ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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A3LZM4 | MKNLFYSFVSGSEYLVLVALDTEGCVYYASAGELNSQASMVELMEKDFLKAPEFRVNSLNSASSSLVNKKSEVKIKDTLEKFKSLIDFENKDEKIPYKVVFGTPLQRKVWDYLVNELPVGSISTYQKIAQHLGMPNSSRAIGNCVGANRIAVVIPCHRVIGSSGKITGYRYGTNIKKTILQNELGSKYGSTITN | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
P24528 | MAEICKMKYTVLDSPLGKIELSGCERGLHGIRFLSGKTPNTDPTEAPACPEVLGGPEGVPEPLVQCTAWLEAYFHEPAATEGLPLPALHHPVFQQDSFTRQVLWKLLKVVKFGEMVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCHRVIRSDGAIGNYSGGGQTVKEWLLAHEGIPTGQPASKGLGLIGSWLKPSFESSSPKPSG | Cofactor: Binds 1 zinc ion.
Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide rea... |
B3R3G1 | MPPKPRIALIAHDHKKDDIVAFAARHRAFLSQCELLATGTTGGRLIDEVGLDVTRMLSGPWGGDLQIGAQLAEGRVSAVVFLRDPMTPQPHEPDINALVRACDVHNVPCATNVASAELLLAGLARENGAAQAG | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 14035
Sequence Length: 133
EC: 4.2.3.3
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A5A616 | MLGNMNVFMAVLGIILFSGFLAAYFSHKWDD | Function: Modulates intracellular Mg(2+) levels to maintain cellular integrity upon Mg(2+) limitation. Acts by binding and stabilizing the Mg(2+) transporter MgtA, thereby leading to increased intracellular level of Mg(2+). May inhibit FtsH proteolysis of MgtA.
Location Topology: Single-pass membrane protein
Sequence M... |
Q49YR9 | MKRSDRYKTYNKPNDSNDSNQLHHNTYFKPVNKPQKKKKGKGIILKLLIPILIIIGIIIGVMYALSLRADTDELKNITEKESFVYASDMRDYTKGAFIAMEDERFYKHHGFDVKGTSRALFSTLSDKSVQGGSTITQQVVKNYYYDNEQSITRKIKELFVAHRVEKEYDKNEILSFYMNNIYYGSDQYTIESAANHYFGVTTDKNNPNLPQISVLQSAILASKINAPSVYNINDMSDNFTNRVKTDLEKMKQQGYISNSQYENAIQELGV | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation using lipid-linked disaccharide-pentapeptide as the substrate.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L... |
Q04613 | MRLSSTNMDARKMLFAAILSICALSSKKILIYNEEMIVALCFIGFIIFSRKSLGTTFKVTLDGRIQAIQEELQQFPNPNEVVLLESNEQQRLLRISLRICGTVVESLPMARCAPKCEKTVQALLCRNLNVKLATLTNAISSRRIRFQDDLVTKFYTLVGKQFAYSCISKAERVEFIRESLVVLRMVRGGGFS | Function: This is one of the chains of the nonenzymatic component (CF(0) subunit) of the mitochondrial ATPase complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21708
Sequence Length: 192
Subcellular Location: Mitochondrion membrane
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P09004 | MRFSGMDMKGINMLFAAIPSICASSPKKISIYNEEMIVARCFIGFLILSWKSLGKTFKETLDGRIESIQESLQQFFNPNEVILEESNEQQRLLNLWISLRICSTVKVVESLPAARCAPKCEKTVQALLCRNLNVKSATLLNATSSRRIRLQDDIVTGFHFSVSERLVSGSTTLVEASTVEQIREAFLLEPRDLIREGFIVLRKVRVGGIPGTCGDGVGL | Function: This is one of the chains of the nonenzymatic component (CF(0) subunit) of the mitochondrial ATPase complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24371
Sequence Length: 219
Subcellular Location: Mitochondrion membrane
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P38477 | MREILIFAILSFSVLSSKKILIYNEEVIVALSFVCFVIFSQKTFGETIKAIFDARSEALLSDLQQWMSYQEAMLSELKKQHELRSISLRSSTQMIGESCINDMVTRCAPKCKQTVKSVLCQQIEQKLKTLLAIQEHSRISLQEKIVTCFRETVCDEFRFSKLRKHQSKLVQQSMVLLKDGVPK | Function: This is one of the chains of the nonenzymatic component (CF(0) subunit) of the mitochondrial ATPase complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21088
Sequence Length: 183
Subcellular Location: Mitochondrion membrane
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P09003 | MRLSSTNMQARKMLFAAILSICASSSKKISIYNEEMIVALCFIGFIIFSWKSLGKTFKVTLDGRIQAIQEESQQFPNPNEVVPPESNEQQRLLRISLRICGTVVESLPMARCAPKCEKTVQALLCRNLNVKSATLPNATSSRRIRLQDDIAIKMHVLVGKRFCPWCSSKAERVEFIRESLVVLRMVWVGDSLKNKELE | Function: This is one of the chains of the nonenzymatic component (CF(0) subunit) of the mitochondrial ATPase complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22436
Sequence Length: 198
Subcellular Location: Mitochondrion membrane
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P68538 | MRFLSTDMKDRNMLFAAIPSICASSPKKISIYNEEMIVARCFIGFLIFSRKSLGKTFKETLDGRIESIQEELLQFFNPNEVIPEESNEQQRLLRISLRICSTVVESLPTARCAPKCEKTVQALLCRNLNVKSATLLNATSSRRIRLQDDIVTGFHFSVSERFVSGSTFKASTIDLIREGLIVLRKVRVGGSI | Function: This is one of the chains of the nonenzymatic component (CF(0) subunit) of the mitochondrial ATPase complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21653
Sequence Length: 192
Subcellular Location: Mitochondrion membrane
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O68965 | MTVRFGLLGAGRIGKVHAKAVSGNADARLVAVADAFPAAAEAIAGAYGCEVRTIDAIEAAADIDAVVICTPTDTHADLIERFARAGKAIFCEKPIDLDAERVRACLKVVSDTKAKLMVGFNRRFDPHFMAVRKAIDDGRIGEVEMVTITSRDPSAPPVDYIKRSGGIFRDMTIHDFDMARFLLGEEPVSVTATAAVLIDKAIGDAGDYDSVSVILQTASGKQAIISNSRRATYGYDQRIEVHGSKGAVAAENQRPVSIEIATGDGYTRPPLHDFFMTRYTEAYANEIESFIAAIEKGAEIAPSGNDGLAALALADAAVRS... | Function: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 35147
Sequence Length: 330
Pathway: Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol:... |
P81860 | AGPQLDVSCFAHDKNIGSRTEQLSVVHVASAQDCMKECQALPTCSHFTYNKNSKKCHLKAGAPEFYTYTGDMTGPRSCEHNCSDACWMDGNNPLAVWDYSGQPPALCWAACMGTPGCDLYTFQGMTCKLYSQTSSKRA | Function: Galactose-binding lectin. Plays a role in adhesion to the host cell. Has a potential role in invasion of host cells.
PTM: Contains six disulfide bonds.
