ids
stringlengths 6
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stringlengths 11
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stringlengths 108
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Q8U4J5 | MLIDKFGRPVTNLRISLTKECNLNCFYCHREGQQDGERTMTPEEIERIVRIASRLGIRNVKLTGGEPTVRPDIYEIIQRIRPYVVDLSMTTNGTTLYASAEKLKEAGLDRVNISLDTLDRKKYKMITGYDVLDQVLKGIRRATNLFYPVKLNMVVMRGINDDEIWDMIRFAGEVNAILQLIEIEVPREMENSQFFKDFFYPLKPLEEKFEKIAVEIRERKMHRRRKYFLPVDGKMVEVEVVRSMHNTTFCMNCTRLRLTADGYLKTCLLRKDDLIDILGPIRRGATDDELVKIFKRAVQLRKPYWIN | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Mass (Da): 36021
Sequence Length: 307
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
|
O57854 | MLIDRFGRPVTNLRISLTKECNLSCFYCHREGQLDGERFMTPEEIERIVRVASRLGIKKVKLTGGEPTIRKDILEIIRRLKPYVVDLSLTTNGTTMYVLAEKLKEAGLDRVNISLDTLDRKKYKMITGFNVLDEVIKGIKKATKLFYPVKLNMVVMKGVNDDEIWDMMRFAGEVNAILQLIELEVPREMENSQFFKDFFYPLKPLEEKFEKLAVKVKERRMHRRRKYFIPIDGKIVEVEVVRSMHNTVFCMNCTRLRLTADGYLKTCLLRRDDLIDILGPLRNGASDADLIEIFKRAVLLRRPYWTSNSS | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Mass (Da): 36163
Sequence Length: 310
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
|
Q8Y0K4 | MPAQGWLADTYGRRLHDLRISVTDRCNFRCIYCMPKDVFDKDYRFLQHSELLSFEEIERMVRLFIEHGVEKIRLTGGEPLLRKDIERLVEMLARLNTRDGKPLDLTLTTNGALLARKAQALKDAGLTRVTVSLDAIDDATFRRMNDVDFAVAEVLHGIEVAQRVGLAPLKINMVVKKGDNDDQIVPLARHFRNSGIILRFIEYMDVGVTNHWEMASVVPSAEVIRRLSAAFALEPLSANYAGETAERWRYADGAGEIGVISSVTQAFCHDCTRARLSTEGKLYLCLFATQGFDLRALLRGGASDLEVSNAIRTVWQARTDRYSELRASGTAPPTGRRIEMSYIGG | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Mass (Da): 38695
Sequence Length: 345
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
|
P94328 | MARKPSKTRPSKAKSGPALTHIGATGEARMVDVSDKPATERLAVAEGRVLMTRATLDLIVSGNAKKGDVLGTARIAGIMAAKRTSELIPLCHPLALSKVTVDIEPDAKLPGCLVRASVKVTGPTGVEMEALTAVSVACLTIYDMIKAVERGVRIEGIHLVEKLGGKSGHYRA | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 18032
Sequence Length: 172
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
|
A6X0K9 | MMSKLTHIDQTGAANMVDVGAKDETERQAVAEGSVRMNLETLALILEGNAAKGDVIGAARLAGIMAAKKTADLIPLCHPLMLTKVAVEIEPDQTLPGLRVRALAKLKGRTGVEMEALTAVSVTCLTIYDMAKAVDKHMEIGGIRVTEKGGGKSGDWKA | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 16652
Sequence Length: 158
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
|
B4EBZ2 | MSGLTHFDAAGHAHMVDVGGKQETQRIAIARGTIRMLPATFALIRDGKAKKGDVLGVARIAAIQGAKRTADLIPLCHPLALTRVAVDFELDDALPGVHCVVQVETFGRTGVEMEALTAVQVGLLTVYDMCKAVDRGMVITDVSVREKRGGKSGDWKAEDVAG | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17192
Sequence Length: 162
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
|
Q8E942 | MSNVFTHINADGNAHMVDVTEKAVTEREARAEAFIEMASTTLEMIMSGSHHKGDVFATARIAGIQAAKKTSDLIPLCHPLMLTKVEVELEAQPEHNRVRITSLCKLSGKTGVEMEALTAASVAALTIYDMCKAVQKDMVISQVRLLEKRGGKSGHFKAE | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17294
Sequence Length: 159
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
|
P07112 | MAIYHLTAKTGSRSGGQSARAKADYIQREGKYARDMDEVLHAESGHMPEFVERPADYWDAADLYERANGRLFKEVEFALPVELTLDQQKALASEFAQHLTGAERLPYTLAIHAGGGENPHCHLMISERINDGIERPAAQWFKRYNGKTPEKGGAQKTEALKPKAWLEQTREAWADHANRALERAGHDARIDHRTLEAQGIERLPGVHLGPNVVEMEGRGIRTDRADVALNIDTANAQIIDLQEYREAIDHERNRQSEEIQRHQRVSGADRTAGPEHGDTGRRSPAGHEPDPAGQRGAGGGVAESPAPDRGGMGGAGQRVAGGSRRGEQRRAERPERVAGVALEAMANRDAGFHDAYGGAADRIVALARPDATDNRGRLDLAALGGPMKNDRTLQAIGRQLKAMGCERFDIGVRDATTGQMMNREWSAAEVLQNTPWLKRMNAQGNDVYIRPAEQERHGLVLVDDLSEFDLDDMKAEGREPALVVETSPKNYQAWVKVADAAGGELRGQIARTLASEYDADPASADSRHYGRLAGFTNRKDKHTTRAGYQPWVLLRESKGKTATAGPALVQQAGQQIEQAQRQQEKARRLASLELPERQLSRHRRTALDEYRSEMAGLVKRFGDDLSKCDFIAAQKLASRGRSAEEIGKAMAEASPALAERKPGHEADYIERTVSKVMGLPSVQLARAELARAPAPRQRGMDRGGPDFSM | Cofactor: Divalent metal cation. Can use Mg(2+), or to a lesser extent, Mn(2+), Ca(2+) or Ba(2+).
Function: Part of the relaxosome complex that is responsible for plasmid transfer during conjugation. Locally unwinds DNA and catalyzes the cleavage of one of the DNA strands at oriT. The cleaved strand is then transferred through the dedicated type IV secretion apparatus. MobA remains covalently linked at the 5' end of the strand, and once in the recipient cell, it probably catalyzes the rejoining of the two ends of the strand, re-forming the circular plasmid DNA. The primase activity of MobA is essential for the synthesis of primers that will initiate the DNA replication events necessary to form the double-stranded plasmid in the recipient cell.
