Sus
MESRQDITNQEELWKMKPRKNLEDDYLNEDSRENSMPKRPMLVHLHQTAHFDEFDCPPELQHKQELFPKWHLPIKIAAIVSSLTFLYTLLREVIHPFVTSHQQYFYKIPILVINKVLPMVSITLLALVYLPGVIAAIVQLHNGTKYKKFPHWLDRWMVTRKQFGLLSFFFAVLHAVYSLSYPMRRSYRYKLLNWAYQQVQQNKEDAWIEHDVWRMEIYVSLGIVTLAILALLAVTSIPSVSDSLTWREFHYIQSTLGIVSLLLGTIHALIFAWNKWVDIKQFIWYTPPTFMIAVFLPTVVLICKVILLLPCLRRKILKIRHGWEDVTKINKTEMSSQL
Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor.
Q9GL50
Q4JU42
GLMU_CORJK
Glucosamine-1-phosphate N-acetyltransferase
Corynebacterium
MAVIVLAAGAGTRMKSTTQKTLHSIGGRTLLSHSLHAAAGIDPARIVAVIGHGREQVGPAVAEVAEQLGRSIDTAIQEQQNGTGHAVQCAMEQLEGFEGTVVVTNADVPLLSPETLQELTATHDGASVTVLSVNQDNPTGYGRILRTNDGMVTAIVEEKDATEKQKEITEVNSGVFAFDAAILRDGLAQLNTDNAQGELYLTDVLSIARRAGHPVRAHIASDAAELAGVNDRVQLAAAGAELNRRTVTAAMRGGATIVDPATTWIDVDVQVGQDVTILPGTQLLGTTTIGDNAQIGPDTTLENVKVGEGAQVVRTHGFDSTIGPRAEVGPFTYIRPGTVLGEEGKLGGFVEAKKANIGRGSKVPHLTYVGDATIGEYSNIGASSVFVNYDGVNKHHTTVGSHVRTGSDSMFIAPVVVGDGAYSGAGTVIKEDVPPGALVVSGGKQRNVEGWVAKKRPGTPAAEAGEAAAKRVAEGGSPTSTPQADQE
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Q4JU42
Q7VP56
MURD_HAEDU
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
Haemophilus
MMQNQYQGKIITIVGLGKTGLSCVAFFAEKQATIQVIDTREQPAGIEHLSDNVALHTGSLNLEWLLASDLIVMSPGLALATPEIQTAIQAGIEVVGDIELFVREAKAPIIAITGSNGKSTVTTLVSEMAQQAGIKVGMGGNIGIPALSLLNKGYELFVLELSSFQLETTYSLKAKAATILNVSQDHMDRYASGEHYRQAKLRIYENAEYVIVNDDDPLTYPLPSQSVGNLRHFAEHDAQYAIKYDQLCSGDQAVINTDQMLLTGRHNQLNALAAIALAEAAGINRTGIINGLRCYGGLAHRFQRVPTNDGVCWVNDSKATNVGSTVAALNGLPLSGTLYLLLGGDGKGADFSMLKALVNQPHIVCYCFGKDGKSLAELTTNSVLVDTMQQAIEQIRPLVKQGDMVLLSPACASLDQFNNFEERGDMFARLAQQAV
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Q7VP56
Q9RAE6
DADA_RHIL3
D-amino acid dehydrogenase
Rhizobium
MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQPGPALETSFANAGEVSFGYCSPWAAPGIPMKAMKWLFMKHAPLILRPKLDMAMLSWMARMLSNCTSERYAINKSRMLRLADYSRIALADLRAETGIAYDERMQGTLQLFRTQQQLEASAKDVKALAADGIPYEVLDRDGCIRFEPALKHVRDKIVGGLLTPKDETGDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVITDRERMSAEAVVVALGSYSPLLLKPLGIRLPVYPVKGYSLTIPIADASRAPESTVMDETYKIAITRLGDRIRVGGMAEISGYTNDLGLARRSTLEYSVTDLFPGGDISKASFWSGLRPMTPDGTPVIGPTKVAGLFLNTGHGTLGWTMSTGSARLIGDLVGGGQPEIDARDLAITRYG
Oxidative deamination of D-amino acids.
Q9RAE6
P64462
LSRG_ECO57
Phospho-AI-2 isomerase
Escherichia
MHVTLVEINVHEDKVDEFIEVFRQNHLGSVQEEGNLRFDVLQDPEVNSRFYIYEAYKDEDAVAFHKTTPHYKTCVAKLESLMTGPRKKRLFNGLMP
Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the conversion of (4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione (P-DPD) to 3-hydroxy-5-phosphonooxypentane-2,4-dione (P-HPD).
P64462
P0AD81
LPL_ECO57
leu operon attenuator peptide
Escherichia
MTHIVRFIGLLLLNASSLRGRRVSGIQH
Involved in control of the biosynthesis of leucine.
P0AD81
Q759G7
SWR1_ASHGO
Helicase SWR1
Eremothecium
MTKANGAEQLADWKFQYDLLTNELFHLHEFTSLLEFDPAFRHESDSFARFLADKHLELRMEEDAGAPGLEESSAMRRIRRRQKRGRGEEEGNALLKGVEELVEQKYADLRARLDRPMLKQGPRKRKQPGDAAKTALPHDSKKRKSAVVRKETNDEEHLKEEKSASPTVWSPESPQRDTYRTIHPSGDHEGYQSSSSDSFYFTTSSEDEEPTVKRSLKRKKAPVRRIKLIVHPPKQTVTNPLHILKPECSSLHEFLQSYKSLDEDISIEEFDSYIASQRKVVSAIRKGLKSGVLTYDRHTDSIQGISLKDVQNSQANKPEPITTFYQEQEKHTLRDHLNNHGVVMSRMFQDRKRGRIARARKISQMIEQHFKHVAGAEERKTKEEEKRRRALARAAVQAVKKRWNLAERAYKVLKKDEEDQLKRIQGKEHLSKMLEQSTQLLGAQLNQNDDSDDETSSQVLSENESSLGDEEMSSSSELDDSEVEAGEDDSKLTVEQLRAKYSALEHITIDGRSQNSEVSSMTENPEEDPQEYKILLSEREKAELHRTFETEENNILDEDHSSSSSFSESEISQTSSSENESLINSNSSQTPGLASLFGNVAEELSDDAHYSTEESLSSTPNEDQEGVQPNADAVSNMEIDSLEMQDKDESTNLEKLSVVDVPVPPLLRGTLRTYQKQGLNWLASLYNNNTNGILADEMGLGKTIQTIALLAYLACEKENWGPHLIIVPTSVLLNWEMEFKRFAPGFKVLSYYGSPQQRKEKRRGWNKLDAFHVCITSYQLVVHDQHSFKRKKWQYMILDEAHNIKNFKSTRWQALLNFNTRRRLLLTGTPLQNNIAELWSLLYFLMPQTALENGKISGFADLDAFQQWFGKPVDKIIAANDSEHDDETRRTVSKLHQVLRPYLLRRLKADVEKQMPAKYEHILYCRLSKRQRFLYDDFMSRAQTKATLASGNFMSIINCLMQLRKVCNHPDLFEVRPILTSFCMDRSVMSNYAHLNQLVLKNLNKHALDTVVNLQCTNLAFTQNDFNMETHYADSCARLQCVRQFSEAVEKLRKDASLPDAKDDPNVLNYQDMHEFYTGYTVRKRLRLIDQYRHTFYLNSLRCEKRPVYGINLVRLVSVHHRPPLECNVMSELMKPLETRLVTHKRIIDEFAIITPTAITLDTRVLSLGLDSEAAVHPVIKSDINTQLSRMKNPFHLLQTKLSIAFPDKSLLQYDCGKLQSLAVLLRRLKEEGHRALIFTQMTKVLDILEQFLNYHGYLYMRLDGATKIEDRQILTERFNTDPRITVFILSSRSGGLGINLTGADTVIFYDSDWNPAMDKQCQDRCHRIGQTRDVHIYRFVSEHTIESNILKKANQKRQLDNIVIQKGEFTTDYFSRLSVKDLLGSDETEEIADERPLLEDPATTADSKKLERLLAQAEDEDDVKAARLAMKEVDVDDRDFRESSTCANPSPDEDVDEEPVEDEYEGTRHVEEYMIRFIANGYLYD
Catalytic component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling.
