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 irreversibly inactivated.
Catalytic Activity: a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein]
Sequence Mass (Da): 21494
Sequence Length: 194
Subcellular Location: Nucleus
EC: 2.1.1.63
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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 reaction: the enzyme is irreversibly inactivated.
Catalytic Activity: a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein]
Sequence Mass (Da): 22244
Sequence Length: 209
Subcellular Location: Nucleus
EC: 2.1.1.63
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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 Mass (Da): 3509
Sequence Length: 31
Subcellular Location: Cell inner membrane
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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-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 31057
Sequence Length: 270
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 2.4.1.129
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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 | MTVRFGLLGAGRIGKVHAKAVSGNADARLVAVADAFPAAAEAIAGAYGCEVRTIDAIEAAADIDAVVICTPTDTHADLIERFARAGKAIFCEKPIDLDAERVRACLKVVSDTKAKLMVGFNRRFDPHFMAVRKAIDDGRIGEVEMVTITSRDPSAPPVDYIKRSGGIFRDMTIHDFDMARFLLGEEPVSVTATAAVLIDKAIGDAGDYDSVSVILQTASGKQAIISNSRRATYGYDQRIEVHGSKGAVAAENQRPVSIEIATGDGYTRPPLHDFFMTRYTEAYANEIESFIAAIEKGAEIAPSGNDGLAALALADAAVRSVAEKRQISIA | 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: step 1/7.
EC: 1.1.1.18
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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 | MNTKPVLVILGPTASGKTELAFRIARQTGGEIISADSRQIYRGMDIGTAKPPRWMLDEVKHHFIDKKEIGEPFSAGDFAEQAAEKIRELHQRGITPVVAGGSTLYLEGLLKGFAELPPADPEIRAQLTRELERHGAEALYRRLEALDPEQAKTLDPTKTQRLIRSLEIIEISGTTVTALQSKTPGPPTGINFTVIGLDLPRELLYERINQRTSAMIQAGLEAEARYLFDKFRDEWRSKNLNALATVGYRELFEHFEELHDLDTAVSLIAQHTRNYAKRQLTFFRNRLDVEWVKAPLDEAEIEALVEFFSTRQDDSVPHSPIAIAKKQNA | 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(37) in tRNA
Sequence Mass (Da): 37067
Sequence Length: 329
EC: 2.5.1.75
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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(37) in tRNA
Sequence Mass (Da): 35639
Sequence Length: 314
EC: 2.5.1.75
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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(37) in tRNA
Sequence Mass (Da): 35061
Sequence Length: 302
EC: 2.5.1.75
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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(37) in tRNA
Sequence Mass (Da): 34593
Sequence Length: 312
EC: 2.5.1.75
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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(37) in tRNA
Sequence Mass (Da): 33300
Sequence Length: 307
EC: 2.5.1.75
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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(37) in tRNA
Sequence Mass (Da): 35687
Sequence Length: 309
EC: 2.5.1.75
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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(37) in tRNA
Sequence Mass (Da): 35747
Sequence Length: 309
EC: 2.5.1.75
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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(37) in tRNA
Sequence Mass (Da): 34500
Sequence Length: 315
EC: 2.5.1.75
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Q6MBT2 | MIGNFSCETDEIKRIVLNFALQVQKKFPSNFQKNKKRIIVIAGPTCCGKSALALNLAQTMDGEIISADSMQVYRGMDIGTAKATKEERLFVPHHLIDIRDIQESFNVVDFYYEARQACQKILDQGNVPIIAGGSGFYLHALLYGPPSGPPSVPEVRKSFEDEIERLGSEILYERLSQLDPQYAKTITKNDKQKIVRALEIMMLTNKKVSKLSWKGRRKPQNYDFRCWFLHRPKEKLYERIDKRCDKMLEEGFMDEVRHLDSLGIRGNSSASQAIGYRQALNFLKTEQTASQYQEFIRSFKQATRHYAKRQFTWFRKEPLFRWLDVDMHDPEVVFDMILKDYELL | 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(37) in tRNA
Sequence Mass (Da): 40057
Sequence Length: 344
EC: 2.5.1.75
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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(37) in tRNA
Sequence Mass (Da): 35674
Sequence Length: 316
EC: 2.5.1.75
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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(37) in tRNA
Sequence Mass (Da): 35310
Sequence Length: 318
EC: 2.5.1.75
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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(37) in tRNA
Sequence Mass (Da): 36282
Sequence Length: 313
EC: 2.5.1.75
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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(37) in tRNA
Sequence Mass (Da): 34942
Sequence Length: 303
EC: 2.5.1.75
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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(37) in tRNA
Sequence Mass (Da): 34993
Sequence Length: 313
EC: 2.5.1.75
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B1XRT3 | MPTEPYIQPMHVLNEAPILCIVGPTGAGKTHLAMSLAEHAKSIGLTIELISMDSALVYRGLDIGSAKPTKAEQDAFIHHLIDIIDPTEVYSAARFANDAKRLCLEIRERGNVPVVVGGTMLYWRAWAHGLSSLPPANSEIRARLDEEGKSIGWPAMHDKLAKVDPETAARLKPNDSQRVQRALEVFEIIGKPMSVLLADSPSEDGREGSAIPSWIDLISLEPRDRKRLHLNLEKRFDEMLTAEFMNEVKALHANTRLHTDLPAIRSVGYRQAWEFLNGEIDAEQMRYKALVATRQLGKRQLTWLRAIEGRKTFDPFNPEELKAALDYCKSNLKK | 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(37) in tRNA
Sequence Mass (Da): 37460
Sequence Length: 334
EC: 2.5.1.75
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Q128B6 | MNEVKSVGAKYIALTGPTASGKTAAAMAIAQQHDVEIISVDSALVYRGMDIGTAKPTVDELAAVPHHLINIRDPLQAYSAAEFVADAQRLIDDIAARGKLPLLVGGTMLYFKALFYGLDDMPKADPAVRAELASEAAAKGWPALHAELATVDPVTAARLAPHDSQRISRALEVFRVSGQPLSFFHQQNAAKTIADDGREERTEILISLEPQERSWLHHRIAERFDAMLAAGFVEEVKTLRARGDLTPDLPSMRCVGYRQAWELLDAQEARSPGGSFPMDELRDKGIIATRQLAKRQVTWLRSMPQRQIITCDTDQALPLVLQAVAQHIEKSSR | 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(37) in tRNA
Sequence Mass (Da): 36518
Sequence Length: 333
EC: 2.5.1.75
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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(37) in tRNA
Sequence Mass (Da): 33289
Sequence Length: 294
EC: 2.5.1.75
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Q057G5 | MNEHDSSIIENILKKTNLYIITKKPEISDILILNTCSIREKAQEKLFHQLGRWKKLKQKNSKILIAVGGCVAVQEGKKIYKRAKFIDIIFGPQTLHKLPKLLIESNKKKSLIINIKKKSLKKFNYTINKNTNIKKKFSSFVTIMEGCNKYCSFCIVPYTRGKEVSRNNKKIISEIIELSKKGVREITLLGQNVNAYKFSDTFNKKNYSFSDLLYSISEIPRIDRIRFITSHPVEFNNNIIEAYKKIPKLTNFLHLPVQSGSNKILKLMKRGYTIEKYENIVNKIKKIRPKINISSDFIIGFPGETKEDFQKTIYFISKINFDTSYSFIYSKRPRTRASKLEDNVTMEEKKKRLYKVQQKINQQAFQWKRRSTEQIVLVEGISKNNIQELYGRTENNRTVFFEGNPKFIGNFIKLKIISIKYNTFLKGKIISNNYF | 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 codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50960
Sequence Length: 435
Subcellular Location: Cytoplasm
EC: 2.8.4.3
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B2VBL4 | MTKKLHIKTWGCQMNEYDSSKMADLLNSTHGYTLTEQAEDADVLLLNTCSIREKAQEKVFALLGRWKKLKESNPDMIIGVGGCVASQEGAQIRQRASCVDIVFGPQTLHRLPEMINSVRGTRSPVVDVSFPEIEKFDRMPEPRADGPTAFVSIMEGCNKYCTFCVVPYTRGEEVSRPSDDILFEVAQLAAQGVREVNLLGQNVNAYRGETFDGGICSFAELLRLVAAIDGIDRIRFTTSHPIEFNDDIIDVYRDTPELVSFLHLPVQSGADRILTLMKRAHTALEYKAIIRKLLAARPNIQISSDFIIGFPGETQADFEQTMKLIGEINFDISYSFIYSARPGTPAADLPDDVSEDEKKQRLYILQDRINQQTTAWSRRKLGTVQRILVEGTSRKNVMELSGRTECNRVVNFEGSPEHIGKFVDVEITDVYANSLRGMLLRGEHQMALRTLETPASVIERTRKENELGVATWLP | 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 read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53243
Sequence Length: 474
Subcellular Location: Cytoplasm
EC: 2.8.4.3
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Q2N950 | MKPTHSPKTYRVKSFGCQMNVYDGERMAEMLDEKGIEPAPEGEDADLVVLNTCHIREKAVDKVYSDIGRLTKGKTQTKAPMIAVAGCVAQAEGEEIMARAPAVSMVVGPQAYHRLPGMIDAAVAGKRSTDTDMPADAKFAALPKRRKSAPSAFLTIQEGCDKFCTYCVVPYTRGAEISRPFSALIDEAKKLVEAGAKEITLLGQNVSAWTGEDAKGRALGMAGLIRELAKDPDLKRVRYTTSHPADMDDELIATHGEVEKLMPYLHLPVQSGNDRVLKAMNRSHTAESYLRLLERFRAARPDLALSGDFIVGFPGETEAEFEDTLKIVDEVRYAQAYSFKYSPRPGTPAATMERQVPKEVMDERLQRLQAALNRDQAAFNAGSVGRTCEVLVERTGKHPGQWLGKSPWLQSVWFDGDVAIGDLVQVELVEAGPNSLAGQLLETVAA | 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 read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 48782
Sequence Length: 446
Subcellular Location: Cytoplasm
EC: 2.8.4.3