Sequence Mass (Da): 15078
Sequence Length: 138
Subcellular Location: Cytoplasmic vesicle
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Q8KDS2 | MNTKPVLVILGPTASGKTELAFRIARQTGGEIISADSRQIYRGMDIGTAKPPRWMLDEVKHHFIDKKEIGEPFSAGDFAEQAAEKIRELHQRGITPVVAGGSTLYLEGLLKGFAELPPADPEIRAQLTRELERHGAEALYRRLEALDPEQAKTLDPTKTQRLIRSLEIIEISGTTVTALQSKTPGPPTGINFTVIGLDLPRELLYERINQRTSAMIQAGLEAEARYLFDKFRDEWRSKNLNALATVGYRELFEHFEELHDLDTAVSLIAQHTRNYAKRQLTFFRNRLDVEWVKAPLDEAEIEALVEFFSTRQDDSVPHSP... | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
O84771 | MFKRTVILLAGPTGSGKTAVSLKLAPLVDGEIISVDSMQVYQGMDIGTAKVSLTDRKEVPHHLIDVCHVQESFNAVDFYYHAVQACQDILSRNKVPILVGGTGFYFHTFLSGPPSGPSPDFVLREQLTLEAQERGISALYQELELLDPVYAATITKHDKNKIIRALEIIRKTGSKVSSYAWQSTVNESKEYHCRRWLLSPDPELLRHNILERCDQMLEEGLLDEVQALLAAGIKGNSSASRAIGYREWIEFLDLGSPPDLFEITKQKFITNTWRYTKKQRTWFKRYSLFRELRPMGMTLDDMAKKIAQDYFLCG | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
A0LZ43 | MSNYLINIIGPTAIGKTSLSIKVARHFITEIISADSRQFFKEMKIGTAVPDKDELAAATHHFIQHISIADAYSVGDFEKDAILKLKELFNKHKVAVMVGGSGLYIKAITEGLDDFPKVDPEIRRNLNQHLEEDGIDWLQKKLYVLDPEYYKTADVMNPHRLIRALEICIETGKPFSSFLNQKKPERNFKNITIGLMADREMIYDRINKRVDLMIRNGLIEEARELYPQKELNALNTVGYKELFSFFDGKTDLETAISEIKKNTRRFAKRQLTWFRKDPEIKWFEFDENSKNIFDYIESKINT | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q1QY27 | MSDTRPLALLLMGPTAAGKTDLAIALRERLGGELISVDSAMIYRGMDIGTAKPSAQELARAPHRLIDIRDPAETYSAAEFRDDALAEMRDISSQGRTPILVGGTMMYIKRLIDGVASLPARDPALREALNARAESEGLVALHRELSRVDPVAAETIHPHNRQRLLRALEVYQLTGRALGELWAEQARETFPWRLVSIALAPNARHVLHARIAERFDSMLAAGFRDEVAALQARGDLHRGLPAIRCVGYRQMWEHLRGETDAATMRERGLAATRQLAKRQLTWLRGWEGVHWIDSDASDAHEQVLKIVRGSST | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
A5CSL4 | MIPIVAVVGATGTGKSGLSLDIADRLRAQGRVAEIVNADAMQLYRGMDIGTAKLPEAARRDVPHHMLDVLDVTAEATVAGYQGEARRVITGILGRGAVPILVGGSGLYVSSVLFDYEFPGTDPEIRQRLERELAETGPGMLHRRLRELDPAAAQRIGAHNGRRLVRALEVVEITGPQPERASAEPRPWHPARILALTLPREELVPRLDARVSGMWADGLVDEVAGLLPAGLADGVTASRAIGYAQAARQLAGELTEEEAMEETRALTRRYARRQVSWFGRYADAVRLDARDERLLEHALDALPAARP | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q97I21 | MKDILIIAGPTAVGKTDISIKIAQKMNGEIISADSMQIYKYMDIGSAKVTKEEMKGIKHHLIDVVDPSEEFSVASFKKMAQNAIDDITSRKKYPIIVGGTGLYINSLICNYDFTGAYKDEAYRESLQAIAKDKGKEYLHEKLKNIDIDSYKKLYPNDLKRVIRALEVYKITGKTISELNSNVDLYDIPYNIHYFILNMDRQKLYERINLRVDIMLRNGLVDEVIKLRDMGYNSNMQSMKGIGYKEILSYLEGCITLEEAVELIKKGSRHYAKRQLTWFRKDERAVWINKDIYKNDDDIVFKILSSIEEI | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
B2TIB7 | MKQKILVLGGPTAVGKTELSIKLAEKLNGEILSADSMQIYKKMDIGSAKVTKEEMRDINHHMIDIVSPEEEFSVADFKNIGEKAIKEIIAKEKLPMIVGGTGLYINSLTCNVTFTESEKDDEYRTYLESLAEANGNNYVHEMLREIDEISYRDIHPNNRKRVIRALEVYKISGKPFSSYNAGNDFYKTDYHVFYYVLTMDREKLYDRINKRVDIMIENGLIDECIELKKLGYTSSMQSMQGIGYKEILYYLDKKISLYEAVNLIKQGSRNYAKRQLTWFRRDPRCTFLDKDVLSDKEILSKIVDDITNN | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
B2T068 | MTSRMPTVVPCLLGPTASGKTAAALALAARRPVEIISVDSALVYREMDIGTAKPTAEERAVAPHHLIDIVDPTDAYSAAQFRADTLRLTAEIHARGRLPLLVGGTMLYYKALTQGLNDLPAADAEVRATLDADAAREGWPALHARLAALDPVTAARLAPNDSQRIQRALEVFMLTGQTMSALLAAPVMQDDSAALWRFVPIALEPSERSVLHARIEKRFDAMLAGGFIDEVVKLRERGDLLPEMASMRCVGYRQVWEYLDGAVDYSTMRDKGVFATRQLCKRQLTWLRSMPERVVVDCCDPHATARVLEAIEALL | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q6MBT2 | MIGNFSCETDEIKRIVLNFALQVQKKFPSNFQKNKKRIIVIAGPTCCGKSALALNLAQTMDGEIISADSMQVYRGMDIGTAKATKEERLFVPHHLIDIRDIQESFNVVDFYYEARQACQKILDQGNVPIIAGGSGFYLHALLYGPPSGPPSVPEVRKSFEDEIERLGSEILYERLSQLDPQYAKTITKNDKQKIVRALEIMMLTNKKVSKLSWKGRRKPQNYDFRCWFLHRPKEKLYERIDKRCDKMLEEGFMDEVRHLDSLGIRGNSSASQAIGYRQALNFLKTEQTASQYQEFIRSFKQATRHYAKRQFTWFRKEPLF... | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q9CMC7 | MPLTTPTAIFLMGPTASGKTDLAIQLRQTLPVEVISVDSALIYRGMDIGTAKPSAEELALAPHRLIDICDPAESYSAANFRQDALREMADIIAAGKIPLLVGGTMLYYKALLEGLSPLPSADEKVRSEIEEKAQLQGWAALHQELAKIDPLAAQRINPNDSQRINRALEVFYLTGKSLSELSQQKGDSLPYQILQFAIAPKDRSILHDRIALRFQKMIEQGFQQEVEKLYQREDLHLDLPAMRCVGYRQMWEYLRGDYDHDEMIFRGICATRQLAKRQITWLRGWKYPIEWLDSLAIESAKQTIIHAVTKISHSNS | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
B4SGR0 | MATAEKKQPSVIVILGPTASGKSALALAVAKKIGGEIISADSRQIYREFDIGAAKPSESALGEIRHHFVNEKNIGEPFTAGDFATEAAERIITLHRRGKRAVVAGGSTLYLEGLIEGFADLPPANPEIRARLLGELEEEGNEKLYAKLFERDPDQAATLDPTKSQRLIRSLEIIEITGLSVTELQARAKKRQHGDLCFVTTGLAMERATLYQRINHRTDNMIDAGLYDEAKGLYHKYHKLIASGKVSSLQSVGYQEFFQYLDGMISFDDAVRLIKQHTRNYAKRQLTFFHNRLSVNWTDAPLNSKELDSLAERLSKGP | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q4FPN1 | MDKQSKIILISGPTASGKSNFAVKIAKKIEGEIINADSMQVYKKLKILTARPNKQEQKNIKHHLYGFVDLNEKFSTGQWLELTIKKIENIQKKKKIPILVGGTGLYFQSLINGLVKIPEIPLKFRNKVRLMSKKEGQKKFYKKLLKLDPKIKDKFDPNDTQRSIRAYEIKSYTNISMYDWLAKTKSEFNDSDFLKLHIDTKREKLVEKINLRTSSMLNNGAISEVKKFLKLKIKKDQSVNKVIGIAELTQYLNDEITLDEAEELISIKTRQYAKRQATWARTRMTSWIKVDPIKLDGYIKKLKKSSLKLDQLT | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
A9BHW9 | MNKVLVIAGPTAVGKTEISIEIARRINGEIICMDSRQIYSHLIIGTATPDEETKKLVPHHLYGSVDPRTHFTAFDYKKLAEKKIGEVLNRGNTPVLVGGTGLYLDALRKGFLNVKSDYGLRTYLRKLETNNPGVLRKILVDLDPQRAQKIHPNDLKRIIRAIEIYVITGIKMGEIVKENRQDENSFDYHIIVLDRERQELHERINKRVHQMIDEGLIEEVRNLLSLGYSTTLNALNTIGYKEVVQYLYGKIDFNEMVHQIKVNTRNYARRQIIYFRKIEGAKWINLSKTSQEEVVDQILSEFI | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q7MAX8 | MSDQKTQHLPTAIFVMGPTASGKTALSVALRQHLPVELISVDSALIYRGMDIGTAKPTTEEQALAPHRLINILDPSQPYSAADFCHDALKEMAEITASGRIPLLVGGTMLYFKALLEGLSPLPSANPVIRAQIEQQAAEQGWDALHQQLQKIDPAAALRIHPNDPQRLSRALEVFLISGKTLTELTTLSGESLPYRVHQFAIAPAKRELLHQRIEARFHQMLESGFEEEVKALYARHDLHVDLPSIRCVGYRQMWSYLSGEIDYDEMIYRGICATRQLAKRQITWLRGWKSVHWLDSSQPEQALSTVMQVVSA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