Q759G7
Q8TRT2
RS8_METAC
30S ribosomal protein S8
Methanosarcina
MVLLDPLANALSTIKNAEAIGKSSCVVRPASKNIGNVLKVMQDLGYIGDFEFIDDGKAGIYSVTLVGRINKCGAIKPRYSVGTASFERWEKQFLPAKNFGALIVTTSSGVMSQYEARDKKIGGQLLAYVY
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Q8TRT2
A5URZ1
NUSB_ROSS1
Antitermination factor NusB
Roseiflexus
MASLRRRVRAIALQILFELDATDHSPDQVVARRLEEERLPPEGERFLRRLVFGAWEHASYLDRIIEETAPNWPVSQMPGVDKAILRIALFEALIDEEEKTPLKAIINEAVELAKQYGSDNSSRFVNGVLGTVVSRYRERRKG
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.
A5URZ1
Q04NF4
CBID_LEPBJ
Cobalt-precorrin-6A synthase
Leptospira
MSTKELREGFTTGACSAAAAKAATRLLLKGEPVLEIETTLPNDRQVLFPVKRCQLEGEVAICSVVKDAGDDPDCTHGAELTARVRLTKESKIVLKGGDGVATVTKTGLGIEVGEPAINPIPRKNISEMILEELKGSSFNGAEVEISVPGGQEMAKKTMNKRLGLIGGISIIGTTGIVKPFSTAAFKASVIQAIRMAREYEVDTVILTTGGKSEKFAMNLFPNLKELSFIQAGDFIGTGIKTSVKEFIRHVIVVGMIGKLSKMADGVMMTHRGGSSVNTKMLSDIARSVGIPEPIAIDIQNANTARHALEICKENGYEIITTKICEIVARNCSKHAGTNMSISCYMVDFDGTLLGKFENFSQKSKLRKGI
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Q04NF4
A1APZ3
QUEA_PELPD
Queuosine biosynthesis protein QueA
Pelobacter
MLVKEFDYHLPEELIARYPAPERDGSRLMLLNRESGTIGHGLFRDIADHLRPGDLLVLNDTRVIPARLFGRKATGGRVEIFLVRRQETQAERWSCLMRSSKGMRPGQLITLAGAMTALVVERLEPEGWLLEFQGAEPFSVWLEREGEMPLPPYLQRPAESGDQLRYQTVFARSAGAVAAPTAGLHFTPELLERLAERGVATACLTLHTGPGTFQPLRVERVQDHRIHSERYHISAETCQAIAETKQRGGRVVAVGTTSARTLEYAADEKGGLCPGSGDADIFIYPGYRFRVVDALVTNFHLPESTLIMLVSAFAGKEYVFHAYHEAARLGYRFYSYGDAMFIE
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
A1APZ3
Q65EC5
SECA_BACLD
Protein translocase subunit SecA
Bacillus
MLGILNKVFDPTKRTLSRYEKKANEIDALKADIEKLSDEALKQKTIEFKERLEKGETVDDLLVEAFAVVREASRRVTGMFPFKVQLMGGVALHEGNIAEMKTGEGKTLTSTMPVYLNALSGKGVHVVTVNEYLASRDAEEMGKIFEFLGLTVGLNLNSLSKDEKREAYAADITYSTNNELGFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAFVRTLKADQDYTYDVKTKGVQLTEEGMTKAEKAFGIENLFDVRHVALNHHIAQALKAHAAMHKDVDYVVEDGQVVIVDSFTGRLMKGRRYSDGLHQAIEAKEGLEIQNESMTLATITFQNYFRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNKPIARDDRPDLIYRTMEGKFKAVAEDVAQRYMVGQPVLVGTVAVETSELISRLLKNKGIPHQVLNAKNHEREAQIIEDAGQKGAVTIATNMAGRGTDIKLGEGVKELGGLAVIGTERHESRRIDNQLRGRSGRQGDPGITQFYLSMEDELMKRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDARKQLLQYDDVLRQQREVIYKQRFEVIDSDNLRSIVENMIKASLERAVASYTPKEDLPEEWNLDGLVELVNANFLDEGGVEKSDIFGKEPEEITELIYDRIKTKYDEKEERYGSEQMREFEKVIVLREVDTKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFENMIAAIEDDVAKFVMKAEIENNLEREEVIQGQTTAHQPKEGDEEKQAKKKPVRKAVDIGRNDPCYCGSGKKYKNCCGRTE
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Q65EC5
F4K5X6
RVE2_ARATH
MYB family transcription factor Circadian 1
Arabidopsis
MAMQERCESLCSDELISSSDAFYLKTRKPYTITKQREKWTEAEHEKFVEALKLYGRAWRRIEEHVGTKTAVQIRSHAQKFFTKVARDFGVSSESIEIPPPRPKRKPMHPYPRKLVIPDAKEMVYAELTGSKLIQDEDNRSPTSVLSAHGSDGLGSIGSNSPNSSSAELSSHTEESLSLEAETKQSLKLFGKTFVVGDYNSSMSCDDSEDGKKKLYSETQSLQCSSSTSENAETEVVVSEFKRSERSAFSQLKSSVTEMNNMRGFMPYKKRVKVEENIDNVKLSYPLW
Positive regulator for cold-responsive gene expression and cold tolerance. Part of a regulatory feedback loop that controls a subset of the circadian outputs and modulates the central oscillator. Negatively self-regulates its own expression.