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A6H119 | MEKIIEESKQGGSLILENKPENTKKLFIESYGCAMNFSDSEIVASILSGNGYNTTNVLEEADLVLVNTCSIRDKAEQTIRKRLEKYNAVKRINPKMKVGVLGCMAERLKDKFLEEEKIVDLVVGPDAYKDLPNLLNEVEEGRDAINVILSKDETYGDISPVRLMSNGITALVAITRGCDNMCTFCVVPFTRGRERSREPQSIMAEIQDLWHKGFKEITLLGQNVDSYLWYGGGLKKDFTNASEIQKATAVDFDQLLEMVAVGFPKMRIRFSTSNPQDMHESILHVMAKHSNICKHIHLPVQSGSNRILKEMNRLHTREEYMILIDKIRAIIPNASISQDMIAGFPTETEEDHQDTISLMQYVKYNFGYMYSYSERPGTLAGRKMKDDVSDEIKARRLQEIVDLQQKHAWWRSEDFIGQTVEVLVEKVSKKSTEEFSGRNSQSITVVFPKEHYKIGDFVNVKIKSCTSGTLKGEAVGYSEMN | 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 read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 54572
Sequence Length: 481
Subcellular Location: Cytoplasm
EC: 2.8.4.3
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Q8RG43 | MKKASIITYGCQMNVNESAKIKKIFQNLGYDVTEEIDNADAVFLNTCTVREGAATQIFGKLGELKALKEKRGTIIGVTGCFAQEQGEELVKKFPIIDIVMGNQNIGRIPQAIEKIENNESTHEVYTDNEDELPPRLDAEFGSDQTASISITYGCNNFCTFCIVPYVRGRERSVPLEEIVKDVEQYVKKGAKEIVLLGQNVNSYGKDFKNGDNFAKLLDEICKVEGDYIVRFVSPHPRDFTDDVIEVIAKNKKISKCLHLPLQSGSSQILKKMRRGYTKEKYLALVDKIKSKIPGVALTADIIVGFPGETEEDFLDTIDVVQKVSFDNSYMFMYSIRKGTKAATMDNQIEESVKKERLQRLMEVQNKCSFYESSKYKGRIVKVLVEGPSKKNKEVLSGRTSTNKIVLFRGNLALKGQFINVKINECKTWTLYGEIV | 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 read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 48996
Sequence Length: 435
Subcellular Location: Cytoplasm
EC: 2.8.4.3
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A9FST8 | MPRYSITTFGCQMNVHDSERMHDVLRCAGYTEAGSADEADVLVLNTCSVREKAEQKLRSEVGRLARWKRERADRVLVVAGCVAQQEGERLLKQMRAIDVVVGPDNIPELPGLLGDLAIGGLPIARTVFDLDAPRFLVASPPSPSSSSSPRAAPTAFVTVMKGCDERCSFCIVPHTRGPERYRPSDEIVAEIAALVAAGTREVTLLGQTVNSYRDPLGALPRAPGASADDPDESEFAALLRRVAADVPGLARLRYTSPHPRHLTPSLVLAHAELPVLPRHVHMPVQSGSDRVLRRMIRRYTRAEYVARTRALVEAVPGLTLSTDIIVGFPGETEDDFAATLSLVREVGFKGLFGFKYSRRPHTPALKLPDDVPEGVKGERLARLFEESEALLAAHLSALVGTTQEVLVEGRDKERGHGGAGGALWSGRTGRHEIAHIDGAGELDLLGEVVEVSIARANKHSLQAELTEAARAAARPRQRGGLEPRPARRSLPVVAAEGG | 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 read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53788
Sequence Length: 498
Subcellular Location: Cytoplasm
EC: 2.8.4.3
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Q9ASV5 | MLRKSVLELSSRLSIKRFPRNLGAQRFHLSSSRNASTSGKNGLPGAKPVGKPDASKVDPPKVTPPPPTKGNSSKVVIGGVAIAGAFLVAYQTGYLDQYLGKEQQKLSERIHSDALTEKLEEAHHLNVPSGVEDSTEKDGKVETQPQVTHSEASEGVQSDIELQPESDLSSDRFTYISSNQEETPQETVIDRAEINLPISASEDSGAKPDMPSEIISEAESVKLEAVPKPGDSPIIVNAQSSSVHRESETESASPKDPAALKTPEDGIEREVQLPGSLLKEYNLEGSDTESTGSSSIGEQITKETEAFPNSTEGLKDSYMTEDGKLVLDFLAAIHAAEKQQAHLDAQVFAEELRALKEKYENELRDLRARELMRIEEAAILDKELKRERTKAAAAIKAIQERMEDKLKAELEQKETEAQLALSKAEELAKAEMISTIAKEKAAQIEKMAEADLNIKALSMAFYARSEEARQSHSVHKLALGALALDDTLSKGLPVQKEIDTLQTYLEGTHKDSILGLVLSSLPEEARSNGTDTVLQLNQKFDTLKGTLRHFSLIPPGGGGILAHSLAHVASSLKFKEVDQANGGIESVIKKVDNYLAEGKLAEAAATLEEGVKGSKAEEIVSDWVRRARNRAITEQALTLLQSYATCVSLT | 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 the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity). Involved in the maintenance of mitochondria morphology . Binds to glycerolipids such as cardiolipin (CL) . Contributes to the export of phosphatidylethanolamine (PE) from mitochondria and to the import of galactoglycerolipids from plastids during phosphate (Pi) starvation . Promotes lipid desorption from membranes, likely as an initial step for lipid transfer, and regulates probably the tethering between the inner and outer membranes of mitochondria by binding to TOM40 proteins .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70553
Sequence Length: 650
Subcellular Location: Mitochondrion inner membrane
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Q754G4 | MLSSRAAAFTGRRLASTLPPVPRKKSHGVRRLLAKAVVATSLFYAGGLTLSAYNDKANELFVEHVPFGEELVERWEDWTSLRRPGRRMIDARRVDEISRDFRAAATPEATPVVVRPLVQLQLPELQMQGSSPVLEALVNNVNDVVVALNARALELPEDTASALSSVYGEIVHSIQALNASLDQEFATEVESRTGKAISSVQEQLEVEYKQRELALAEQYIQNFEVFKSQLQKATAEQLETELKAHEQALLARHRNEVAQLSIRQVEEFNKIIEKKLDQERNGRLAKLSELNSAVESLAPVLDRLELRAVKNECVTQLSTLISDIQGKLSRGGDEPLDLSSDLQRLTLLADILPRPKRCCSEGPALLDVAMAELQAKAQAPVASNEQLYNRWQLLQPELKTTSLLPPNAGFLGHLTAKLFSMLLFTKEGFSTTQDMDAVTARIAENLRLNKLDCALEEAVNMKGWSRKSADAWVDLARRRLEVLTLLDVIEAEVKTL | 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 boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 55227
Sequence Length: 496
Subcellular Location: Mitochondrion inner membrane
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A2QI68 | MVVRPMMLRSSVAPGRQLLLSSARQRTASQWLSRAGASSRLSGQRFFADIKPPTTAAPTPATPSSESAVPPETVPKPSPAGQESTLPPSTPPTPAPKGGRFRRFLLYLLLTSGFAYGGGVFLALKFDNFHDFFTEYIPYGEESVLYFEERDFYRRFPNTLRNQNRLNPTPRDEGNKITIPSKSGLTSKVAEEEISGADVSQKGPHMSATPAQKSSEAQTKPAAAKPEDKTTAVVKAKEDKAAKEAEKKEEPRQPAIPAVTPLEFAQVNEGDEAIVQELVKTFNDMITVISADENSGKYSQPVAKAKEELQKVGEKIIAVREEARRAAQEEIQQAHATFDESARELIRRFDEMRAADAAQYREEFEAEREKLAHAYQEKIRTELQRAQEVAEQRLKNELVEQAIELNRKYLHEVKELVEREREGRLSKLNELTANVSELEKLTSGWREVIDSNLRTQQLQVAVDAVRSVVDRSAVPRPFVRELVAVKELAAEDPVVEAAISSINPAAYQRGIPSTSQIIERFRRVADEVRKASLLPEDAGIASHAASVVLSKVMFKKDAVAGSDDVESVLYRTESLLEEGNLDAAAREMNSLSGWAKILSKDWLVDVRRVLEVKQALEVIETEARLQCLRVE | 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 boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70199
Sequence Length: 631
Subcellular Location: Mitochondrion inner membrane
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C5JIS0 | MLRTSIASSRQVLSSPICPNPSVQWLHTSRARRVNAAASRRYYAVARKPNAGVRSSSTPNAAATPELSQKATNSTSTKPPGPNDPDVRSPASPSTGSTLHPETVSKPPQSPAVQGQTSPGSSVQPPEHEPSPPPPRPPPAPKTGLLRKLLYLFLTTGLAYAGGVWYSLRSDNFYDFFTEYIPYGEEAVLYLEERDFRSRFPSIARQINRRVSAPRDEGAQVMIPGRSGLSWKVAEEQQEASDVTKQGQHISATDANELTEETKVAEKAKEDVKSKPVAKKAEAAEPKSSPKVVEPHPAKAEENTSLEAPRQPVVPAAAAIEHLGLDNEDEPVVQDLVKVFNDIITVISADESASKFSVPIAKAKEELEKIGDRIVALKNDAQESAKEEIRNAQAALDKSAAELVRHINEVRAQDAAEFREEFESEREKISKSYQEKVTTELQRAHEVAEQRLRNELVEQAIELNRKFLADVKTLVENEREGRLSKLAELTANVAELERLTAGWSDVIDINLRTQQLQVAVDSVRTTLENSEVPRPFIRELAAVKELASNDEVVAAAIASISPTAYQRGIPSPAQLVDRFRRVASEVRKASLLPENAGITSHAASLVLSKVMLKKQGTPVGNDVESILTRTENLLEEGNFDEAAREMNSLQGWAKLLSKDWLADVRRVLEVKQALEVIETEARLRCLQVE | 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 boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75756
Sequence Length: 689
Subcellular Location: Mitochondrion inner membrane
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Q5A044 | MIRITSRSVKGAAGIRSVSSSTVRLNIAPKVVSPPVPPPVKPQGSEIPPPPPPPPPPPKAKRFSLFGFLFKTTLLATVVYGGTLYAATKNDKVMDFVIDKQLPFHEELIDLIENGSTEDLQEAWEQLKNKFTDVKLPTKDDIDELTQKLEHRGEDIIKETKKKIASTHIGHKSGTDLTPTEQLQRGVEIESVKKDVAHLPLIELNSDLGKSVDETVKQTITSFNNFIQSIDASSLATKDDKLITSINTSVNQLASRLNSLTKDFDNELQNKLKVSQTELFSSFTKKELELTENLLHQFSTEKQQLEAKLNQKLSQEIQAARAAISQAASNAVAMVRIEQTKNFEKLVSEKLNEERNGRLANLEKLNDRIVELEKFAEGFETQIVSNHKKAIIHQAVSKLKSLLLAPAAGDKPQPIKPYIDELTKIATDDEVLALAIKDLSPLITNESTHSILTNAQLLSRWEQLAPELRSASLLPPNAGLLGHLASIVFSKLLLPVKGVKEDGKDIESVIGRVESSLARGELDIAVEEAANLKGWSRKLANDWVVEGRKRLEIEFLLGLIESESKII | 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 boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 62702
Sequence Length: 567
Subcellular Location: Mitochondrion inner membrane
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Q6FSU7 | MLRTKITGSSHVLRTAFKRYSSTIDSGAVEVVKPKKTSFTRRLFRLGLAVTAFYAGGVAVSQYDDDLGTLFTEKVPGAEKLVDSYVTYRYDPTISKMLSTEYLLNLFKGENTEVKPSTSSRLVPIHDAIKELHLELLELDSENNSEPEMQKIINSLNSTINMINEQKLRIGGKKSRSIEENYKQLIEDILHLDKNLKETVSKSINEKTEEVVKKVREQYKRKLAVSEVELQDKYKNEFIHLKEEMEKHYQDILNQKLEANKQHLEAKHANEIALLSITQVSEFNKIIKEKVDSERNGRLAKIEDLDKKAENLTEALKHVNKVVTRNEAVKQIAQQIEIIRSKLNSHDLNSISLHDDLTRLRTLTDIAVPGPKPCCKHKDLTPSLFRVALDELESVAGSSESKILSEEQIYNRWNLLESDFKTASLLPPNAGMLGHFTAKLFSLFLFTKRGSALPDATDLDSVFARINENLRHSKLDKAVADVVTLKGWTHVLCDDWLKNARRKLEVEKLVDVLDSELKSL | 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 boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59193
Sequence Length: 520
Subcellular Location: Mitochondrion inner membrane
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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 membrane insertion of MifM is impaired, which induces arrest of MifM translation and unfolding of the mRNA hairpin. Unfolding leads to translation of the downstream gene, which encodes the secondary membrane protein insertase MisCB/YqjG. Translation arrest of MifM is mediated by interaction of its C-terminal domain with the ribosomal polypeptide exit tunnel. Undergoes multisite stalling, which may allow a sufficient duration of ribosomal stalling and consequently sufficient levels of MisCB/YqjG.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11144
Sequence Length: 95
Subcellular Location: Cell membrane
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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 tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity.