B1XRT3 | MPTEPYIQPMHVLNEAPILCIVGPTGAGKTHLAMSLAEHAKSIGLTIELISMDSALVYRGLDIGSAKPTKAEQDAFIHHLIDIIDPTEVYSAARFANDAKRLCLEIRERGNVPVVVGGTMLYWRAWAHGLSSLPPANSEIRARLDEEGKSIGWPAMHDKLAKVDPETAARLKPNDSQRVQRALEVFEIIGKPMSVLLADSPSEDGREGSAIPSWIDLISLEPRDRKRLHLNLEKRFDEMLTAEFMNEVKALHANTRLHTDLPAIRSVGYRQAWEFLNGEIDAEQMRYKALVATRQLGKRQLTWLRAIEGRKTFDPFNPEE... | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q128B6 | MNEVKSVGAKYIALTGPTASGKTAAAMAIAQQHDVEIISVDSALVYRGMDIGTAKPTVDELAAVPHHLINIRDPLQAYSAAEFVADAQRLIDDIAARGKLPLLVGGTMLYFKALFYGLDDMPKADPAVRAELASEAAAKGWPALHAELATVDPVTAARLAPHDSQRISRALEVFRVSGQPLSFFHQQNAAKTIADDGREERTEILISLEPQERSWLHHRIAERFDAMLAAGFVEEVKTLRARGDLTPDLPSMRCVGYRQAWELLDAQEARSPGGSFPMDELRDKGIIATRQLAKRQVTWLRSMPQRQIITCDTDQALPLV... | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q97RW5 | MKTKIIVIVGPTAVGKTALAIEVAKRFNGEVVSGDSQQVYRGLDIGTAKASPEEQAAVPHHLIDVREITESYSAFDFVSEAKMTIEGIHNRGKLAIIAGGTGLYIQSLLEGYHLGGETPHEEILAYRASLEPYSDEELAHLVDQAGLEIPQFNRRRAMRALEIAHFGQDLENQETLYEPLIICLDDERSQLYERINHRVDLMFEAGLLDEAKWLFDHSPNVQAAKGIGYKELFPYFRGEQTLEEASESLKQATRRFAKRQLTWFRNRMQVTFYQIGESGVQDRILSQIEEFLDD | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q057G5 | MNEHDSSIIENILKKTNLYIITKKPEISDILILNTCSIREKAQEKLFHQLGRWKKLKQKNSKILIAVGGCVAVQEGKKIYKRAKFIDIIFGPQTLHKLPKLLIESNKKKSLIINIKKKSLKKFNYTINKNTNIKKKFSSFVTIMEGCNKYCSFCIVPYTRGKEVSRNNKKIISEIIELSKKGVREITLLGQNVNAYKFSDTFNKKNYSFSDLLYSISEIPRIDRIRFITSHPVEFNNNIIEAYKKIPKLTNFLHLPVQSGSNKILKLMKRGYTIEKYENIVNKIKKIRPKINISSDFIIGFPGETKEDFQKTIYFISKIN... | Cofactor: Binds 1 [4Fe-4S] cluster, which is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codo... |
B2VBL4 | MTKKLHIKTWGCQMNEYDSSKMADLLNSTHGYTLTEQAEDADVLLLNTCSIREKAQEKVFALLGRWKKLKESNPDMIIGVGGCVASQEGAQIRQRASCVDIVFGPQTLHRLPEMINSVRGTRSPVVDVSFPEIEKFDRMPEPRADGPTAFVSIMEGCNKYCTFCVVPYTRGEEVSRPSDDILFEVAQLAAQGVREVNLLGQNVNAYRGETFDGGICSFAELLRLVAAIDGIDRIRFTTSHPIEFNDDIIDVYRDTPELVSFLHLPVQSGADRILTLMKRAHTALEYKAIIRKLLAARPNIQISSDFIIGFPGETQADFEQ... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
Q2N950 | MKPTHSPKTYRVKSFGCQMNVYDGERMAEMLDEKGIEPAPEGEDADLVVLNTCHIREKAVDKVYSDIGRLTKGKTQTKAPMIAVAGCVAQAEGEEIMARAPAVSMVVGPQAYHRLPGMIDAAVAGKRSTDTDMPADAKFAALPKRRKSAPSAFLTIQEGCDKFCTYCVVPYTRGAEISRPFSALIDEAKKLVEAGAKEITLLGQNVSAWTGEDAKGRALGMAGLIRELAKDPDLKRVRYTTSHPADMDDELIATHGEVEKLMPYLHLPVQSGNDRVLKAMNRSHTAESYLRLLERFRAARPDLALSGDFIVGFPGETEAE... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
A6H119 | MEKIIEESKQGGSLILENKPENTKKLFIESYGCAMNFSDSEIVASILSGNGYNTTNVLEEADLVLVNTCSIRDKAEQTIRKRLEKYNAVKRINPKMKVGVLGCMAERLKDKFLEEEKIVDLVVGPDAYKDLPNLLNEVEEGRDAINVILSKDETYGDISPVRLMSNGITALVAITRGCDNMCTFCVVPFTRGRERSREPQSIMAEIQDLWHKGFKEITLLGQNVDSYLWYGGGLKKDFTNASEIQKATAVDFDQLLEMVAVGFPKMRIRFSTSNPQDMHESILHVMAKHSNICKHIHLPVQSGSNRILKEMNRLHTREEY... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
Q8RG43 | MKKASIITYGCQMNVNESAKIKKIFQNLGYDVTEEIDNADAVFLNTCTVREGAATQIFGKLGELKALKEKRGTIIGVTGCFAQEQGEELVKKFPIIDIVMGNQNIGRIPQAIEKIENNESTHEVYTDNEDELPPRLDAEFGSDQTASISITYGCNNFCTFCIVPYVRGRERSVPLEEIVKDVEQYVKKGAKEIVLLGQNVNSYGKDFKNGDNFAKLLDEICKVEGDYIVRFVSPHPRDFTDDVIEVIAKNKKISKCLHLPLQSGSSQILKKMRRGYTKEKYLALVDKIKSKIPGVALTADIIVGFPGETEEDFLDTIDVV... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
A9FST8 | MPRYSITTFGCQMNVHDSERMHDVLRCAGYTEAGSADEADVLVLNTCSVREKAEQKLRSEVGRLARWKRERADRVLVVAGCVAQQEGERLLKQMRAIDVVVGPDNIPELPGLLGDLAIGGLPIARTVFDLDAPRFLVASPPSPSSSSSPRAAPTAFVTVMKGCDERCSFCIVPHTRGPERYRPSDEIVAEIAALVAAGTREVTLLGQTVNSYRDPLGALPRAPGASADDPDESEFAALLRRVAADVPGLARLRYTSPHPRHLTPSLVLAHAELPVLPRHVHMPVQSGSDRVLRRMIRRYTRAEYVARTRALVEAVPGLTL... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
Q9ASV5 | MLRKSVLELSSRLSIKRFPRNLGAQRFHLSSSRNASTSGKNGLPGAKPVGKPDASKVDPPKVTPPPPTKGNSSKVVIGGVAIAGAFLVAYQTGYLDQYLGKEQQKLSERIHSDALTEKLEEAHHLNVPSGVEDSTEKDGKVETQPQVTHSEASEGVQSDIELQPESDLSSDRFTYISSNQEETPQETVIDRAEINLPISASEDSGAKPDMPSEIISEAESVKLEAVPKPGDSPIIVNAQSSSVHRESETESASPKDPAALKTPEDGIEREVQLPGSLLKEYNLEGSDTESTGSSSIGEQITKETEAFPNSTEGLKDSYMT... | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane (By similarity). Plays a role in keeping cristae membranes connected to... |
Q754G4 | MLSSRAAAFTGRRLASTLPPVPRKKSHGVRRLLAKAVVATSLFYAGGLTLSAYNDKANELFVEHVPFGEELVERWEDWTSLRRPGRRMIDARRVDEISRDFRAAATPEATPVVVRPLVQLQLPELQMQGSSPVLEALVNNVNDVVVALNARALELPEDTASALSSVYGEIVHSIQALNASLDQEFATEVESRTGKAISSVQEQLEVEYKQRELALAEQYIQNFEVFKSQLQKATAEQLETELKAHEQALLARHRNEVAQLSIRQVEEFNKIIEKKLDQERNGRLAKLSELNSAVESLAPVLDRLELRAVKNECVTQLSTL... | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner bound... |
A2QI68 | MVVRPMMLRSSVAPGRQLLLSSARQRTASQWLSRAGASSRLSGQRFFADIKPPTTAAPTPATPSSESAVPPETVPKPSPAGQESTLPPSTPPTPAPKGGRFRRFLLYLLLTSGFAYGGGVFLALKFDNFHDFFTEYIPYGEESVLYFEERDFYRRFPNTLRNQNRLNPTPRDEGNKITIPSKSGLTSKVAEEEISGADVSQKGPHMSATPAQKSSEAQTKPAAAKPEDKTTAVVKAKEDKAAKEAEKKEEPRQPAIPAVTPLEFAQVNEGDEAIVQELVKTFNDMITVISADENSGKYSQPVAKAKEELQKVGEKIIAVR... | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner bound... |
C5JIS0 | MLRTSIASSRQVLSSPICPNPSVQWLHTSRARRVNAAASRRYYAVARKPNAGVRSSSTPNAAATPELSQKATNSTSTKPPGPNDPDVRSPASPSTGSTLHPETVSKPPQSPAVQGQTSPGSSVQPPEHEPSPPPPRPPPAPKTGLLRKLLYLFLTTGLAYAGGVWYSLRSDNFYDFFTEYIPYGEEAVLYLEERDFRSRFPSIARQINRRVSAPRDEGAQVMIPGRSGLSWKVAEEQQEASDVTKQGQHISATDANELTEETKVAEKAKEDVKSKPVAKKAEAAEPKSSPKVVEPHPAKAEENTSLEAPRQPVVPAAAAI... | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner bound... |
Q5A044 | MIRITSRSVKGAAGIRSVSSSTVRLNIAPKVVSPPVPPPVKPQGSEIPPPPPPPPPPPKAKRFSLFGFLFKTTLLATVVYGGTLYAATKNDKVMDFVIDKQLPFHEELIDLIENGSTEDLQEAWEQLKNKFTDVKLPTKDDIDELTQKLEHRGEDIIKETKKKIASTHIGHKSGTDLTPTEQLQRGVEIESVKKDVAHLPLIELNSDLGKSVDETVKQTITSFNNFIQSIDASSLATKDDKLITSINTSVNQLASRLNSLTKDFDNELQNKLKVSQTELFSSFTKKELELTENLLHQFSTEKQQLEAKLNQKLSQEIQAA... | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner bound... |
Q6FSU7 | MLRTKITGSSHVLRTAFKRYSSTIDSGAVEVVKPKKTSFTRRLFRLGLAVTAFYAGGVAVSQYDDDLGTLFTEKVPGAEKLVDSYVTYRYDPTISKMLSTEYLLNLFKGENTEVKPSTSSRLVPIHDAIKELHLELLELDSENNSEPEMQKIINSLNSTINMINEQKLRIGGKKSRSIEENYKQLIEDILHLDKNLKETVSKSINEKTEEVVKKVREQYKRKLAVSEVELQDKYKNEFIHLKEEMEKHYQDILNQKLEANKQHLEAKHANEIALLSITQVSEFNKIIKEKVDSERNGRLAKIEDLDKKAENLTEALKHVN... | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner bound... |
P91850 | MPYFTIDTNIPQNSISSAFLKKASNVVAKALGKPESYVSIHVNGGQAMVFGGSEDPCAVCVLKSIGCVGPKVNNSHAEKLYKLLADELKIPKNRCYIEFVDIEASSMAFNGSTFG | Function: Tautomerization of the methyl ester of L-dopachrome (By similarity). Inhibits migration of human peripheral blood mononuclear cells.