F4K5X6
Q08DJ7
AAR2_BOVIN
AAR2 splicing factor homolog
Bos
MAAMQMDPELARRLFFEGATVVILNMPKGTEFGIDYNSWEVGPKFRGVKMIPPGIHFLHYSSVDKANPREVGPRMGFFLNLQQRGLKVLRWDAAREEVDLSPAPEAEVEAMRANLQELDQFLGPYPYTTLKKWISLTNFISEATVEKLQPESRQICAFSEVLPVLSMRHTKDRVGQNLPRCGAECKSYQEGLARLPEMKPRAGTEIRFSELPTQMFPAGATPAEITRHSMDLSYALETVLSKQFPCSPQDVLGELQFAFVCFLLGNVYEAFEHWKRLLNLLCRSEEAMVKHHSLYVNLISILYHQLGEIPADFFVDIVSQDNFLTSTLQVFFSSARSVAVDATLRQKAERFQAHLTKKFRWDFEAEPEDCAPVVVELPDGVGTG
Component of the U5 snRNP complex that is required for spliceosome assembly and for pre-mRNA splicing.
Q08DJ7
Q0T048
AAEB_SHIF8
p-hydroxybenzoic acid efflux pump subunit AaeB
Shigella
MGIFSIANQHIRFAVKLATAIVLALFVGFHFQLETPRWAVLTAAIVAAGPAFAAGGEPYSGAIRYRGFLRIIGTFIGCIAGLVIIIAMIRAPLLMILVCCIWAGFCTWISSLVRIENSYAWGLAGYTALIIVITIQPEPLLTPQFAVERCSEIVIGIVCAIMADLLFSPRSIKQEVDRELESLLVAQYQLMQLCIKHGDGEVVDKAWGDLVRRTTALQGMRSNLNMESSRWARANRRLKAINTLSLTLITQSCETYLIQNTRPELITDTFREFFDTPVETAQDVHKQLKRLRRVIAWTGERETPVTIYSWVAAATRYQLLKRGVISNTKINATEEEILQGEPEVKVESAERHHAMVNFWRTTLSCILGTLFWLWTGWTSGSGAMVMIAVVTSLAMRLPNPRMVAIDFIYGTLAALPLGLLYFLVIIPNTQQSMLLLCISLAVLGFFLGIEVQKRRLGSMGALASTINIIVLDNPMTFHFSQFLDSALGQIVGCVLAFTVILLVRDKSRDRTGRVLLNQFVSAAVSAMTTNVARRKENHLPALYQQLFLLMNKFPGDLPKFRLALTMIIAHQRLRDAPIPVNEDLSAFHRQMRRTADHVISARSDDKRRRYFGQLLEELEIYQEKLRIWQAPPQVTEPVHRLAGMLHKYQHALTDS
Forms an efflux pump with AaeA. Could function as a metabolic relief valve, allowing to eliminate certain compounds when they accumulate to high levels in the cell.
Q0T048
Q4G3A5
RPOC2_EMIHU
Plastid-encoded RNA polymerase subunit beta''
Emiliania
MQPDFKKIHSFENNLINKRSLKDLMYQAFLNYGIVKSSIIADRVKNLTFHFATQSGVSLSVEDLRVPAKKRELIGLTRNEVETTQKRYEIGSITSVEKFQKTIDIWNNANNFLKDDVLTYFRESDPLNPLYIMAFSGARGNISQVRQLVGMRGLMSNPQGQIIDLPIKSNFREGLTVTEYIISSYGARKGLVDTALRTADSGYLTRRLVDVAQDIIVRESDCGTTEGLWATELASNNFLNLRGRLLAEPIFTQEGNLFAPANTEITETFLQTLKTLKDHSPIKVRSSLTCTSTRSVCQNCYGWHLSHSKLVDLGEAVGIVAAQSIGEPGTQLTMRTFHTGGVFSGDLTRQVRSPMEGKIEYWEGHKASLFRTMHGKMGFRLKEEVNLIIKNSFGTTISFEIPAESLLLVNTDQYVYENEIIAEIQKDTNLILEEEQKEIYSETSGEVFFNALDVKVQADKQGNTYKTNNKAGLIWILQGSFYELPAFSETLLKPGLNLSKNTLLSRTPLYNKYPGWVQIDKSDNGTGICVQNFSVTLTNAFINEKVENSSRLQIKTDNQDFQFQLTTEPNSVLKQGDTIAVLDDNTYRTTTGGIVTYSLENPQASKKRKSVKNLFKGYFYWIPEETFKFSTLDEVRLSFSKNESIVGVGEEIMPNTFSKVGGFFQIKEAEQEVTIKPGELFELTSAESQIFDKSDRFVKPGNFIVPGKIITQQLVYLEFFELNEKQYILARPVQVFEVPKEEDLSLSQSFFPYNSHEHIKLKVIKRVFYKNWEKIISNNGINLLQTFIVFDFKQEQQGLEPRLEFTPSKVPGKSFLKIALYEVIKTFENNRKSSHSSLPTTTRNFVSNKQYVASNTLIGQIETTAGLVNKLAAINPHLNSGNMKEVLILNPSDLKKVFCPNVELLKKVSVGDLVRIGTLLNDNVKSPYSGQILEIFEDHILIRLSQPYLISAGTILHATSNNLVKAGDILATLVYETIKTTDIVQGLPKVEELLEARKVLHNALLAPCPGYAYVRFNKHGESTVQLIGLDNEVQTLALKPGIKTKFNSGDFVEVSSALTDGLISPHTKLETLFSYFKNRYTSFEACKLSFKLLQLFLIGEIQRTYRSQGVDIADKHVELIVKQMTSKVCIEDSGTTTFLPGEVLNFQKMADIALVAENKGEIPPSYVPLLLGITKASLNSDSFISAASFQETTRVLTEAAIEGRKDWLTGLKENVIIGRLIPAGTGFNYLENQERLAREKGEIDATFHREAKPLSENILDLRLVKKE
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q4G3A5
Q07436
EXPA_DROME
Protein expanded
Sophophora
MRAFCTVSAPLEVCASSAEQLSPGSRFLALRLLGQQQPKTLYFLVDAKSRVREVYTQTCLHFATQGMLDTELFGLAVLIDGEYMFADPESKLSKYGPKSWRSSHTHGLDANGRPLLELHFRVQFYIESPFMLKDETSRHNYYLQLRHNILQRDLPREQAEQALVFLAGLALQADLGDAPPGTSNSKDDSGEETSASPSNGGRGLSATTTLPKISKRANERMLRLSTYVASTSKRETIPLPPSLPPNGADYYRIEDYLPSGLHTPWARSAMRACHREHLGMATAEAELLYIQQACSLHETINAHTYRMRLAKSEQGSGSAWFVVYAKGIKILGGESTNSSSNPETTTFLWPNITKLSFERKKFEIRSGESRITLYAASDEKNKLLLTLCKDTHQWSMKLAARLKEVSKREEEEAAESQRLHASYACSRSLLLPYKSKNEQRISVISSTSSNTTSGIVSDRVHSEDELEIMINTPPAPLAAPSTESLALAHLLDRPSVSRQTSSVGQMSLKDLEEQLAALSVRPQDASSNGATIVTNSSVQRNSMGTTANDSSTATDSPSSQHNIGSQCSSTCSTVVVTSPVNGAGASSSGAPIPVHSTSSSLELGFSHTAQNSALSETSPDDFLSTSAREETESVSGASGVYTLAHGAPPTETSGVYTMHSSELTGQSSEIAESEKSSHYGMFQPQKLEETHVQHSDSVDGKKKEDFRPRSDSNVSTGSSFRGDGSDPTDNKHSLLSAEELTNLIVGRGTYPSRKTVSSSLHSDCDYVTLPLGDQGEEEVDQPPAPPPPYSARHEKTGLCGPPIAKPIPKPIAVVAPKPDSPPCSPPVPPAPIPAPPPAIRRRDPPPYSISSKPRPTSLISVSSSAHPAPSAAGSMSSLKSEEVTARFITTRPQISILKAHTSLIPDGAKPSYAAPHHCSSVASSNGSVCSHQLSQQSLHNSNYAGGSQASLHHHHVPSHHRHSGSAAIGIVPYGLHKSTASLHHQQSCVLLPVIKPRQFLAPPPPSLPRQPPPPPPPNHPHLASHLYEREMARKQLELYQQQLYSDVDYVIYPIQDPAVSQQEYLDAKQGSLLAAMAQAAPPPPHHPYLAMQVSPAIYRSTPYLPLTLSTHSRYASTQNLSDTYVQLPGPGYSPLYSPSMASLCSSYEPPPPPPLHPAALAAAAAAGAGSSSSSMFARSRSDDNILNSLDLLPKGKRLPPPPPPPYVNRRLKKPPMPAPSEKPPPIPSKPIPSRMSPIPPRKPPTLNPHHANSPLTKTSSGAQWAGERPRPDLGLGLGLNRGNNSILAQLQASMVAQSHAQAQAQALDIALLREKSKHLDLPLISALCNDRSLLKQTKVVINPKTGQEMPTSSAQPSGATTNGVANSSAGAGTLSKARKGSTVSHRHPQDKLPPLPVQQLAEANNYVIDPAVMMKQQQQQQQHNKTS