Catalytic Activity: 3-phenylpyruvate = enol-phenylpyruvate
Sequence Mass (Da): 12343
Sequence Length: 115
Subcellular Location: Secreted
EC: 5.3.2.1
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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 | MDDSTPYPVPQELYIPQKMKAFMAEPQGCALVAALEGQFQCSIVVINDHLSVISSADGVAVDINQIEKILRDVWRKRDVQIMIREAALNASCTHICHTLLPRAYCAVVLFFSSDLQRRSRCTDIIIDQFTGKVTMFGTEQAVNKAREMMIECLTEHFGLLEMNIPPTQRTTRMGYTNSYNPEIRTHLPPNSFLNSVFPMGEPNAILTSTPPTTSIMDEPLLSASLEKHLLFPSDFSVPPPRLSPVQELPLTPPKTCVVEKIKQWIPTTEVGKILGNRAAVKKHIERQFNCVITVHTEVQSSFGATPVEIVAQNKEQCQEARNAVMSLMQSHQDKPASNPPDSGFSTPGSPFTSDSSSTTPEKRGNSRQYHRGSFRDQPKVMLALTPRKLSPSD | 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 germline .
Sequence Mass (Da): 43736
Sequence Length: 393
Domain: The KH-like 3 domain is required for binding to RNA.
Subcellular Location: Cytoplasm
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O34375 | MSVQWGIELLKSAGLFFLHPLFWFFIIITLAFGYVRIKRERKTFHTRIADIYDDLKFTYTKGLIPGLLLSVILGGLGISIPLGLLAIIAVITAAAAFTLRANWMSAAYIVSVSMLIGFGLQIYQAEPFLERFPQGFAVVWPAVAVFLGLLIITEGAVAYRSAHVRTSPALVVSSRGLPIGQQLANRVWLLPLFLLVPGNGLESHLSWWPVFTVPGGSFHFLWIPYFVGFGQRVQGSLPETSIRITAKRVCILGLAVAVLGAASLLWTPLAGAAVCTALLGRIFLSIKQRVNDNAAPFYFSKRDQGLMVLGIIPNTPAEDLELKIGEIITKVNGIPVKNVSDFYEALQHNRAYVKLEIIGLNGEIRFDQRASYEGEHHELGILFVKDDREDEAVASGS | 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 MinD.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43666
Sequence Length: 397
Subcellular Location: Cell membrane
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F2M971 | MAVVVALLINPVGLVFWLALGLTIWFAVNRTDRERRRYLRAIHPKHPEIGRFFWIGLVVGALVSLVMVIGRLQISLAALLALSGLTLVALLFSKWRFSPWWLGLASLAAVGQSGLLAEQHAANLAILVGLLWLTQAGLARFNRGDEIESPVIQQDRRQRQSAAFELRQLFWVPLILPVAVENVSNLPLLAVTVQSLTFVGLPLLLGATFMTPRDRAQTAWRRSWPWYGGAGGVLIVYGIVARTMTLPLLVSLVFPAVVSLVLVGGFIWQGRQVHLTVTLADQGVVLIGVVPHTPAAEMGLQPGDRVLACNHHSVNNSRELYDAIQKEPTYCRLRLRQADGELRLAETAIFAGAPHELGMILFPEETA | 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 MinD (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40349
Sequence Length: 367
Subcellular Location: Cell membrane
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Q54ND5 | MMVKIKNIIILFCIFGLLSNVSSLSSSSSSSQSSDNNGNLSPIQDYDLEFLSKHLTTKTPYWILTKNGDSNSQGDGSSGNSNSNSNSNSNSNSNSDSSNEPPEQCKLISIDFIARHGSRMPVLNSIEKLKEMTTSILEYKEQVNQGFNWIFNYSVPYPSDIAGNLILQGQYEHYNISKRLLKKYPLFFEPMKYKPQSYSITSTAISRTGISASAFSYGLLQGTGSLGVDGFQPVFIETASLDQDILLRFFATCNQYVDQLKNGTLINKDEQTKWNQMVFPNISNEISERLGLSDIWLPTSNVISDIFEACAYEISINNISDHWCSLLSKQNILDWEYSQDLSNYWLKSYGHEINYQIATPLLNDILSGFDIYINNNNNGSSSSSSSSSSNNGDNSGSNGSSGSGSSTSTSSNDNGSTNNNDNKVEPTSILRFGHAETIIPFISLLGLYKDEQKLFANSSTEQIENRKFRTSVVSPYASNIAMFLFDCGSAADGFKILVQHNELPVLVPGCDEIYCDYQQFKSIFKQGIDNFKWNSYCNINDDDSGSSGGDSGNGNGNDSHSKKSSYFLAIFIPITFLVGGTIGGIFTYFSYEKIMQVKNRKKLTQYGNDEFISSPKSKSFSFKPTKFDSRSPLIQ | 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-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate.
Catalytic Activity: (2R)-2,3-bisphosphoglycerate + H2O = (2R)-2-phosphoglycerate + phosphate
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 70382
Sequence Length: 635
Subcellular Location: Membrane
EC: 3.1.3.62
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Q9VV72 | MRLLILLLLPLVAIAQDDYCFSKDTSRLQTRQFSSKTAYQIVKGTDIDKQYLVPGCQPQKMWIFHRHGTRLPKKSMINKASRVAELRDLIINNYQVARTKPETDALCQTDLIAIKLWKWNSSITPDMEEYLTAQGYEDLRGTAKLYQRYYPTVLTANYNDTYYQFRHTDTQRTTESFKAFAEGLFGSQNAAHPVEIPKQDLLLRPYDYCSSFKNVNYKDEGSEYYKFHQSKLYNDTLADISTRLGFLYTLEEADIKLMYDMCRYEQAWNVDRNSVWCGAFLPEQITVFEYLEDLKYYYGSGYGFPENAHLNCRLVQDLLTHLSNPVSPHVVAHFGHSTGLLTLLTALGIQKDDIKLRADNYDSLTSRRWKSSLIDPFAANFVAVKYDCPADLDREKVVFFLNQQAVQLDWCSVGLCKWSDVLEKYKTIADADCGEYYCRTGGAPSLGSGVGGLLATTLAAMLVYLMH | 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 phospho-D-glycerate without formation of 3-phosphoglycerate (By similarity). Has a role in embryonic tracheal development where it localizes to the leading edge of actively migrating branches . In these leading cells, enhances formation and/or maintenance of filopodia which may drive branch migration and elongation by cell-cell intercalation . The function in tracheal morphogenesis is dependent on its inositol polyphosphate phosphatase activity .
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Catalytic Activity: (2R)-2,3-bisphosphoglycerate + H2O = (2R)-2-phosphoglycerate + phosphate
Sequence Mass (Da): 53571
Sequence Length: 467
Subcellular Location: Cell membrane
EC: 3.1.3.62
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Q9UNW1 | MLRAPGCLLRTSVAPAAALAAALLSSLARCSLLEPRDPVASSLSPYFGTKTRYEDVNPVLLSGPEAPWRDPELLEGTCTPVQLVALIRHGTRYPTVKQIRKLRQLHGLLQARGSRDGGASSTGSRDLGAALADWPLWYADWMDGQLVEKGRQDMRQLALRLASLFPALFSRENYGRLRLITSSKHRCMDSSAAFLQGLWQHYHPGLPPPDVADMEFGPPTVNDKLMRFFDHCEKFLTEVEKNATALYHVEAFKTGPEMQNILKKVAATLQVPVNDLNADLIQVAFFTCSFDLAIKGVKSPWCDVFDIDDAKVLEYLNDLKQYWKRGYGYTINSRSSCTLFQDIFQHLDKAVEQKQRSQPISSPVILQFGHAETLLPLLSLMGYFKDKEPLTAYNYKKQMHRKFRSGLIVPYASNLIFVLYHCENAKTPKEQFRVQMLLNEKVLPLAYSQETVSFYEDLKNHYKDILQSCQTSEECELARANSTSDEL | 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 phospho-D-glycerate without formation of 3-phosphoglycerate. May play a role in bone development (endochondral ossification). May play a role in the transition of chondrocytes from proliferation to hypertrophy (By similarity). Through the regulation of intracellular inositol polyphosphates, may control intracellular cation homeostasis, including that of calcium and iron, hence affecting free cation availability required for neural cell signaling .
Catalytic Activity: myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate (mixed isomers) + phosphate.