Catalytic Activity: L-dopachrome = 5,6-dihydroxyindole-2-carboxylate
Sequence Mass (Da): 12320
Sequence Length: 115
Subcellular Location: Secreted
EC: 5.3.2.1
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P81530 | PIFTFASNVPADTITGFFL | Function: Tautomerization of the methyl ester of L-dopachrome.
Catalytic Activity: L-dopachrome = 5,6-dihydroxyindole-2-carboxylate
Sequence Mass (Da): 2058
Sequence Length: 19
EC: 5.3.3.12
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P81529 | MPIFTLNTNIKATDVPSDFLSSTSALVGNILSKPGSYVAVHINTDQQLSFGGSTKPAAFGTLMSIGGIEPSRNRDHSAKLFDHLNKKLGIPKNRMYIHFVNLNGDDVGWNGTTF | Function: Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells.
Catalytic Activity: L-dopachrome = 5,6-dihydroxyindole-2-carboxylate
Sequence Mass (Da): 12337
Sequence Length: 114
Subcellular Location: Secreted
EC: 5.3.2.1
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P81748 | MPIFTFSTNVPSENISVDFLKSTSKLIAGMLGKPESYVAVHINGGQKITFGGTDAPAGFGQLLSLGGVGGEKNRSHSAKLFKHLTDGLGIPGNRMYINFVDMRGSDVGYNGSTF | Function: Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells (By similarity).
Catalytic Activity: L-dopachrome = 5,6-dihydroxyindole-2-carboxylate
Sequence Mass (Da): 12043
Sequence Length: 114
Subcellular Location: Secreted
EC: 5.3.2.1
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Q7WY64 | MTMFVESINDVLFLVDFFTIILPALTAIGIAFLLRECRAGEQWKSKRTDEHQTVFHINRTDFLIIIYHRITTWIRKVFRMNSPVNDEEDAGSLLL | Function: Sensor protein that up-regulates translation of the secondary membrane protein insertase (MisCB/YqjG) when activity of the primary membrane protein insertase (MisCA/SpoIIIJ) is limited. Acts as a ribosome-nascent chain complex. When the primary membrane protein insertase activity or level is reduced, the memb... |
P80177 | MPMFVVNTNVPRASVPDGLLSELTQQLAQATGKPAQYIAVHVVPDQLMTFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLTERLRISPDRIYINFCDMNAANVGWNGSTFA | Function: Pro-inflammatory cytokine involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tauto... |
P20774 | MKTLQSTLLLLLLVPLIKPAPPTQQDSRIIYDYGTDNFEESIFSQDYEDKYLDGKNIKEKETVIIPNEKSLQLQKDEAITPLPPKKENDEMPTCLLCVCLSGSVYCEEVDIDAVPPLPKESAYLYARFNKIKKLTAKDFADIPNLRRLDFTGNLIEDIEDGTFSKLSLLEELSLAENQLLKLPVLPPKLTLFNAKYNKIKSRGIKANAFKKLNNLTFLYLDHNALESVPLNLPESLRVIHLQFNNIASITDDTFCKANDTSYIRDRIEEIRLEGNPIVLGKHPNSFICLKRLPIGSYF | Function: Induces bone formation in conjunction with TGF-beta-1 or TGF-beta-2.
PTM: O-glycosylated with a core 1 or possibly core 8 glycan.
Sequence Mass (Da): 33922
Sequence Length: 298
Subcellular Location: Secreted
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Q62000 | METVHSTFLLLLFVPLTQQAPQSQLDSHVNYEYATGNSEETKFSQDYEDKYLDGKSIKEKETMIIPDEKSLQLQKDEVIPSLPTKKENDEMPTCLLCVCLSGSVYCEEVDIDAVPPLPKESAYLYARFNKIKKLTAKDFADMPNLRRLDFTGNLIEDIEDGTFSKLSLLEELTLAENQLLRLPVLPPKLTLLNAKHNKIKSKGIKANTFKKLNKLSFLYLDHNDLESVPPNLPESLRVIHLQFNSISSLTDDTFCKANDTRYIRERIEEIRLEGNPIALGKHPNSFICLKRLPIGSYF | Function: Induces bone formation in conjunction with TGF-beta-1 or TGF-beta-2.
PTM: Contains keratan sulfate.
Sequence Mass (Da): 34012
Sequence Length: 298
Subcellular Location: Secreted
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Q8MJF1 | MKTLRSTLLLLLFVPLIKPAPPAPQESPLTFDYAADHLEEAIFSQDYEDKYLDGKNIEEKQTMVRSVKRSLELQKDESVTPAPPKKENDEMPTCLLCVCLSGSVYCEEVDIDAVPPLPKESAYLYARFNKIKKLTAKDFADMPNLRRLDFTGNLIEDIEDGTFSKLALLEELSLAENQLLKLPVLPPKLTLFNAKYNKIKSRGIKANTFKKLNNLSFLYLDHNALESVPPNLPESLRVIHLQFNNITSITDDTFCKANDTRYIRDRIEEIRLEGNPIALGKHPNSFICLKRLPIGTYF | Function: Induces bone formation in conjunction with TGF-beta-1 or TGF-beta-2.
PTM: Contains keratan sulfate.
Sequence Mass (Da): 33918
Sequence Length: 298
Subcellular Location: Secreted
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Q93367 | MDDSTPYPVPQELYIPQKMKAFMAEPQGCALVAALEGQFQCSIVVINDHLSVISSADGVAVDINQIEKILRDVWRKRDVQIMIREAALNASCTHICHTLLPRAYCAVVLFFSSDLQRRSRCTDIIIDQFTGKVTMFGTEQAVNKAREMMIECLTEHFGLLEMNIPPTQRTTRMGYTNSYNPEIRTHLPPNSFLNSVFPMGEPNAILTSTPPTTSIMDEPLLSASLEKHLLFPSDFSVPPPRLSPVQELPLTPPKTCVVEKIKQWIPTTEVGKILGNRAAVKKHIERQFNCVITVHTEVQSSFGATPVEIVAQNKEQCQEA... | Function: RNA-binding protein which binds to its own mRNA and target mRNAs to negatively regulate gene expression to modulate apoptosis and differentiation in the germline . Negatively regulates the expression of the argonaute protein wago-4, and may thus play a role in RNA-mediated gene silencing (RNAi) in the germlin... |
O34375 | MSVQWGIELLKSAGLFFLHPLFWFFIIITLAFGYVRIKRERKTFHTRIADIYDDLKFTYTKGLIPGLLLSVILGGLGISIPLGLLAIIAVITAAAAFTLRANWMSAAYIVSVSMLIGFGLQIYQAEPFLERFPQGFAVVWPAVAVFLGLLIITEGAVAYRSAHVRTSPALVVSSRGLPIGQQLANRVWLLPLFLLVPGNGLESHLSWWPVFTVPGGSFHFLWIPYFVGFGQRVQGSLPETSIRITAKRVCILGLAVAVLGAASLLWTPLAGAAVCTALLGRIFLSIKQRVNDNAAPFYFSKRDQGLMVLGIIPNTPAEDL... | Function: The main function of the Min system is to promote the disassembly of the cytokinetic ring after cell division, thereby ensuring that division occurs only once per cell cycle. MinJ acts as a bridge between DivIVA and MinD. May modulate activity and localization of MinD and MinC through direct interaction with ... |
F2M971 | MAVVVALLINPVGLVFWLALGLTIWFAVNRTDRERRRYLRAIHPKHPEIGRFFWIGLVVGALVSLVMVIGRLQISLAALLALSGLTLVALLFSKWRFSPWWLGLASLAAVGQSGLLAEQHAANLAILVGLLWLTQAGLARFNRGDEIESPVIQQDRRQRQSAAFELRQLFWVPLILPVAVENVSNLPLLAVTVQSLTFVGLPLLLGATFMTPRDRAQTAWRRSWPWYGGAGGVLIVYGIVARTMTLPLLVSLVFPAVVSLVLVGGFIWQGRQVHLTVTLADQGVVLIGVVPHTPAAEMGLQPGDRVLACNHHSVNNSREL... | Function: The main function of the Min system is to promote the disassembly of the cytokinetic ring after cell division, thereby ensuring that division occurs only once per cell cycle. MinJ acts as a bridge between DivIVA and MinD. May modulate activity and localization of MinD and MinC through direct interaction with ... |