Activates the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis . The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. Ex acts synergistically along with Mer and Kibra to regulate the Hippo signaling pathway . Involved in the control of cell proliferation in imaginal disks . May bind to certain proteins of signal transduction pathways by interaction with their SH3 domains . Required for apical localization of Schip1 .
Q07436
P0DJ36
KKX31_HETPE
HSP040C.1
Heterometrus
MKSTLMTASVLILVLLSIVDYASVYAEFIDSEISLERQWINACFNVCMKISSDKKYCKYLCGKN
Potassium channel inhibitor (Kv).
P0DJ36
Q1ISA8
RS8_KORVE
30S ribosomal protein S8
Candidatus Koribacter
MSLTTDPVADFLSRVRNAIKARHQKVDAPASKLKTELARILKEEGYIANYKAVEEEGKKLIRVYLKYGSDNVSPISNVTRISRPGCRVYVGSKEIPRVLGGLGISILTTPKGVMTGRQARKEGVGGEVLCEIY
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Q1ISA8
Q02T96
COAX_PSEAB
Pantothenic acid kinase
Pseudomonas
MILELDCGNSLIKWRVIEGAARSVAGGLAESDDALVEQLTSQQALPVRACRLVSVRSEQETSQLVARLEQLFPVSALVASSGKQLAGVRNGYLDYQRLGLDRWLALVAAHHLAKKACLVIDLGTAVTSDLVAADGVHLGGYICPGMTLMRSQLRTHTRRIRYDDAEARRALASLQPGQATAEAVERGCLLMLRGFVREQYAMACELLGPDCEIFLTGGDAELVRDELAGARIMPDLVFVGLALACPIE
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Q02T96
A4JDB7
PPK1_BURVG
Polyphosphoric acid kinase
Burkholderia cepacia complex
MSARYPLLNRELGILGFNERVLAQAADPQVPLLERLRFICITSSNLDEFFEVRMAGLQEQIRDNPGALTPDGMSLQHAYDLVVERAQRLVHRQYTMLHETVLPALEQEGIYFHASDTWNDAQLEWARGYFLDELLPVLTPIGLDPAHPFPRVLNKSLNFVVELEGRDAFGRQAVMGIVQAPRALPRVVRMPQSLSGFEHGFVLLSSFMQRFVGELFPQLVVKSCNQFRITRNSELFVDEDEITNLRVALQGELPARHLGNAVRLEVSADTPAHIVRRLLDESSLGDKDCYRVAGSVNLVRLMQIPDLVDRPDLKFAPFVASIPPAIANAPTMFDAIDAGDILLHHPYESFQPVLELLQQAAKDPSVVAIKQTIYRTGTDSPLMDALMEAARNGKEVTVVVELLARFDEETNINWASQLEAVGAHVVYGVVGHKCHAKMMLIVRRVVEGGKATLRRYVHLGTGNYHPRTARLYTDFGLMTADQKICEDVHHVFQQLTGIGGELTLHELWQSPFTLHPRIIDSIRAEIDNARAGKRARIVAKMNALLEPSVIAALYEASQAGVKVDLIVRGVCALKPGVPGLSENITVRSIVGRFLEHHRIYYFHAGGAEEVYLSSADWMDRNLFRRVEVAFPIRARKLKRRVIAEGLSVCLGDNQSAWLMQSDGHYRRRRAGKTVRNAQLGLLAKFCS
Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
A4JDB7
Q96133
COX3_CARAU
Cytochrome c oxidase polypeptide III
Carassius
MAHQAHAYHMVDPSPWPLTGAIAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIIREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLALTILLGFYFTALQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Q96133
Q8Y5R1
DEOC_LISMO
Phosphodeoxyriboaldolase
Listeria
MTIAKMIDHTALKPDTTKEQILTLTKEAREYGFASVCVNPTWVKLSAEQLAGAESVVCTVIGFPLGANTPEVKAFEVKDAIQNGAKEVDMVINIGALKDKDDELVERDIRAVVDVAKGKALVKVIIETCLLTDEEKVRACEIAVKAGTDFVKTSTGFSTGGATAEDIALMRKTVGPNIGVKASGGVRTKEDVEKMIEAGATRIGASAGVAIVSGEKPAKPDNY
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Q8Y5R1
A0PM49
MFTC_MYCUA
[Mycofactocin precursor peptide]-tyrosine decarboxylase
Mycobacterium
MTTAVPRLIEQFEHGLDAPICLTWELTYACNLACVHCLSSSGKRDPGELSTRQCQDIIDELERMQVFYVNIGGGEPTVRPDFWELVDYATAHHVGVKFSTNGVRINPEVAARLAASDCVDVQISLDGATAEVNDAVRGAGSFAMAVRALENLAAAGFADAKISVVVTRHNVGQLDDFAALADRYGATLRITRLRPSGRGADVWEELHPTAAQQVALYDWLVAKGERVLTGDSFFHLAPLGSSGALAGLNMCGAGRVVCLIDPVGDVYACPFAIHDRFLAGNVLTDGGFDQVWKNAPLFRQLREPQSAGACGSCGHYDSCRGGCMAAKFFTGLPLDGPDPECVQGYGAPALAQERHAPRPRVDHSRGSRE
Radical S-adenosylmethionine (SAM) enzyme responsible for the first step of the biosynthesis of the enzyme cofactor mycofactocin (MFT). Catalyzes two reactions at the C-terminus of the mycofactocin precursor (the MftA peptide). The first one is the oxidative decarboxylation of the C-terminal L-tyrosine of MftA, forming an unsaturated tyramine moiety . The second reaction is the cross-linking of the tyramine with the penultimate L-valine residue, forming a five-membered lactam ring . Its activity requires the presence of the MftB chaperone .