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Mass (Da): 77952
Sequence Length: 709
Subcellular Location: Cytoplasm
|
B2I3G6 | MNKGYPITDLVILAGGQARRMNGLNKLLQQFDGDTQLLKIHQKLKSSVSEIWVNSHRDYSIYQSIVPDIKCFQDDASGFFGPLMGMKSAWSHVRADYVLFIPCDVTYIPTQVVAKLHSALRKNKQAQAAYVSINGDALYPFCLLKRESLEVLEQQIDKQQLSLKNCFKLLHAQVAIFQKQNLFFHSINSLDELQQYKQIKAFKEIFSTN | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 23919
Sequence Length: 209
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
|
A5FZ90 | MADPSGSHLRAVILAGGAGRRLGGVDKALLILHGRTMLDHAIATVSGQVGAVALSAAGDPARFARFGIPVLEDGRHRGKGPLAGVLAGMRWAAASGGETLLSLPVDTPFAPRDLAARLGAAPAVAASHGRTHHLVALWPVAAADALERFLDGPGPYRVSGFAAEIGMRAVAFADERDPFVNINTQADLDAAEAGRC | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 20020
Sequence Length: 196
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
|
Q8UEQ7 | MIAPPRKIPGLVPPGLILAGGLSRRMGSNKAMVTLGDAPLLSHVIRRVTPQVSDVTINAAITDKGSWAEGFGLPLLPDTLNGHAGPLAGVLAGMRHFRDRETAGSHFLTAPADSPFFPNDLVVRLCEHLSDDAIVIAASSGQLHPVFALWPVALADDLEDWLKNDANRRIRAFLARHVTIGVAFPPLETARGSLDPFFNINTPDELALARSQLETMET | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 23402
Sequence Length: 218
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
|
Q21YF3 | MIPAQDITGLILAGGRGSRMGGVDKGLQTFNGMPLALHTLTRLQMGGGVGQIMINANRNLAAYESFGASVWPDGLADYAGPLAGFLTGLEHCETPFLVTVPCDTPRLPLDLVPRLAAALEAENADIAMVAAPEIGKDGQVRLRPQPVFCLLRVELLESLVRFTQEGGRKIDAWTALHKTAVAPFDLPHDDPLAFFNANTLAELHQLENNPA | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 22559
Sequence Length: 211
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
|
O67413 | MRTFTWRKGSLSKVNTCYVLAGGKSKRFGEDKLLYEIKGKKVIERVYETAKSVFKEVYIVAKDREKFSFLNAPVVLDEFEESASIIGLYTALKHAKEENVFVLSGDLPLMKKETVLYVLENFKEPVSVAKTEKLHTLVGVYSKKLLEKIEERIKKGDYRIWALLKDVGYNEVEIPEELRYTLLNMNTKEDLKRILAIENHY | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 23350
Sequence Length: 201
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
|
Q5JIH9 | MIGAVLAGGRGRRFGGDKLLFRISGKPLLLYTIERLEQAEKIDEIVLVASKENAEKLRDFGHDVVVDELMIGPMGGIFTALSLGDAFVVAGDMPLLVPEFIDFIVERFEEAKKPACVPRWSNGYLEPLHAAYSSSFRDFLEERIKSRNYAINQAIRESDACYIEIEKLPEGWRESFFNVNTREDLRRLTPLRTRDNPDTLR | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 22866
Sequence Length: 201
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
|
Q87PK5 | MLQPTQTSWVILAGGQASRMGGKDKGLIELNQKPLIEHVIERLSPQTPRILINANRNQDAYSKFGFVFSDQFKDFPGPMGGIHAGLMHAETDWVGFVPCDSPQINTDLVERFCQAVKEDSDILVAHDGDHQQPVFTLYHKRVLPKLTAFLERGDRKIILLYKECNTSYVDFSDSPNCFVNLNTPEELAQFGQLES | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 21952
Sequence Length: 195
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
|
Q3BTU8 | MTLQRPWTGVVLAGGRSSRMGQDKALLPWHGRPLLEQMQALLRQAGAQHVVVSGNRPEYAGIADVHPDLGPLGGLASVIANAADATTLVVVPVDMPLLSAALLGKLLAPSQHRCVAFEDQMLPMCLRLDASVREALTVLMAGAASSRSLRALQHSLQCHRVTVTASERAEFVNCNTPEQWSRLIHENPD | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 20335
Sequence Length: 189
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
|
Q1C231 | MQPNITGVILAGGRSSRMGGNDKGLIPLNGKPLFQYVIDRFKPQVSDLVINANRNQGLYKESGIPVIDDIITGFVGPLAGMHAGLSYASTEWVVFAPCDVPALPSDLVSQLWQGKKQALAAYANDDERAHPTFALMHISLKTQLADYLIRGDRKLMLFLDSINAQRVKFSGKADLFSNLNTPADCDLWEQKRRGQ | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 21445
Sequence Length: 195
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
|
P0AF02 | MILTDPEWQAVLLSLKVSSLAVLFSLPFGIFFAWLLVRCTFPGKALLDSVLHLPLVLPPVVVGYLLLVSMGRRGFIGERLYDWFGITFAFSWRGAVLAAAVMSFPLMVRAIRLALEGVDVKLEQAARTLGAGRWRVFFTITLPLTLPGIIVGTVLAFARSLGEFGATITFVSNIPGETRTIPSAMYTLIQTPGGESGAARLCIISIALAMISLLISEWLARISRERAGR | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24939
Sequence Length: 229
Subcellular Location: Cell inner membrane
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P45322 | MEISAINLSLSVAVSSMLWSLPLAIFVAWLLARKNFYGKSLITGVIHLPLVLPPVVIGYLLLVAMGRNGFIGKYLYQWFGLSFGFSWKGAVLSSAVVAFPLVVRAIRLSLENIDIKLEQAAQTLGASAWRVFFTITLPLSLPGVLAGLVLGFARSLGEFGATITFVSNIAGETQTIPLAMYSFIQTPGAEEQTARLCLFAIILSLISLLLSEWLSKRMQKKLGQGNVAD | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24823
Sequence Length: 229
Subcellular Location: Cell inner membrane
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P0A625 | MHPPTDLPRWVYLPAIAGIVFVAMPLVAIAIRVDWPRFWALITTPSSQTALLLSVKTAAASTVLCVLLGVPMALVLARSRGRLVRSLRPLILLPLVLPPVVGGIALLYAFGRLGLIGRYLEAAGISIAFSTAAVVLAQTFVSLPYLVISLEGAARTAGADYEVVAATLGARPGTVWWRVTLPLLLPGVVSGSVLAFARSLGEFGATLTFAGSRQGVTRTLPLEIYLQRVTDPDAAVALSLLLVVVAALVVLGVGARTPIGTDTR | Function: Part of the binding-protein-dependent transport system ModABCD for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27676
Sequence Length: 264
Subcellular Location: Cell membrane
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Q08382 | MTEGILFDAAMLTTLALTLKLATVTTVLLLALGTPLAWWLSRGGGLWKEIVATLVSLPIVLPPTVLGFYLLIAMGPNSPLTDLLGFKLSFTFAGLVVGSVIYSLPFVVNPIRNAFVAMGPRPMEVAATLRASPLDAFFTVALPQAAPGLITGAILGFAHTVGEFGVVLMIGGGIPGRTKVLSVTIFDYVETLEWDKAHVLAGGMLAMSFVVILAMMLIERRYGTGARR | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24161
Sequence Length: 228
Subcellular Location: Cell inner membrane
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P37732 | MPADGIRARFRVDYAGFALDVDLTLPGHGVTALFGHSGSGKTTLLRCVAGLERAAEARLEINGELWQDSAAGVFLPTHRRALGYVFQEASLFPHLSVRRNLEYGMKRVDAASRQVSWERVLELLGIGHLLERLPGRLSGGERQRVGIARALLTSPRLLLMDEPLAALDLKRKNEILPYLERLHDELDIPMLFVSHLPDEVARLADHVVLLDQGRVTAQGSLQDIMARLDLPTAFHEDAGVVIESVVAEHDDHYHLTRLAFPGGAVLVARRPEAPGQRLRLRVHARDVSLANSRIEDSSITNVLPATVREVVEADTPAHVLVRLEAEGTPLIARITRRSCDQLGIAPGRRMWAQIKAVALLG | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39769
Sequence Length: 361
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q89TQ9 | MGGFTKEAKKGYIEVAFNGSLASILLDTQFSVPAKGVTAIFGPPGCGKTTLARCIAGVQRLPNGFCAIDGEIWQDETTFRPPHLRRVAYVFQLPILSSHLSVRRTLLYNASNSEPTLIDFDGVVELLGLAPLLERTPSHLSKTERQRLALGSALLGQPRLLLLDDPLIVRDRSAKCEILPFLERILQSLALPMIYISHDITDIERLADHLVMMKDGTVTAAGPLNVTQSDPALASRSEAAICLDTMVGGYDGRYGLVKLRLKSARFLIPAVPLRPGARLRLRIAAGDVSIACEPPRASSILNVFRARITASLPHGDAEVTLVLTLETGHSGVPLLARITRRSFDALRLSIGAEVFAEELCGKLGDDGMR | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39965
