ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q8WN98 | MKDPDPSQVYRPDMDPEAAKDKGSFRNYTSGPLLDRVFRTYKLMHTWQTVDFVRKKHAQFGGFSYKRMTVLEAVDMLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLGKVLVLAGEPQWAVVGDTFPVGCRPQASVVFCDSTFQDNPDLQDPVYSTELGMYQPHCGLENALMSWGHDEYMYQMMKFNKFSLPGEAFYIIRFHSFYPWHTGGDYRQLCNEQDLAMLPWVQEFNKFDLYTKGSDMPDVDELRPYYQGLIDKYCPGVLCW | Cofactor: Binds 2 iron ions per subunit.
PTM: The N-terminus is blocked.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 32653
Sequence Length: 282
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Locat... |
P38162 | MVDNRRTFTAPQSLLETNLTFPNDEPSLTTITVTRERCVDPSLIDSFLRFLRHGSDDIIRQKLNNYRKGSINGKNKCKEFLKQELYPNWQIRNNIISFCEKEAAEMKNETDQQCGNNKKTTAEPLIDARIDPYAARERAEKQEAQYKDWTKVTEWVANNRKIEQILTSTTEGILRQNCEQNNDYLKEFTQFCKDNS | Function: Regulator of the mitochondrial protein import machinery that is localized in the mitochondrial intermembrane space (IMS) and facilitates the transport of proteins from the cytosol into the mitochondrial matrix . Not essential for mitochondrial protein import but induced and required when mitochondrial import ... |
Q9H2W2 | MATAESRALQFAEGAAFPAYRAPHAGGALLPPPSPAAALLPAPPAGPGPATFAGFLGRDPGPAPPPPASLGSPAPPKGAAAPSASQRRKRTSFSAEQLQLLELVFRRTRYPDIHLRERLAALTLLPESRIQVWFQNRRAKSRRQSGKSFQPLARPEIILNHCAPGTETKCLKPQLPLEVDVNCLPEPNGVGGGISDSSSQGQNFETCSPLSEDIGSKLDSWEEHIFSAFGNF | Function: Transcription factor that play a central role in proper axial mesendoderm morphogenesis and endoderm formation. Required for efficient differentiation of cells from the primitive streak stage to blood, by acting early in the recruitment and/or expansion of mesodermal progenitors to the hemangioblastic and hem... |
D7SSD8 | MEKRERHFVLVHGACHGAWCWYKVTTFLRSAGHKVTALDLAAAGANGKRLDELNSISDYHEPLMKFMTSLVAGEKVILVAHSLGGVSVSVAMERFPQKISVAVFVSAYMPGPDFNLSTVYQELHQRRQGASKDTQYTFDRGSNNPPTSIIFSPEDLAAKLYQLSPPEDLTLATTLMRPTKLFRGENLLKETTVTREKYGTVRRVYIVCDKDNILKEDFQRWMIKNNPSDEVKVIMGSDHMPMFSKPLDLCAYLQEIVESYS | Function: Methylesterase that catalyzes the hydrolysis of methyl jasmonate (MeJA) into jasmonate (JA) . Can also use methyl salicylate (MeSA) as substrate with a lower efficiency .
Catalytic Activity: H2O + methyl (-)-jasmonate = H(+) + jasmonate + methanol
Sequence Mass (Da): 29486
Sequence Length: 261
Pathway: Plant ... |
Q57604 | METYEKIELGIIVIILLILIESVILMTVEGWDFFTAFYTAVVTISTVGYGDYTPQTFLGKLSVIIYIFAGVGAVAYTMGNIASFFIEGHFRKYFRLRKMMDRIKKLNNHYIICGYGRLGKVIAEEFKKCNIPFVIIDSDEKLLEEALEKDPNLICIVGDATSDDILKKAKIEKAKGLISVVSSDAENVFITLSAKKLNPNIYIVAKAEKPSTLDKLIKAGADRAVCPYIVGGMEIARIAINPDIVEFIHSLVATEEDMEVRRYIVKNKELDNKLLKDSGIREKTGATILAVKKGDKTITSPPPDTVINIGDIIYAFGTKE... | Function: Potassium channel protein. Seems to conduct potassium at low membrane potentials.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37150
Sequence Length: 333
Subcellular Location: Cell membrane
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Q58752 | METSKKLVIVAVLSITLILTYAYLISIIEGVDYFTALYFSVITITTTGYGDFTPKTFLGRTLTVVYLCVGVGIVMYLFSLIAEFIVEGKFEEFVRLKKMKNKIKTLKDHYIICGYGRLGKVVGEKFIEENIPFIAIDINEDVLKEEYEKYPDKFLYIVGDAKKEEVLKKAKIDKAKGLIATLPSDADNVFLTLTARELNPNILITAKADEKEAIRKLKIAGANRVVSPYLIGGLRMAEVSVRPGILDFLSTFIKIAKDEYEEDIELRKFVIEKDSELAYKSLKDANIRGKTGATILGIRREKEFCINPYPEFILKPGDVI... | Function: Probable potassium channel protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38884
Sequence Length: 343
Subcellular Location: Cell membrane
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Q501Q9 | MSGPEVEDHISQKYDIKKRLGKGAYGIVWKAIDRKSGEIVAVKKIFDAFRNRTDAQRTFREIMFLQEFGEHPNIIKLLNVIRAQNDKDIYLVFEHMETDLHAVIKKGNLLKDIHMRYILYQLLKATKFIHSGNVIHRDQKPSNILLDGDCLVKLCDFGLARSLYQIQEDVGNPALTEYVATRWYRAPEILLASNRYTKGVDMWSVGCILGEMLLGKPLFPGTSTINQIERIMSIIEPPTHEDIVSIKSEYGASVISRMSSKHKVPMAELFPASCPREALDLLSKLLVFNPGKRLTAEEALEHPYVSRFHSPAREPALDYD... | Function: Atypical MAPK protein that regulates ciliogenesis by phosphorylating rcsd1 through its binding with dvl2.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 64989
Sequence Length: 586
Subcellular Location: Cytoplasm
EC: 2.7.11.24
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O62618 | MSVSITKKFYKLDINRTEWEIPDIYQDLQPVGSGAYGQVSKAVVRGTNMHVAIKKLARPFQSAVHAKRTYRELRLLKHMDHENVIGLLDIFHPHPANGSLENFQQVYLVTHLMDADLNNIIRMQHLSDDHVQFLVYQILRGLKYIHSAGVIHRDLKPSNIAVNEDCELRILDFGLARPTENEMTGYVATRWYRAPEIMLNWMHYDQTVDIWSVGCIMAELITRRTLFPGTDHIHQLNLIMEMLGTPPAEFLKKISSESARSYIQSLPPMKGRSFKNVFKNANPLAIDLLEKMLELDAEKRITAEEALSHPYLEKYAEPSV... | Function: Kinase involved in a signal transduction pathway. May down-regulate insect immunity gene expression after prolonged infection.
PTM: Dually phosphorylated on Thr-184 and Tyr-186, which activates the enzyme.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da... |
O61443 | MSRKMAKFYKLDINRTEWEIPETYQNLQPVGQGAYGQVCKAVVRGTSTKVAIKKLARPFQSAVHAKRTYRELRLLKHMDHENVIGLLDVFHPGQPADSLDQFQQVYMVTHLMDADLNNIIRTQKLSDDHVQFLVYQILRGLKYIHSAGVIHRDLKPSNIAVNEDCELRILDFGLARPAESEMTGYVATRWYRAPEIMLNWMHYNQTADIWSVGCIMAELLTGRTLFPGTDHIHQLNLIMEVLGTPADEFMSRISSESARNYIRSLPVMPRRNFRDIFRGANPLAIDLLEKMLELDADKRITAEQALAHPYMEKYHDPTDE... | Function: Kinase involved in dpp signal transduction pathway in the process of wing morphogenesis when the levels of dpp are enhanced or inhibited. May down-regulate insect immunity gene expression after prolonged infection.
PTM: Dually phosphorylated on Thr-183 and Tyr-185, which activates the enzyme.
Catalytic Activi... |
Q75A60 | MGSLSDISFFDHLQELARRDCCVNALLWCAFTVGAVKLTTFMLSLISIALETTVLPSASYKKYGARKGAYALVTGASDGIGKEFALQLASKGFNVLLVSRTEAKLLELKQEIMAKYKVDARVLSVDFGVDNRLTYTAISELCGELPVTVLVNNVGVSHSIPVSFLETTEEELRGIITVNNTATLMVTQTVAPLVIANARRLQCRGLVLTMGSFGGLLPTPLLATYSGSKAFLQAWSAALAGELAPHNVDVQIVLSYLVTSAMSKVRRASALIPTPRAFVRSTLASLGRRVGAQERYATCTPYWSHALYHFLIENTVGVHS... | Function: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide an... |
A1C6J8 | MDFVSKYMSCLSSWGLDLQPGLQSVGAAVLLATGGLFLASRVLTFVRVLLSLFVLPGKPLRSFGPKGSWAVVTGASDGLGKEFALQLARAGFNIVLVSRTASKLATLAEEITAKHSVQTRTLAMDFAANDDTDYEDLKTLVDGLDVSILINNVGKSHDIPVPFALTPEDEMTDIVTINCLGTLRATQLVIPGMMQRRRGLVLTMGSFGGLLPTPLLATYSGSKAFLQQWSTSLGSELEPYGITVELVQAYLITSAMSKVRRTSALIPSPRAFVSSVLSKIGRNGGSPTYSYSSSPYWSHGLMAYFLTCVLQPMGKLVVGQ... | Function: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide an... |
B0FHH8 | MAALHWLLLAALLGCTLAEEQAIFYNCEEASEAVCSVKEVRINPCNPNKKCIFKKGVNASISFDFEPNFASSKLVTTLYGPFDVEFDEMTNVDACQYTKCPTEPGKSQVLDYTLYIGKKLPQGTYTFKWKLWNPEETSQLCCFKTTIKIRK | Function: Binds to lipopolysaccharide from a variety of Gram-negative bacteria and to lipid A.