A0PM49
A4Y843
TRPD_SHEPC
Anthranilate phosphoribosyltransferase
Shewanella
MSTNHIQPLLDLLYQGKSLSREQAFEIFSALIRGEMSEATMAGMLVALKMRGETIDEISGAADAMRAAAKTFPYSNGDSLGNGIVDIVGTGGDGFNTINISTTAAFVAAAAGAKVAKHGNRSVSSKSGSSDLLAQFGIDLTMSPDTASRCLDALNLCFLFAPHYHGGVKHAGPVRQALKTRTLFNVLGPLINPARPEFMLLGVYSPELVLPIAKVLKALGTKRAMVVHGSGLDEVALHGNTQVAELKDGDIIEYQLTPADLGVPLAQISELEGGEPAQNALITEAILRGRGTDAHANAVAINAGCALYVCGIADSVKTGTLLALSTIQSGKAFELLSQLAKVSSETKE
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
A4Y843
Q84JK8
MAKR6_ARATH
Probable membrane-associated kinase regulator 6
Arabidopsis
MEEGKQEASMPLVPIDSFSYSWLVNFPSLEATIDDHHQTYEDSSSSSSFIEMDPRLPPSRRFFIKTSHESSFKFDNFVSFSDEDHSLVHADELFRDGYVMPYRLKPTSAATEEESEPLDTTTSEKIDTRGLNSKPSPTSSRKLRRVSKWVLLKYLDFLTPLCKRLRRCRSAVTTGSIGMDSRIRVTTSCRSRVYSDEMTSSPRISVADDYYWRRSCDSESSIYEAVLHCKKSFEK
May be involved in abscisic acid signaling by acting as a kinase regulator.
Q84JK8
A9AJG2
ATPA_BURM1
F-ATPase subunit alpha
Burkholderia cepacia complex
MQLNPSEISELIKSRIQGLEASADVRNQGTVISVTDGIVRIHGLSDVMQGEMLEFPGNTFGLALNLERDSVGAVILGEYEHISEGDVVKTTGRILEVPVGPELIGRVVDALGNPIDGKGPVNAKLTDAIEKIAPGVIWRKSVSQPVQTGIKSIDAMVPIGRGQRELIIGDRQTGKTAVALDAIINQKGKDLICIYVAIGQKASSIMNVVRKLEETGAMAYTIVVAASASDSAAMQYLAPYAGCTMGEYFRDRGQDALIIYDDLTKQAWAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAARVSEEYVEKFTNGEVKGKSGSLTALPVIETQAGDVTAFVPTNVISITDGQIFLETDLFNAGIRPAINAGVSVSRVGGAAQTKVVKKLSGGIRTDLAQYRELAAFAQFASDLDEATRKQLERGRRVTELLKQPQYQPLQVWELAVSLFSANNGYLDDLDVKQVLPFEKGLREFLKTSHADLIKRIEDTKDLSKDDEGALRAAIESFKKSGAY
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
A9AJG2
A3PF45
RL23_PROM0
50S ribosomal protein L23
Prochlorococcus
MSKLFNSRLADVIRKPVITEKATNALDFNQYTFEVDHRAAKPQIKAAIEALFSVKVIGVNTMNPPRRTRRVGKFSGKRSQVKKAIVRLAEGDKIQLFPES
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.
A3PF45
Q9ALN9
SPNR_SACSN
dTDP-4-keto-2,3,6-trideoxy-D-glucose 4-aminotransferase
Saccharopolyspora
MINLHQPILGTEELDAIAEVFASNWIGLGPRTRTFEAEFAHHLGVDPEQVVFLNSGTAALFLTVQVLDLGPGDDVVLPSISFVAAANAIASSGARPVFCDVDPRTLNPTLDDVARAITPATKAVLLLHYGGSPGEVTAIADFCREKGLMLIEDSACAVASSVHGTACGTFGDLATWSFDAMKILVTGDGGMFYAADPELAHRARRLAYHGLEQMSGFDSAKSSNRWWDIRVEDIGQRLIGNDMTAALGSVQLRKLPEFINRRREIATQYDRLLSDVPGVLLPPTLPDGHVSSHYFYWVQLAPEIRDQVAQQMLERGIYTSYRYPPLHKVPIYRADCKLPSAEDACRRTLLLPLHPSLDDAEVRTVADEFQKAVEHHISQRSPLRK
Involved in the biosynthesis of forosamine ((4-dimethylamino)-2,3,4,6-tetradeoxy-alpha-D-threo-hexopyranose), a highly deoxygenated sugar component of several bioactive natural products such as the insecticidal spinosyns A and D . In the presence of pyridoxal 5'-phosphate (PLP) and alpha-ketoglutarate, catalyzes the C-4 transamination of dTDP-4-keto-2,3,6-trideoxy-alpha-D-glucose to yield dTDP-4-amino-2,3,4,6-tetradeoxy-alpha-D-glucose . It can also use pyruvate, but less efficiently than alpha-ketoglutarate . Also able to catalyze the C-4 transamination of dTDP-4-keto-2,6-dideoxy-alpha-D-glucose to yield dTDP-4-amino-2,4,6-trideoxy-D-glucose .