Sequence Length: 369
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q44538 | MPEQGIEAQLRLQRGAFRLDAHLQLPANGISVLLGRSGSGKTTLLRAIAGLERAEGFLQVGGQLWQDATCFRPPHQRSLGYVRQASELLPHLDVRANLEFGYRRIPRARRRLGLDEVIALFGLEDLLDQRAEWLPNGPRQRVAIACALLTSPDLLLLDAPLICLDRHSRAQILPALEQLRGQLRIPLLYVTHSQDEVTRLADHLILLDKGKTFASGPPGRLLSDPRLPLNHPDEAAVVLIGQVEHHDPHYRLSTVRVPGGTLSVSLSRLPPGAETRVRIFARDVSLSLDPPHNSSILNILRVRIADLFHEQDSARVMVRLDLDSACILARITRLSADRLGLAPGLQVYAQIKSVALME | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39648
Sequence Length: 358
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q89EW7 | MTADGRGRIDAAFRGRLGRFVLDASLSVPATGVTAIFGPSGCGKTTIARCIAGLQRLSDGFCAIDGEIWQDGMAFRPAHRRPVGYVFQEPSLFPHLSVRGNLLYGAPKAAATSIGFDEVVELLGLTALLGRSPHRLSGGERQRVAIGRALLSQPRLLLMDEPLAALDRTTKNEILPFLERLHERLSLPVLYISHDMAEIERFADYLVLMERGRVVGAGPLHILQSDPALPLAYSRDAAVSIDGLVEAYDERYGLLTLAVNGGLLHVPSHRIAVGARQRLRIAASDVSIVRARPSESSILNILPARIVTQSPPGAGEVTIVLGLDSDGSGAPILSRISSRSRDLLGLSDGMAVFAQVKGVSLVRASGCAIGNMGPTAPGQLDHCSTQDTGVRSEAGTTAMPIDFAEIDPNRVAAILYRPQDDLDTLLADFAQDLVRAGERIGGIVQRNIKDGSGCQVGMQAIDLMTGREISICQPLGSGAMACKLDAAGLADASVAVASAIAQDVDLIVINKFSKQEAAGRGLRDELAGAIAAGIPVLTAVPEKCFEAWISFTGGIGTTLLCERQVIEAWWRDTSSRMKRMREDHDAVVAQCIEISGALPLVQRVVARQLVVTHDLPLDPERAEAEVVVRGVVERTNVEVLDGAADEADEAPDAGFPVGPERIERLPDIGPVPRRHEALQVEREVLSPDACLQRSAGERVDVFKEGKTKVGTVLVDRGDAELVEGPIVLELHEGAPVLVEMNVGVDLQTLYEIAVRGRVAGAERRCAIGLEAFAQRRPQRDVAFRIGGPKRDVFEPVKRFGTQPGIGKDRPVLCPAVRLDRRPLGDRSVLGPREPDAGAKGRKRQNDPEVAHIAPCQHRRTSPHLASARDALFGPREWISATYPPGNMTNAADRLLDV | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 96174
Sequence Length: 897
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q8UCD5 | MTLSVSARHRLGTFELDASFTSEGGVTALFGRSGSGKTSMIRIIAGLLRPDEGQISLDGEVLADSGKRLFLPAHKRRFGYVFQEARLFPHLSVAQNLRYGRWFTTGKDTNANDDRIIDMLGISHLLQRRPNRLSGGEKQRVAIGRALLSSPRLLLMDEPLASLDEQRKAEIIPYLERLRDETKIPIVYVSHSIQEVARLADRVVVMKDGKVEAEGKAAEVLSRPDFSTYLERREAGSILSGNIESFDERHGLAAVRLNAALLQVPAKKATAGTPARVLIPARDVMLALVKPEGLSALNILEGHVTGISESEDGMVTIQMDCGGDIIQSRITDLSRERLHLEPGKPVHAIIKSAALDPY | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39285
Sequence Length: 358
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q21UI2 | MNTRPEQASKDTSGLTLQVALQRQDFRLEIDLELAGHGITALFGPSGSGKTTALRVLAGLEPAAQGRVCVQGDMWQDSAQGVFKPVHQRALGYVFQEASLFDHLNVQENLQYGFKRTPASERFRNWDHTLDLLGIAHLLKRWPHELSGGERQRVAIARALAASPRLLLLDEPMAALDAPRKAEILPYLERLQSRLEIPVIYVTHAIDEVARLADQLVLLEAGQVTAHGPTAELLTRLDLPLAHGDSAGAVLHCSVVSHDEADHLTLTRFAGIDLVVPRQNAAVGQTLRVRVAARDASLTLQRQTDTSILNILPASVLALSADGPGQVMVALEVGGSALLARITARSAHTLGLVPGLAVYAQIKGVAILG | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39702
Sequence Length: 369
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q0VQ44 | MSLALSISGRRGAFQLQVDATLQPEGVTVLFGASGAGKSSLLRMVAGLDPCEGTIRFADQLWRSSGLSSERKNDVDLAVWQRPIGMMFQQPTLFHHLTVQGNLNYVARRRRSPIGQVEQVIKQTGIAPLLSRRVDGLSGGESQRVALARALLGTPRLLLLDEPLSALGEEHKQGLLDLIALAAQTVPVLYVTHNMDELLRLADQVWLMEQGRVVAQGPVGQELSRLDGVLAQRADATALLAGEVGSYVREDHLQGIRVGSHTLWLPGLQRLTPGEPVRLRIAARDVSLCLSAPNDSSILNILPAQVVGLRDVGPGQCLVQLRLAGQCILARISGRSARQLSLFPGTDLYAQIKAVALV | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38602
Sequence Length: 358
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q5E0T4 | MLLIDIKKQLGDLLLDVKLSLPSSGISAIFGRSGAGKSSLANVISGLTSPEEGRITLNNRVLFDSESKVSMPPEKRNIGYVFQDARLFPHYKVEGNLLYGCGGKRTPHFNDVVKLLDIESLLTRYPHSLSGGEKQRVAIGRAILSEPALLIMDEPLASLDLPRKHEVMPYLERLAKEIKIPILYVSHSLDEILRLADNMVLLNQGSVSLSGDITSVWGSPLMRPWLNASEHSALLEGTISELHSDHPMTKVTLNNSQQGIWVKSPCDCVEEGKKIRLRIRANDVSLIKQQPQHSSIRNILPVVIEDLSEDKENDVVAVKLNLSGHVLWANITLWARDELQLGIGQSWFAQIKGVSVTQSDLCSK | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40271
Sequence Length: 364
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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Q5P4W2 | MSGAVPFGAGAVRTGAITGDEAIRARFGLGWPGFRLDVDLALPGRGVIALFGHSGSGKTTLLRCLAGLERAADGYLAVRGELWQDEAQRLFVPTHRRPLGYVFQEASLFAHLTVRRNLEFGLKRVPAASRRIPLDQAIALLGIEPLLDRMSGRLSGGERQRVAIARALATSPRLLLMDEPLAALDVKRKQEILPYLERLHAELDIPVVYVSHAPEEVARLADHVVLLADGRALAAGPIGEVMARLDLPFAHDEDAFVVIDARVAAHDEAYALTRLEFAGLPLWITGLDMPLASRVRARVLARDVSLALTERHDSSILNVLPARVVSLDEADPGRTLVRLDVAGTALLARITRRSAAQLGIVPGRDVYAQVKGVALLR | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40796
Sequence Length: 377
Subcellular Location: Cell inner membrane
EC: 7.3.2.5
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O02193 | MSEAELEQTPSAGHVQEQPIEEEHEPEQEPTDAYTIGGPPRTPVEDAAAELSASLDVSGSDQSAEQSLDLSGVQAEAAAESEPPAKRQHRDISPISEDSTPASSTSTSSTRSSSSSRYDDVSEAEEAPPEPEPEQPQQQQQEEKKEDGQDQVKSPGPVELEAQEPAQPQKQKEVVDQEIETEDEPSSDTVICVADINPYGSGSNIDDFVMDPDAPPNAIITEVVTIPAPLHLKGTQQLGLPLAAPPPPPPPPAAEQVPETPASPTDDGEEPPAVYLSPYIRSRYMQESTPGLPTRLAPRDPRQRNMPPPAVVLPIQTVLSANVEAISDDSSETSSSDDDEEEEEDEDDALTMEHDNTSRETVITTGDPLMQKIDISENPDKIYFIRREDGTVHRGQVLQSRTTENAAAPDEYYVHYVGLNRRLDGWVGRHRISDNADDLGGITVLPAPPLAPDQPSTSREMLAQQAAAAAAASSERQKRAANKDYYLSYCENSRYDYSDRKMTRYQKRRYDEINHVQKSHAELTATQAALEKEHESITKIKYIDKLQFGNYEIDTWYFSPFPEEYGKARTLYVCEYCLKYMRFRSSYAYHLHECDRRRPPGREIYRKGNISIYEVNGKEESLYCQLLCLMAKLFLDHKVLYFDMDPFLFYILCETDKEGSHIVGYFSKEKKSLENYNVACILVLPPHQRKGFGKLLIAFSYELSRKEGVIGSPEKPLSDLGRLSYRSYWAYTLLELMKTRCAPEQITIKELSEMSGITHDDIIYTLQSMKMIKYWKGQNVICVTSKTIQDHLQLPQFKQPKLTIDTDYLVWSPQTAAAVVRAPGNSG | Function: Histone acetyltransferase that plays a direct role in the specific histone acetylation associated with dosage compensation as part of the male-specific lethal (MSL) complex . Dosage compensation ensures that males with a single X chromosome have the same amount of most X-linked gene products as females with two X chromosomes . May be directly involved in the acetylation of histone 4 at 'Lys-16' on the X chromosome of males where it is recruited by the MSL complex . As part of the nonspecific lethal (NLS) complex may associate with promoters of X chromosomal as well as autosomal genes and positively regulate their transcription through chromatin modification .