Sequence Mass (Da): 55051
Sequence Length: 487
Subcellular Location: Endoplasmic reticulum lumen
EC: 3.1.3.62
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Q9Z2L6 | MLRGARSHLPASVAPAAVLAAALLSSFARCSLPGRGDPVASVLSPYFGTKTRYEDANPWLLVDPVAPRRDPELLAGTCTPVQLVALIRHGTRYPTTKQIRKLKQLQGLLQTRESRDGGSQVAAALAEWPLWYGDWMDGQLVEKGRQDMRQLALRLAALFPDLFSRENYDRLRLITSSKHRCVDSSAAFLQGLWQHYHPGLPPPDVSDMECGPPRINDKLMRFFDHCEKFLTDVERNETALYHVEAFKTGPEMQKVLKKVAATLQVPMNSLNADLIQVAFFTCSFDLAIKGVHSPWCDVFDVDDARVLEYLNDLKQYWKRSYGYTINSRSSCNLFQDIFLHLDKAVEQKQRSQPVSSPVILQFGHAETLLPLLSLMGYFKDKEPLTAYNFEEQVNRKFRSGHIVPYASNLIFVLYHCDNAQSPEEQFQIQLLLNEKVLPLAHSQRPVGLYEELKTHYRDILQSCQTSKECSPPKANITSDEL | 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 inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). May play a role in bone development (endochondral ossification). May play a role in the transition of chondrocytes from proliferation to hypertrophy (By similarity). Through the regulation of intracellular inositol polyphosphates, may control intracellular cation homeostasis, including that of calcium and iron, hence affecting free cation availability required for neural cell signaling .
Catalytic Activity: myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate (mixed isomers) + phosphate.
Sequence Mass (Da): 54537
Sequence Length: 481
Subcellular Location: Endoplasmic reticulum lumen
EC: 3.1.3.62
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Q5NU14 | MAEAAVASTVTLPVTGGWTKHVTCRYFMHGLCKEGDNCRYSHDLTSSKPAAMMCKFFQKGNCVFGERCRFEHCKPTKSEEVSNPQMLLLSSTPPPIDPECSESGPRLKTQDWANAAEFVPGQPYCGRAESVDVEISIPLIEELNGDATTDKEELRKQLCPYAAVGECRYGVNCAYLHGDVCDMCGLQVLHPTDSSQRSEHTKACIEAHEKDMEISFAIQRSKDMMCGVCMEVVFEKANPSERRFGILSNCSHCYCLKCIRKWRSAKQFESKIIKSCPECRITSNFVIPSEYWVEDKEDKQKLIQKYKDGMGRKPCRYFDEGRGICPFGANCFYKHAFPDGRLEEAQPQRRQTGSSSRNRNSRRTQLWDIIDERESTGSLDNDDEEMVTFELSEMLLMLLAAGNDEEVTDSEDEWDLFHEELDDFYEIYL | 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.
Sequence Mass (Da): 48903
Sequence Length: 429
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q9H000 | MSTKQITCRYFMHGVCREGSQCLFSHDLANSKPSTICKYYQKGYCAYGTRCRYDHTRPSAAAGGAVGTMAHSVPSPAFHSPHPPSEVTASIVKTNSHEPGKREKRTLVLRDRNLSGMAERKTQPSMVSNPGSCSDPQPSPEMKPHSYLDAIRSGLDDVEASSSYSNEQQLCPYAAAGECRFGDACVYLHGEVCEICRLQVLHPFDPEQRKAHEKICMLTFEHEMEKAFAFQASQDKVCSICMEVILEKASASERRFGILSNCNHTYCLSCIRQWRCAKQFENPIIKSCPECRVISEFVIPSVYWVEDQNKKNELIEAFKQGMGKKACKYFEQGKGTCPFGSKCLYRHAYPDGRLAEPEKPRKQLSSQGTVRFFNSVRLWDFIENRESRHVPNNEDVDMTELGDLFMHLSGVESSEP | 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 (By similarity). Plays a role in the regulation of spermiation and in male fertility (By similarity).
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.
Sequence Mass (Da): 46940
Sequence Length: 416
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q9ERV1 | MSTKQVTCRYFMHGVCREGSQCLFSHDLANSKPSTICKYYQKGYCAYGARCRYDHTKPPAAAGGAVGPAPNPSPSSGLHSPHPSPDIATSVMRTHSNEPGKREKKTLVLRDRNLTGLAEDKTPPSKVNNPGGCSDPQTSPEMKPHSYLDAIRTGLDDLEASSSYSNEPQLCPYAAAGECRFGDACVYLHGDMCEICRLQVLHPFDPEQRKAHEKMCMSTFEHEMEKAFAFQASQDKVCSICMEVILEKASASERRFGILSNCSHTYCLSCIRQWRCAKQFENPIIKSCPECRVISEFVIPSVYWVEDQNKKNELIEAFKQGMGKKACKYFEQGKGTCPFGSKCLYRHAYPDGRLAEPEKPRKQLSSEGTVRFFNSVRLWDFIENRETRQVPSTDDVDVTELGDLFMHLSGVESSEP | 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 in the regulation of spermiation and in male fertility .
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.
Sequence Mass (Da): 46597
Sequence Length: 416
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q13064 | MEEPAAPSEAHEAAGAQAGAEAAREGVSGPDLPVCEPSGESAAPDSALPHAARGWAPFPVAPVPAHLRRGGLRPAPASGGGAWPSPLPSRSSGIWTKQIICRYYIHGQCKEGENCRYSHDLSGRKMATEGGVSPPGASAGGGPSTAAHIEPPTQEVAEAPPAASSLSLPVIGSAAERGFFEAERDNADRGAAGGAGVESWADAIEFVPGQPYRGRWVASAPEAPLQSSETERKQMAVGSGLRFCYYASRGVCFRGESCMYLHGDICDMCGLQTLHPMDAAQREEHMRACIEAHEKDMELSFAVQRGMDKVCGICMEVVYEKANPNDRRFGILSNCNHSFCIRCIRRWRSARQFENRIVKSCPQCRVTSELVIPSEFWVEEEEEKQKLIQQYKEAMSNKACRYFAEGRGNCPFGDTCFYKHEYPEGWGDEPPGPGGGSFSAYWHQLVEPVRMGEGNMLYKSIKKELVVLRLASLLFKRFLSLRDELPFSEDQWDLLHYELEEYFNLIL | 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.
Sequence Mass (Da): 55645
Sequence Length: 507
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q9N373 | MPRHETDCRYFANGYCSKGNTCTFTHDVATRNENICHFNLVGKCSYGRACRFLHTRPRNDELPSCSTPQTSQNQQNLQNSGQRVRPKQLPELKFNAQAAEFVPRWKMPQRGPVTSYAGAAASADHGESSSSFQSSHEQAQLMMCPYHQKSGDCNRQDMDCPFAHGNYCDMCQQWSLHPYNAELRKKHENECVANHTTEMERAFLLQKTEQKTCGICMENIFEKNLRFGILNGCQHCFCLDCIRQWRSKDQENVELATKTVRSCPECRQHSDYVIPSLFWVESGQEKDLLIEMYKENTKRKICKYYSNERSRGACPFGNKCFYKHQLPDGSIDPGEAPSSRRRPRLVDFLFDDNSDSDEETFRRFQEEHEEEQEELLRFVAETLPEADEESELFRQITEVLRHYQISGHRRGFQ | 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 degradation of lin-28 also controls the timing of the sexual differentiation of individual neurons in males including the AIM, AWA, ADF, ASJ and CEM neurons . Plays a role in governing the developmental timing of male tail tip morphogenesis . Plays a role in two aspects of male mating behavior: response to hermaphrodite contact and vulva location . May play a role in the detection of preferred food sources .
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.
Sequence Mass (Da): 48090
Sequence Length: 413
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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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 | MKDVRLPTLFEIIIVLGVFLALVLSFTVFLDLPIQLALFVSWFIAMLLGIRLGYSYKDLQNAIVHGISNGLEAVLILVSVGALIGTWIAGGVVPTLIYYGLEFIHPSIFLLATLIICSIMSVATGTSWGTVGTAGIAMIAIGEGLGIPLPLVAGAILSGAYFGDKLSPLSDSTVLASSLSKVDVLAHVRAMLYLSIPAYVITAILFTVVGFMYGGKNIDLDKVEFLKSSLQNTFDIHIWMLIPAVLVIVLLAMKKPSMPVIVIGALLGAIWAVVFQGMDIAHAIATAYNGFSIKTDVEFLNGLLNRGGIVGMLDSLVVIIFGLGFGGLLEKLGVLKVIVSTFEKKLTSAGNVTLSTLIVAFLANIFGCAMYVSLILTPKIMEDSYDRLHLDRRVLSRNSEVGGTLTSGMVPWSDNGIYMAGILGVSTFSYLPFMWLSFVAIGLAIIYGYTGKFIWYTKNNTVKAEKLG | 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
Sequence Length: 468
Subcellular Location: Cell membrane
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A0A095AMW7 | MNTTGYDILRNPFLNKGTAFSEAERQQLGLTGTLPSQIQTIEEQAEQAYKQFQAKSPLLEKRIFLMNLFNENVTLFYHLMDQHVSEFMPIVYDPVVAESIEQYNEIYTNPQNAAFLSVDRPEDVENALKNAAAGRDIKLVVVTDAEGILGMGDWGVNGVDIAVGKLMVYTAAAGIDPATVLPVSIDAGTNNKELLHNPLYLGNKHERIAGEQYLEFIDKFVTAEQNLFPESLLHWEDFGRSNAQVILDKYKESIATFNDDIQGTGMIVLAGIFGALNISKQKLVDQKFVTFGAGTAGMGIVNQIFSELKQAGLSDDEARNHFYLVDKQGLLFDDTEGLTAAQKPFTRSRKEFVNPEQLINLETIVKELHPTVLIGTSTQPGTFTETIVKSMAENTERPIIFPLSNPTKLAEATAEDLIKWTGGKALVATGIPAADVDYKGVTYKIGQGNNALIYPGLGFGLVASTAKLLTQETISAAIHALGGLVDTDEPGAAVLPPVSNLTDFSQKIAEITAQSVVNQGLNREKIVDPKQAVQDAKWSAEY | 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: 4.1.1.101
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Q48796 | MTDPVSILNDPFINKGTAFTEAEREELGLNGLLPAKVQALQEQVDQTYAQFQSKVSNLEKRLFLMEIFNTNHVLFYKLFSQHVVEFMPIVYDPTIADTIENYSELFVEPQGAAFLDINHPENIQSTLKNAANGRDIKLLVVSDAEGILGIGDWGVQGVDIAVGKLMVYTVAAGIDPSTVLAVVIDAGTNNEKLLKDPMYLGNKFNRVRGDKYYDFIDKFVNHAESLFPNLYLHWEDFGRSNASNILNSYKDKIATFNDDIQGTGIVVLAGVLGALKISGQKLTDQTYMSFGAGTAGMGIVKQLHEEMVEQGLSDEEAKKHFFLVDKQGLLFDDDPDLTPEQKPFAAKRSDFKNANQLTNLQAAVEAVHPTILVGTSTHPNSFTEEIVKDMSGYTERPIIFPISNPTKLAEAKAEDVLKWSNGKALIGTGVPVDDIEYEGNAYQIGQANNALIYPGLGFGAIAAQSKLLTPEMISAAAHSLGGIVDTTKVGAAVLPPVSKLADFSRTVAVAVAKKAVEQGLNRQPIDDVEKAVDDLKWDPKY | 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 (Da): 59118
Sequence Length: 541
EC: 4.1.1.101
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P46057 | MAVAPTSYDILMGTFRSPYLYTLTFDVLARKLQVREVNEATGGHNWLDVSPDGNTLYATVWGEPPKLTSYDIVRGGEYATTKLSRNVASQYMSGYVCSNNKAMYSACGPQVDTFLVDDNGTLLDQPAVQSFNLLQGQEKNKANGTLDFGGLRHGGHSADLSPDGTKLYVADIGRNCVWMYHVDRETGLLTEASKNIATRPHDGPRHAWPHPNGRIVYSLQEHSSYVDAFRLTDDNKLEFLEGGCIIPDEKDHDKYWADEVRLSPMADVVFGSTRGLEEGTPGFVTAWNLRPDGTFASTEATHRFQTKTSGGWANAIAVCPNLGPNGEVFMTLTDSEVGFIQILAYTSDKGFEVVDELKISTEKEHIMPATTVWL | 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. Suppresses COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus.