Q9ALN9
Q8PY53
RL11_METMA
50S ribosomal protein L11
Methanosarcina
MTSIVEALVPGGKANPGPPLGPALGPLGVNIKEVVEKINEKTRDYNGMQVPVKVIVDDKKNVEIEVGTPPTASLVMKELGIQKGSGNAGSEVVGNLTIPQVAKIARMKKEDVLSYDLKATMKEVMGTCVPMGVNVEGMKAKDCQKALDEGKFDDLLANEAW
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Q8PY53
B1YX25
PPNP_BURA4
Xanthosine phosphorylase
Burkholderia cepacia complex
MTSATQFDNVSVVKRANVYFDGKCVSHTVLFPDGTRKTLGVILPCALNFGTDAAELMEVQAGKCRVKLDGSSEWQTYGAGESFSVPGKSRFDIEVLETLDYVCSYL
Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
B1YX25
B1HUD1
DNAK_LYSSC
Heat shock protein 70
Lysinibacillus
MSKIIGIDLGTTNSCVSVLEGGEPKVIPNPEGNRTTPSVVAFKNGERQVGEVAKRQSVTNPNTIISIKSKMGTAEKVTVEDKDYTPQEVSAMILQYLKGYAEDYLGEKVTKAVITVPAYFNDAQRQATKDAGKIAGLEVERIINEPTAAALAYGLDKQDQDQKVLVFDLGGGTFDVSILELGDGVFEVLATAGDNKLGGDDFDDAIIEYLVAEFKKENGIDLSKDKMAMQRLKDAAEKAKKDLSGVTSTQISLPFITAGEAGPLHLEISLTRAKFDEITLPLVNRTVGPVRQALSDAGLSTSEIDQVILVGGSTRIPAVQEAVRKETNKEPHRGVNPDEVVAMGAAVQGGVLTGDVKDVVLLDVTPLSLGIETMGGVFTKLIDRNTTIPTSKSQVFSTAADNQPAVDIHVLQGERSMAADNKTLGRFQLADIPPAPRGVPQIEVTFDIDKNGIVSVKAKDLGTNKEQTIVIQSDSGLSEAEIERMVKDAEANADADAKRKEEADLRNEADQLVFQVDKTITDLGEQITEDEKKSVEDARDELKKALEAGELEGIKAAKEKLEGVLQPLVMKVYEQAAAAAQAAQGGEADAGAGKKDDGVVDADFEEVKDDK
Acts as a chaperone.
B1HUD1
F1MJW3
SCNNG_BOVIN
SCNEG
Bos
MAPGEKIKAKIKKNLPVTGPQAPNIKELMQWYCLNTNTHGCRRIVVSRGRLRRLLWILFTLTAVALIFWQCALLISSFYTVSVSIKVHFQKLDFPAVTICNINPYKYSAVRHLLADLEQETRAALKTLYGFSEITSRKRREAQSWSSVRKGTDPKFLNLAPLMAFEKGDTGKARDFFTGRKRKVNARIIHKASDVMHIHNSKEVVGFQLCSNDTSDCAVYTFSSGVNAIQEWYKLHYMNIMAQVSQEKKINMSYSADELLVTCFFDGVSCDARNFTLFHHPMYGNCYTFNNRQNETILSTSMGGSEFGLQVILYINEEEYNPFLVSSTGAKVIIHRQDEYPFVEDVGTEIETAMATSIGMHLTESFKLSDPYSQCTEDWSDVQITNIYNATYSLQICLHSCFQAKMVENCGCAQYSQPLPRGADYCNYQQHPNWMYCYYQLHQAFVREELGCQSVCKEACSFKEWTLTTSLAQWPSEVSEKWLLSILTWDQSQQIKKKLNKTDLAKLLIFYKDLNQRSIMENPANSIEQLLSNIGGQLGLWMSCSVVCVIEIIEVFFIDSLSIIARHQWHKAKGWWARRRAPACPEAPRAPQGRDNPSLDIDDDLPTFTSALSLPPAPGSQVPGTPPPRYNTLRLERAFSSQLTDTQTTFPH
Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception.
F1MJW3
Q1BZF4
SECA_BURCA
Protein translocase subunit SecA
Burkholderia cepacia complex
MTTGFLQKIFGSRNQRLVKQYQKTVATINALETQIEKLTDDQLRGKTDEFRQRVAAGESLDKLLPEAFAVCREASRRVLKMRHFDVQMIGGMVLHYGKIAEMRTGEGKTLVATLPVYLNALAGRGVHVVTVNDYLAQRDAEWMARLYNFLGLSVGINLSGMEHDQKQQAYAADITYGTNNEFGFDYLRDNMVYETDARVQRALNFAVVDEVDSILIDEARTPLIISGQAEDHTELYVRMNALPPLLERQIGEEKADGTGVEKPGDYTLDEKARQVFLTESGHEKAERLLAEWGLIGEGESLYAPQNITLMHHVYAALRAHTLFHKDQHYVVQNGEVVIVDEFTGRLMAGRRWSDGLHQAVEAKEHVKIQSENQTLASITFQNYFRMYAKLAGMTGTADTEAYEFNEIYGLETVVIPTNRPPKRIDKQDQIYKTAKERYDAVIRDIRDCYERGQPVLVGTTSIENSELLSHLLKQVGLPHEVLNAKQHEREAAIVAEAGRPKRITIATNMAGRGTDIVLGGNAEKQAAFIEADDAIPADEKARRIQKLHDEWETLHEEVKAAGGLHIIGTERHESRRIDNQLRGRAGRQGDPGSSRFYLSLDDPLLRIFAGDRVRSIMDRLKMPEGEAIEAGIVTRSIESAQRKVEARNFDIRKQLLEYDDVSNDQRKVIYQQRNELLEAHDITETITAMRHGVITEVVRQFVPEGSIEEQWDVPELEEALRNDWQLDLAIQEMVNESSSITAEEILDAVMTAADEQYEAKVAMVGRESFSAFERSVMLQTVDRLWREHLAALDHLRQGIHLRGYAQKNPKQEYKREAFELFAAMLDAIKQEVTRIVMNVQIQSPEQLEEAAEQIEERGGHLENVEYQHADYADAGAPVANVTAAAAATATADMVGSAMTHSGPGGEMPKVGRNDPCPCGSGKKYKQCHGKLS
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Q1BZF4
Q24T61
CHEB_DESHY
Protein-glutamate methylesterase/protein-glutamine glutaminase
Desulfitobacterium
MNQPKSPITVLIVDDSPFMRLTLQKILSQDPEIKVLDTARDGKEGIEKLQALRPQVVTMDIEMPQIDGLQALGEIMRWQPTPIIILSALTTEGAQASVKALEAGAFDVVAKPSGGPGADIQALARDLIDKVKAAAQVNLGRLGKKGAVSRISSASGSRPPWTAGAASENTNRLSSPGSTSSTLGSAKGRSLDSGEALPKYPVEIVAIGTSTGGPSALQAVLTQLPGNLPVPVLVAQHMPPGFTAPLAQRLNGMSPLTIREGVHGEALKAGTIYFAPAGKQMQVQSRGSQLILHIGDESPITTLYHPSVDVMFMSLAKEVGKGTLGVVMTGMGNDGLRGMREIKERGGYAIAEAEETCVVYGMPRAIVDAGLANRVAPLGEIARHIVECVQRR
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
Q24T61
Q9I321
EXSD_PSEAE
Transcriptional antiactivator ExsD
Pseudomonas
MEQEDDKQYSREAVFAGRRVSVVGSDARSRGRVPGYASSSLYRESGIISARQLALLQRMLPRLRLEQLFRCEWLQQRLARGLALGREEVRQILLCAAQDDDGWCSELGDRVNLAVPQSMIDWVLLPVYGWWESLLDQAIPGWRLSLVELETQSRQLRVKSEFWSRVAELEPEQAREELARVAKCQARTQEQVAELAGKLETASALAKSAWPNWQRGMATLLASGGLAGFEPIPEVLECLWQPLCRLDDDVGAADAVQAWLHERNLCQAQDHFYWQS
Negative regulator of the type III secretion system regulon. Acts by disrupting transcriptional activator ExsA self-association and DNA-binding activity in absence of inducing signals . Upon host cell contact, this interaction is disrupted by the anti-antiactivator protein ExsC leading to ExsA activation .