PTM: Autoacetylation at Lys-638 is required for binding histone H4 with high affinity and for proper function.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 92657
Sequence Length: 827
Subcellular Location: Chromosome
EC: 2.3.1.48
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Q7X7A4 | MRRERDATQIPENPMEGIPQTAAAAAAAAAAEASEPPRKRARVDGGGGGAGEEEEDRLSDLPDCLLEDILAHLGSRQAVQTSVLSRRWRNLWRGVRVVVIDVGSFRLPGADGDPPRFRLDRIEDFADGVLSPSLHPGAARELDALRMRLDEDAVTTNFQRWIRRALWRRPATVDLYYLPRRSFSWPPAVPLTPVTAVSRLKTLRIFGLRPTVVFGADEFPALEDLHIERCSYAHGTIASPTLKRLALVSPINGCFVREQRLTAPGLTSLRLVLPYSREEGVRVITDAPLTSLVDASITIVDTDPGDPRNRRVNQFKVDFLVAISNLLGRLTSVRNLDLTGLNATALLDNKSQEFPMFPYLTTLLLNECDIGYKYHVLRSILQNAPNLEQLRLHNCKFVGKSRRKAGQTQSKEKTSKCSSSTLSSACSSLKSVEIKHPRGEPSHDLLHEFLKEIPHNQWRKRSIDEETISIELNRK | Function: Probable component of a SCF (SKP1-CULLIN-F-box protein) E3 ubiquitin-protein ligase complex and may function through the ubiquitin-mediated protein degradation or signaling pathway. Required for male meiotic prophase I progression. Required for telomere bouquet formation, homologous chromosome pairing and for the formation of the synaptonemal complex (SC), which stabilizes initial chromosomal axial associations and promotes crossover formation. Involved in meiotic DNA double-strand break (DSB) end-processing and repair, and is important in the recruitment of DSB repair proteins to the DSB sites.
Sequence Mass (Da): 53064
Sequence Length: 475
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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A3KPP3 | MSRPLFGGALSAVFPSSVMDISELRQIPDNQEVFAHSQTDQSIIIELLEYQSQVQDADAARYHFEDVAGSNKAIENGTWEVRVVEQVPQSEISMQECSSAWLLSGAQLVSKFNEEAKNTVNVHQCLFRLPQFTTDILMTFNDPVFINPLSSSAAGNMEAIPWTLQDFQGVLQSLRLLDSGVFG | Function: May regulate the intracellular trafficking of RAN. Promotes guanine nucleotide release from RAN and inhibits binding of new GTP. Plays a role in the regulation of the levels of GTP-bound RAN in the nucleus (By similarity). Required for normal expression of the ion channel hcn4 and for normal expression of the cardiac transcription factors nkx2.5, gata4 and hand2 during embryonic development. Required for normal embryonic heart development and normal heart rate .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20301
Sequence Length: 183
Subcellular Location: Nucleus
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Q9HD47 | MEPTRDCPLFGGAFSAILPMGAIDVSDLRPVPDNQEVFCHPVTDQSLIVELLELQAHVRGEAAARYHFEDVGGVQGARAVHVESVQPLSLENLALRGRCQEAWVLSGKQQIAKENQQVAKDVTLHQALLRLPQYQTDLLLTFNQPPPDNRSSLGPENLSPAPWSLGDFEQLVTSLTLHDPNIFGPQ | Function: May regulate the intracellular trafficking of RAN . Promotes guanine nucleotide release from RAN and inhibits binding of new GTP by preventing the binding of the RAN guanine nucleotide exchange factor RCC1 . Regulates the levels of GTP-bound RAN in the nucleus, and thereby plays a role in the regulation of RAN-dependent mitotic spindle dynamics . Enhances the expression of SCN5A at the cell membrane in cardiomyocytes .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20448
Sequence Length: 186
Subcellular Location: Nucleus
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Q14149 | MAAQPPRGIRLSALCPKFLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGSMRLGKDAIVFTKNGESMSVGLLSQTYLEVIKAEHVVVPIVAFNKHRQMINLAESKASLAAILEHSLFSTEQKLLAELDAIIGKKGTRIIIWNLRSYKNATEFDFEKDKYDIRIPEDLDEITGKKGYKKQERMDQIAPESDYSLRAYCSILYLKPRMQIILRGQKVKTQLVSKSLAYIERDVYRPKFLSKTVRITFGFNCRNKDHYGIMMYHRNRLIKAYEKVGCQLRANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTITALGEKLNDYWNEMKVKKNTEYPLNLPVEDIQKRPDQTWVQCDACLKWRKLPDGMDQLPEKWYCSNNPDPQFRNCEVPEEPEDEDLVHPTYEKTYKKTNKEKFRIRQPEMIPRINAELLFRPTALSTPSFSSPKESVPRRHLSEGTNSYATRLLNNHQVPPQSEPESNSLKRRLSTRSSILNAKNRRLSSQFENSVYKGDDDDEDVIILEENSTPKPAVDHDIDMKSEQSHVEQGGVQVEFVGDSEPCGQTGSTSTSSSRCDQGNTAATQTEVPSLVVKKEETVEDEIDVRNDAVILPSCVEAEAKIHETQETTDKSADDAGCQLQELRNQLLLVTEEKENYKRQCHMFTDQIKVLQQRILEMNDKYVKKETCHQSTETDAVFLLESINGKSESPDHMVSQYQQALEEIERLKKQCSALQHVKAECSQCSNNESKSEMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQQTATDVSTSSNIEESVNHMDGESLKLRSLRVNVGQLLAMIVPDLDLQQVNYDVDVVDEILGQVVEQMSEISST | Function: Nuclear matrix protein which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism and plays a role in innate immunity by restricting different viruses through modulation of the IFN response . Mechanistically, possesses a primary antiviral function through a MORC3-regulated element that activates IFNB1, and this function is guarded by a secondary IFN-repressing function . Sumoylated MORC3-NBs associates with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity . Binds RNA in vitro . Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3 . The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0 .
PTM: Sumoylation is involved in interaction with PML and localization to PML nuclear bodies.
Sequence Mass (Da): 107113
Sequence Length: 939
Domain: The CW-TYPE zinc finger mediates its binding to trimethylated histone H3K4me3.