Q54ND5 | MMVKIKNIIILFCIFGLLSNVSSLSSSSSSSQSSDNNGNLSPIQDYDLEFLSKHLTTKTPYWILTKNGDSNSQGDGSSGNSNSNSNSNSNSNSNSDSSNEPPEQCKLISIDFIARHGSRMPVLNSIEKLKEMTTSILEYKEQVNQGFNWIFNYSVPYPSDIAGNLILQGQYEHYNISKRLLKKYPLFFEPMKYKPQSYSITSTAISRTGISASAFSYGLLQGTGSLGVDGFQPVFIETASLDQDILLRFFATCNQYVDQLKNGTLINKDEQTKWNQMVFPNISNEISERLGLSDIWLPTSNVISDIFEACAYEISINNIS... | Function: Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) (By similarity). Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-B... |
Q9VV72 | MRLLILLLLPLVAIAQDDYCFSKDTSRLQTRQFSSKTAYQIVKGTDIDKQYLVPGCQPQKMWIFHRHGTRLPKKSMINKASRVAELRDLIINNYQVARTKPETDALCQTDLIAIKLWKWNSSITPDMEEYLTAQGYEDLRGTAKLYQRYYPTVLTANYNDTYYQFRHTDTQRTTESFKAFAEGLFGSQNAAHPVEIPKQDLLLRPYDYCSSFKNVNYKDEGSEYYKFHQSKLYNDTLADISTRLGFLYTLEEADIKLMYDMCRYEQAWNVDRNSVWCGAFLPEQITVFEYLEDLKYYYGSGYGFPENAHLNCRLVQDLLT... | Function: Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) . Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce ... |
Q9UNW1 | MLRAPGCLLRTSVAPAAALAAALLSSLARCSLLEPRDPVASSLSPYFGTKTRYEDVNPVLLSGPEAPWRDPELLEGTCTPVQLVALIRHGTRYPTVKQIRKLRQLHGLLQARGSRDGGASSTGSRDLGAALADWPLWYADWMDGQLVEKGRQDMRQLALRLASLFPALFSRENYGRLRLITSSKHRCMDSSAAFLQGLWQHYHPGLPPPDVADMEFGPPTVNDKLMRFFDHCEKFLTEVEKNATALYHVEAFKTGPEMQNILKKVAATLQVPVNDLNADLIQVAFFTCSFDLAIKGVKSPWCDVFDIDDAKVLEYLNDLK... | Function: Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) . Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce ... |
Q9Z2L6 | MLRGARSHLPASVAPAAVLAAALLSSFARCSLPGRGDPVASVLSPYFGTKTRYEDANPWLLVDPVAPRRDPELLAGTCTPVQLVALIRHGTRYPTTKQIRKLKQLQGLLQTRESRDGGSQVAAALAEWPLWYGDWMDGQLVEKGRQDMRQLALRLAALFPDLFSRENYDRLRLITSSKHRCVDSSAAFLQGLWQHYHPGLPPPDVSDMECGPPRINDKLMRFFDHCEKFLTDVERNETALYHVEAFKTGPEMQKVLKKVAATLQVPMNSLNADLIQVAFFTCSFDLAIKGVHSPWCDVFDVDDARVLEYLNDLKQYWKRS... | Function: Acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate (By similarity). Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of ino... |
Q5NU14 | MAEAAVASTVTLPVTGGWTKHVTCRYFMHGLCKEGDNCRYSHDLTSSKPAAMMCKFFQKGNCVFGERCRFEHCKPTKSEEVSNPQMLLLSSTPPPIDPECSESGPRLKTQDWANAAEFVPGQPYCGRAESVDVEISIPLIEELNGDATTDKEELRKQLCPYAAVGECRYGVNCAYLHGDVCDMCGLQVLHPTDSSQRSEHTKACIEAHEKDMEISFAIQRSKDMMCGVCMEVVFEKANPSERRFGILSNCSHCYCLKCIRKWRSAKQFESKIIKSCPECRITSNFVIPSEYWVEDKEDKQKLIQKYKDGMGRKPCRYFDE... | Function: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequ... |
Q9H000 | MSTKQITCRYFMHGVCREGSQCLFSHDLANSKPSTICKYYQKGYCAYGTRCRYDHTRPSAAAGGAVGTMAHSVPSPAFHSPHPPSEVTASIVKTNSHEPGKREKRTLVLRDRNLSGMAERKTQPSMVSNPGSCSDPQPSPEMKPHSYLDAIRSGLDDVEASSSYSNEQQLCPYAAAGECRFGDACVYLHGEVCEICRLQVLHPFDPEQRKAHEKICMLTFEHEMEKAFAFQASQDKVCSICMEVILEKASASERRFGILSNCNHTYCLSCIRQWRCAKQFENPIIKSCPECRVISEFVIPSVYWVEDQNKKNELIEAFKQ... | Function: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (By similarity). Promotes the polyubiquitination and proteasome-dependent degradation of RELA/p65, thereby suppressing RELA-mediated NF-kappaB transactivation and negatively regulating inflammatory responses (... |
Q9ERV1 | MSTKQVTCRYFMHGVCREGSQCLFSHDLANSKPSTICKYYQKGYCAYGARCRYDHTKPPAAAGGAVGPAPNPSPSSGLHSPHPSPDIATSVMRTHSNEPGKREKKTLVLRDRNLTGLAEDKTPPSKVNNPGGCSDPQTSPEMKPHSYLDAIRTGLDDLEASSSYSNEPQLCPYAAAGECRFGDACVYLHGDMCEICRLQVLHPFDPEQRKAHEKMCMSTFEHEMEKAFAFQASQDKVCSICMEVILEKASASERRFGILSNCSHTYCLSCIRQWRCAKQFENPIIKSCPECRVISEFVIPSVYWVEDQNKKNELIEAFKQ... | Function: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins . Promotes the polyubiquitination and proteasome-dependent degradation of RELA/p65, thereby suppressing RELA-mediated NF-kappa-B transactivation and negatively regulating inflammatory responses . Plays a role ... |
Q13064 | MEEPAAPSEAHEAAGAQAGAEAAREGVSGPDLPVCEPSGESAAPDSALPHAARGWAPFPVAPVPAHLRRGGLRPAPASGGGAWPSPLPSRSSGIWTKQIICRYYIHGQCKEGENCRYSHDLSGRKMATEGGVSPPGASAGGGPSTAAHIEPPTQEVAEAPPAASSLSLPVIGSAAERGFFEAERDNADRGAAGGAGVESWADAIEFVPGQPYRGRWVASAPEAPLQSSETERKQMAVGSGLRFCYYASRGVCFRGESCMYLHGDICDMCGLQTLHPMDAAQREEHMRACIEAHEKDMELSFAVQRGMDKVCGICMEVVYE... | Function: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequ... |
Q9N373 | MPRHETDCRYFANGYCSKGNTCTFTHDVATRNENICHFNLVGKCSYGRACRFLHTRPRNDELPSCSTPQTSQNQQNLQNSGQRVRPKQLPELKFNAQAAEFVPRWKMPQRGPVTSYAGAAASADHGESSSSFQSSHEQAQLMMCPYHQKSGDCNRQDMDCPFAHGNYCDMCQQWSLHPYNAELRKKHENECVANHTTEMERAFLLQKTEQKTCGICMENIFEKNLRFGILNGCQHCFCLDCIRQWRSKDQENVELATKTVRSCPECRQHSDYVIPSLFWVESGQEKDLLIEMYKENTKRKICKYYSNERSRGACPFGNKC... | Function: E3 ubiquitin ligase which catalyzes the covalent attachment of ubiquitin moieties onto substrate proteins (By similarity). Promotes the larval to adult transition by binding to the long non-coding RNA lep-5 to target the heterochronic protein lin-28 for degradation by the proteasome . This association and deg... |
Q8LGD5 | MDPSEYFAGGNPSDQQNQKRQLQICGPRPSPLSVHKDSHKIKKPPKHPAPPPNRDQPPPYIPREPVVIYAVSPKVVHATASEFMNVVQRLTGISSGVFLESGGGGDVSPAARLASTENASPRGGKEPAARDETVEINTAMEEAAEFGGYAPGILSPSPALLPTASTGIFSPMYHQGGMFSPAIPLGLFSPAGFMSPFRSPGFTSLVASPTFADFFSHIWDQD | Function: Regulator of plant defense response. May contribute to MPK4-regulated defense activation by coupling the kinase to specific WRKY transcription factors.
PTM: Phosphorylated on serine residue by MPK4.