PTM: N-glycosylated.
Sequence Mass (Da): 17102
Sequence Length: 151
Subcellular Location: Secreted
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P81446 | MNGHLASRRAWVWYFLMLGQVFGATVKAETKFSYERLRLRVTHQTTGEEYFRFITLLRDYVSSGSFSNEIPLLRQSTIPVSDAQRFVLVELTNEGGDSITAAIDVTNLYVVAYQAGDQSYFLRDAPRGAETHLFTGTTRSSLPFNGSYPDLERYAGHRDQIPLGIDQLIQSVTALRFPGGSTRTQARSILILIQMISEAARFNPILWRARQYINSGASFLPDVYMLELETSWGQQSTQVQQSTDGVFNNPIRLAIPPGNFVTLTNVRDVIASLAIMLFVCGERPSSSDVRYWPLVIRPVIADDVTCSASEPTVRIVGRNG... | Function: The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for c... |
Q47XX8 | MTKFTSLLLVIFTTVLLSACDKENDSSSLSRILARGYINVGTIFGPTNYYTTANGFAGFEYELAKQYADSLNVELRIVPTYSLDELFIKLNTGEVDLLASGLSITDKRLQRFRFAPSYETISQKLVFKQGNVRPRKVADLTGTLMVTSGSSYVENLEKLKQTNSELAWQESTEFDSEELLRKVLSGEIDYTIIDSNNLAINRRYYPEISIGFSINEPEPLAWMVSENSHDDILASLVEFFGTVHHDGTLLALDDKYYGHIEQFNYVETRTFIKAVAGTLPEYQPLFEKYAQELDWRLLAAISYQESHWNPTARSYTGVRG... | Function: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates... |
A8ZWR8 | MRRPLRRVTVVLLWVALAIGVAWFYDYRRSMQSLWKIRQHGKIVVLTENNANSYYIYKETPMGFEYDLAKAFAGHLGVDLEVKTPGWDALFASLQRGDGDFIAASMTHTRKREQYADFSEPYLSVRQHLILHKSDHSIVTPAGLAGRTVHVREDTTYQQRLEALQADGIDLQLVLHRNTPTEELIEQVAKRQIDITVADSAIALLNRRYYPDIRIAFPIEKEQPLAWAVRKGDRGLRTEINRFFDEIKENGTFTRIYNRYYTAVDTFDYVDVKKFHQRIYTRLPRFRPLIEKAADRHGFDWQMIAAVIYQESHFDPFAQS... | Function: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates... |
Q8XA45 | MKKLKINYLFIGILALLLAVALWPSIPWFGKADNRIAAIQARGELRVSTIHTPLTYNEINGKPFGLDYELAKQFADYLGVKLKVTVRQNISQLFDDLDNGNADLLAAGLVYNSERVKNYQPGPTYYSVSQQLVYKVGQYRPRTLGNLTAEQLTVAPGHVVVNDLQTLKETKFPELSWKVDDKKGSAELMEDVIEGKLDYTIADSVAISLFQRVHPELAVALDITDEQPVTWFSPLDGDNTLSAALLDFFNEMNEDGTLARIEEKYLGHGDDFDYVDTRTFLRAVDAVLPQLKPLFEKYAEEIDWRLLAAIAYQESHWDAQ... | Function: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates... |
P82679 | MQTIPSTTETAADFDAVIXGAGFXGLYALHR | Function: Catalyzes the NADPH- and oxygen-dependent oxidation of the monocyclic monoterpene ketones 1-hydroxy-2-oxolimonene, dihydrocarvone and menthone. Is able to convert all enantiomers of these natural substrates with almost equal efficiency. Is thus involved in the conversion of the monocyclic monoterpene ketone i... |
O51798 | MFAWYKAGSPQQKKTFWACYSGWALDSFDMQMFSFLLPALTLTWGLTKAEVGVLGTVALVVTAIGGWGAGILSDRYGRARILVLAIIWFTLFGVLAGFAQSYQQLLIARTLQGLGFGGEWAVGAALMAEVIDSRHRGKAIGFVQSGFALGWALAVVVATLLLAWLPKEMAWRVAFWSGIIPALIVLFIRRHVKDSSMFERARQSRAPRASLSSVFNRKYARTLALSSVLVIGLQAGCYAILVWLPSLLNQRQVAAGSMIVTVFIMAFGSFCGFAVTADLSDRIGRRPTLILLSVCAWIVTVSYMLLPLNTTLTAILGFLV... | Function: Probable uptake of 4-methylmuconolactone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45804
Sequence Length: 428
Subcellular Location: Cell membrane
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Q6CAP9 | MSQFVLPAVASEGIINWPFLTGFMLGQFSVGLVLLIFVRFFIFSDQTEPDINTQRRTAKVLPTGNPSTDAILEKTYYNTKTHQPESLDWFSVLVAQALYQLRDEVRGNDEVLERLNEILKSDKLPGFLDTINVVDLDIGDAFPQFGACKVNKDESGDLEAEIKVSLEDTIKLGVETKMLLNFPIPKFASVPVSLSVSLVKFSGTLTVAIRSAFNSGEANRVLVSFAPDYELQWKIESSVGSTQKLQNAEKISRLIESRIRRWFKDRCVYPEYQQFELPKLWRKTSAPPPSAGAGTGTSTGVPPSPFPQPANPSSVPKPLE... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
Q6CA06 | MVIPAELIQKALKQQSGWGFTEGLVLGQLSVIITVIIILKFVIFAENKSPKKGNDMTAVSAKDKEAEHVAMGGQTANGVKTSGVRRNKSSTNLRNRLATGAAGASISRPGSSRVSMVRSTSGAVPVLGQNGGATPRGMAGSSVAGSTSNLAVPVPTTPTIAEGIEPENDSTLQDDSAIIDLDLDLDLSPVDEILHKTCYQLSSHAPESLDWFNVLVAQIITQLRFDAKANNNLNLLNSLDAAFNSKRPDFIDRINVTEINLGDDYPILSNCKITHKGTGPAGSGAASGNNMPNNAEYDDSRLEAQMDIDLSDTITLGIET... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
Q75FA5 | MKGVENTLSQSESVNRGYNGWMGMESETSARATHSSEQMISLEEYVREMLPMHLQKLLMERIIEAEQTGAAHTSVFAAPTGVAAQYPAMGPPMLPGQTFSSRSFAEGLVVGQLSVIVVLIFFIKFFIFSDGPAKTGGGGGSSAESRSSGFTGSPLTSTTSRLLSTLIKRGGKEGTEFAEDSENERTRQINAILEKTYYDVETHSPESLDWFNVLIAQTIQKFREEALQKDNIVHSLNDFISRKSSQLPNYLDAVKITELDIGDDFPIFSNCRIKYSPPLNKKRLEAKIDIDLSDRLTLGIETRLLMNYPKYLTASLPVKL... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
A1CM86 | MSSQPGDPATLPAQSSLSFTQGFLLGQLSVVLVLAAFIKFFIFGEAPPPPSRGLSHRSATHRRSNSIYSNSPQEAGSRSLREKPSTSNVLRPVPSSSTNTRSILRKTYYSAIPTNPAKHGRLRIHHSSHQPESLDWFNVLIAQTIAQYRQTAYSLKDSPTSSILNSLTAALNNPEKKPAFIDKITVTDISLGEEFPIFSNCRIIAVDDPNSDGGRLQALMDVDLSDDNLSIAIETQLLLNYPKPCSAILPVALSISVVRFSGTLCISLVPASTPPLDTPSHSPSPPTADTATSGRSKPGDKAGGNQPRSNGSTEDPAGGN... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
P50282 | MSPWQPLLLVLLALGYSFAAPHQRQPTYVVFPRDLKTSNLTDTQLAEDYLYRYGYTRAAQMMGEKQSLRPALLMLQKQLSLPQTGELDSETLKAIRSPRCGVPDVGKFQTFDGDLKWHHHNITYWIQSYTEDLPRDVIDDSFARAFAVWSAVTPLTFTRVYGLEADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGAVVPTYFGNANGAPCHFPFTFEGRSYLSCTTDGRNDGKPWCGTTADYDTDRKYGFCPSENLYTEHGNGDGKPCVFPFIFEGHSYSACTTKGRSDGYRWCATTAN... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cl... |
G5EGM1 | MFTGLHDILIILFLLVTLKIAQNVDHTKFLQKYGYLTSGDNQLSSESLSDALKNMQRMAGLEETGELDERTIQMMERPRCGHPDVEDHQKSRGKRYAPPQFKWKEKIITYGCKAVGTSTRISLDDLRRTMHQAASQWSELADVEIVESSVKNPMMVISAGRENHYPCTVRFDTKTLAHAFFPTNGQIHINDRVQFAMTNYTERMGANSLYSVVAHEMGHALGFSHSPDIDSVMFAYDTPRKWKFTSMDKYNMRSYYGAKASKKENEEEERKTENEDKRRKTEKDRGRTREHESDDIRPNECRVENPIVVQYRGEYLIFKS... | Function: Metalloprotease which, together with cadherin cdh-3 and hemicentin him-4, plays a role in anchor cell (AC) invasion during postembryonic vulval development probably by promoting the degradation of the basement membrane separating the gonad from the vulva epithelium.