Subcellular Location: Nucleus
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F4KAF2 | MEPIVKQENPVTTSTLSTWKPAARNKTIPPPESVIELSSSNEGSELGENLDEIAEIQSVDRTGGDDVSGTKRARSDSIASPAKRLAVMIPDDDEEFLLSTTSGQAILALPATPCNVVAAPSSWGSCKQFWKAGDYEGTSGGDWEVSAGGFDHVRVHPKFLHSNATSHKWSLGAFAELLDNALDEVRSGATFVNVDMIQNRKDGSKMILIEDNGGGMNPEKMRHCMSLGYSAKSKLADTIGQYGNGFKTSTMRLGADVIVFSRCLGKDGKSSTQSIGLLSYTFLKSTGKEDIVVPMLDYERRDSEWCPITRSSVSDWEKNVETVVQWSPYATEEELLCQFNLMKKHGTRIIIYNLWEDDEGMLELDFDTDPHDIQLRGVNRDDKNIVMASQFPNSRHYLTYKHSLRSYASILYLKISHEFRIILRGKDVEHHNIVNDMMQTEKITYRPKEAADVSQLSAVVTIGFVKDAKHHVDVQGFNVYHKNRLIKPFWRIWNAAGSDGRGVIGVLEANFVEPAHDKQGFERTTVLSRLEARLLHMQKDYWRSKCHKIGYAKRQGRKSAKDTEKDTEDRESSPEFDPKGSASSRKRTVPSSFKTPTAAPRFNTPTAASEKFNPRSNVNGGGKGSVKVSKDIGYKSSEKGGKLGNSFSKSNKRAKPQGARAVEVTNSDDDYDCDSSPERNVTELPGKSSELPKPQSGPRTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEENLRIKLEEASNTIQKLIDGKARGR | Function: Exhibits ATPase activity. Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair. Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. May also be involved in the regulation of chromatin architecture to maintain gene silencing. Together with MORC7, acts to suppress a wide set of non-methylated protein-coding genes, especially involved in pathogen response. Positive regulator of defense against the oomycete Hyaloperonospora arabidopsidis (Hpa) .
Sequence Mass (Da): 89695
Sequence Length: 800
Subcellular Location: Nucleus
EC: 3.6.-.-
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Q8TE76 | MLLYRGAPAGPGAPGCGLARPGGGPQAFGIRLSTMSPRYLQSNSSSHTRPFSAIAELLDNAVDPDVSARTVFIDVEEVKNKSCLTFTDDGCGMTPHKLHRMLSFGFTDKVIKKSQCPIGVFGNGFKSGSMRLGKDALVFTKNGGTLTVGLLSQTYLECVQAQAVIVPIVPFNQQNKKMIITEDSLPSLEAILNYSIFNRENDLLAQFDAIPGKKGTRVLIWNIRRNKNGKSELDFDTDQYDILVSDFDTEEKMTGGVTSELPETEYSLRAFCGILYMKPRMKIFLRQKKVTTQMIAKSLANVEYDTYKPTFTNKQVRITFGFSCKNSNQFGIMMYHNNRLIKSFEKVGCQVKPTRGEGVGVIGVIECNFLKPAYNKQDFEYTKEYRLTINALAQKLNAYWKEKTSQDNFETSTVARPIPKVPDQTWVQCDECLKWRKLPGKIDPSMLPARWFCYYNSHPKYRRCSVPEEQELTDEDLCLSKAKKQEQTVEEKKKMPMENENHQVFSNPPKILTVQEMAGLNNKTIGYEGIHSPSVLPSGGEESRSPSLQLKPLDSSVLQFSSKYKWILGEEPVEKRRRLQNEMTTPSLDYSMPAPYRRVEAPVAYPEGENSHDKSSSERSTPPYLFPEYPEASKNTGQNREVSILYPGAKDQRQGSLLPEELEDQMPRLVAEESNRGSTTINKEEVNKGPFVAVVGVAKGVRDSGAPIQLIPFNREELAERRKAVESWNPVPYSVASAAIPAAAIGEKARGYEESEGHNTPKLKNQRELEELKRTTEKLERVLAERNLFQQKVEELEQERNHWQSEFKKVQHELVIYSTQEAEGLYWSKKHMGYRQAEFQILKAELERTKEEKQELKEKLKETETHLEMLQKAQVSYRTPEGDDLERALAKLTRLRIHVSYLLTSVLPHLELREIGYDSEQVDGILYTVLEANHILD | Function: Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3 . The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0 .
Sequence Mass (Da): 106348
Sequence Length: 937
Domain: The CW-TYPE zinc finger mediates its binding to trimethylated histone H3K4me3.
Subcellular Location: Nucleus
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F4K2G3 | MAESGSTNPKSPSVVPDSTLGGLKRDLRNYHDGDDSNNLSIKKSKTTKMENNCREIVPLDVTPLSIVPPDTPKLSRQFWKAGDDDEAAPVPLYCSNDAAVRVHPQFLHANATSHKWALGALAELLDNSLDEVSNGATYVHVDSTINKRDGKSSILIVEDNGGGMNPSTFRECLSLGYSRKRNMANRVGQYGNGFKTSTMRLGADAIVFSRSRGINGNNPTQSIGMLSYTFLYETRKCEAIVPTVDYELVDNKWKEIVYNSTNEWLDNLETILRWSPYLSQQDLLDQFNHLEEQGTRIVIYNLWEDDEGKMELDFDTDPHDIQLRGVNRDEKNIDMAKTYPNSRHFLTYRHSLRSYASILYLKRPDNFRIILRGEDVEHHSVLDDMMKIEEKTYKPMRSPEWPDQEEMVASLKLGFVKDAHHHIDIQGFNVYHKNRLIKPFWRVWNAAGSDGRGVIGILEANFIQPAHNKQGFERTVVLAKLESRLVTHQKNYWSSRCHEIGYAPRRKQKNYESSVTETPRPFNNINVVKGSSSSTPVPVRVFRPNVEPSGRNQIPQVETRERSFDINPEIGAKNRSYYGLGISSFKETGSVNLEAELQKVKQESAKLVSELQRQKQLLELQLQESKAKIQNLEKAQREKEVLELQLKESKARIQNLENRQEGVSTIFQQERARRDVTEDGLRKKLREASDVIDGLRKQVDTFKGKRIL | Function: Exhibits ATPase activity. Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair. Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. May also be involved in the regulation of chromatin architecture to maintain gene silencing.
Sequence Mass (Da): 80919
Sequence Length: 708
Subcellular Location: Nucleus
EC: 3.6.-.-
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Q56Y74 | MSHDRSVNVSHDAVIAKPERGTMLQSFSPRSHGSKGYSLPQDSEENRGSVGQSAGQSSTSVVDQVRSPADDAGVTSSSTICPAPVCRQFWKAGSYNDELSSKSQQPNGKNYLHVHPMFLHSNATSHKWAFGAVAELLDNAVDEIQNGATFVIVDKTTNPRDGATALLIQDDGGGMDPQAMRHCMGFGFSDKKSDSAIGRYGNGFKTSTMRLGADVIVFSRHSKNQTLTQSIGLLSYTYLTRTGHDRIVVPILDYEFNASAGEFKTLQDREHFISSLSILLEWSPFSTEAELLQQFDDVGPHGTKVIIYNMWLNSDAKLELDFDSVAEDILIEGSIKKTGSKIVNDHIASRFSYSLRVYLSILYLRIPETFKIILRGKVVEHHNVADDLMHPQYILYKPQAAGSEEALVVTTIGFLKEAPKVNLHGFCVYHKNRLIMPFWQVINYSSSRGRGVVGVLEANFVEPTHNKQDFEKTVLLQKLENRLKEMTVEYWSCHCVLIGYQVNKKPRLQIPQKVQPAGRQALSPPPGFQAVFPQGNTTSLPRVSTQPVLLEKRKEHPDSVASAALKRKVGNDDFTVPGHIRVEQFIHGSASQSQDIETVKLMEENKKLRAKCLDRKVRSQNLEVKAMNLRSELENYKSEYERLMVELQALDLVKDEHRRNVNT | Function: Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing . Together with SUVH2 and SUVH9, regulates the silencing of some transposable elements (TEs) . Exhibits ATPase activity . May also be involved in the regulation of chromatin architecture/condensation to maintain gene silencing . Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair (By similarity). Positive regulator of defense against the oomycete Hyaloperonospora arabidopsidis (Hpa) .