Sequence Mass (Da): 23582
Sequence Length: 222
Subcellular Location: Nucleus
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P54571 | MKDVRLPTLFEIIIVLGVFLALVLSFTVFLDLPIQLALFVSWFIAMLLGIRLGYSYKDLQNAIVHGISNGLEAVLILVSVGALIGTWIAGGVVPTLIYYGLEFIHPSIFLLATLIICSIMSVATGTSWGTVGTAGIAMIAIGEGLGIPLPLVAGAILSGAYFGDKLSPLSDSTVLASSLSKVDVLAHVRAMLYLSIPAYVITAILFTVVGFMYGGKNIDLDKVEFLKSSLQNTFDIHIWMLIPAVLVIVLLAMKKPSMPVIVIGALLGAIWAVVFQGMDIAHAIATAYNGFSIKTDVEFLNGLLNRGGIVGMLDSLVVII... | Function: Couples proton uptake and Na(+) efflux to the substrate-product malate/lactate antiport, in an electroneutral malate-2H(+)/Na(+)-lactate exchange. Plays a role in supporting growth to high density on malate at reduced protonmotive force.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50212... |
A0A095AMW7 | MNTTGYDILRNPFLNKGTAFSEAERQQLGLTGTLPSQIQTIEEQAEQAYKQFQAKSPLLEKRIFLMNLFNENVTLFYHLMDQHVSEFMPIVYDPVVAESIEQYNEIYTNPQNAAFLSVDRPEDVENALKNAAAGRDIKLVVVTDAEGILGMGDWGVNGVDIAVGKLMVYTAAAGIDPATVLPVSIDAGTNNKELLHNPLYLGNKHERIAGEQYLEFIDKFVTAEQNLFPESLLHWEDFGRSNAQVILDKYKESIATFNDDIQGTGMIVLAGIFGALNISKQKLVDQKFVTFGAGTAGMGIVNQIFSELKQAGLSDDEARN... | Function: Involved in the malolactic fermentation (MLF) of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. Catalyzes the decarboxylation of L-malate to L-lactate.
Catalytic Activity: (S)-malate + H(+) = (S)-lactate + CO2
Sequence Mass (Da): 59205
Sequence Length: 542
EC: 4.1.... |
Q48796 | MTDPVSILNDPFINKGTAFTEAEREELGLNGLLPAKVQALQEQVDQTYAQFQSKVSNLEKRLFLMEIFNTNHVLFYKLFSQHVVEFMPIVYDPTIADTIENYSELFVEPQGAAFLDINHPENIQSTLKNAANGRDIKLLVVSDAEGILGIGDWGVQGVDIAVGKLMVYTVAAGIDPSTVLAVVIDAGTNNEKLLKDPMYLGNKFNRVRGDKYYDFIDKFVNHAESLFPNLYLHWEDFGRSNASNILNSYKDKIATFNDDIQGTGIVVLAGVLGALKISGQKLTDQTYMSFGAGTAGMGIVKQLHEEMVEQGLSDEEAKKH... | Function: Involved in the malolactic fermentation (MLF) of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. Catalyzes the decarboxylation of L-malate to L-lactate. It can also use pyruvate as substrate.
Catalytic Activity: (S)-malate + H(+) = (S)-lactate + CO2
Sequence Mass (D... |
P46057 | MAVAPTSYDILMGTFRSPYLYTLTFDVLARKLQVREVNEATGGHNWLDVSPDGNTLYATVWGEPPKLTSYDIVRGGEYATTKLSRNVASQYMSGYVCSNNKAMYSACGPQVDTFLVDDNGTLLDQPAVQSFNLLQGQEKNKANGTLDFGGLRHGGHSADLSPDGTKLYVADIGRNCVWMYHVDRETGLLTEASKNIATRPHDGPRHAWPHPNGRIVYSLQEHSSYVDAFRLTDDNKLEFLEGGCIIPDEKDHDKYWADEVRLSPMADVVFGSTRGLEEGTPGFVTAWNLRPDGTFASTEATHRFQTKTSGGWANAIAVCP... | Function: Catalyzes a syn cycloisomerization.
Catalytic Activity: (S)-muconolactone = cis,cis-muconate + H(+)
Sequence Mass (Da): 41263
Sequence Length: 374
Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydro-2-furylacetate from catechol: step 2/3.
EC: 5.5.1.1
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P58340 | MFRMLNSSFEDDPFFSESILAHRENMRQMIRSFSEPFGRDLLSISDGRGRAHNRRGHNDGEDSLTHTDVSSFQTMDQMVSNMRNYMQKLERNFGQLSVDPNGHSFCSSSVMTYSKIGDEPPKVFQASTQTRRAPGGIKETRKAMRDSDSGLEKMAIGHHIHDRAHVIKKSKNKKTGDEEVNQEFINMNESDAHAFDEEWQSEVLKYKPGRHNLGNTRMRSVGHENPGSRELKRREKPQQSPAIEHGRRSNVLGDKLHIKGSSVKSNKK | Function: Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppress... |
Q9QWV4 | MFRMLSSSFEDDPFFADSFLAHRESMRNMMRSFSEPLGRDLLSISDGRGRTHNRRERDDGEDSLTHADVNPFQTMDRMMANMRSGIQELQRNFGQLSMDPNGHSFCSSSVMTYSKVGDEPPKVFQASTQTRRAPGGVKETRKAMRDSDSGLERMAVGHHIHDRGHVIRKSKNNKTGDEEVNQEFINMNESDAHAFDDEWQNEVLKYKSIGRSGNTGMRSVGHEHPGSRELKRREKIHRNSAIESGRRSNVFVDKLNVKGSPVKITKK | Function: Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppress... |
Q9CLB8 | MKKYIIYALIPFLFACGGTKTHRSSQFDEAFAKDTRGLDILTGQFSHNIDRIWGVNELLVASRKDYVKYTDRFYTRSHVSFDEGLITVETQSDLRHLQNAIVHILLMGSDANGIDLFASGDVPISSRPFLVGQVIDHLGGSITNTTTAGNFANYLLQNKLQTRRLSNGHTVQYVVIPMIANHVAVRAQRYLPLVRKMARRYNMDESLILGIMQTESSFNPYAISYANAIGLMQVVPTTAGRDIFKMKGKGGQPSKSYLFDPEKNIDAGTSYLWLLQNKYLDGITNPTSKRFAMISAYNSGAGAVLRVFDQDRDAAIVKIN... | Function: Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division.
Catalytic Activity: Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reduc... |
Q30PQ0 | MKRGSVALFAISFFAFGWMTHALYNDAYKMIKESTLKKIKKSGALNVVLLNAPSTYYIGSDGPKGFEYDLLESYANHLGVKLNITTANTIKEALELSKNPDIHITSASLTKTPEREKEFNFGPSYFEAQEQVVCNKSLLLDGRFPSDADSLSGLRVVVGDSTSYSETIESLKKEGFDINATYTAEYSTEELISQVDTHEIDCTIIDSNIYALNQRYFKNIVLAFDISNRRQQAWILTPDSKMLKNDMYSWLNTVNQSGEMARLKDHYYSYVLFFDYYDTVMFYKRIKTRLPKYESYFKEAAVKYEIPYSALAALSYQESH... | 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... |
Q3SJH8 | MPSLKTKGAAGKFASLLLVLALSACSRPAPPPETSGELRVGTRNSPATFYIGHDGETAGFEHDLILAFSRAQNWTLSWTEKSRPQALFDMLERREIHLAAAALPQAVVKDRHLISGPILFETPVHVVYRTADRAPRGVAGLAGKKLAFIIGSGHGPMLMRLKRKHPELSWAAVENVWPEELLAQLQAGKYDAVIINGMDFDAMRNFYPGLAVAFDLPYKQKIVWALSPGSSHAFRNALARFVERARSDGTIKRALERYFGHVKRLGSSDILGILQRRPQRLPDLREHFQEAQTLSGIDWRLLAAIGYQESQWNRLATSPT... | 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... |
Q87RW1 | MQIRHFNRLKRSVLLFASVLLLSACQIESQPKSEFEKIQERGVLRVGTLNNQLSYYIGPDGPAGLDYELARKFAEELGVKLEIKPAFRQADLFPALKKGDIDIIATGLNQTSQAVKRFRPGPAYYYVSQQVVYKKGQLRPRDIEQLIEYQASKDSQSEEDVNAGAQTLKIVEQSQYVPTLTALKKQYPELQFEIVGDADTRDLLKHVSTGELRFTVTDSVELSLAQRLYPDLALAFELTEDQPVSWFTRRSEDESLYAMLIEFFGNIKQSGELASLEEKYIGHIEAFDYVDTRAFIRALDDKLPRWAPLFQKYSEEFDWR... | 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... |
O77656 | MHPRVLAGFLFFSWTACWSLPLPSDGDSEDLSEEDFQFAESYLKSYYYPQNPAGILKKTAASSVIDRLREMQSFFGLEVTGRLDDNTLDIMKKPRCGVPDVGEYNVFPRTLKWSKMNLTYRIVNYTPDLTHSEVEKAFRKAFKVWSDVTPLNFTRIHNGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPYSKHPKTPDKCDPSLSLDAITSLRGETLIFKDRFFWRLHPQQVEAEL... | Cofactor: Can bind about 5 Ca(2+) ions per subunit.
Function: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II col... |
P45452 | MHPGVLAAFLFLSWTHCRALPLPSGGDEDDLSEEDLQFAERYLRSYYHPTNLAGILKENAASSMTERLREMQSFFGLEVTGKLDDNTLDVMKKPRCGVPDVGEYNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIFKDRFFWRLHPQQVDAEL... | Cofactor: Can bind about 5 Ca(2+) ions per subunit.
Function: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II col... |
P23097 | ATFFLLSWTHCWSLPLPYGDDDDDDLSEEDLEFAEHYLKSYYHPVTLAGILKKSTVTSTVDRLREMQSFFGLDVTGKLDDPTLDIMRKPRCGVPDVGVYNVFPRTLKWSQTNLTYRIVNYTPDISHSEVEKAFRKAFKVWSDVTPLNFTRIHDGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNLGGDAHFDDDETWTSSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPEKCDPALSLDAITSLRGETMIFKDRFFWRLHPQQVEPELFLTKS... | Cofactor: Can bind about 5 Ca(2+) ions per subunit.