Location Topology: Single-pass type I membr... |
Q9A710 | MIGFLIMLVSLLFVLSVVVTVHELGHYWAARACGVAIERFSIGFGAPLISWRDKRGVEWCVASIPLGGYVRFAGDENAASVPDQNDLDAMRNEIRRREGDDAVNRYFHFKPVWQRAFIAVAGPMANFILAILVFAVILVSFGAQKTSTTVGEVVAGTPAAAAGFKPGDVILKADNRQIRSFQDIQGYVALRANMPIDFAVERDGRTVHLTATPRLVERQNEISGRVKVGELGLRSAPGGRFERSSLLSAIPDATVEVWDMIKTIAFYLGRLLMGQLPADQISGIIGIGHTAGAVTNGVVEQAPNGKALAIGLIYSQFWLI... | Function: Involved in the regulated intramembrane proteolysis (RIP) of the short isoform of PodJ protein (PodJS), during the swarmer-to-stalked transition. The cleavage occurs near or within the single transmembrane of PodJS thereby releasing the N-terminal segment into the cytoplasm for subsequent degradation. It cont... |
O44836 | MTKWSPNGNPLSTIYLILSLFTLAHTAPTTQHSRTTTQLRLEDEDGGGGVDEDSIHFVKGQMEKYGYLKGIDHSSPQEFRQALMFFQEVLEVEQTGNVDEMTVEAASKPRCTQTDVRQEQTKRTKRFTLSKRAKWAHASGQSVTLKWYISDYTSDIDRLETRKVVEKAFKLWSSQSYIKNEKKVTLTFQEASSKDEADINILWAEGNHGDEHDFDGANGKIEGNKKENVLAHTFFPGYARPLNGDIHFDDAEDWEIDVDQVGHGSNKRFFPYVLAHEIGHALGLDHSQKADALMHPYYKNVPINEIQLDIDDKCGVIWNY... | Function: Metalloprotease involved in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed . Plays a role in thermotolerance probably by preventing the accumulation of oxidized lipoproteins and cholesterol .
Sequence Mass (Da): 59254
Sequence Length: 519
Domain: The conse... |
G5EBU3 | MRLIYVIAILLVSTCQAGFFSSLVSRFTGGGNSSPSSSSSSSSFSNSRKPSLSDEKARSYLQTFGYVPPSNSLQSRNGMAGDIQSAEQVFKSAIRKFQEFAGIAKTGFLDAATKAKMALSRCGVTDAPLALTSGSSQFKWSKTRLTYSIESWSSDLSKDDVRRAISEAYGLWSKVTPLEFSEVPAGSTSDIKIRFGVRNHNDPWPFDGEGGVLAHATMPESGMFHFDDDENWTYKDARKIHNNEATDLLAVAIHEGGHTLGLEHSRDENAIMAPFYQKTTDSSGNYVYPNLKSDDISAIQAIYGAGSGRSSSGSDFGGSS... | Function: Metalloproteinase.
Sequence Mass (Da): 62540
Sequence Length: 579
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellul... |
A0QP27 | MFAWWGRTVYQFRYIVIGVMVALCLGGGVYGISLGNHVTQSGFYDEGSQSVAASLIGDEVYGRDRTSHVVAILTPPDDKKVTDKAWQKKVTEELDQVVKDHEDQIVGWVGWLKAPDTTDPTVSAMKTQDLRHTFISIPLQGDDDDEILKNYQVVEPELQQVNGGDIRLAGLNPLASELTGTIGEDQKRAEVAAIPLVAVVLFFVFGTVIAAALPAIIGGLAIAGALGIMRLVAEFTPVHFFAQPVVTLIGLGIAIDYGLFIVSRFREEIAEGYDTEAAVRRTVMTSGRTVVFSAVIIVASSVPLLLFPQGFLKSITYAII... | Function: Transports trehalose monomycolate (TMM) to the cell wall . Flips TMM across the inner membrane. Membrane potential is not required for this function . Transports probably phosphatidylethanolamine (PE) as well. Binds specifically both TMM and PE, but not trehalose dimycolate (TDM). Binds also diacylglycerol (D... |
P9WJV5 | MFAWWGRTVYRYRFIVIGVMVALCLGGGVFGLSLGKHVTQSGFYDDGSQSVQASVLGDQVYGRDRSGHIVAIFQAPAGKTVDDPAWSKKVVDELNRFQQDHPDQVLGWAGYLRASQATGMATADKKYTFVSIPLKGDDDDTILNNYKAIAPDLQRLDGGTVKLAGLQPVAEALTGTIATDQRRMEVLALPLVAVVLFFVFGGVIAAGLPVMVGGLCIAGALGIMRFLAIFGPVHYFAQPVVSLIGLGIAIDYGLFIVSRFREEIAEGYDTETAVRRTVITAGRTVTFSAVLIVASAIGLLLFPQGFLKSLTYATIASVML... | Function: Transports trehalose monomycolate (TMM) to the cell wall. Flips TMM across the inner membrane . Membrane potential is not required for this function. Transports probably phosphatidylethanolamine (PE) as well. Binds specifically both TMM and PE, but not trehalose dimycolate (TDM). Binds also diacylglycerol (DA... |
P9WJV1 | MIVQRTAAPTGSVPPDRHAARPFIPRMIRTFAVPIILGWLVTIAVLNVTVPQLETVGQIQAVSMSPDAAPSMISMKHIGKVFEEGDSDSAAMIVLEGQRPLGDAAHAFYDQMIGRLQADTTHVQSLQDFWGDPLTATGAQSSDGKAAYVQVKLAGNQGESLANESVEAVKTIVERLAPPPGVKVYVTGSAALVADQQQAGDRSLQVIEAVTFTVIIVMLLLVYRSIITSAIMLTMVVLGLLATRGGVAFLGFHRIIGLSTFATNLLVVLAIAAATDYAIFLIGRYQEARGLGQDRESAYYTMFGGTAHVVLGSGLTIAGA... | Function: Part of an export system, which is required for biosynthesis and secretion of siderophores.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 104785
Sequence Length: 964
Subcellular Location: Cell inner membrane
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P41218 | MVNEYKKILLLKGFELMDDYHFTSIKSLLAYDLGLTTKMQEEYNRIKITDLMEKKFQGVACLDKLIELAKDMPSLKNLVNNLRKEKSKVAKKIKTQEKAPVKKINQEEVGLAAPAPTARNKLTSEARGRIPVAQKRKTPNKEKTEAKRNKVSQEQSKPPGPSGASTSAAVDHPPLPQTSSSTPSNTSFTPNQETQAQRQVDARRNVPQNDPVTVVVLKATAPFKYESPENGKSTMFHATVASKTQYFHVKVFDINLKEKFVRKKVITISDYSECKGVMEIKEASSVSDFNQNFEVPNRIIEIANKTPKISQLYKQASGTM... | Function: May act as a transcriptional activator/repressor in the myeloid lineage. Plays a role in the granulocyte/monocyte cell-specific response to interferon. Stimulates the DNA binding of the transcriptional repressor protein YY1.
Sequence Mass (Da): 45836
Sequence Length: 407
Domain: Its N-terminal half (200 amino... |
A0A0H3AJF5 | MFVYGSIINPCPTEHVMSVLAISITTVALAEIGDKTQLLSLLLASRYRKPIPIIAAIFLATLANHALAAWLGVVVADYLSPDILKWVLVVSFLTMAGWILIPDKLDGEESISTRGPFVASFIAFFMAEIGDKTQIATSILGAQYADALSWVIVGTTLGMLLANVPVVLIGKLSADKMPLGLIRKVTAGLFLLMALATAFF | Function: Involved in manganese homeostasis. May function as a manganese exporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21380
Sequence Length: 200
Subcellular Location: Cell inner membrane
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C0SP78 | MASEREQISRKVALIALIANLILMAGKVFFGLVGDSEAVFADGIHSAADVVASIAVLAVIGISNKPPDQDHPFGHGKAEVISEAIVGIILVIVSVYILIEAILSFVKGPSVPQYSALFAALISYVAKEILYRYSIKQGKKWNSKAIIAIAYDHKGDIVASLAAFIGVLLAIIGNSRGWSYLLYADAIASAIVAYLIFKISMELIRPSVDVLMEKSVDPELIEEYKAVIFQCDQVKRIDRIRAREHGHYKLLDVRLSLDHDLTIKQGHDIAREIRNEIKRQFSDVEEVLIHVNPYFEE | Function: Primary efflux pump for manganese. May prevent manganese intoxication.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32854
Sequence Length: 297
Subcellular Location: Cell membrane
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P46348 | MERYDELKKGESGALVSIAAYLVLSAIKLIIGYLFHSEALTADGLNNTTDIIASVAVLIGLRISQKPPDEDHPYGHFRAETIASLIASFIMMVVGLQVLFSAGESIFSAKQETPDMIAAWTAAGGAVLMLIVYRYNKRLAKKVKSQALLAAAADNKSDAFVSIGTFIGIVAAQFHLAWIDTVTAFVIGLLICKTAWDIFKESSHSLTDGFDIKDISAYKQTIEKISGVSRLKDIKARYLGSTVHVDVVVEVSADLNITESHDIANEIERRMKEEHAIDYSHVHMEPLEQK | Function: Secondary manganese efflux system. May prevent manganese intoxication.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31785
Sequence Length: 290
Subcellular Location: Cell membrane
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P54745 | MVLFYRAHWRDYKNDQVRIMMNLTTLTHRDALCLNARFTSREEAIHALTQRLAALGKISSTEQFLEEVYRRESLGPTALGEGLAVPHGKTAAVKEAAFAVATLSEPLQWEGVDGPEAVDLVVLLAIPPNEAGTTHMQLLTALTTRLADDEIRARIQSATTPDELLSALDDKGGTQPSASFSNAPTIVCVTACPAGIAHTYMAAEYLEKAGRKLGVNVYVEKQGANGIEGRLTADQLNSATACIFAAEVAIKESERFNGIPALSVPVAEPIRHAEALIQQALTLKRSDETRTVQQDTQPVKSVKTELKQALLSGISFAVPL... | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane . This system is involved in mannosyl-D-glycerate transport . ... |
P54746 | MKAVSRVHITPHMHWDREWYFTTEESRILLVNNMEEILCRLEQDNEYKYYVLDGQTAILEDYFAVKPENKDRVKKQVEAGKLIIGPWYTQTDTTIVSAESIVRNLMYGMRDCLAFGEPMKIGYLPDSFGMSGQLPHIYNGFGITRTMFWRGCSERHGTDKTEFLWQSSDGSEVTAQVLPLGYAIGKYLPADENGLRKRLDSYFDVLEKASVTKEILLPNGHDQMPLQQNIFEVMDKLREIYPQRKFVMSRFEEVFEKIEAQRDNLATLKGEFIDGKYMRVHRTIGSTRMDIKIAHARIENKIVNLLEPLATLAWTLGFEY... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: May hydrolyze 6-phospho-mannosyl-D-glycerate to mannose-6-phosphate and glycerate.