PTM: Phosphorylation is required for binding to YWHAZ.
Sequence Mass (Da): 30627
Sequence Length: 268
Subcellular Location: Cytoplasm
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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. Suppresses COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus.
PTM: Phosphorylation is required for binding to YWHAZ.
Sequence Mass (Da): 30432
Sequence Length: 267
Subcellular Location: Cytoplasm
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Q9CLB8 | MKKYIIYALIPFLFACGGTKTHRSSQFDEAFAKDTRGLDILTGQFSHNIDRIWGVNELLVASRKDYVKYTDRFYTRSHVSFDEGLITVETQSDLRHLQNAIVHILLMGSDANGIDLFASGDVPISSRPFLVGQVIDHLGGSITNTTTAGNFANYLLQNKLQTRRLSNGHTVQYVVIPMIANHVAVRAQRYLPLVRKMARRYNMDESLILGIMQTESSFNPYAISYANAIGLMQVVPTTAGRDIFKMKGKGGQPSKSYLFDPEKNIDAGTSYLWLLQNKYLDGITNPTSKRFAMISAYNSGAGAVLRVFDQDRDAAIVKINSLYPEQVYRILTTQHPSAQARNYLLKVDQAQKSYRVRR | 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 reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Location Topology: Lipid-anchor
Sequence Mass (Da): 40294
Sequence Length: 358
Subcellular Location: Cell outer membrane
EC: 4.2.2.n1
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Q30PQ0 | MKRGSVALFAISFFAFGWMTHALYNDAYKMIKESTLKKIKKSGALNVVLLNAPSTYYIGSDGPKGFEYDLLESYANHLGVKLNITTANTIKEALELSKNPDIHITSASLTKTPEREKEFNFGPSYFEAQEQVVCNKSLLLDGRFPSDADSLSGLRVVVGDSTSYSETIESLKKEGFDINATYTAEYSTEELISQVDTHEIDCTIIDSNIYALNQRYFKNIVLAFDISNRRQQAWILTPDSKMLKNDMYSWLNTVNQSGEMARLKDHYYSYVLFFDYYDTVMFYKRIKTRLPKYESYFKEAAVKYEIPYSALAALSYQESHWNPNAVSYTGVRGLMMLTQDTASMLGVKNRIDPQESIFGGAKHLDQMIKSVHADVTGEDRLKFALAAYNVGLGHVADAQKLAQQLGLNQNSWADLKKVLPMLSQKKYYRTLKHGYARGNEAVKYVDAIYDYRDILQKNDVEVSLTTK | 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 space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.
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 reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53052
Sequence Length: 467
Domain: The N-terminal domain does not have lytic activity and probably modulates enzymatic activity. The C-terminal domain is the catalytic active domain.
Subcellular Location: Cell outer membrane
EC: 4.2.2.n1
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Q3SJH8 | MPSLKTKGAAGKFASLLLVLALSACSRPAPPPETSGELRVGTRNSPATFYIGHDGETAGFEHDLILAFSRAQNWTLSWTEKSRPQALFDMLERREIHLAAAALPQAVVKDRHLISGPILFETPVHVVYRTADRAPRGVAGLAGKKLAFIIGSGHGPMLMRLKRKHPELSWAAVENVWPEELLAQLQAGKYDAVIINGMDFDAMRNFYPGLAVAFDLPYKQKIVWALSPGSSHAFRNALARFVERARSDGTIKRALERYFGHVKRLGSSDILGILQRRPQRLPDLREHFQEAQTLSGIDWRLLAAIGYQESQWNRLATSPTGVRGVMMLTGETADRMGVSDRLNARESILGGARYLALLKDALPARIAEPDRTWLALAAYNQGQGHLEDARRIAQARGGDPNSWADVKEALPYLSRGSYAKVMKYGYARGGEALRFAENIRNYYDILLRLEPEYDPLINLGRGEDGLPPPG | 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 space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.
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 reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 52024
Sequence Length: 470
Domain: The N-terminal domain does not have lytic activity and probably modulates enzymatic activity. The C-terminal domain is the catalytic active domain.
Subcellular Location: Cell outer membrane
EC: 4.2.2.n1
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Q87RW1 | MQIRHFNRLKRSVLLFASVLLLSACQIESQPKSEFEKIQERGVLRVGTLNNQLSYYIGPDGPAGLDYELARKFAEELGVKLEIKPAFRQADLFPALKKGDIDIIATGLNQTSQAVKRFRPGPAYYYVSQQVVYKKGQLRPRDIEQLIEYQASKDSQSEEDVNAGAQTLKIVEQSQYVPTLTALKKQYPELQFEIVGDADTRDLLKHVSTGELRFTVTDSVELSLAQRLYPDLALAFELTEDQPVSWFTRRSEDESLYAMLIEFFGNIKQSGELASLEEKYIGHIEAFDYVDTRAFIRALDDKLPRWAPLFQKYSEEFDWRLIAALAYQESHWKPKAKSPTGVRGMMMLTLPTAKSVGVTDRLNPEQSVRGGVEYLRRIVARVPDTINEHEKIWFALASYNIGYGHMMDARRLTKAQGGDPNAWADVKDRLPLLRQKRYYSQTRYGYARGDEARNYVENIRRYYQSIIGHVSQKPSIDEDTDDLQVIPPLNPELLISGAVETIAEEVSGASDITNEVDEDLDQEEE | 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 space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.
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 reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59886
Sequence Length: 525
Domain: The N-terminal domain does not have lytic activity and probably modulates enzymatic activity. The C-terminal domain is the catalytic active domain.
Subcellular Location: Cell outer membrane
EC: 4.2.2.n1
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O77656 | MHPRVLAGFLFFSWTACWSLPLPSDGDSEDLSEEDFQFAESYLKSYYYPQNPAGILKKTAASSVIDRLREMQSFFGLEVTGRLDDNTLDIMKKPRCGVPDVGEYNVFPRTLKWSKMNLTYRIVNYTPDLTHSEVEKAFRKAFKVWSDVTPLNFTRIHNGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPYSKHPKTPDKCDPSLSLDAITSLRGETLIFKDRFFWRLHPQQVEAELFLTKSFGPELPNRIDAAYEHPSHDLIFIFRGRKFWALSGYDILEDYPKKISELGFPKHVKKISAALHFEDSGKTLFFSENQVWSYDDTNHVMDKDYPRLIEEVFPGIGDKVDAVYQKNGYIYFFNGPIQFEYSIWSNRIVRVMTTNSLLWC | 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 collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion (By similarity).
PTM: The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro) (By similarity).
Sequence Mass (Da): 53921
Sequence Length: 471
Domain: The C-terminal region binds to collagen.
Subcellular Location: Secreted
EC: 3.4.24.-
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P45452 | MHPGVLAAFLFLSWTHCRALPLPSGGDEDDLSEEDLQFAERYLRSYYHPTNLAGILKENAASSMTERLREMQSFFGLEVTGKLDDNTLDVMKKPRCGVPDVGEYNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRKFWALNGYDILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVWRYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPANSILWC | 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 collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.
PTM: The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro).
Sequence Mass (Da): 53820
Sequence Length: 471
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 (By similarity).
Subcellular Location: Secreted
EC: 3.4.24.-
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P23097 | ATFFLLSWTHCWSLPLPYGDDDDDDLSEEDLEFAEHYLKSYYHPVTLAGILKKSTVTSTVDRLREMQSFFGLDVTGKLDDPTLDIMRKPRCGVPDVGVYNVFPRTLKWSQTNLTYRIVNYTPDISHSEVEKAFRKAFKVWSDVTPLNFTRIHDGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNLGGDAHFDDDETWTSSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPEKCDPALSLDAITSLRGETMIFKDRFFWRLHPQQVEPELFLTKSFWPELPNHVDAAYEHPSRDLMFIFRGRKFWALNGYDIMEGYPRKISDLGFPKEVKRLSAAVHFEDTGKTLFFSGNHVWSYDDANQTMDKDYPRLIEEEFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSLLWC | 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 collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion (By similarity).
PTM: The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro) (By similarity).
Sequence Mass (Da): 53375
Sequence Length: 466
Domain: The C-terminal region binds to collagen.
Subcellular Location: Secreted
EC: 3.4.24.-
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P50281 | MSPAPRPPRCLLLPLLTLGTALASLGSAQSSSFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQKFYGLQVTGKADADTMKAMRRPRCGVPDKFGAEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGESGFPTKMPPQPRTTSRPSVPDKPKNPTYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGGGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPRRLLYCQRSLLDKV | 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 involved in actin cytoskeleton reorganization by cleaving PTK7 . Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2 . Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis .
Catalytic Activity: Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.
PTM: The precursor is cleaved by a furin endopeptidase.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 65894
Sequence Length: 582
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.