Q9I321
A1SSM6
LEPA_PSYIN
Ribosomal back-translocase LepA
Psychromonas
MKNIRNFSIIAHIDHGKSTLSDRLINTCGGLSDREMESQVLDSMDIERERGITIKAQSVTLDYHAKDGETYQLNFIDTPGHVDFAYEVSRSLAACEGALLVVDAGQGVEAQTLANCYTAMEMNLEVVPILNKIDLPAADPDRVAKEIEDIIGIDAADAVRCSAKTGVGIDLVLEEIVRCIPPPVGDLTGPLQALIIDSWFDNYQGVVSLVRVMHGQIKVGDRMKVMSTGQVNPVAKVGYFTPKQKETGILKAGEVGYVIAGIKDILGAPVGDTLTISGHEAAKALPGFKRAKPQVYAGLFPVSSDDYENFRDALAKLSINDASLFYEPENSSALGFGFRCGFLGLLHMEIVQERLEREYDLNLITTAPTVVYEVETTRGEVLHIDSPAKFPAMNDIEEIREPIAECNILVPQEYLGNVITLCVQKRGMQTKMVYHGKQVALTYHIPMGEVVMDFFDRLKSTSRGYASLEYNFVKFEAADMVRVDVLINSERVDALALITHRANSESYGRDLVDKMKDLIPRQMFNIALQAAIGSKIIARSTVKQLTKNVLAKCYGGDISRKKKLLKKQKEGKKRMKSVGNVDIPQEAFLAVLHIGKDK
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.
A1SSM6
C5CCC6
YBEY_MICLC
Endoribonuclease YbeY
Micrococcus
MAVEILNESGIEVPEDALLRMARHVYARLHVHERAETAVTVVDAARMAELHEEWMDLPGPTDVMSLPMDELTPGSPEAPAEGVLGDVVLCPEVAAEQAARGGHSRDDELLLLLTHGMLHLLGYDHVEDAEREEMFTLQDRLVSEVLGRPAPAPTVED
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
C5CCC6
Q8XHL5
COAX_CLOPE
Pantothenic acid kinase
Clostridium
MILLIDVGNTNIVLGIHDNEKYIASWRISTDSKKTSDEYSIQVMQLFNQAKLNPEDVEGIIISSVVPNIMHSLENMVRKCFCKEPIVVGPGIKTGINIKYDNPKEVGADRIVNAVAAFEKHKKPMIIIDFGTATTFCAITEKGDYLGGNICPGIQISADALFERAAKLPRIELEKPKSVICKNTVTSMQAGIIYGYIGKVEYIVKRMKKEMMDLGEKEPFVLATGGLAKLVYSETDVIDEVDRKLTLEGLKILYEKNKE
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Q8XHL5
Q2IK81
EFG2_ANADE
Elongation factor G 2
Anaeromyxobacter
MYTDFSKLRNIGISAHIDSGKTTLTERILFYTKRIHAIHEVKGKDGVGATMDSMELERERGITIASAATHCEWKGLHLNIIDTPGHVDFTIEVERSLRVLDGAILVLCSVAGVQSQSLTVDRQMRRYNVPRLAFVNKCDRSGANPIRVKDQLREKLQHNPVLMQLPIGLEDKFEGVVDLVKMKAFRFSGDDGEVITESEIPADMQADAARAREELLDAASMFSDELTDAILEDRVTEELIKAAVRKGTLALKLTPVFMGSAYKNKAVQKLLDGVVDYLPDPTEVVNEAHDLTKDEEKVALTIDNEKPTVALAFKLEDGRYGQLTYLRIYQGKLSRDMFITNMRTKKDHRIGRLVRMHSDQMEDIDAAGSGDIVAMFGVDCNSGDTFTDGTVKLNMTSMHVPEPVIALSIKPVDSKSETNMGKALRRFTREDPTFRAGLDEESGETIIRGMGELHLEVYIERMKREYNCIVEVSPPQVAYRETVSQRADFAYTHKKQTGGSGQFGRVCGYIEPCEQQFEFVDDVVGGAIPREFISAVEKGFRSMLAKGRLLGFPVVNTRVVINDGASHAVDSSDIAFQEAARGAWREGFDRAKPRLLEPIMRVVCEGPAEFSGGILGTLMQRRAMIIGSQDDGGLARIEAEVPLAEMFGYSTTLRSATQGKAEFSMEFSRYLPVPAAMAEELMTKASKKAEGGKK
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Q2IK81
Q5XIQ2
ELMD3_RAT
RNA-binding motif and ELMO domain-containing protein 1
Rattus
MSETSCSFLIEKEFQDGQVESVSAGLSPSYKDNGALMAFRGIPISELKNHGILQVLTAETNGWQPGVVSAEMLRAQEEWEVVDTIHPDIESGVSSQQPGQFISFNEALEHFQTVDLSSFKKRIQPTIQRTGLAALRHCLFGPPKLHQGLQEERDLVLTIAQCGLDSQNPTHGRVLQTIYKKLTGSKFDCALHGDHWEDLGFQGANPATDLRGTGFLALLHLLYLVMDSKTLLMAQEILRLSHHHIQQFPFCLMSVNITRIAIQALREECLSRECNRRRKVIPVVNSFYAATFLHLARMWRTQHNTILDSGFVLKELGIEPRALRSIGKRSTAELNPQPAPAFLVWDYSRAFMHGSR
Acts as a GTPase-activating protein (GAP) for ARL2 with low specific activity.