Catalytic Activity: (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate + H2O = (R)-glycerate + alpha-D-mannose 6-phosphate
Sequence Mass (Da): 100015
Sequence Length: 877
EC: 3.... |
Q9KER1 | MKKTAHIISHSHWDREWYMPFEGHRYYLIQLMDDLLELFATDPNFRSFHMDGQTIMLEDYLNIRPEKEAEVRKYIQDGRLVIGPWYILQDAFLTSAEANVRNLLYGIKDTETFGQKREQIGYFPDTFGIYGQAPQLLAQAGIRAAVFGRGVTPTGFNNQVQHDDYSSPFSELIWEAPDGSQVIGILLANWYSNGNEIPTDEDEAQTFWVKKLRDAERFASTSQLLFMNGCDHQPVQKDVTQAIKVAETLFPDVAFKHSNFHDYLTQIKEELPKELQKITGELRNQKTDGWSTLVNTASARIYLKQANDRCQTLLTNVLEP... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: May hydrolyze 6-phospho-mannosyl-D-glycerate to mannose-6-phosphate and glycerate.
Catalytic Activity: (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate + H2O = (R)-glycerate + alpha-D-mannose 6-phosphate
Sequence Mass (Da): 102540
Sequence Length: 896
EC: 3.... |
Q49W87 | MAIQILVNLILSVFWLFVTGSYNFNNFILGYLFALLLVYIMRGVLPGRFYLITVYKIIKLFLVFLIELIKANIDVIRIVVKPNIDNEPAFFTYNTDLKKDWQIVLLSNLITLTPGTIVLGISDDRTKIYIHSIDFSTKEEEVESIKSSLEKVVREVGENE | Function: Mnh complex is a Na(+)/H(+) antiporter involved in Na(+) excretion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18439
Sequence Length: 160
Subcellular Location: Cell membrane
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B2UPK4 | MARILVGLSGGVDSSVAAALLVEQGHDVVGAYMKNWVNDEGIPGECPWEQDIQDALAVAKTTGIEFRVIDLVDEYRARIVNYLIEGYRAGYTPNPDVLCNREMKFGVFLDYALEQGFDYVATGHYARRMDTPQGAFILRGRDPNKDQSYFLSLMRPDQIARAVFPLGDLLKPEVRVLAEKYGLPTARKKDSQGICFIGQVKMSDFLRHYLPDKPGNIVDTEGRTLGTHNGLHLFTMGQRKGHGVASPREGVAYVVVGKDVRRNRLILGYEDASTRGLYASRAVVGGISNTLAPLPARVMAQPRYRAKAEWASCEYLEEGK... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 39372
S... |
Q5WHN4 | MKKREDTRVVVGMSGGVDSSVTALLLKEQGYDVIGIFMKNWDDSNDSGFCSATEDYEDVERVAQQLGIPYYAVNFEKQYWDKVFTYFLEEYKAGRTPNPDVMCNKEIKFKAFLNHAISLGADYVATGHYAQLQELDGEYRLIKGADANKDQTYFLNALSQKQLSKVMFPLGHLQKAEVRKIAAEAELATATKKDSTGICFIGERDFKEFLQTFLPAQPGRMETMDGIDKGQHDGLMYYTLGQRQGLGIGGAGEPWFVIDKDLERNVLIVGQGYHHPGLYSDGLWATDMNWIAKEERTSPFTCKAKFRYRQEDQGVTVFPK... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 41035
S... |
A7HCV7 | MRVLVALSGGVDSSTAAALLVAEGHDVIGVSMRVADYSDARRGRSCCAPDDLEDARAAARRLDIPFYVANVEARFRERVIEPFVRDYVEGRTPNPCVACNSDVKFDWLLARARALGAKLATGHYARVERRGGRFALCRAGDPAKDQTYFLYGLGQEALRDVLFPVGDLAKRDVRAVAAQAGLPNAEKAESQEICFVTQGDAGDFVALRAPGSVRAGEIVSTAGEVLGRHDGVHRFTVGQRRGLGLAGPAPRYVVRLEPGTARVVVGSAGEASRDRFAVTEVRWIAGAPPPRPVAARVKVRHRHEGEEGTVTPDGGGGQVR... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 37156
S... |
O67274 | MRVAVGMSGGVDSSVTALLLKEQGHDVIRVTLRFHTVEACEVNETHNVCCSPKDVQDASRVAKRLGIPHLVFSWEEIFKSKVIDYFVEEYKRGRTPNPCALCNREVKTGFFARYLKQVADIDKLATGHYAKIEEDKKYGLVIKRPKDRKRDQTYFLSLVRREDLELLTFPLGAYTKEEVREIAKRYGLEVAQKRDSQEVCFLMGKSPGEYLEGILGKQRGLIKHVSGKVLGEHEGVYRYTIGQRRGLGISYGKPVYVIDIDAKTNTLIVGEEEYLYNDKLLVKEINFHVPLEKWENVSAQIRYRHKPVPVERIEKTEEGF... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 40574
S... |
Q2NIM9 | MTKVVVGLSGGVDSAVAAFLLKKQGYLVEAVFMRNWDSNLNFDIQGNPTLNDICPQELDYKDALKVSEQLGIKLHRVDFIEEYWQKVFMSFIKAFENNLTPNPDILCNNEIKFRAFIEYVTTKLAPRYIAMGHYANIIYETFSEQKLFPQLACAVDQNKDQTYFLSQLATKQLQNILFPLGNLTKQEVRQIALENNLINATKKDSTGICFIGERNFFQFLSNYLPAQKGDIKTLDGTFLAHHKGVMYYTIGQRKNLGLGDFSSQKPWFVVGKHLQTNTLYVEQGNTHPYLYSDKALISDIVWRGKKTNLHLQAKMRYRQP... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 43380
S... |
Q4JUL5 | MRVVAAMSGGVDSAVAASRALEAGHEVIGVHLALSQSPEAVRAGSRGCCSLEDSADARRVADKLGIPFYVWDFSDRFKADVIDDFVDSYAIGETPNPCLRCNEKIKFEALLDRSIALGFDAVVTGHYARLHDGVMRRGVDANKDQSYVLGVLTDEQLAHCMFPVGDTIKPEIREEAKDHGFGVASKPDSHDICFIPDGQTQAFLGKKIGLRPGLMKDQDGSTVAEHDGVYGFTIGQRKGLGLPREGLDGKPRYVTDIDAATGTVTIGQRDDLRVGGITADRLKRLDPAVHGREFECEVQVRAHGGVVPATARLVDDPERT... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 42232
S... |
A9KE87 | MPNFEQNQVIAVGLSGGVDSSVAALVLKEKGYEVIGLFMQNWETDSKDPFCTAEQDLSDAKAIADHIGIPLYVVNFSKAYWNHVFQHCLDEFAQGRTPNPDVWCNREIKFKSLLDHAKKLGATHLATGHYACIQNENNEYRLLKSNDSHKDQSYFLHLLNQYQLANSVFPIGGYQKSEVRAIAKKRGFINHAKKDSTGICFIGERKFKDFLNEFLLAQPGNIETPEGKIIGKHDGIMFYTVGQRKGLHIGGRPDAGEAPWYVVDKDVKRNVLIVVQGYEHPLLYSQELTCTNLHWIRDTEPSFPLTCKAKTRCRQADQTC... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 40870
S... |
B1X0U7 | MKKVVVGLSGGVDSSVAAASLHHQGYDVIGLTLWLMKGKGQCCSEGMVDAAFICEQLGVPHHIVDTRELFEANIINYLVSGYESGVTPLPCSQCNRAVKFGPMLAYAKEELNCDRIATGHYARIRYDEQTRRYQLLRAIDRNKDQSYFLYDLSQDILKGTIFPLGEQTKEETRRIAAEFDLKTASKPESQDLCLIEAHGSMASFLDQYIKPKEGEIVDLDGKVLGTHQGIHHYTIGQRKGLGIAAPEPLYVVKLDAVMNRVIVGNRAAGGRSDCTVGRLNWVSIAEPSSPITVEVQVRYRSKAVPVSIIPIENNRVTLQF... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 39043
S... |
Q1D6N0 | MRVVVAMSGGVDSSAAAALLKEQGHEVIGITLRVWSYEGKATCGSCCSPDDIDDARAVAQTLGIPFYVANAEEIFQDRVINPFVQSYLGGRTPIPCVACNRDVKFNFLLKRARALGARLATGHYARVEEVDGRFVLRRAVDAAKDQSYFLFTLGQDELRDILFPVGGMTKAEVRAVAERHGLVTSQKPESMEICFVPDGDYAGFVEKVAGPQPAGDIVDTEGNVLGTHQGIHRYTVGQRKGLNLGGGEIRYVHRLEPETQRVVVGPAEGTGRDNFGLLQPHWVDGPPPASQPVEVRIRHRHSGAQGRVHVSPHGLVSVKL... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 37577
S... |
B2A5K1 | MMMSNRVLVAMSGGVDSSVAALMLKEQGYEVIGAHMRIWYREEDEELYEQNVKGCCSLAAVHDAKRVADKIGIPFYVLNFKEPFYDWVVKNFIDEYLQGRTPNPCIACNRFIKWEEFLKRAMALECDYIATGHYSKIVYDNLKNRYLLYRGKDKTKDQSYMLSQLTQEQLARTLFPLGDYYKEDVRNIAEQNELGVADKPDSQEICFVPNNDYGEFLQSVVPEHINPGPILDAQGNKLGEHKGIAFYTIGQRRGLGISLGRPVYVIDIDADNNALIVGDKEELYSDGLIAEEINLIPYEQIENSIDIECKIRYNSRNVSS... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 41737
S... |
Q9JTJ9 | MNTTANPSNIIVGLSGGVDSSVTAALLKQQGYQVRGVFMQNWEDDDNDEYCSIKQDSFDAIAVADIVGIDIDIVNFAAQYKDKVFAYFLQEYSAGRTPNPDVLCNAEIKFKCFLDYAVGQGADTIATGHYARKEVRNGVHYLLKGLDQNKDQSYFLYRLKPFQLERAIFPLGGLEKPEVRRLAAEFNLPTAAKKDSTGICFIGERPFREFLQKYLPTDNGKMVTPEGKTVGEHVGLMFYTLGQRKGLGIGGGGEPWFVAAKDLTKNELMVVQGHDHPLLYTRSLVMNDLSFTLPERPKEGHYTCKTRYRMADAPCELRYL... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 40900