Sequence Mass (Da): 74175
Sequence Length: 663
Subcellular Location: Nucleus
EC: 3.6.-.-
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F4JRS4 | MDNSIHVKREIQLPSTSPAGFPGRESVTVVDLCSSDDDSDIGEVAGGLEKVGNNFVGLKRGRDTFGGSSEVDRNNVKKVTTLAELGVGLPEGFGQSNPPESLTHPIPANPCNVFRPVPPPPPPPYAGTSGKIGGCKQFWKAGDYEGAAGDNWDLSSGGFDHVRVHPKFLHSNATSHKWALGAFAELLDNALDEVASGATYVKVDMLENNKGGNRMLLIEDNGGGMDPEKMRQCMSLGYSAKSKLANTIGQYGNGFKTSTMRLGADVIVFSRCPGKDGKSSTQSIGLLSYTFLRSTGKEDIVVPMLDYERRDPEWSKIIRSSTRDWDKNVETIIQWSPFSSEEDLLHQFDLMKDRGTRIIIYNLWEDDQGMLELDFDADPYDIQLRGVNREERNIKMASQFPNSRHFLTYKHSLRSYVSILYLRIPPGFRIILRGIDVEHHSVVNDMMQTEQITYRPQSESYGVVTNMSAIVIIGFVKDAKHHVDVQGFNVYHKNRLIKPFWRIWNATGSDGRGVIGVLEANFVEPAHDKQGFERTTVLARLESRLVQMQKTYWSTNCHKIGYAPRRREKSAYGYDNRDSSPENDREGPSSIKTPTPASDKFYSSSYPNHNGDNGVSGKDGARLQEELRREKERRKALEVEVQLSRQKIEEMKKEQENLIEIFSEERDRRDGEEEVLRNKLEEASNTIDDLLNKIKKMEGSKVPSWRH | Function: Exhibits ATPase activity. Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair. Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. May also be involved in the regulation of chromatin architecture to maintain gene silencing. Together with MORC4, acts to suppress a wide set of non-methylated protein-coding genes, especially involved in pathogen response. Positive regulators of defense against the oomycete Hyaloperonospora arabidopsidis (Hpa) .
Sequence Mass (Da): 79573
Sequence Length: 707
Subcellular Location: Nucleus
EC: 3.6.-.-
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A0A0R8YXT5 | MISPVSSILASIWDNSKLLLDHTSVLSIALIGVACAISIRSILYVRLACANYSILLLTHAQRLRLAYSTPLRHVPGPWYAKFTALGLRANDVAGNRWYYVQGLHKKYGSIVRIAPEEVAISDPKVVSKVHALGTEFRKRQQPGTPFNIFSISDPKAHRTRQRFYAKAFSDETLKASTEPAVRQLIKTAVASIKRDAALRKDHTADVYKWCMLFGSDVAFQVIYGNSNTEGLMATQKTTDEVIMGAYLQRMNAWAQFCFPVFLLGRWLSPLSPTLHNIFRVEEKYGDFWQEGQRQREIAARTVFVQNTKYSKNDGVFSVSDEVKLSDVDIAHDITTFLGAGGEPVGASLVFLIWQVLRMPDLQRELEAEVAGLTEPITDATTAQLPILNGVIYETLRLYGGGVTQMPRYAPIATELGGYVIPPGTAVTTHTGALHRNPAAWDDPEK | Function: Methylphloroacetophenone oxidase; part of the gene cluster that mediates the biosynthesis of usnic acid, a dibenzofuran lichen product possessing a broad spectrum of biological activities . Two genes, mpas and mpao, comprise the usnic acid biosynthetic gene cluster with a single post-PKS enzyme, the methylphloracetophenone oxidase (mpao) . The methylphloroacetophenone synthase (mpas) is a non-reducing polyketide synthase that produces methylphloracetophenone from acetate via a methylated tetraketide intermediate . The methylphloroacetophenone oxidase then carries out the oxidative dimerization of methylphloracetophenone to usnic acid .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 49443
Sequence Length: 445
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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P0DKB6 | MARMAVLWRKMRDNFQSKEFREYVSSTHFWGPAFSWGLPLAAFKDMKASPEIISGRMTTALILYSAIFMRFAYRVQPRNLLLMACHCTNVMAQSVQASRYLLYYYGGGGAEAKARDPPATAAAATSPGSQPPKQAS | Function: Mediates the uptake of pyruvate into mitochondria.
Catalytic Activity: H(+)(out) + pyruvate(out) = H(+)(in) + pyruvate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15138
Sequence Length: 136
Subcellular Location: Mitochondrion inner membrane
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Q949R9 | MATSRFQAFLNSPIGPKTTHFWGPIANWGFVAAGLVDMQKPPEMISGNMSSAMCVYSALFMRFAWMVQPRNYLLLACHASNETVQLYQLSRWARAQGYLSSKKEEEKPSQ | Function: Mediates the uptake of pyruvate into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12438
Sequence Length: 110
Subcellular Location: Mitochondrion inner membrane
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Q21828 | MSRVISKVTTYFKQHSTAEWKHYFLSTHFWGPVANWGLPLAALGDLKKNPDMISGPMTSALLIYSSVFMRFAWHVQPRNLLLFACHFANFSAQGAQLGRFVNHNYLHYVEDPVHHKLMMKKEVLEHEHDAEVISKAH | Function: May mediate the uptake of pyruvate into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15832
Sequence Length: 137
Subcellular Location: Mitochondrion inner membrane
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Q55GU4 | MAERWTKMVGFLGAAANWTIPIASFMNLKNDPEKVDPIMTTTLAVYSAVFMRWAIAIYPPNYWLLGCHVANEVAQLTQLGRYGKWKVFDSKQESDKQ | Function: May mediate the uptake of pyruvate into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11072
Sequence Length: 97
Subcellular Location: Mitochondrion inner membrane
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P30307 | MSTELFSSTREEGSSGSGPSFRSNQRKMLNLLLERDTSFTVCPDVPRTPVGKFLGDSANLSILSGGTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSPAQLLCSTPNGLDRGHRKRDAMCSSSANKENDNGNLVDSEMKYLGSPITTVPKLDKNPNLGEDQAEEISDELMEFSLKDQEAKVSRSGLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVKKKYFSGQGKLRKGLCLKKTVSLCDITITQMLEEDSNQGHLIGDFSKVCALPTVSGKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIVFHCEFSSERGPRMCRCLREEDRSLNQYPALYYPELYILKGGYRDFFPEYMELCEPQSYCPMHHQDHKTELLRCRSQSKVQEGERQLREQIALLVKDMSP | Function: Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. When phosphorylated, highly effective in activating G2 cells into prophase. Directly dephosphorylates CDK1 and activates its kinase activity.
PTM: Phosphorylated by CHEK1 and MAPK14 at Ser-216. This phosphorylation creates a binding site for 14-3-3 protein and inhibits the phosphatase. Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-191 promotes nuclear translocation. Ser-198 is a minor phosphorylation site. Was initially reported to be phosphorylated by PLK3 at Ser-216 . However, such phosphorylation by PLK3 was not confirmed by other groups. Phosphorylation at Thr-48, Thr-67, Ser-122, Thr-130, Ser-168 and Ser-214 occurs at G2 and G2-M transition and is probably catalyzed by CDK1. Ser-168 phosphorylation levels are lower than those at the other 5 CDK1 sites. Phosphorylation by CDK1 leads to increased activity.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 53365
Sequence Length: 473
Subcellular Location: Nucleus
EC: 3.1.3.48
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P48968 | MSTGPFPSSRREESSVSAPSFRFSQRKMLNLLLERNTSFTQDFPRSPGDKLLDSTNLSILSGGTPKRCLDLSNLSNGEMSASPLITSADFDDTGSLDSSGPQDVQLTEKNHHQDPMKGIPVQLLCSTPNALDHSHRKKDAVRGLSANKENINTNLKTLQWESPRIPRFQNTPGDPLASPLPLLGNGVSMDTEVRSLGSPITAVPKLSKNLNLEDQEEISEEPMEFSLEDHDTKECVLPTVSGKHQDLKYITPDTVAALLSGKFQGLIEKFYIIDCRYPYEYLGGHILGAINLCSQKELHEFFLKKPIVPLDIQKRVIIVFLCEFSSERGPRMCRSLRRKDRALNQYPALYYPELYILKGGYRDFFPEYTELCEPQGYCPMHHQDHQAELLMWRNQSKAQEGERQLSEQIALLMKKGVSLP | Function: Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. Directly dephosphorylates CDK1 and activates its kinase activity. When phosphorylated, highly effective in activating G2 cells into prophase (By similarity).