Subcellular Location: Membrane
EC: 3.4.24.80
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Q95220 | MSPAPRPSRRLLLPLLTLGTALASLGSAQSNSFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQRFYGLRVTGKADTDTMKAMRRPRCGVPDKFGAEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVHYAYIRDGREKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTEKFLLPDDERRGIQQLYGSQSGSPTRCLLNPGQPSGLLFRISPGNPTYGPKICDGNFDTVAVFRGEMFVFKERWFWRVRNNQVMDGYPMPIGQLWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPAGGRPDEGTEEETEVIIIEVDEEGSGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPKRLLYCQRSLLDKV | 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 cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15 in association with pro-MMP2. Involved in the formation of the fibrovascular tissues in association with pro-MMP2. Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis.
Catalytic Activity: Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.
PTM: Tyrosine phosphorylated by PKDCC/VLK.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 65963
Sequence Length: 582
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.
Subcellular Location: Membrane
EC: 3.4.24.80
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P51511 | MGSDPSAPGRPGWTGSLLGDREEAARPRLLPLLLVLLGCLGLGVAAEDAEVHAENWLRLYGYLPQPSRHMSTMRSAQILASALAEMQRFYGIPVTGVLDEETKEWMKRPRCGVPDQFGVRVKANLRRRRKRYALTGRKWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYEDIRLRRQKEADIMVLFASGFHGDSSPFDGTGGFLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLRGIQQLYGTPDGQPQPTQPLPTVTPRRPGRPDHRPPRPPQPPPPGGKPERPPKPGPPVQPRATERPDQYGPNICDGDFDTVAMLRGEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPGDISAAYERQDGRFVFFKGDRYWLFREANLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFFFQEDRYWRFNEETQRGDPGYPKPISVWQGIPASPKGAFLSNDAAYTYFYKGTKYWKFDNERLRMEPGYPKSILRDFMGCQEHVEPGPRWPDVARPPFNPHGGAEPGADSAEGDVGDGDGDFGAGVNKDGGSRVVVQMEEVARTVNVVMVLVPLLLLLCVLGLTYALVQMQRKGAPRVLLYCKRSLQEWV | 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: 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.
Subcellular Location: Membrane
EC: 3.4.24.-
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P51512 | MILLTFSTGRRLDFVHHSGVFFLQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRMSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFHIRRKRYALTGQKWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSELENGKRDVDITIIFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPTRPLPTVPPHRSIPPADPRKNDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLITLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITVWKGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRVKEGHSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV | 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 lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.
PTM: The precursor is cleaved by a furin endopeptidase.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 69521
Sequence Length: 607
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.
Subcellular Location: Cell membrane
EC: 3.4.24.-
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Q9ULZ9 | MRRRAARGPGPPPPGPGLSRLPLPLLLLLALGTRGGCAAPAPAPRAEDLSLGVEWLSRFGYLPPADPTTGQLQTQEELSKAITAMQQFGGLEATGILDEATLALMKTPRCSLPDLPVLTQARRRRQAPAPTKWNKRNLSWRVRTFPRDSPLGHDTVRALMYYALKVWSDIAPLNFHEVAGSAADIQIDFSKADHNDGYPFDGPGGTVAHAFFPGHHHTAGDTHFDDDEAWTFRSSDAHGMDLFAVAVHEFGHAIGLSHVAAAHSIMRPYYQGPVGDPLRYGLPYEDKVRVWQLYGVRESVSPTAQPEEPPLLPEPPDNRSSAPPRKDVPHRCSTHFDAVAQIRGEAFFFKGKYFWRLTRDRHLVSLQPAQMHRFWRGLPLHLDSVDAVYERTSDHKIVFFKGDRYWVFKDNNVEEGYPRPVSDFSLPPGGIDAAFSWAHNDRTYFFKDQLYWRYDDHTRHMDPGYPAQSPLWRGVPSTLDDAMRWSDGASYFFRGQEYWKVLDGELEVAPGYPQSTARDWLVCGDSQADGSVAAGVDAAEGPRAPPGQHDQSRSEDGYEVCSCTSGASSPPGAPGPLVAATMLLLLPPLSPGALWTAAQALTL | 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 process. Cleaves pro-TNF-alpha at the '74-Ala-|-Gln-75' site. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin.
PTM: The precursor is cleaved by a furin endopeptidase.
Location Topology: Lipid-anchor
Sequence Mass (Da): 66653
Sequence Length: 603
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.
Subcellular Location: Cell membrane
EC: 3.4.24.-
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O49543 | MASKVISATIRRTLTKPHGTFSRCRYLSTAAAATEVNYEDESIMMKGVRISGRPLYLDMQATTPIDPRVFDAMNASQIHEYGNPHSRTHLYGWEAENAVENARNQVAKLIEASPKEIVFVSGATEANNMAVKGVMHFYKDTKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKTDGLVDLEMLREAIRPDTGLVSIMAVNNEIGVVQPMEEIGMICKEHNVPFHTDAAQAIGKIPVDVKKWNVALMSMSAHKIYGPKGVGALYVRRRPRIRLEPLMNGGGQERGLRSGTGATQQIVGFGAACELAMKEMEYDEKWIKGLQERLLNGVREKLDGVVVNGSMDSRYVGNLNLSFAYVEGESLLMGLKEVAVSSGSACTSASLEPSYVLRALGVDEDMAHTSIRFGIGRFTTKEEIDKAVELTVKQVEKLREMSPLYEMVKEGIDIKNIQWSQH | 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: 2.8.1.7
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Q8I113 | MFFLDNTDSMTSSSRGITMPNTISSHEDVGGYSPRKVGIQHDYSAVGGGGAAFHHLHTSAATPRHVATSEFYDDEEATSPRGGIEIGAGGGKMMANLRRHRQRERETYEDEDVLSSSDESSGRPIPRYVGRDTDHVFGEFEMDDEDVVMRREDGYGEDETDEDYFDEEEPVAELLPLGGGTRRVPRTPGRKNSSKCGFFDYYKLTDEHLGSGAYGSVTTCKSIKSGVEYAVKIVDKQGETHSRKRILREVNIFKTCKDHPNIVQLLDWFEDETNFYLVMEKMRGGPLLQHILQRKYFTEEEARRVTKDISLALKFMHDRGIAHRDVKPENVLCTDPNHVSPVKLCDLDLASQRPPQHERHPLSQVASEPDLASPVGSAEFMAPEVVDAYVGDSLKYDKKCDTWSLGVILYIMLAGYAPFQGMCDDEDCGWSEGKPCEDCQQDLFHRIQDGYYEFPEEEWGMISEEAKDLVSNLLKRDPVDRFNADQILSHRWLQQSAASTILQTPSNLINRKDSARDVQQMSEHFNLMNRLADTRLSARFDNKMTMSECGSDLGTATIHGDGSFLSMGGEPFGTFPRKKSVGIAIEKSRSGEFTPPISRASPTTPPPSMLNLSEDLTDSPVKRRSADDSGTFSLFSPASSNGDDSICSPPMVFVDMPSIQLFGTGALLTSVQMTPRHTTEDDASLKSFEDEQENANPIHRIETQVNV | 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
Sequence Length: 707
Subcellular Location: Nucleus
EC: 2.7.11.1
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P38888 | MVCCLWVLLALLLHLDHVACEDDAYSFTSKELKAYKQEVKELFYFGFDNYLEHGYPYDEVKPISCVPKKRNFEDPTDQGTNDILGNFTITLIDSLTTIAILEDRPQFLKAVRLVERTFPDGNFDIDSTIQVFEITIRVIGSLLSSHLYATDPTKAVYLGDDYDGSLLRLAQNMADRLLPAYLTSTGLPMPRRNIKRKWDVSEFPEFLETENNVAAMASPMFEFTILSYLTGDPKYEKVTRYAFDKTWSLRTGLDLLPMSFHPEKLTPYTPMTGIGASIDSLFEYALKGAILFDDSELMEVWNVAYEALKTNCKNDWFFANVMADTGHLFVPWIDSLSAFFSGLQVLAGDLDDAIANHLMFLKMWNTFGGIPERWNFSPPEFPPLSPLERSGAVALDNILPLEWYPLRPEFFESTYFLYRATKDPFYLNIGVHLLKDLKQRFKSNCGFAGFQNVITGELQDRMETFVLSETLKYLYLLFDEENELHNSASDVIFSTEAHPMWLPQEVRSNYKRNAKFNNSVYSSHLEICQKKDREQAGENTLSQRIVGFAKSIFHKGPPDEEATDPIIDYTIDTELPGTCSIKPHHVIGDEFWYSPMLSNFDRLFEIDSRFAATLIKPSHMHNYNAIELEPGFYNRWSNPQFSTCLIPPTTEIFELLFDLPGYHQLNPLMLENKTITFETFGGRSRLKIEKLQIYQIDYYGDLITASTFQDVSRKDIFSNACDAVASLYSPTYLYRVVAINGRILPRHGSVQIKKHSPVLTSNGTREEDEFKMDGIGINDHSQLMLECTPIINLFIV | 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.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
Sequence Mass (Da): 91246
Sequence Length: 796
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum lumen
EC: 3.2.1.24
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Q12205 | MSIARLVYSLFRRVRSVLLLFITISLLFYYTFQNEIDILNSYALNDSLPSINNYEHNTEGSSKLDPPDLSSTGSDRIATDKENGNVAVDLSDPATLREKNKYFPLLLKGSSHQIGSNLPISSLLTYKEKYPVLFEYSSPSLTSISQNDVHKIQPAMQLPPDVDMIKQIKDIFMKSWNQEQLLLKSNLRRESTWPIDLIDSLDTLYLCGETKLFQDSVNIIEDFDFRVPPLAMEVIDIPDITTRVLEGLLSAYELSMDKRLLNKAKHVADFILRSFDTPNRIPILKYFWKSDLRNRFPDRTVPSGQLTTMALAFIRLSQLTRLNKYFDAVERVFTTIRQSYNEFDMEFMLPDVVDASGCQLLTQEEIENGAHLKGSSIMKSINENFKFVHCQQLGKFLNPPIDDNSLQEQSQYQAYRINEKTVPILENLFKINDLFQSSYDILDGSSKNANAATMDPSIGSEVEAVDEIIEKRNFKDGTKKDSTKNTVGDKSLIDSQTFLTNSISNIFKFMTFRPMLPKQTENKKFNFLNSILTKSQFMPTTNELDVTIRKSYDVSLYSCRLGGILGLSSRVPHRGGVNTKYILPSSLLEMSEIITESCFMLMEEFDGLLPQKFELDPCTDETNGNCEFNGETKSRMIANGEYETFENDLDVGIKVSNYGKGGNDQKAKRNVLSKDGITETQNIKGDTVGSSKSIAEIDGDEVTQIRRVFTLGKDIKPHITTDDTMGSQWKNHPDWPFWVNKVESRRLLDSNIIESIFYMYRISGEQKWRSMGKQSFGILMQELMELNSGAKGLWQIKEFYENGEKVNNDLPSYWFSRTLKYYLLLFSDGDKVSLDKHILTQGGHIIKKK | 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; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.2.1.-
|
Q4WA38 | MMVFSDCLIFSSLIISYALGLPVVPGQTVMEPSAALPDDGDHLYTLPMFDIRPWERVSEVRLAREGYLYGPPLLGNTSFFPTGVLGDAMVARDKAAWFRDVEYVTNNVYPEWDKAAIALAKAGGIQSLSSYAVIYENQWATTLPDGVASGMLTNWTQDLLFSMERLSINPYVVRRLHPRKDRLPFAVDDRVVQHLAAGSTLEALHCDGRLFFANHSYQAPYPKTPGRWTAACTAYFFIHPRSGAFLPLAIKTNMGSDLTYTPMDETNDWLFAKMAFEMNDLFHSQLYHLANTHDVAEPVHQAALRTMSARHPVRGYLDRLMYQAYAVRPIGEEFLFNEGGFYDSSFALPNWAGKKYATDAYWEHAGHFKATNFYQDLFDRGLVDCTYGPPLTSFPFYETVAPMVEAIEEFTRAFVEAYYPDKTLMDVDNELQDWIIEATEAAKVIDFVPAPMREPEQLISVLSHMAFLAGIAHHALNGATVSEASGVLPLHPSSFNRPLPEAKGSIDSLLPWLHNETEALKQASLLVRFNRPLLDEQEGSLPYMFSGSSFLARTGAPIHDAERRFREKMWAISDEIRMRQFDERGLSQGMPFLWRSIDPRKIPYYLCV | 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. Specific towards 13-HPODE yielding 89% of the total HPODE.