S... |
Q2GDU3 | MKLMQELAEIIPGKAYNDVKVMVAMSGGVDSSTVAAYLHRVGYKVIGVTLQLHNNFTSTQTNRKTCCAGSDIFDAKRVAAQFGFLHYVVNMEETFRKEVIENFAESYLKGETPVPCVKCNQTVKFRDLMKIAKSLSVDALATGHYVRRLTTTNGVELHKGIDPSKDQSYFLFNTTREQLEFLRFPLGNLKKSETRDLARKLSVDISEKPESQDICFVNGKSYADVIKKFRPDAQRPGKILSTDGEVLGTHNGTIHYTIGQRHGLQLSAPIPLYVVKIDAQNNIIIVGTRDKLQQRSLYVKEVNWLDRKELTAGLECEVKL... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 41283
S... |
Q8DRS4 | MTDNSKTRVVVGMSGGVDSSVTALLLKEQGYDVIGVFMKNWDDTDEFGVCTATEDYKDVAAVADQIGIPYYSVNFEKEYWDRVFEYFLAEYRAGRTPNPDVMCNKEIKFKAFLDYAMTLGADYVATGHYAQVSRDADGTVHMLRGADNNKDQTYFLSQLSQEQLQKVMFPLGHLQKPRVREIAEKAGLVTAKKKDSTGICFIGEKNFKEFLSSYLPAQKGRMMTIDGRDMGEHNGLMYYTIGQRGGMGIGGQKGGDNAPWFVVGKDLSQNILYVGQGFYHDALMSTSLTASQVHFTQNMPDKFTLNCTAKFRYRQPDSKV... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 41689
S... |
Q5ZVA8 | MSSPFVPIITADIDWRDDLPYSLQFDDIYYSAEGGINQSLYVFVEGNNLINRWQQLPTNESNVFTIAETGFGTGMNFLLTWKLWEKFAPQNARLHYISCDKHPLKKNDLIKCLQKWPELSVQAEKLIAHYPVLTPGYHHLTFSNNQITLTLMLGDVLECYEQLLFCGDINLEHQLRESYVNAWYLDGFSPSKNQSMWSDNLFTVIAMLSKESTTVATYSASSIVKTALTNAGFVIEKRKGFGPKRHMICAHYEKAYSSSKKNRHTPWHINYPVTKDERTALIVGGGLAGCFIANSLAKRGWEVTILEEKEKVGCGGSANQ... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
B1Y222 | MRRSNPITPARLGRSAEGLPFSEDFGAPYHPSAGALAQAEQVFLRGTDLPARWAGQARHVILETGFGLGHNFLATWAAWRRDPRRCERLVYLAIDKHPPAPADLADVHRDSPLADLAAQLIAAWPLATPDLHLLDFEGGRVQLMLALGDIHDVLPGLQAEAHSLYLDGFVPARNPAMWSADVFKRIARLAAPGAMAASGHADSAVRDGLVRQGFEVRATGADATVARYAPRFQPEPPRGWRWPHAAAREALVIGGGLAGCAVAQALALQGWRSTVIDRQAGPAQETSGNAGGLMHGIFNAPDSPHARWFRAAAMHTARNA... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
Q8F0E4 | MLTWKNNLTPVSEQFDDIYFSPENGLEETKHVFIKGNDLYNRWRNWNIQNAFCILELGFGTGLNFLTTWKEYLEYKDRFRLHFISIEKFPLNREEISKALSIFSELVEIKKEFLSSYQDLIPGMNYFQFLGGKIHFSLFLGDVSSALCEISGKVDAIFLDGFAPSKNPEMWDKSVLENLKYVSKKGTTLSTFTVARMVRDSLSFSGFKLEKRPGFGRKREMLIGSYSDSFLESNPKEKPWCKRAYPELQIKTVAIVGAGIAGTTLAYSLSRRGIQVFLIDPSGIAKETSGIPMAISHPHLTKIPGPISLFTLRAFRYALS... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
A0LA84 | MSKQQAPNTTGIGTADLQWHSDETPYSPRFDDIYYAPTHGAEESTHVFLEGINAPACWQQRPHYTLAETGFGTGLNFLLTLDLWLATAPAHGRLHYIAVEAYPMDQAALARAHAPFAWLAPHSAALVQAWPPAVAGFHQRSLAQGRVTLTLLFGPAASMLAQLSATVDGWYLDGFAPSRNPEMWSDTLFAQLSRLSRLGTRLASFTVAGTVKRGLRAQGFTLHKAPGFGQKRECLRGVLENPLPHKPNIPPWYAPPQRSEPVSSVAIIGAGIAGAACAYACRRAGLQVTLFERHAQPGAEASGNPSGLFSPRLTAGVSLD... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
Q0ALP0 | MTPDGLYCDPAELDWSQPSGPRARAYGDVYFSAEDGLEEARAVFLRGCGLPEAWTGRRHYVVGELGFGTGLNALALWQLWRQTRPTDGWLDFVTVEKHPLDRDAAARAFAAWPELSDLASRLLTQWPSRLRGPQRLVFPEDGFAITIFQDEVEAALSQMTRPVDAWFLDGFAPDRNAAMWSQAVFNRLGELSVPGTRVGTFTVAGFVRRGLAEAGFDVAKRPGFGRKRERLEAVWPGEAVDGSLANVDGPVAVLGAGIAGASLVHALRRRGIETVLIDAHGVASGASGAPAGLLTPRLEKADRPHVRATLAAFDFARRLY... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
A6W0S5 | MLTSYQLESPALSWGEDGAPHSNQFDDVYFDKESGLEETRHVFLKNNQLSGRWASLQKNAFVIAETGFGTGLNFLCAWQAFLTEAASDKQLHFISVEKYPMTKSMLTDALKMWPSISHLSQQLIDAYPEVCHGLHRIELEQGRIQLTLWFGEAEDGFAALDADVDAWFLDGFAPSKNPEMWSDNLFKHIHRLSHQGTTFSTFTAAGIVRRGLKNVGFDVRKVKGFGQKREMTVGELNSSTAPLSARMSQGQAWFNLRQDKTSEITKVLVVGAGLAGANTAYALAKQGIKVEVWEQGNCIAGGASGNPQGMLYPKLASQDT... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
A1TZU2 | MITDLRPPAMEPAELIWQDGVPESARFGDVYFSRDDGLAETRYVFIERNGLPGRFAELDRNSHFVIAETGFGTGLNFLATWAEWLAQRPDDQDHAILHFISVERYPLALADLEKALESWPGLQPLARELIDNYPPLIKGTHRLVLGGGAIRLTLCFGDVLDAWNELEFVADAWFLDGFAPSLNPDMWLEKAIHQIRAHSQPGTTLATFTSVGRVRRALADEGFEMAKVPGFGRKREMLTGRLPTSEDVSAPTVGTDPIVIIGAGIAGAALARNLAERGVPVVLADQASGPGAGASGNDQGALYVKLGVEYNDQTELAATA... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
Q1H1H9 | MSIPPFSQASLEWHEGQPYSAHFGDVYFSRESGLEETRHVFLRHNQLAERWQTMQQDAFTIVETGFGTGLNFLCAWQMWEHTAPSHVRLHFVSIEKFPLSHADLARALALWPELRQYSTALLAQYHQIVPGWQRLVFCQGRVQLTLLVGDVLALLPQLSSHADAWFLDGFAPSRNPEMWQEALFDNMAAFSHKHTTFATFTSAGIVKRGLQAAGFEVHKVAGHGRKRDMLCGRFTLNERPAMRAGRAVVIGGGIAGTASSHMLAERGWQVNLVEQEPALAQHASGNPVGVLYPKLARKDVPLGRLSLAGYLHSLRLLQQL... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
A2SH83 | MKTAPITPGRLAFSPDGVPLAPEFGDVYHPAAGALQQAHHVFLGGNRLPARWGGRGRFVILETGFGLGNNFLATWDAWQRDPQRCERLVFVSIEKHPLTREDLARAHAASPLPELARALVSAWPLSTPNLHPIAFEGGRVQLLLGFGDVALLLPQLVVSVDAFFLDGFAPARNPEMWEPRRLQRLGRLAAPGATAATWSAARVVRDGLSAAGFTVETTAGTGGKRDITVARFTPRHIAVPPPGGWHAHDAASREALVIGAGLAGCAAAWALSQQGWQCQLLDRAAEPADVTSGNPAGLFHGSFHRDDGPHARTLRAAALA... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
Q2Y7P9 | MLDWQNGQLYSTRFGDVYFSRDSGLEEKQYVFLQGNRLADRFESLQPDTAFSIGETGFGTGLSFLCTWRLFIQIAPLRTSLDFFSVEKYPLDEKELSAALALWPELGPYADELMLRWQRRVPGWNRWSFAGGRVRLTLAIEDVTRALPETHGIDAWFLDGFSPARNPEMWTLQIFHWIARASRAGATFATYTSAGVVRRGLEQAGFQVKKISGFGHKREMLQGDLPGPPPVRLAPTTAIVIGGGIAGCAAASALASRGLIVELLESHTLGAGASGNPIGILHARLSAGMNALHRFVLASYGHALALLDEKIPVDGVMRSE... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
Q8R6K8 | MEFDTIAAISTFPGEAGIGIVRISGDEALEIISKIFRPFRKKDIKSVKSHTIHYGHIVDPETGEVYDEVLVTVMRKPNTYTREDVVEINCHGGIVVSSKILELVLKHGARLAEPGEFTKRAFLNGRIDLSQAEAVIDIITSKTMLANRYAQKQLAGVLGQKMKDLKNKIMELLSHLLALIDFPEEDVEELEREEIKRRAKDILNDIEYLIASSESGRIIREGLKTAIIGKPNVGKSSLLNALLKQNRAIVTDIPGTTRDVIEEYMNIKGIPIKLIDTAGIRHTDELVEKIGVEKSKEVLAEADLILFVLDASRDLTKEDY... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 51369
Sequence Length: 460
Subcellular Locatio... |
A4XN51 | MEFDTIAAISTPIGTGGIGIIRISGQNSIEVAGKIIKSKRFNSIYDIPVRYAALVEVYDNDEFIDQAILIKFKAPHSYTGEDVVEIQSHGGMVVLRRILEVVIKNGARHAMPGEFTKRAFLNGRLDLSQAEAIIDIINSKTELLQKNAAKQLKGVLSKKIDEIAEILLNLISSIEASIDFSEHEVDEISPQEIEKSIDTALEMIYRLLKTYETGRAIKSGIYTVIVGRPNVGKSSLLNRLLKEERSIVTDIPGTTRDVIEEVLDIEGIPIILVDTAGVRQTEDIVERIGVERTLKSVERADLVIFMIESDGITKEDIEIF... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50811
Sequence Length: 455
Subcellular Locatio... |