PTM: Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-219 promotes nuclear translocation. Ser-226 is a minor phosphorylation site (By similarity). Phosphorylation by CDK1 occurs at G2 and G2-M transition and leads to increased activity (By similarity).
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 47327
Sequence Length: 420
Subcellular Location: Nucleus
EC: 3.1.3.48
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P48967 | MSTGPIPPASEEGSFVSAPSFRSKQRKILHLLLERNTSFTIRSDFPESPKDKLHDSANLSILSGGTPKCCLDLSNLSSGEMSASPLTTSADLEDNGSLDSSGPLDRQLTGKDFHQDLMKGIPVQLLCSTPNAMNHGHRKKIAKRSTSAHKENINTSLKALEWEAPRTPRFRKMPGGPLTSPLCELEMKHLGSPITTVPKLSQNVKLEDQERISEDPMECSLGDQDAKGLSLRKMVPLCDMNAIQMEEEESGSELLIGDFSKVCVLPTVPGKHPDLKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNLHSQKELHEFFLRKPVVPLDIQKRVIIVFLCEFSSERGPRMCRSLREKDRALNQYPALYYPELYILKGGYRDFFPEYMELCDPQSYCPMLHQDHQAELLSWRSQSKAQEGERQLQGQIALLVKGASPQ | Function: Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. Directly dephosphorylates CDK1 and activates its kinase activity. When phosphorylated, highly effective in activating G2 cells into prophase (By similarity). May be involved in regulating the proliferation of T-lymphocytes following cytokine stimulation.
PTM: Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity (By similarity). Phosphorylated by CHEK1 and MAPKAPK2. This phosphorylation creates a binding site for 14-3-3 protein and inhibits the phosphatase activity. Phosphorylation by PLK3 at Ser-213 promotes nuclear translocation. Ser-220 is a minor phosphorylation site (By similarity). Phosphorylation by CDK1 occurs at G2 and G2-M transition and leads to increased activity (By similarity).
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 50046
Sequence Length: 447
Subcellular Location: Nucleus
EC: 3.1.3.48
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Q29029 | MAEGGRPGSGPSFRSNHRKILNLLLERETSFSMSSDRPGTPLKKKLFGDSANLSILSGGTPKRCLDLSNLSSGEMSATQFTTSADLDETGHLDSTGSEEIQLAGMSYHQHLLKCSPAQLLCSTPNALDHGRRKKDAICSSSENKENENNTSKPLEWWAHRNLLFQKRPGGPYMSPLSLLDNGNLVEGEMKHLGSPITAVSKLDKNPERGEDQAEEISDELMEFSLEDQEEAKVSLNTSCLYRSFSLPDSLNSPGLKQVVKFKDHTLPDKVKKKYCSSHEELRKGLGVKKMVSLCNINMIQMLEEDSNQGPLIGDFSKVCALPTVSGRHQDLKYVNPETVAALLSGKFQGLIEKFYIIDCRYPYEYLGGHIQGALNLYSQEELCNFFLKKPIIPLDTQKRIIVVFHCEFSSERGPRMCRSLREEDRALNQYPALYYPELYILKGGYRDFFPEYMELCEPQSYCPMHHQDHKAELLRCRSQNKAWEGERQLQEQIALLVKDVSP | Function: Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. Directly dephosphorylates CDK1 and activates its kinase activity. When phosphorylated, highly effective in activating G2 cells into prophase (By similarity).
PTM: Phosphorylated by CHEK1 and MAPK14 at Ser-245. This phosphorylation creates a binding site for 14-3-3 protein and inhibits the phosphatase (By similarity). Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-217 promotes nuclear translocation. Ser-224 is a minor phosphorylation site (By similarity). Phosphorylation by CDK1 occurs at G2 and G2-M transition and leads to increased activity (By similarity).
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 56639
Sequence Length: 502
Subcellular Location: Nucleus
EC: 3.1.3.48
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P20483 | MLWETIVEENNCSMDCNISNNTSSSSSINKMSGSRRARRSLELMSMDQEELSFYDDDVVPQDQQRSASPELMGLLSPEGSPQRFQIVRQPKILPAMGVSSDHTPARSFRIFNSLSSTCSMESSMDDEYMELFEMESQSQQTALGFPSGLNSLISGQIKEQPAAKSPAGLSMRRPSVRRCLSMTESNTNSTTTPPPKTPETARDCFKRPEPPASANCSPIQSKRHRCAAVEKENCPAPSPLSQVTISHPPPLRKCMSLNDAEIMSALARSENRNEPELIGDFSKAYALPLMEGRHRDLKSISSETVARLLKGEFSDKVASYRIIDCRYPYEFEGGHIEGAKNLYTTEQILDEFLTVQQTELQQQQNAESGHKRNIIIFHCEFSSERGPKMSRFLRNLDRERNTNAYPALHYPEIYLLHNGYKEFFESHVELCEPHAYRTMLDPAYNEAYRHFRAKSKSWNGDGLGGATGRLKKSRSRLML | Function: This protein functions as a dosage-dependent inducer in mitotic control. It is a tyrosine protein phosphatase required for progression of the cell cycle. It may directly dephosphorylate Cdk1 and activate the Cdk1 activity.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 54095
Sequence Length: 479
EC: 3.1.3.48
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P30303 | MEHSSPLAAMQPPSVMLGHCFRSDAPTSYHGFSPLPGLGPGGFNFKDLSMKRSNGDYFGTKVVRGSSPTASLAADLSQNFHIDQSPQVATPRRSLFSACLLGNGNRRGVDDAMTTPPLPSSSPAPAMDIMDMSPLPHKPPFISTPEIELDSPTLESSPMDTTMMSTDGLVPDSPTVLPKDGKQERRRPTFLRPSLARSKAQSFQVGMTRPAPESQGPPFKFQTNGINKTSSGVAASLEDMFGESPQRERPMMRINSTSGLNSRLRPPLGSGSHVRGNGSPSAASVRKSAHPNMRPRKQCRRSLSMYEHPEDVIADSEVSYTSNAPLQSISDFEETQALQLPHFIPEEQADNLPRIDKATLVDIKEGKYDNMFDNIMIIDCRFEYEYDGGHIVGAVNYNDKENLAAELFADPKPRTAIVFHCEYSVHRAPLMAKYIRHRDRAYNVDHYPQLSYPDMYILEGGYSGFFAEHRSLCYPQNYVEMSAKEHEFACERGLGKVKQRSKLSRAQTFAFGQQSPEMEDSPTGRCRNNPGDRKLLASPFNDSPGSRFPGRRMLSY | Function: This protein functions as a dosage-dependent inducer in mitotic control. It is a tyrosine protein phosphatase required for progression of the cell cycle. It may directly dephosphorylate p34(cdc2) and activate the p34(cdc2) kinase activity.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 61626
Sequence Length: 556
EC: 3.1.3.48
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P06652 | MDSPLSSLSFTNTLSGKRNVLRPAARELKLMSDRNANQELDFFFPKSKHIASTLVDPFGKTCSTASPASSLAADMSMNMHIDESPALPTPRRTLFRSLSCTVETPLANKTIVSPLPESPSNDALTESYFFRQPASKYSITQDSPRVSSTIAYSFKPKASIALNTTKSEATRSSLSSSSFDSYLRPNVSRSRSSGNAPPFLRSRSSSSYSINKKKGTSGGQATRHLTYALSRTCSQSSNTTSLLESCLTDDTDDFELMSDHEDTFTMGKVADLPESSVELVEDAASIQRPNSDFGACNDNSLDDLFQASPIKPIDMLPKINKDIAFPSLKVRSPSPMAFAMQEDAEYDEQDTPVLRRTQSMFLNSTRLGLFKSQDLVCVTPKQSTKESERFISSHVEDLSLPCFAVKEDSLKRITQETLLGLLDGKFKDIFDKCIIIDCRFEYEYLGGHISTAVNLNTKQAIVDAFLSKPLTHRVALVFHCEHSAHRAPHLALHFRNTDRRMNSHRYPFLYYPEVYILHGGYKSFYENHKNRCDPINYVPMNDASHVMTCTKAMNNFKRNATFMRTKSYTFGQSVLASPDVNDSPTAMHSLSTLRRF | Function: Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic and meiotic progression . Directly dephosphorylates cdc2 and stimulates its kinase activity (By similarity). Required for the G2/M transition of the cell cycle . Required for induction of meiosis II .