Catalytic Activity: (9Z,12Z)-octadecadienoate + O2 = 13-hydroperoxy-(9Z,11E)-octadecadienoate
Sequence Mass (Da): 68749
Sequence Length: 608
Subcellular Location: Secreted
EC: 1.13.11.-
|
Q8X151 | MRSRILAIVFAARHVAALPLAAEDAAATLSLTSSASSTTVLPSPTQYTLPNNDPNQGARNASIARKRELFLYGPSTLGQTTFYPTGELGNNISARDVLLWRQDAANQTATAYREANETFADITSRGGFKTLDDFALLYNGHWKESVPEGISKGMLSNCTSDLLFSMERLSSNPYVLKRLHPTKDKLPFSVESKVVKKLTATTLEALHKGGRLFLVDHSYQKKYTPQPGRYAAACQGLFYLDARSNQFLPLAIKTNVGVDLTYTPLDDKDDWLLAKIMFNNNDLFYSQMYHVLFHTIPEIVHEAAFRTLSDRHPVMGVLNRLMYQAYAIRPVGGAVLFNPGGFWDQNFGLPASAAIDFPGSVYAQGGGGFQAGYLEKDLRSRGLIGEDSGPRLPHFPFYEDAHRLIGAIRRFMQAFVDSTYGADDGDDGALLRDYELQNWIAEANGPAQVRDFPAAPLRRRAQLVDVLTHVAWITGGAHHVMNQGSPVKFSGVLPLHPAALYAPIPTAKGATGNGTRAGLLAWLPNERQAVEQVSLLARFNRAQVGDRKQTVRDAFAAPDLLAGNGPGYAAANARFVEDTGRISREIAGRGFDGKGLSQGMPFVWTALNPAVNPFFLSV | 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-hydroperoxy fatty acids. At the end of lipoxygenation, the intermediate product 11S-HPODE from linoleic acid is then transformed into 13R-HPODE as the final product. It also acts on alpha-linolenic acid producing 11S-HPOTrE and 13R-HPOTrE with subsequent transformation of 11S-HPOTrE to 13R-HPOTrE as final product.
PTM: N- and O-glycosylated.
Catalytic Activity: (9Z,12Z)-octadecadienoate + O2 = (11S)-hydroperoxy-(9Z,12Z)-octadecadienoate
Sequence Mass (Da): 67583
Sequence Length: 618
Subcellular Location: Secreted
EC: 1.13.11.-
|
M5EES5 | MVHNISLSSRKALHNVHLPYMVQLPKPTGYNVALKNAAEGYDKARRMVAWLYDIADYESSIPQTFTLQQKTDKYTWELSDNFPPHLAVVPPDQSVSAPSIFSPVRLAQTLLIMSSLWYDDHTDLAPGPEQNTMQKLTQWNQERHKDQGWLIKDMFNAPNIGLRNDWYTDEVFAQQFFTGPNSTTITLASDVWLTAFTSEAKAQGKDKVIALFESAPPNSFYVQDFSDFRRRMGAKPDEELFNDSDGAMRYGCAAVALFYLTAMGKLHPLAIIPDYKGSMAASVTIFNKRTNPLDISVNQANDWPWRYAKTCVLSSDWALHEMIIHLNNTHLVEEAVIVAAQRKLSPSHIVFRLLEPHWVVTLSLNALARSVLIPEVIVPIAGFSAPHIFQFIRESFTNFDWKSLYVPADLESRGFPVDQLNSPKFHNYAYARDINDMWTTLKKFVSSVLQDAQYYPDDASVAGDTQIQAWCDEMRSGMGAGMTNFPESITTVDDLVNMVTMCIHIAAPQHTAVNYLQQYYQTFVPNKPSALFSPLPTSIAQLQKYTESDLMAALPLNAKRQWLLMAQIPYLLSMQVQEDENIVTYAANASTDKDPIIASAGRQLAADLKKLAAVFLVNSAQLDDQNTPYDVLAPEQLANAIVI | 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 acids.
Catalytic Activity: (9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-octadecadienoate
Sequence Mass (Da): 72324
Sequence Length: 643
EC: 1.13.11.12
|
Q8KBD3 | MSSPQHVIIGLSGGVDSAVAACLLIKQGYHVTGLNIRVLDTPEDTPTLAPSAMRISDSEEFDFPVFTLNLSAKFARDVVGYFHDDYLAGRTPNPCMVCNKAIKWFGLFEAMRLLRADLVATGHYARTELRDAVTRLLKGVDPEKDQSYFLWMLTQAELAKTLFPLGGYTKAEVRELARSFGVHAAEKKESQEICFVPHDDYCAYLANAIPGLEARVAGGEIVDQAGKVIGHHRGYPFYTIGQRRGLGVSTGEPVYVTEIDAEHNRIHVGSKADLECRSLIASGMNWIGIATPDKSFEAEARIRYRDRQSACMIEPMDDNRAWVSFREPKQGVACGQAVVFYDGDEVLGGGIIAKVNPEAPPQKILG | 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
Sequence Length: 366
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
Q18BE2 | MFMNKKVMIGMSGGVDSSVAAYLLKQQGYDVIGVTMKLWQDDDVVEIEGGCCSLSAVEDARRVANKIGIPFYVLNFREVFKEKVIDYFIDEYLEGKTPNPCIACNKHIKFDDFYKKARQIGCDYVATGHYAKIEKDESTGRYLLKKSVTDKKDQTYALYNLTQEQLEHTLLPIGDYEKDRVREIAKEMGMAVHNKPDSQEICFVKDNDYANYVKKHSKKRIEEGFFVDTKGNILGKHKGILYYTIGQRKGLGITFGKPMFVIDINPINNTIVLGDNEDLFKKELIAKDVNFISIDTLEEPLRVQAKIRYSAKPSPATIHRVGEDTIKIVFDEAQRAITKGQSVVMYDGDIVVGGGIIEKSL | 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
Sequence Length: 361
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
Q7NBZ0 | MLSIINLTSKTIKEVNKGVDLVIGFFDGIHKGHAKLFKQSDRFNLLTFDHIPKKQRLLYPKVDEIEQLSALSGLEQLLVYDLLNNNLSAQEFIDNYIKLIQPKRIIVGSDFKFGSDQVDYSLFAKNGYEVVVVKKDHCSTSEIKKLIINCDLDQANKLLLTPFYLKGTVIKNAQRGRTIGFVTANIILDNQLIELTEGSYVCKVIVDNKTYQGICFIGKPKTFDEKQRQCEAHIFDFDQDIYGKKIKVELYQFIRPTVKFNSINELKEAIENDKKAALSFFHKQEKPKVVVALSGGVDSAVCAYLLQQQGYDVVAAFMQNWDKDLNFELLSDHADDQIQGCDAKQDYEDTQKLCEQLKIKLYHFNFVEQYWNDVFLKVLEDYKKGLTPNPDVLCNQFGKFGWFINALRKQFGDDIKIAFGHYAKLITKDDEVFLVHTKDHNKDQTYFLTMLKKEQLKNIIFPLSELDKPTVREIAKQANLYVANKKDSTGICFIGERNFKQFLSNYLAIKKGPIILIDENKKIGEHDGLYFYTIGQSRRLHVGGTKEKIFVCDKDYNNNTLYVCYESSKDQYLSSVSCELEKFNWLIDTKDQLFNKKLWIRFRHRQKLQECEIVSYHDDKVIVKYTKQIGVTPGQYGVIYDQNLWVVGGGKITKIIK | 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
|
Q6MTG1 | MKQKVIVGLSGGVDSSVACYLLLEQGYEVEGLFMRNWDSATNNDILGNRNINDDICPQEQDYLDAKAVADKLNIKLYRVDFIKEYWDYVFSYFIEEYKKARTPNPDILCNKYIKFDKFLNYAINQLNADYIAMGHYAKVEFNKTTNQYELIKASDTNKDQTYFLSQLNQKQLSKTLFPLANLTKEQVRKIALKQNLITANKKDSTGICFIGERSFTNFLQNYIPNQTGDIVDIKTNKVLGQHIGVMYYTIGQRKGINLSGMSEPYYVADKDVKKNILYVCSTSDQSYLHSTSCLVNDINWILDISKYVDDINQFECQAKFRYRQIDNKVVVKKIDDNNYQVIFKKPLKAITIGQQAVFYLNDICLGGAVIDKVIK | 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
Sequence Length: 375
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
P75365 | MQNKTVFVGISGGVDSAVSALLLKQQYREVIGIFMECWDNTLNNDQLGHRAFNEHKSGCSSKEDFREAQAIAQLLGIKLIKQNLVEPYWKQVFLPTIDAFKNGLTPNPDMLCNRLIKFGLMRDYCKQLDPNSDFATGHYAALSWDNNQPLLAIPKDKHKDQTYFLAHVKPAQLQDVVFPLAHLLKTEVRQIALAHHFSVATKKDSTGICFIGERHFSDFLKNYLPVKPGVIYDWKTQRQLGSHEGVWFYTTGQRSGLNLGGQAARNFVVEKDLKTNTLYVSSDPEDLQRRGITLSHFNWLYQPNPLTQTVLVRIRHAQPLVQGHITVQPNNVVQVQLDQPIDRVTNGQYGVLYTQNGICLGSGIITASQI | 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
Sequence Length: 370
Subcellular Location: Cytoplasm
EC: 2.8.1.13
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Q98Q11 | MSKIVIGLSGGVDSSVAAYLLKQQGHEVIGLFMRNWDSLVNSDILGNSSLNQSLCPQEQDFQDASRVAKQIGIPIYRVDFIKEYWDSVFENLIEQYQNGFTPNPDILCNKYIKFDKFFNYAIEKFGADYVAMGHYAIAKEGNLYRGIDQSKDQSYFLTQVRSQVLEKVIFPLGNMEKSEVRRIAQEANLYTANKKDSTGICFIGERKFTDFLQNYIPTQPGTIVDITTKKIVGNHIGAMYYTLGQRKGLNLGGMKEPYFVVGHDLEKKQVFVAPASEKKWLTSNWLFAQNLNLNNHDFNPENLSAKFRYRQKDVRVKVEFLENDQIKVYYPEGFEAVTPGQQIALYDGQKCLGGAVIKNIYWNENELNYSV | 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