A0RNG2 | MNIVALASAYGVGSISIVRLSGDGAYDLAINLCKKPLTPRYAHLRKLYCENMVFLDEAIVIYYKAPFSFTGEDVVEFQTHGGVVVANLIIDELLRLGARVANPGEFSKRAFLNGKMDLVKAESIQSLINARSEGAAKILARTMNGELSVFVNSLRDELIKILAYTETCIDYADDDLPSDILHSSKDLLLNSYKKLEHIINISNSKKGLIDGYKVAIIGRPNVGKSSILNSLLHYERAITSETAGTTRDTIEEQIKFGSHLVRIIDTAGIRDEFDSSIEAAGIEYSKRAAREADIIFCVFDSSQKASLEDRQILEFISNLN... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 48565
Sequence Length: 438
Subcellular Locatio... |
A7I145 | MSETIVAVATAHGIGGISIVRLSGENALSLSDILINKNRKKNKTQNSVSSSQNRIQNFKKINLKPRYATLCELYDNDGNFMDESVVIYYKSPNSFTGEDIVEFQIHGGFTLENLIMDELITNGARIAMPGEFSKRAFLNDKMDLSKAEAIQSIILSRSKSAAKILARNLHGELKNFVIDLRKEIVKTMAFVETCIDYADDDLPNDILDKIQNLLSENITKIDEITQISASRRGLLEGFKVAIIGKPNVGKSSILNSLLKFSRAIVSDEAGTTRDRIEENLQIGSHLIRIIDTAGIRKSENSVENIGISYSIKAANEADII... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 52097
Sequence Length: 466
Subcellular Locatio... |
Q9PNX9 | MSDTIAAIATAHGVGSISIVRLSGERALEFALKLSHKTKLTPRHATFTKLFNQNNEIIDEAIMIYFKAPYSFTGEDIVEFQTHGGFSVSEVLLEELVSLGARLALAGEFSKRACLNGKMTPLKALNIQDLILSKSALAAKIIARNMQGNLGELLEKIRTDLVKTLAFVETSIDYADDDLPSDLLEQISTMCEENSKILKEIYTLSQSKKGLIEGFKIAIVGKPNVGKSSLLNALLSYERAIVSDIAGTTRDTIEENFKLGTHLLRIIDTAGIRESKDVIEQIGVALSKKSLEDADIILAVFDASRVQDKEDEKIFDLLAN... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 49145
Sequence Length: 442
Subcellular Locatio... |
Q3AG56 | MMEDTIAAISTPLGEGGIGIVRVSGPGAIEAVKNVFIPRQSKDLSKVPSFTLHYGKIVDPADGKIVDEVLVSVMRAPKSYTGEDVVEINCHGGIVAVEKVLELILKQGIRLAEPGEFTKRAFLNGRIDLSQAEAVIDIIRAKTEASLKLAGRQLSGELREKINAVRQKIINILAFIEVSIDYPEYEFDEVTPETALKNIDEIINDVRRLLSSYERGRILREGITAVIAGKPNVGKSSLLNALLRKKRAIVTDIPGTTRDVIEDYLNLKGIPVKIVDTAGIRETEDLVEKLGVEKTREYLNQADVTLFVVDVSIGIDEDDE... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50656
Sequence Length: 461
Subcellular Locatio... |
Q05FY9 | MNTIFSRITPLGNGTLCVIRISGKNVKFLIQKIVKKNIKEKIATFSKLFLDKECVDYAMIIFFKKPNTFTGEDIIEFHIHNNETIVKKIINYLLLNKARFAKAGEFLERRYLNGKISLIECELINNKILYDNENMFQLTKNSEKKIFLCIIKNLKFKINSLIICIEIANFNFSFFFFNDFLFIKYTFKKLLKLLKILIDKITVINYLKKNFTIMILGRRNVGKSTLFNKICAQYDSIVTNIPGTTKNIISKKIKILSKKIKMMDTAGLKIRTKNLIEKIGIIKNINKIYQGNLILYMIDKFNIKNIFFNIPIDFIDKIKL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 51218
Sequence Length: 438
Subcellular Locatio... |
B0T6E0 | MNDTIYAPATGAGAAAVAVVRISGARSADIVRGLAGDLPKPRRAVLRQLTRDGVALDDALVLWFQGPASYTGEDAAEFHVHGGRAVVEAVLEALAAEGLRLAEPGEFTRRAFENGKLDLTQAEGVADLIDAETEAQRRQALGQLGGALSQRYEAWRGLLVQALAMLEAAVDFPDEELPEDVAARARPGLEALEAEIGAALVDASRGRRVRDGYRIALVGAPNAGKSTLLNALVERDAAIVTSTPGTTRDIIEVPLTLGGYKTLLADTAGLRKTEDTIEAEGVRRARAWAAGADLRLWVIDAAMFHVKQDDELAVIQRGDW... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 47622
Sequence Length: 447
Subcellular Locatio... |
P0CAX2 | MTDTIFALATAAGRSAVAVVRVSGPRSSEIAAALCGRLPSPRLASVRTLKHNGVALDAALVLRFEKPASYTGEDSVEFHVHGGRAVVEALLAALSELGARLAEAGEFTRRAFENGKLDLAQAEGVADLIDAETEAQRRQALGQVGGALSQRYDRWRDLLVQALAMLEAAVDFPDEDLPEEVAERARPGLRQLSAELNAALADVSRGRRVRDGFRIALIGAPNAGKSTLLNGLAERDAAIVTDVAGTTRDVIEVPLVLGGYKVLVADTAGIRETADVIEAEGVRRAKAWAEAADLRLWVVDGFHVKQADARPEAIRVGDWL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 47394
Sequence Length: 446
Subcellular Locatio... |
Q4AAC5 | MLSDTICAIASGQINQAISIIRISGPNAFKIMEKIFLGKVGRSMEITFGWIHDDNQKIDQVLVLWFAGNKNFVGEDTVEINAHGGVLNTNLILELILKTKLARLANPGEFSLRAFLNGKIDLVKAQAINDLIHAEVKVQHQAALNQFLGKSSNFIKNLIEKIEEIIGIIEVNIDYPEYDDVEILTSDVLLPRINQLLADFDQLIKIANNSRLIYQGIKTCLVGAPNSGKSSLLNILINENKAIISEIPGTTRDVVEGNFVLDGLLFKLFDTAGIRKTTEKIEQIGIEKSYESIKKADLILHIIDASEKNRQNLDLKAKTR... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 49516
Sequence Length: 442
Subcellular Locatio... |
A2SMI8 | MLLPRHHDPIVAIATAPGRGAVGIVRVSGRGLGALIEAVCGRALQPRHAHYGPFLDAQGEAIDQGLALHFPAPHSYTGEEVLELQAHGGPVLLQLLLARCLEAAAQPDARSGLPRLRGLRVAEPGEFTERAFLNDKLDLAQAEAVADLIDASTEAAARSAGRALAGAFSQQVDTLRDRLIELRMLVEATLDFPEEEIDFLEKADARGRLARIAEALDAVLARAKQGALLREGLRVVLAGQPNVGKSSLLNALAGAELAIVTPIAGTTRDKVAETIQIEGVPLHVVDTAGLRAEDDARDEVERIGMQRSWGAIGEADAVIF... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50101
Sequence Length: 471
Subcellular Locatio... |
B1M0E0 | MNETDTLFAPASGFGRAAVAVIRISGPAAGGVLATLGGRLPTPRRLSLRSLRDPRDGTELDRALVAWFPGPDTYSGEDMAELHLHGGAAVRMRVLATLARLPGCRAAEPGAFTRRAVLNGRMDLAEAEAVADLIDAETEGQRRQALRQLDGALSRQVAAWRAEAIDCLAAAEAALDFADEGDVDDAGLDAALFDRAARLRDAVAATLRDGHRGERLREGFTVVLAGAPNSGKSTLLNALSRRDVAIVSDSPGTTRDAIEVRLDLGGLPVLLVDTAGLRETAEPIEAQGIVRTRARIDTADLVVALVPPGGAVPDLGPGCR... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 45736
Sequence Length: 441
Subcellular Locatio... |
Q7NAD9 | MINKIMKKYETIYALATAPYNSAIHVIRLSGPDAFEIINKICDKQITKEGYRIQNARIVDNDQIIDDVLLMKFVAPKSFTGEDSIEINCHGGLFVINKIMALLNKHGAHLARRGEFSKRSYINKKIDLNQATAIHDLIFAKNNLSHSASIKALSGEFSKDIKNIQQEIFRLIGLVEIAIDYPEYEDEKKELTEEFKNLTNIRQKLQRIVNKSLKLKQISEGIKIAIVGEPNAGKSSLLNALLNEQKAIVTNIPGTTRDTVEGQIVLNDELIINLIDTAGIRKSSDQIEQIGINKSFKTIDKSDLVIYLIDLNKYQNYDKT... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 51666
Sequence Length: 453
Subcellular Locatio... |
P47254 | MKSEINIFALATAPFNSALHIIRFSGPDVYEILNKITNKKITRKGMQIQRTWIVDENNKRIDDVLLFKFVSPNSYTGEDLIEISCHGNMLIVNEICALLLKKGGVYAKPGEFTQRSFLNGKMSLQQASAVNKLILSPNLLVKDIVLNNLAGEMDQQLEQIAQQVNQLVMQMEVNIDYPEYLDEQVELSTLNNKVKLIIEKLKRIIENSKQLKKLHDPFKIAIIGETNVGKSSLLNALLNQDKAIVSNIKGSTRDVVEGDFNLNGYLIKILDTAGIRKHKSGLEKAGIKKSFESIKQANLVIYLLDATHPKKDLELISFFK... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50806
Sequence Length: 442
Subcellular Locatio... |
Q98RJ5 | MFDNIVAISSGAKVNQAISIIRLSGPDVFEIMKKIFTGKVGKDKSITYGYIKNDQEIIDEVLVMWFKGPNNFVGEDTVEINAHGGIVVSTLILETIVANGARLAEPGEFSKRAFLNGKLDLVKAEAINDLIHSKTVQQAKINIKKFDRKTSMFINDLINKLVFIIGTCEVNIDYPEYDDIEELTLEVLLPKLKDLEKEISKAVELSERSRIYFNEIPIAIVGRPNVGKSSLLNALLEEDKSIVTNIEGTTRDVVEARFVLNGINFLLKDTAGIRHSENVIEKIGIEKSFKQIQDSEIIIHLVLENQDEDDFERKIKELSE... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 49933