Function: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II col... |
P50281 | MSPAPRPPRCLLLPLLTLGTALASLGSAQSSSFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQKFYGLQVTGKADADTMKAMRRPRCGVPDKFGAEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGESGFPTKMPPQPRTTSRPSVPDKPKNPTYGPNICD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (By similarity). May be inv... |
Q95220 | MSPAPRPSRRLLLPLLTLGTALASLGSAQSNSFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQRFYGLRVTGKADTDTMKAMRRPRCGVPDKFGAEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVHYAYIRDGREKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTEKFLLPDDERRGIQQLYGSQSGSPTRCLLNPGQPSGLLFRISPGNPTYGPKICD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Endopeptidase that degrades various components of the extracellular matrix, such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development. May be involved in actin ... |
P51511 | MGSDPSAPGRPGWTGSLLGDREEAARPRLLPLLLVLLGCLGLGVAAEDAEVHAENWLRLYGYLPQPSRHMSTMRSAQILASALAEMQRFYGIPVTGVLDEETKEWMKRPRCGVPDQFGVRVKANLRRRRKRYALTGRKWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYEDIRLRRQKEADIMVLFASGFHGDSSPFDGTGGFLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLRGIQQLYGTPDGQPQPTQPLPTVT... | Cofactor: Binds 1 zinc ion per subunit.
Function: Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A.
PTM: The precursor is cleaved by a furin endopeptidase.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75807
Sequence Length: 669
Domain... |
P51512 | MILLTFSTGRRLDFVHHSGVFFLQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRMSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFHIRRKRYALTGQKWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSELENGKRDVDITIIFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPTRPLPTVPPHRSIPPADPRKN... | Cofactor: Binds 2 zinc ions per subunit.
Function: Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lo... |
Q9ULZ9 | MRRRAARGPGPPPPGPGLSRLPLPLLLLLALGTRGGCAAPAPAPRAEDLSLGVEWLSRFGYLPPADPTTGQLQTQEELSKAITAMQQFGGLEATGILDEATLALMKTPRCSLPDLPVLTQARRRRQAPAPTKWNKRNLSWRVRTFPRDSPLGHDTVRALMYYALKVWSDIAPLNFHEVAGSAADIQIDFSKADHNDGYPFDGPGGTVAHAFFPGHHHTAGDTHFDDDEAWTFRSSDAHGMDLFAVAVHEFGHAIGLSHVAAAHSIMRPYYQGPVGDPLRYGLPYEDKVRVWQLYGVRESVSPTAQPEEPPLLPEPPDNRS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral p... |
O49543 | MASKVISATIRRTLTKPHGTFSRCRYLSTAAAATEVNYEDESIMMKGVRISGRPLYLDMQATTPIDPRVFDAMNASQIHEYGNPHSRTHLYGWEAENAVENARNQVAKLIEASPKEIVFVSGATEANNMAVKGVMHFYKDTKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKTDGLVDLEMLREAIRPDTGLVSIMAVNNEIGVVQPMEEIGMICKEHNVPFHTDAAQAIGKIPVDVKKWNVALMSMSAHKIYGPKGVGALYVRRRPRIRLEPLMNGGGQERGLRSGTGATQQIVGFGAACELAMKEMEYDEKWIKG... | Function: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 50296
Sequence Length: 453
Subcellular Location: Mitochondrion
EC... |
Q8I113 | MFFLDNTDSMTSSSRGITMPNTISSHEDVGGYSPRKVGIQHDYSAVGGGGAAFHHLHTSAATPRHVATSEFYDDEEATSPRGGIEIGAGGGKMMANLRRHRQRERETYEDEDVLSSSDESSGRPIPRYVGRDTDHVFGEFEMDDEDVVMRREDGYGEDETDEDYFDEEEPVAELLPLGGGTRRVPRTPGRKNSSKCGFFDYYKLTDEHLGSGAYGSVTTCKSIKSGVEYAVKIVDKQGETHSRKRILREVNIFKTCKDHPNIVQLLDWFEDETNFYLVMEKMRGGPLLQHILQRKYFTEEEARRVTKDISLALKFMHDRG... | Function: Serine/threonine-protein kinase which is required in the germline to regulate positively lifespan . May play a role in body wall muscle contraction . May be involved in embryonic cytokinesis .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 78934
Sequ... |
P38888 | MVCCLWVLLALLLHLDHVACEDDAYSFTSKELKAYKQEVKELFYFGFDNYLEHGYPYDEVKPISCVPKKRNFEDPTDQGTNDILGNFTITLIDSLTTIAILEDRPQFLKAVRLVERTFPDGNFDIDSTIQVFEITIRVIGSLLSSHLYATDPTKAVYLGDDYDGSLLRLAQNMADRLLPAYLTSTGLPMPRRNIKRKWDVSEFPEFLETENNVAAMASPMFEFTILSYLTGDPKYEKVTRYAFDKTWSLRTGLDLLPMSFHPEKLTPYTPMTGIGASIDSLFEYALKGAILFDDSELMEVWNVAYEALKTNCKNDWFFAN... | Function: Alpha-1,2-specific exomannosidase involved in endoplasmic reticulum-associated degradation (ERAD). Delivers misfolded glycoproteins to proteasomes. Forms a complex with PDI1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded protein response.
Catal... |
Q12205 | MSIARLVYSLFRRVRSVLLLFITISLLFYYTFQNEIDILNSYALNDSLPSINNYEHNTEGSSKLDPPDLSSTGSDRIATDKENGNVAVDLSDPATLREKNKYFPLLLKGSSHQIGSNLPISSLLTYKEKYPVLFEYSSPSLTSISQNDVHKIQPAMQLPPDVDMIKQIKDIFMKSWNQEQLLLKSNLRRESTWPIDLIDSLDTLYLCGETKLFQDSVNIIEDFDFRVPPLAMEVIDIPDITTRVLEGLLSAYELSMDKRLLNKAKHVADFILRSFDTPNRIPILKYFWKSDLRNRFPDRTVPSGQLTTMALAFIRLSQLT... | Function: Putative mannosidase involved in glycoprotein quality control since it is involved in the targeting of misfolded glycoproteins for ER-associated protein degradation (ERAD).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 96997
Sequence Length: 849
Pathway: Protein modification; pro... |
Q4WA38 | MMVFSDCLIFSSLIISYALGLPVVPGQTVMEPSAALPDDGDHLYTLPMFDIRPWERVSEVRLAREGYLYGPPLLGNTSFFPTGVLGDAMVARDKAAWFRDVEYVTNNVYPEWDKAAIALAKAGGIQSLSSYAVIYENQWATTLPDGVASGMLTNWTQDLLFSMERLSINPYVVRRLHPRKDRLPFAVDDRVVQHLAAGSTLEALHCDGRLFFANHSYQAPYPKTPGRWTAACTAYFFIHPRSGAFLPLAIKTNMGSDLTYTPMDETNDWLFAKMAFEMNDLFHSQLYHLANTHDVAEPVHQAALRTMSARHPVRGYLDRL... | Cofactor: Three His residues, the carboxyl oxygen of the C-terminal Ile or Val residue, and a fifth residue, usually Asn, ligate the metal, which binds water to form a catalytic base Mn(2+)OH(2) for hydrogen abstraction.
Function: Lipoxygenase that metabolizes linoleic acid to 9- and 13-hydroperoxy fatty acids. Specifi... |
Q8X151 | MRSRILAIVFAARHVAALPLAAEDAAATLSLTSSASSTTVLPSPTQYTLPNNDPNQGARNASIARKRELFLYGPSTLGQTTFYPTGELGNNISARDVLLWRQDAANQTATAYREANETFADITSRGGFKTLDDFALLYNGHWKESVPEGISKGMLSNCTSDLLFSMERLSSNPYVLKRLHPTKDKLPFSVESKVVKKLTATTLEALHKGGRLFLVDHSYQKKYTPQPGRYAAACQGLFYLDARSNQFLPLAIKTNVGVDLTYTPLDDKDDWLLAKIMFNNNDLFYSQMYHVLFHTIPEIVHEAAFRTLSDRHPVMGVLNR... | Cofactor: Three His residues, the carboxyl oxygen of the C-terminal Ile or Val residue, and a fifth residue, usually Asn, ligate the metal, which binds water to form a catalytic base Mn(2+)OH(2) for hydrogen abstraction.
Function: Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 11S- and 13R-hydroper... |
M5EES5 | MVHNISLSSRKALHNVHLPYMVQLPKPTGYNVALKNAAEGYDKARRMVAWLYDIADYESSIPQTFTLQQKTDKYTWELSDNFPPHLAVVPPDQSVSAPSIFSPVRLAQTLLIMSSLWYDDHTDLAPGPEQNTMQKLTQWNQERHKDQGWLIKDMFNAPNIGLRNDWYTDEVFAQQFFTGPNSTTITLASDVWLTAFTSEAKAQGKDKVIALFESAPPNSFYVQDFSDFRRRMGAKPDEELFNDSDGAMRYGCAAVALFYLTAMGKLHPLAIIPDYKGSMAASVTIFNKRTNPLDISVNQANDWPWRYAKTCVLSSDWALH... | Cofactor: Three His residues, the carboxyl oxygen of the C-terminal Ile or Val residue, and a fifth residue, usually Asn, ligate the metal, which binds water to form a catalytic base Mn(2+)OH(2) for hydrogen abstraction.