Q5XIQ2
Q4IQK7
RMT2_GIBZE
Type IV protein arginine N-methyltransferase
Fusarium
MAATTSKIDDSMPARISSDCPEEIREVLYYAWGHDRSGLKKLLKTTGKATAQDPKTGETPLHAAIRACGPASPDDDGQEEDGSVEEAKDIVHDLFLQGAIWNDVDSNNETPGCLALRLGRKSLYQLCIEAGVRAELLFALMGDYEELSSGSEDGDEEMEVQQDDDEEAPQLVSTEDVEPTVEEPKFIPPDAKEKQVTSEEYLNSKLVYDDAKLVDSDLNGVMMAWETDIMRRSVAALIPDSAPGKRILNIGFGMGIVDGMFAELKPSRHHIIEAHPSVLEHLSKDESKFGPSWEKSGPEEGAFKVHKGKWQDIVPKLLEDGEIYDAIYFDTFGEDYSQLRYFFSECIIGIMDQEGKFSFFNGLGADRKICYDVYTKVVEMQCADAGLDVEWEESDVDMSGLEKAGEGEWEGVRRRYWTLDSCRQP
S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that methylates the delta-nitrogen atom of arginine residues to form N5-methylarginine (type IV) in target proteins. Monomethylates ribosomal protein L12.
Q4IQK7
P44878
GALU_HAEIN
Uridine diphosphoglucose pyrophosphorylase
Haemophilus
MKAVIPVAGLGTRMLPATKAIPKEMLTLVDKPLIQYVVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELETMLEKRVKRQLLEEVRSICPKNVTIMHVRQGNAKGLGHAVLCGRPLVGNESFAVMLPDVLLAEFSADQKKENLAAMIQRFNETGASQIMVTPVPQENVSSYGVADCGGIELNGGESAKINSIVEKPSIEDAPSNLAVVGRYVFSAAIWDLLEKTPIGVGDEIQLTDAIDMLIEKETVEAFHMTGETFDCGDKIGYMEAFVEYGIRHEKLGKEFKSFIKNLAKTL
May play a role in stationary phase survival.
P44878
Q8GU83
AB41G_ORYSJ
Pleiotropic drug resistance protein 2
Oryza sativa
MEDKKQQQQQQREEAEAEEEAPVVPSSLRAAATCRSLSSLSSSLRWDHRGDDDEEEAELRWAAIERLPTLDRMRTSVLSSEAVDVRRLGAAQRRVLVERLVADIQRDNLRLLRKQRRRMERVGVRQPTVEVRWRNVRVEADCQVVSGKPLPTLLNTVLATARGLSRRPHARIPILNDVTGILKPSRLTLLLGPPGCGKTTLLLALAGKLDKNLKVTGEVEYNGANLNTFVPEKTSAYISQYDLHVPEMTVRETLDFSARFQGVGTRAEIMKEVIRREKEAGITPDPDIDTYMKAISVEGLERSMQTDYIMKIMGLDICADIIVGDIMRRGISGGEKKRLTTGEMIVGPSRALFMDEISTGLDSSTTFQIVSCLQQVAHISESTILVSLLQPAPETYDLFDDIILMAEGKIVYHGSKSCIMNFFESCGFKCPERKGAADFLQEVLSKKDQQQYWSRTEETYNFVTIDHFCEKFKASQVGQNLVEELANPFDKSEVYNNALSLNIYSLTKWDLLKACFAREILLMRRNAFIYITKVVQLGLLAVITGTVFLRTHMGVDRAHADYYMGSLFYALILLLVNGFPELAIAVSRLPVFYKQRDYYFYPAWAYAIPSFILKIPLSLVESITWTSISYYLIGYTPEASRFFCQLLILFLVHTGALSLFRCVASYCQTMVASSVGGTMSFLVILLFGGFIIPRLSMPNWLKWGFWISPLSYAEIGLTGNEFLAPRWLKTTTSGVTLGRRVLMDRGLDFSSYFYWISASALIGFILLLNVGYAIGLTIKKPTGTSRAIISRDKFSTFDRRGKDMSKDMDNRMPKLQVGNALAPNKTGTMVLPFSPLTISFQDVNYYVDTPVEMREQGYKERKLQLLHNITGAFQPGVLSALMGVTGAGKTTLLDVLAGRKTGGVIEGDIRVGGYPKIQQTFARISGYCEQTDVHSPQITVEESVAYSAWLRLPTEVDSKTRREFVDEVIQTIELDDIRDALVGLPGVSGLSTEQRKRLTIAVELVSNPSVIFMDEPTSGLDARAAAIVMRAVKNVADTGRTVVCTIHQPSIEIFEAFDELMLMKRGGELIYAGPLGLHSCNVIHYFETIPGVPKIKDNYNPSTWMLEVTCASMEAQLGVDFAQIYRESTMCKDKDALVKSLSKPALGTSDLHFPTRFPQKFREQLKACIWKQCLSYWRSPSYNLVRILFITISCIVFGVLFWQQGDINHINDQQGLFTILGCMYGTTLFTGINNCQSVIPFISIERSVVYRERFAGMYSPWAYSLAQVAMEIPYVLVQILLIMFIAYPMIGYAWTAAKFFWFMYTIACTLLYFLYFGMMIVSLTPNIQVASILASMFYTLQNLMSGFIVPAPQIPRWWIWLYYTSPLSWTLNVFFTTQFGDEHQKEISVFGETKSVAAFIKDYFGFRHDLLPLAAIILAMFPILFAILFGLSISKLNFQRR
May be a general defense protein.
Q8GU83
Q4GZK3
ORR8_ORYSI
Type A response regulator 8
Oryza sativa
MSSPHVLVVDDTHVDRHVVSMALMRHNVRVTAVESVMQALMFLDSEHDVDMIVSDYCMPDMTGYNLLMEVKKSPKLAHLPVVIASSDNIPERIRKCLDGGAKDYILKPVKIVDVPRIMKYI
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.
Q4GZK3
B7LKA4
ACEK_ESCF3
Isocitrate dehydrogenase kinase/phosphatase
Escherichia
MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFYPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTEMLGTDNLAESHLQVANELFYRNKAAWLVGKLNTPFGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPTLMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPSRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYRPQV
Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
B7LKA4