Sequence Length: 442
Subcellular Locatio... |
Q4A647 | MNYQSYSDTICAISSGNNINQPISIIRISGKNAQSIVSKIFSGKVGENKTITYGFIKENSEIVDEVLVSWFLGEPQGDITVYNNYVGEPLIEINAHGGMIVTNKILELLISNGARLAEPGEFTRRAFLNGKLDLSKADAIHNLIMSKTRLQARNEASKLKGSASKVIKDLLKELSLLIGSIEVGIDYPEYIDDYEEDLKANSKEDINLTRINKLIARLEKIVKSSETALNYFEGIKLAIVGKPNVGKSSLLNTMLKEDKAIVTNVAGTTRDIVEGIYYLDNFIFKIIDTAGIRKTRQEIEKIGIERSYKAILDADIVLHL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 52215
Sequence Length: 463
Subcellular Locatio... |
Q1CVG4 | MTSSSMTIAALATAPAAGAVGILRLSGPEALDVGRLLAPGVPAQPTPRHAYLASFVDAEGRSLDEGLFLYFRGPQSFTGEDVVELQAHGSPRLLRLLLTRALEDARVRHAAPGEFTRRAFLNGRLDLTRAEAVADLVAADSEAAVRAAAAGLSGALASRVQALEEPLRALHADMEGVLSFPDEAEGADEDVGERVTALRAQAETLLAEVGRGRLVRRGARVALFGPVNAGKSTLFNRLVGEARALVDDEPGTTRDALEARVEWDGLAVTLFDTAGLRETPGRVEALGIARTRALLTGVDLAVLVLPPGVTQAEVEAWTRD... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 46134
Sequence Length: 442
Subcellular Locatio... |
Q67J33 | MGEETIAAIATGAGEGGIGIVRISGADALQVAERIFRPRRGRPLGCRRSHTVTYGWVVTPGGDRIDEALALVMRGPHSYTGEDVVELQCHGGQLAVRRVLEQALQAGARLAEPGEFTRRAFLNGRLDLSQAEAVVDLIRAKTDRAMAAAVAHLRGSLRQAIGRIRERLMEMMAHLEADIDFPELELEVQTREEVAAGCAWCLGEVERLLGGARTGRILREGLRAVLAGRPNVGKSSLLNRLVRENRAIVTPIPGTTRDVIAEWVELGGVPVQLFDTAGLRPTDDPVERIGVARTHEALAQAHLVLVVVDAAAGLGPEDRE... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 48885
Sequence Length: 457
Subcellular Locatio... |
Q8Y652 | MLFLEGLMQYSFLQKALITSVTVGIVSGVIGSFIILRGMSLMGDAISHAVLPGVAISYMMGMNFFIGAATFGIAAALGIGFVNQKSRIKNDTAIGIVFSAFFALGIILISFAKSSTDLYHILFGNVLAVRSSDMWMTIIIAIIVISLVALFYKEFLVSSFDPVMAEAYGLNVKFLHYFLMLLLTLVTVSALQTVGIILVVAMLITPAATAYLLTNKLSKMIVLASTFGAVSAIIGLYFSYIFNLASGAAMVLVATIIFFIAFLFAPKQGLLFSKKREVIE | Function: This protein is probably a component of a manganese permease, a binding protein-dependent, ATP-driven transport system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30174
Sequence Length: 280
Subcellular Location: Cell membrane
|
O34500 | MSFEAWIIATGVLVGVSCGLIGTFLVLRSMAMLADAISHTVLLGIVGAFLVTGSLDGIYMFIGAAATGLLTAFLVQLLHSKGVQSDAAIGVVFTSLFAIGVILLSVYGANVHLDIEHSLMGEIAFVPWNTVTVFGVDIGPKAFWMLASVLVLNVVLISVCYKEFKIASFDPQMALALGIPVLLIHYVQMGMLSLTTVASFDSVGAVLVVAMLIVPPAAAHLLTDRLLYMLILSALIGGLSAVMGYFFATWLNVSISGAMAAMTGVCYASAFLFSPANGVITKKLRTLNMQKERAG | Function: Probably part of the ABC transporter complex MntABCD involved in manganese import. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31058
Sequence Length: 295
Subcellular Location: Cell membrane
|
Q9RPF3 | MKYSLPTTATAPFCPSAVSHSVAVPADASPLRKLALFVGPGLLVSVGYMDPGNWATAIEAGSRFGYALLFVVVLASFSGMLLQSLCSRLGIATGRDLAQLSRERYRPGVARGQWLLAELSIVATDLAEVLGAALAFHLLLGVSITTGVVLTAFDTLIVLALQGANFRRLEAIVLGLIATIGACFFVELVLIGPYWPDVAAGLRPSWDTLSSQEPLYLAIGILGATVMPHNLYLHSSVVQTRVSGDDAASKRSAIRFSRLDTIGSLSLALLVNAAILILAAAAFHGSGHTEVVEIQDAYHLLDPLVGGALASFLFGFALLA... | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46603
Sequence Length: 439
Subcellular Location: Cell inner membrane
|
Q9RPF2 | MSAKDTPAPQAAEPGRAQPVEVPGGGHWWRRLLAFAGPGYLVAVGYMDPGNWATDVAGGAQLGYLLLSVILLSSLMAMLLQALSARLGIASGLDLAQACRERYSPSTCRLLWLACETAIIACDLAEVIGTAIALKLLFGLPLAWGALLCVGDALLVLVLIGRGQRPLEAFVVALLTLIFACFAVQLLLSRPELGEVLQGFLPSPRVLSDPAALYLAIGIVGATVMPHNLYLHSSLVQSRAYPRSLAGKRKALRWAVADSSLALTLALLVNAAILIVAASVFHRNGHTEVVDIEQAHALLSPLLGLELASLLFAVALLASG... | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46380
Sequence Length: 438
Subcellular Location: Cell inner membrane
|
A0KG66 | MQPALTTAIPARKFKLTLLGPAFIAAIGYIDPGNFATNIQAGSTFGYQLLWVVVWANLMAMLVQTLSAKLGIVTGKNLAEHIRDRLPKPAVWAYWVQAEIIAMATDLAEFIGAAVGFKLLLGVTLLEGAGITAVVTWGILMLQSRGQKPLEFVVGGLLLFVAAAYIVELVFSRPHLPSLLEGALFPGLPNSDAVYLAAGVLGATVMPHVIYLHSALTQHTQDQGSVPQRLHTTRVDVAIAMTIAGFVNLAMMAMAAAAFHSSGNQQVAELESAYQTLTPLLGQAAATLFGLSLVASGISSTVVGTLAGQVVMQGFVRFTI... | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43101
Sequence Length: 407
Subcellular Location: Cell inner membrane
|
Q8UEM1 | MFFMRMICNCINSISMKAQKMDKPVFGWRRNGDDLSLSDVHSSIRIKPDASTFRRAMAFFGPGYLVAVGYMDPGNWATSLAGGSKFGYTLLAVALVSNIMAIVLQSLCARLAIASGRDLAQACRDAYPKPVAMVLWLLAEIAIIATDIAEVIGTAIGLNLIFGIPLELGVLITALDVFLILYLQKLGFRWVEALVITLLGVIAVCFAIQLALADPDWGQVILGFAPTTEIVTNPDMLYLALGILGATVMPHNLYLHSGIVQTREIGPTIAEKREALKFATLDSTIALMFALLINASILILAAATFNKTGQTNVAELGEAH... | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49460
Sequence Length: 461
Subcellular Location: Cell inner membrane
|
P96593 | MMNKDITAQSPRSKAVQDALDGKIRGFRGLLPFLGPAFIAAIAYIDPGNFATNISAGSKYGYMLLWVILFSNIMALLIQSLSAKLGIATGKNLPEVAREEFPKPVSIGLWIQGELVIIATDLAEFIGAALGLYLLFGIPMLEASIIAAIGSFAILELQRRGYRSLEAGIAGMLFVVVIAFALQTFFAKPDAVSVMKGLFVPAFHGTDSVLLAAGILGATVMPHAIYLHSALTQRRVVGKTDAERKKIFRFEFIDILIAMLIAGAINASMLIVAAALFFKNGLFVEDLDVAFQQFGHLVSPMSAALFGIGLLVAGLSSSSV... | Function: H(+)-stimulated, divalent metal cation uptake system. Involved in manganese uptake. Can probably also transport cadmium, cobalt, copper and zinc, but not iron. May be the predominant transporter of manganese during logarithmic phase growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45... |
Q0B8F7 | MIPVTSKSSSGFALPDLSTDRAHRAVPAEGAARAALEGRRTGIAALLPFVGPAVIASIGYMDPGNFATNIQAGAAYGYRLLWVVLAANAIAMLFQAMSAKLGIVTGRNLAELCREHFPAPIVWGMWIASEIAAMATDLAEFLGGALAFALLCHLPLFAGMIATALATCAILALEKRGFRPLEAAIAALVGVIGACYLGELMIAPQDWHAAAFHLVVPQIPDRAALTIAVGIIGATIMPHTLYLHSGLTQDRIAPRDDTERRRLMRFSNREVVVALGLAGFVNLAMVMMAASAFHASAPGMADIGDAYHTLIPVLGPAAGV... | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46420
Sequence Length: 441
Subcellular Location: Cell inner membrane
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Q8R7S2 | METREIASQRRKNLYLGIELKKFLKYLGPAFIVSVAYVDPGNFATNISGGSLFDYHLIWVILWSNVIAIFLQIQSAKLGIATGYNLPEMCSIIFPRKWNWFLWITAELAAMATDLAEFLGGTMGLYLLFHIPMTYAAFLTGVVTFAIVYMEKYGQKVVEGIIFGLVAVISLAYAFELFIARPDWSKVLYHTFIPSIPNKDAMLIAVGILGATVMPHVIYLHSQLVQYRNKDGSLQAKKEHLKMEKIDILVAMNTAFIINAAMLIVSAAVFYKNGIVIESIEEAHKTLEPLLGVFSSWAFGIALLASGFSSSAVGTMAGQT... | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46518