Function: Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 13S-hydroperoxy fatty... |
Q8KBD3 | MSSPQHVIIGLSGGVDSAVAACLLIKQGYHVTGLNIRVLDTPEDTPTLAPSAMRISDSEEFDFPVFTLNLSAKFARDVVGYFHDDYLAGRTPNPCMVCNKAIKWFGLFEAMRLLRADLVATGHYARTELRDAVTRLLKGVDPEKDQSYFLWMLTQAELAKTLFPLGGYTKAEVRELARSFGVHAAEKKESQEICFVPHDDYCAYLANAIPGLEARVAGGEIVDQAGKVIGHHRGYPFYTIGQRRGLGVSTGEPVYVTEIDAEHNRIHVGSKADLECRSLIASGMNWIGIATPDKSFEAEARIRYRDRQSACMIEPMDDNR... | 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): 40211
S... |
Q18BE2 | MFMNKKVMIGMSGGVDSSVAAYLLKQQGYDVIGVTMKLWQDDDVVEIEGGCCSLSAVEDARRVANKIGIPFYVLNFREVFKEKVIDYFIDEYLEGKTPNPCIACNKHIKFDDFYKKARQIGCDYVATGHYAKIEKDESTGRYLLKKSVTDKKDQTYALYNLTQEQLEHTLLPIGDYEKDRVREIAKEMGMAVHNKPDSQEICFVKDNDYANYVKKHSKKRIEEGFFVDTKGNILGKHKGILYYTIGQRKGLGITFGKPMFVIDINPINNTIVLGDNEDLFKKELIAKDVNFISIDTLEEPLRVQAKIRYSAKPSPATIHR... | 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): 40848
S... |
Q7NBZ0 | MLSIINLTSKTIKEVNKGVDLVIGFFDGIHKGHAKLFKQSDRFNLLTFDHIPKKQRLLYPKVDEIEQLSALSGLEQLLVYDLLNNNLSAQEFIDNYIKLIQPKRIIVGSDFKFGSDQVDYSLFAKNGYEVVVVKKDHCSTSEIKKLIINCDLDQANKLLLTPFYLKGTVIKNAQRGRTIGFVTANIILDNQLIELTEGSYVCKVIVDNKTYQGICFIGKPKTFDEKQRQCEAHIFDFDQDIYGKKIKVELYQFIRPTVKFNSINELKEAIENDKKAALSFFHKQEKPKVVVALSGGVDSAVCAYLLQQQGYDVVAAFMQN... | Function: Involved in FAD and FMN biosynthesis.
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Mass (Da): 75974
Sequence Length: 657
Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
Subcellular Location: Cytoplasm
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Q6MTG1 | MKQKVIVGLSGGVDSSVACYLLLEQGYEVEGLFMRNWDSATNNDILGNRNINDDICPQEQDYLDAKAVADKLNIKLYRVDFIKEYWDYVFSYFIEEYKKARTPNPDILCNKYIKFDKFLNYAINQLNADYIAMGHYAKVEFNKTTNQYELIKASDTNKDQTYFLSQLNQKQLSKTLFPLANLTKEQVRKIALKQNLITANKKDSTGICFIGERSFTNFLQNYIPNQTGDIVDIKTNKVLGQHIGVMYYTIGQRKGINLSGMSEPYYVADKDVKKNILYVCSTSDQSYLHSTSCLVNDINWILDISKYVDDINQFECQAKF... | 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): 43199
S... |
P75365 | MQNKTVFVGISGGVDSAVSALLLKQQYREVIGIFMECWDNTLNNDQLGHRAFNEHKSGCSSKEDFREAQAIAQLLGIKLIKQNLVEPYWKQVFLPTIDAFKNGLTPNPDMLCNRLIKFGLMRDYCKQLDPNSDFATGHYAALSWDNNQPLLAIPKDKHKDQTYFLAHVKPAQLQDVVFPLAHLLKTEVRQIALAHHFSVATKKDSTGICFIGERHFSDFLKNYLPVKPGVIYDWKTQRQLGSHEGVWFYTTGQRSGLNLGGQAARNFVVEKDLKTNTLYVSSDPEDLQRRGITLSHFNWLYQPNPLTQTVLVRIRHAQPL... | 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): 41773
S... |
Q98Q11 | MSKIVIGLSGGVDSSVAAYLLKQQGHEVIGLFMRNWDSLVNSDILGNSSLNQSLCPQEQDFQDASRVAKQIGIPIYRVDFIKEYWDSVFENLIEQYQNGFTPNPDILCNKYIKFDKFFNYAIEKFGADYVAMGHYAIAKEGNLYRGIDQSKDQSYFLTQVRSQVLEKVIFPLGNMEKSEVRRIAQEANLYTANKKDSTGICFIGERKFTDFLQNYIPTQPGTIVDITTKKIVGNHIGAMYYTLGQRKGLNLGGMKEPYFVVGHDLEKKQVFVAPASEKKWLTSNWLFAQNLNLNNHDFNPENLSAKFRYRQKDVRVKVEF... | 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): 42409
S... |
Q97T38 | MSDNSKTRVVVGMSGGVDSSVTALLLKEQGYDVIGIFMKNWDDTDENGVCTATEDYKDVVAVADQIGIPYYSVNFEKEYWDRVFEYFLAEYRAGRTPNPDVMCNKEIKFKAFLDYAITLGADYVATGHYARVARDEDGTVHMLRGVDNGKDQTYFLSQLSQEQLQKTMFPLGHLEKPEVRRLAEEAGLSTAKKKDSTGICFIGEKNFKNFLSNYLPAQPGRMMTVDGRDMGEHAGLMYYTIGQRGGLGIGGQHGGDNAPWFVVGKDLSKNILYVGQGFYHDSLMSTSLEASQVHFTREMPEEFTLECTAKFRYRQPDSKV... | 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): 41682
S... |
Q12P60 | MPSCYEHSAQSPRPLSVLAEYFPKGYSVFYKANTETCPEANQYSKALVDFYTQELNQAEDTNLTLGQMGLGDGVSLLLLWQSLLQCRKNNPELSRLKVHLLIFEPHAISALELKQLWQALGLFDANSPVAPQAEQFIAGKMAQINGAQRFILEQGQLRIDVHFGDLHSNLTELMTPEHRVTHWHCLPHIAHTQTEFAETQASQLQFNQVQSNANQLNQAILWQMGRLSQDNASLYLDGENFKPSASDNNALTDCTLIKMATQAGFSRYSPNLFQASSDSCNAIPLGERRALRQQQENRQAHCPVPNSLGERRQAVNNSDS... | 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... |
Q084S3 | MNKTPLLSVSPNLHELHICELLGNNANQNSRYSHIVKQYIAEVLQSSDDKIAATNTQPHLLTLGQLGFGDGHEIILLLAALQEANLQNPLIQQQTRIHISVFEQGPVNCKQLQHTWQQQGLLDSDHHLFDFTQALLNGEIAAIEGCQRLSLLQNQIIIDLYQGSPLAQAKTIATPNKQRITHWFALPHTNQEAHSDQYFHQRSVWEYGRLSVDNATFLAASTNDENIAPTIKKQLAFCGFLSSTSFKSTDDIAIAERNALRQQLQQQFAYNPLPPLHSNNNSPIAIIGGGIASASLALSLAERGKDVIIYCKDDTLGQGA... | 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... |
A3QFM9 | MPNIPLRVNSLATEHPNNAQNSDKMPTFDAIFSHLSAIASHNSHQIIALLPSSDANWPAALIAERLTQAGSKQHLQKQHLHLHLFAQHQASWLKALAESETLASPAKEQIKAICDARVSGSHRLKLVNARLIIDIHLGDPLTQLKDLVSPSLASQAIQGWLANTQATDEALIWQMARLSQDNAEFLLLENNDVNLDKTSNNANTNLLTQLIIKAGFTCYRLNLSLKDDQLVTLAEKPSLASLEIAMVERRALRRQQLDKFAFNPLTQGREGETAIIGGGVASANLALSLAERGKKVSFFCMDKAPGEQASGNKQGAIYPL... | 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... |
A8H2Z3 | MTVSKILKQIIDSQTTKNVVIGQLGLGSITKLKQLITLLAHHKDKQLTLKLFVDISDTSGILLANEELTTLLCPQGSISLTAIEGCQRVIVSNCKLTIDFYLGQYLTQLQALPMVNDGFVDGWHVTSDADQTQLRQILFWQLAKLSKNDAQFSLDDTFTEVSQLELYTQAEQVGLYRYADNIPGNIQSGDEICFQERAAMRAQSRALQAPYPICSAAVTTHATCSNLGIAIIGGGVASACLALSLAERGQQVTLFCEDHALAQAASGNKQGAIYPLLTPDNNTLSQYFQQAYLFSLQRLKSLAAQGHPIDFDLCGVVHTG... | 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... |
A0KV89 | MTAKPHKSCQFKRDYPQLINLYPPCALTTAQSLDNFTRLRRSRLTTPSAQLGQELYVMGQWGLGDGLELLSLLHHWQTQTQSNTRLLVKVFEPNPINDYELKLLWDQSQSLISTPHLQPIANAILKAKPARIIGCQRLIFDDGRITVDLHFGDLHTSLTNLPHSPAHPIQQWLVLPHLASQLSGKLAWQMARLSADDAQLIGVNLAETVQQLAHSSGFSTLNVSQDALNGDASDALPSQIITDEILLHERKLLRQQADTAQAFTPKPATLAAIDHPVAIVGGGLASANLMLSLAERGQSSTLFCKDNELGQGASGNRQGA... | 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... |
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