Sequence Length: 371
Subcellular Location: Cytoplasm
EC: 2.8.1.13
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Q97T38 | MSDNSKTRVVVGMSGGVDSSVTALLLKEQGYDVIGIFMKNWDDTDENGVCTATEDYKDVVAVADQIGIPYYSVNFEKEYWDRVFEYFLAEYRAGRTPNPDVMCNKEIKFKAFLDYAITLGADYVATGHYARVARDEDGTVHMLRGVDNGKDQTYFLSQLSQEQLQKTMFPLGHLEKPEVRRLAEEAGLSTAKKKDSTGICFIGEKNFKNFLSNYLPAQPGRMMTVDGRDMGEHAGLMYYTIGQRGGLGIGGQHGGDNAPWFVVGKDLSKNILYVGQGFYHDSLMSTSLEASQVHFTREMPEEFTLECTAKFRYRQPDSKVTVHVKGEKTEVIFAEPQRAITPGQAVVFYDGEECLGGGLIDNAYRDGQVCQYI | 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
Sequence Length: 373
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
Q12P60 | MPSCYEHSAQSPRPLSVLAEYFPKGYSVFYKANTETCPEANQYSKALVDFYTQELNQAEDTNLTLGQMGLGDGVSLLLLWQSLLQCRKNNPELSRLKVHLLIFEPHAISALELKQLWQALGLFDANSPVAPQAEQFIAGKMAQINGAQRFILEQGQLRIDVHFGDLHSNLTELMTPEHRVTHWHCLPHIAHTQTEFAETQASQLQFNQVQSNANQLNQAILWQMGRLSQDNASLYLDGENFKPSASDNNALTDCTLIKMATQAGFSRYSPNLFQASSDSCNAIPLGERRALRQQQENRQAHCPVPNSLGERRQAVNNSDSIAIIGGGIAGACLALSLAERGKAVTLYCKDDKLGDGATGNRQGAIYPLLTPENSHLSQFFQQAFLFSRRRLLALLHEVYPIGHQLCGVLQTGFDERSEARLEKIIQGQHWPEEIAYAVSPEQASALAGVSIDKPGFYYPNGGWICPFEFARACLEKAKSLANVEVKLNSTISCIKPLAANVDSKDASGCTSQASGTLWGLYHQGEIVGSHQQVVLASGASITAFEQTQALQMSGFRGQVSHVPSKGELAKLNTVICANGYLTPAFNSTHCVGASYVKDPEHLDFCSDEQAENGQKMQQSFPNLEWPQDIDVSDRNARVGVRMVTRDHFPMMGCAPDIEEIISRYQTLNASPQASQNNYAKQCQQYWQQTPAPVHHNLFVLGGLGSRGLSSAPLAAECLAAQLCGEIAPISATTLALLNPNRMWMRKLLKGKALC | 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 form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 82848
Sequence Length: 754
Subcellular Location: Cytoplasm
|
Q084S3 | MNKTPLLSVSPNLHELHICELLGNNANQNSRYSHIVKQYIAEVLQSSDDKIAATNTQPHLLTLGQLGFGDGHEIILLLAALQEANLQNPLIQQQTRIHISVFEQGPVNCKQLQHTWQQQGLLDSDHHLFDFTQALLNGEIAAIEGCQRLSLLQNQIIIDLYQGSPLAQAKTIATPNKQRITHWFALPHTNQEAHSDQYFHQRSVWEYGRLSVDNATFLAASTNDENIAPTIKKQLAFCGFLSSTSFKSTDDIAIAERNALRQQLQQQFAYNPLPPLHSNNNSPIAIIGGGIASASLALSLAERGKDVIIYCKDDTLGQGASGNKQGAIYPLLTPENGSLSQFFQQVFLYSRRRIQALVDDGYDIGHEWCGVLHTGFDQRSQTRLDKIIDGQAWPSEIAFAVSPHQATQLANVDIDKPGFYYPLGGWACPFEFAQASIAKAQTLTKVRIVYNSDISSLESHSSGWQLFSAEDNTPIATHEQVVIASGAQLTQYKQTKNLQITGFRGQVSHVPPQGELAQLNTVICANGYLTPQHNQLHCVGASYVKDPQHLDFCPIEQHENSLKMKQSFPNSNWPNDIDVSNNDARVGVRMVSRDHFPVMGCAPDVEALFTRYAVQQQSKDKPSLWQHYWQTTPAPIYDGLYVLGGLGSRGLSSGPLVAECLAANLCGELSPLSVELQALLSPNRMWLRKLLKGKALM | 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 form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 77136
Sequence Length: 697
Subcellular Location: Cytoplasm
|
A3QFM9 | MPNIPLRVNSLATEHPNNAQNSDKMPTFDAIFSHLSAIASHNSHQIIALLPSSDANWPAALIAERLTQAGSKQHLQKQHLHLHLFAQHQASWLKALAESETLASPAKEQIKAICDARVSGSHRLKLVNARLIIDIHLGDPLTQLKDLVSPSLASQAIQGWLANTQATDEALIWQMARLSQDNAEFLLLENNDVNLDKTSNNANTNLLTQLIIKAGFTCYRLNLSLKDDQLVTLAEKPSLASLEIAMVERRALRRQQLDKFAFNPLTQGREGETAIIGGGVASANLALSLAERGKKVSFFCMDKAPGEQASGNKQGAIYPLLTPEHGSLSHYFLLGYLFSRQRIKQLLESGHEIPHDFCGVLQTGHDERSHKRLTKIINAQPWAESIARPVDALQATALAGVTIEHQGIYYPLAGWVSPQAFTRAAISQAERLGKQTSHYQCQITAIRFENQQWYLSAIQDGQKVEFGPYANLVLANGRHLTDFAQTDHLPISGFRGQVSHIPERAPLKDLKTVLCAHGYLTPAHDKLHCTGASYVKDASNLDYSAVEQVENLDKIRTSYGGEWTKAVDITGHSARVGVRMVTRDHAPMMGCAPDFEAISATYISHQQTKKSTKESAKCWQTTSAPVHQGLFILGGLGSRGLTSGPLAAEILAAQLCGELLPATQDILALLNPNRMWMRKLIKGKAL | 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 form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 75269
Sequence Length: 686
Subcellular Location: Cytoplasm
|
A8H2Z3 | MTVSKILKQIIDSQTTKNVVIGQLGLGSITKLKQLITLLAHHKDKQLTLKLFVDISDTSGILLANEELTTLLCPQGSISLTAIEGCQRVIVSNCKLTIDFYLGQYLTQLQALPMVNDGFVDGWHVTSDADQTQLRQILFWQLAKLSKNDAQFSLDDTFTEVSQLELYTQAEQVGLYRYADNIPGNIQSGDEICFQERAAMRAQSRALQAPYPICSAAVTTHATCSNLGIAIIGGGVASACLALSLAERGQQVTLFCEDHALAQAASGNKQGAIYPLLTPDNNTLSQYFQQAYLFSLQRLKSLAAQGHPIDFDLCGVVHTGHDERSRKRVAKIINGQNWQPSIARAITAEQASSIAGLKIDDGGIFYPMGGWVSPQDFTRAAFNQAKAIAGASLKLNTQITDIHYKDGGWELTSNTERFGSFKALILANGKSITQFPQTQYLQATGFRGQVSHVPSRAKLSKLSSVLCAHGYMTPSNNTLHCLGASYVKNAPNTDYCPNEQVENLHKIQHSYVGQEWVEDIDVSGHSARVGVRMVTRDHAPMMGPAPDIDSIMTLYQDHQLTPQSRKYWQSHNAPVHQGLYVLGGLGSRGLSSGPLAAESLAAQICGDLMPISRDFVALLNPNRMWMRKLLKGKALEVGVEV | 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 form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 70019
Sequence Length: 641
Subcellular Location: Cytoplasm
|
A0KV89 | MTAKPHKSCQFKRDYPQLINLYPPCALTTAQSLDNFTRLRRSRLTTPSAQLGQELYVMGQWGLGDGLELLSLLHHWQTQTQSNTRLLVKVFEPNPINDYELKLLWDQSQSLISTPHLQPIANAILKAKPARIIGCQRLIFDDGRITVDLHFGDLHTSLTNLPHSPAHPIQQWLVLPHLASQLSGKLAWQMARLSADDAQLIGVNLAETVQQLAHSSGFSTLNVSQDALNGDASDALPSQIITDEILLHERKLLRQQADTAQAFTPKPATLAAIDHPVAIVGGGLASANLMLSLAERGQSSTLFCKDNELGQGASGNRQGAIYPLLTPENDELSRFFQQAFLFSRRRIEALSQASMMDTNAAPHVTVISHDFCGVLQTGHDERSQQRLDKIIQSQDWPAEIAYAVDANEANEIAQIGIDKAGFFYPLGGWVCPFEYAKAAVDKASQLANVQCHFNTEITEIECDAQAWYLHSQGQRFGPFRQLVLANGAQLTQFSASERLQISPFRGQVSHVPAQFKLSQLATVLCANGYLTPSHQGLHCLGASYVKAAEHFDFCPQEQRENLGKMQESYPNQAWVDDIDISGNSARVGVRMVTRDHFPMMGCAPDVAEILARYELHQLNQQQAEQSKHYWQTTPAPILDGLYILGGLGSRGLSSGPLAAECLAAQLTGEPLPLDWSTLNKLNPNRMWLRKLLKGKAL | 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 form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 77032
Sequence Length: 697
Subcellular Location: Cytoplasm
|
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