Sequence Length: 421
Subcellular Location: Cell membrane
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Q9RTP8 | MDSRSPSLPDDRPDPPEQHLDARAGATLRGTAGPRGVRRILPFLGPAVIASIAYMDPGNFATNIEGGARYGYSLLWVILAANLMAMVIQNLSANLGIASGRNLPELIRERWPRPLVWFYWIQAELVAMATDLAEFLGAALAIQLLTGLPMFWGAVVTGVVTFWLLNLQKRGTRPLELAVGAFVLMIGVAYLVQVVLARPDLAAVGAGFVPRLQGPGSAYLAVGIIGATVMPHVIYLHSALTQGRIQTDTTEEKRRLVRLNRVDVIAAMGLAGLINMSMLAVAAATFHGKNVENAGDLTTAYQTLTPLLGPAASVLFAVAL... | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46652
Sequence Length: 436
Subcellular Location: Cell membrane
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A7H1P4 | MDFYSLIFLSCALGMDAFAVSLCKSFSVKKLHLKHYLIVGIYFGGFQALMPTIGYFIGITFASFIASIDHWIAFILLSLIGLKMIKESLENENCNSNAKQFGFKTMLALAIATSIDALAVGVSFAFLNVNLLLAIFLIGIITFILCIIALKIGNKFGIYLKNKAELLGGLVLIILGVKILIEHLFFD | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20558
Sequence Length: 187
Subcellular Location: Cell inner membrane
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Q3A931 | MSLWEIFLLAVALGTDSFSLCVGLGMGKIKRKEIIALSLTVLVYHIVMPILGWFAGDLTGRFLGKVATYIGGAILIYLGYKMIRHGISQEEELPHVTYNLVGLLLIGLSVSMDALSVGFTLGTVKVNLWFVALITGIVAGVMTLSGLLLGRRVSKVLGERAQIVGGLILLLIAGKLIFRG | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19299
Sequence Length: 180
Subcellular Location: Cell membrane
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Q1R175 | MNPASLILLAFAMSTDAFAASIGRGAELRKVRLLSALRIGAVFGVVEAIMPLLGWALGHVAMRFVSGVDHWIAFVMLALLGGHMIWAGVKKEDCAAIKAAETQPENRSIWLIAFTALATSIDAMAVGITLALTDINIIAASVAIGLATALMVTLGTLLGRAIGTIVGKWAEILGGLILIGIGIAVLYEHLAGLASA | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20269
Sequence Length: 196
Subcellular Location: Cell inner membrane
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Q898D6 | MDFYSLFLIAIALSLDAFGVALCIGLNNNVDLKYKSSCAIYFGFFQFLFAIIGGYAGFLFNKYIATMPQIVGGVVICIVGIIMIKEGIENEDSCKILKPGMNIILGISVSIDAMVVGFTALNKIQSGLLILRDTLFIGIVTLFVSILAFITSKYLKKIDVIGKYADYIGGIILIFFGLKMIFF | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20052
Sequence Length: 183
Subcellular Location: Cell membrane
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Q47ZC7 | MIEVIILAIALSMDAFAVSIGLGATKQQSKVAPLGIIVALYFGLFQGIMPIIGYLGGKGVLSWAESYTPWIAFLLLFLIGVKMIFDSFSEGIEEDISKITHRVLLILAIATSIDAMAAGFSLTLLPVNPLIACLIIASVTFIFSWLGVLVGTKGGTWLENKAEFVGGITLIVMAIKIIITS | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19278
Sequence Length: 181
Subcellular Location: Cell inner membrane
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Q8NQG6 | MPFLQISLLSIGVAADAFACSVVRGTAIQVNLFKRALVLAGIFGVFQAAMPLIGWFIGRFFAGITFIAEIDHWIAFALLGIVGTKMIWDAFQPEDDETIVDDGRVQFRPAIILGLATSIDALAVGMGLAFVEVSILKVALSMGSITFALSLAGAWIGHHGGGKFGKWATILGGIILIGIGANIVYEHLSA | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20062
Sequence Length: 190
Subcellular Location: Cell membrane
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Q171H3 | MNYLKLTFDKLEVGEINDLVAHESCGAISLFVGTTRDNFDGKTVVLLEYEAYEAMALKTMNQICEELRARWPDIKHIGIHHRLGTVPVKEASVVIAVSSPHRKSSLEAVHFAIDELKKSVPVWKKEQYADGEGCSEWKENKECSWSKSHRDNHIL | Function: Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group.
Catalytic Activity: 2 [molybdopterin-synthase ... |
Q8TD46 | MLCPWRTANLGLLLILTIFLVAEAEGAAQPNNSLMLQTSKENHALASSSLCMDEKQITQNYSKVLAEVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSCTKAYKKETNETKETNCTDERITWVSRPDQNSDLQIRTVAITHDGYYRCIMVTPDGNFHRGYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAAHISWIPEGDCATKQEYWSNGTVTVKSTCHWEVHNVSTVTCHVSHLTGNKSLYIELLPVPGAKKSAKLYIPYIILTIIILTIVGFIWLLKVNGCRKYKLNKTESTPVVEEDEMQPYASYTEK... | Function: Inhibitory receptor for the CD200/OX2 cell surface glycoprotein. Limits inflammation by inhibiting the expression of pro-inflammatory molecules including TNF-alpha, interferons, and inducible nitric oxide synthase (iNOS) in response to selected stimuli. Also binds to HHV-8 K14 viral CD200 homolog with identic... |
Q9ES58 | MLCFWRTSHVAVLLIWGVFAAESSCPDKNQTMQNNSSTMTEVNTTVFVQMGKKALLCCPSISLTKVILITWTITLRGQPSCIISYKADTRETHESNCSDRSITWASTPDLAPDLQISAVALQHEGRYSCDIAVPDGNFQNIYDLQVLVPPEVTHFPGENRTAVCEAIAGKPAAQISWTPDGDCVAKNESHSNGTVTVRSTCHWEQSHVSVVFCVVSHLTTGNQSLSIELGRGGDQLLGSYIQYIIPSIIILIIIGCICLLKISGCRKCKLPKSGATPDIEEDEMQPYASYTEKSNPLYDTVTTTEAHPASQGKVNGTDCL... | Function: Inhibitory receptor for the CD200/OX2 cell surface glycoprotein. Limits inflammation by inhibiting the expression of pro-inflammatory molecules including TNF-alpha, interferons, and inducible nitric oxide synthase (iNOS) in response to selected stimuli (By similarity).
PTM: Phosphorylated on tyrosine residues... |
Q6Q8B3 | MSAPRLLISIIIMVSASSSSCMGGKQMTQNYSTIFAEGNISQPVLMDINAVLCCPPIALRNLIIITWEIILRGQPSCTKAYKKETNETKETNCTVERITWVSRPDQNSDLQIRPVDTTHDGYYRGIVVTPDGNFHRGYHLQVLVTPEVNLFQSRNITAVCKAVTGKPAAQISWIPEGSILATKQEYWGNGTVTVKSTCPWEGHKSTVTCHVSHLTGNKSLSVKLNSGLRTSGSPALSLLIILYVKLSLFVVILVTTGFVFFQRINHVRKVL | Function: May be a receptor for the CD200/OX2 cell surface glycoprotein.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 29920
Sequence Length: 271
Subcellular Location: Membrane
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Q8ZYE5 | MLFDKYGRSLQKLRYVVNDECNYNCVFCHFEGQSRRQGRYLTAEDYGFVTSVFKSLGVADFKITGGEPLLRGDIDLIVANIAKTGAYVTLTTNGYLLRKWVRKLQAAGLKRANVSIHTTDPEKYSKITGVPPSAFREVLRGLTEARDVGISLKLNAVVLRGINTDRDSVKNLVKLAASLGAALQFIELMPSGWGASVFNELYEPIETLVNIIFELGGRPAGVRKELHNRPLYNIAGVTVELIKNFSNPTFCSGCTTMRLTSDGKLKTCIYADSSVDLMPYIKSRDVEGLLYAVRTALARREPRFKLYSSS | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Ca... |
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