PTM: Phosphorylated by srk1 in the N-terminus; phosphorylation promotes nuclear exclusion.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 66566
Sequence Length: 596
Subcellular Location: Cytoplasm
EC: 3.1.3.48
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P23748 | MNNIFHGTEDECANEDVLSFQKISLKSPFGKKKNIFRNVQTFFKSKSKHSNVDDDLINKENLAFDKSPLLTNHRSKEIDGPSPNIKQLGHRDELDENENENDDIVLSMHFASQTLQSPTRNSSRRSLTNNRDNDLLSRIKYPGSPQRSSSFSRSRSLSRKPSMNSSSNSSRRVQRQDGKIPRSSRKSSQKFSNITQNTLNFTSASSSPLAPNSVGVKCFESCLAKTQIPYYYDDRNSNDFFPRISPETLKNILQNNMCESFYNSCRIIDCRFEYEYTGGHIINSVNIHSRDELEYEFIHKVLHSDTSNNNTLPTLLIIHCEFSSHRGPSLASHLRNCDRIINQDHYPKLFYPDILILDGGYKAVFDNFPELCYPRQYVGMNSQENLLNCEQEMDKFRRESKRFATKNNSFRKLASPSNPNFFYRDSHQSSTTMASSALSFRFEPPPKLSLNHRRVSSGSSLNSSESTGDENFFPILSKSSMSSNSNLSTSHMLLMDGLDTPSYFSFEDERGNHQQVSGDEEQDGDFTFVGSDREDLPRPARRSLFPSLETEDKK | Function: Terminates the cell cycle delay. Reverses the CDC28 phosphorylation catalyzed by SWE1.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 63358
Sequence Length: 554
EC: 3.1.3.48
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Q66WM4 | MPPVPLLRLQCGVNSYDWGKVGHESAAAKYAATTAASDFSIQSDKPYAELWMGTHPSLPSKDLETQRTLLDMVQDNQALISQEVSERYGGKLPFLFKVLSIRKALSIQAHPNKKLAEKLHARDPRNYPDDNHKPEMTIAITPFEGLCGFRPLVEIIHFLKAVAPLRQLVGERAASEFENTVKGSEESEDPAVTEKNKQALRTLFTSLMRSSPESIEAATKELVAIAQNSPETFTTSSSTPETNPTNPAELAAITVRLNGQFPNDIGSFVFFFLNFVKLEPGEAMFLKADDIHAYISGDIIECMASSDNVVRAGFTPKFKDVDTLVDMLTYSYAPIAEQKLEPTDYPYAVLNAPAYSSGSSCILYDPPIEEFSVVKTDLKRQGAKATFDGISGPSIVICTAGAGKITVGPKTEEVNEGYVFFVGANAECIIESTGEDTFTTFKAFCDLTGKEDMVNGN | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Mass (Da): 49930
Sequence Length: 457
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.3.1.8
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P34650 | MLLKLKCTVNNYAWGPKGNSSMAGSLALDGGHIPNLDKDKPYAEFWVGTHANGPAHVIEKDIALKQLLATSPELQGKHEKGNLSFLFKVLSVLGPLSIQIHPTKEQGKLLHATDPKNYPDDNHKPEIAIALTEFELLSGFRQHSQISEYLKLYSEIQELLTEEEKSQIDSLGSYGESSAQVLKKIFSRIWRTPKEKLQIVVDKLARRIQGHENKTALDEIIVYLFTLYPGDVGVFAPIFLNYFKLQPGEATFLEPNMPHAYLKGDCVECMADSDNTIRAGLTPKYIDVESLVEMLNYDETLLPKYIPNELDDGSLLFTPRGIDEFWVQEVKGPAGSIYQLPYSESCSVLTVLYGTATVTLGDASQVLNRGEVVFIGATHDAERPKINISDDFLAFRAFTPSPRALESLSNKRLIID | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Mass (Da): 46384
Sequence Length: 416
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.3.1.8
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Q9HFU4 | MSPSVFKISPGINSYDWGKKGSASLAAQLATTSIPDFSIDEDKAYAELWMGTHPNNPSRLSDNTLLSEHLKSHPELIGSSVSSKFEDCKDGSLPFLFKVLSIGTALSIQAHPDKPLAKKLFDEKPDVYKDPNHKPEMAIALTPFLAFLNFLPLSVLLLHLLTVPELQEFVDSSLTESLASSLGLPTSQPPDTSLFKPTESPATAEQKDILKQIFAALMSADKKLVEEAISKLIKRYQAKRDIKENEKSLVDLALRLNDQYPGDVGVLCVFLLNVVELKRGEAAFLGANEPHAYIEGDIIECMATSDNVVRAGLTPKLRDVDTLVSMLTYEAAPGNKQLLQPTPFQKGDDTTKLYDPPIAEFSVLRTELSKGMKTSHRPVEGPSLCVITEGEGVVRNGNDRSEFVRGDVIFVGAGKEVEWEAIKGLEMFRAYVEA | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Mass (Da): 47590
Sequence Length: 434
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.3.1.8
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Q643C8 | MSTEVSEAQARRAVADIFNSTLASSAIGAAWELGALDELRENGKLDVSDFAVRHDLHEPAVVGMFTALASVGIVRREGATVVVGPYFDEANHHRSLFHWLNQGSGELFRRMPQVLPNENRTGKFYQRDAGAISYACREISERYFDPAFWAAVDGLGYTPTTVADLGSGSGERLIQIARRFPGVRGLGVDIADGAIAMAEKEVAAKGFGDQISFVRGDARTIDQVSARGEFAEVDLLTCFMMGHDFWPRENCVQTLRKLRAAFPNVRRFLLGDATRTVGIPDRELPVFTLGFEFGHDMMGVYLPTLDEWDGVFEEGGWRCVKKHAIDSLSVSVVFELE | Function: S-adenosyl-L-methionine-dependent methyltransferase involved in synthesis of the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin.
Catalytic Activity: 3-phenylpyruvate + S-adenosyl-L-methionine = (3S)-2-oxo-3-phenylbutanoate + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37186
Sequence Length: 337
Pathway: Antibiotic biosynthesis.
EC: 2.1.1.281
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Q643C1 | MLTLHLQDDDVAAIDAVADELSRRYDSVESTEFQAESRLYADELPRRVRRALHEYRSTEKSGILVVTGLPVDDSALGATPADRRHKPVPSTSLRQDIAFYLIANLLGDPIGWATQQDGFIMHDVYPVQGFEHEQIGWGSEETLTWHTEDAFHPLRTDYLGLMCLRNPDGVETTACDIADVEIDDETRETLSQERFRILPDDAHRIHGKAPGDESARESALRERSRQRVASALESPDPVAVLFGDRDDPYLRIDPHYMQGVQGETEQRALETIGAAIDDAMSGVVLSPGDIVFIDNYRVVHGRKPFRARFDGTDRWLRRLNIARDLRKSREARLAATTRVIY | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Hydroxylates the beta carbon of free L-enduracididine to produce (3S)-3-hydroxy-L-enduracididine in biosynthesis of the nonproteinogenic amino acid beta-hydroxyenduracididine, a component of antibiotic mannopeptimycin.
Catalytic Activity: 2-oxoglutarate + L-enduracididine + O2 = (3S)-3-hydroxy-L-enduracididine + CO2 + succinate
Sequence Mass (Da): 38548
Sequence Length: 341
Pathway: Antibiotic biosynthesis.
EC: 1.14.11.40
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E9P8D2 | MDAESIEWKLTANLRNGPTFFQPLADSIEPLQFKLIGSDTVATAFPVFDTKYIPDSLINYLFKLFNLEIESGKTYPQLHSLTKQGFLNYWFHSFAVVVLQTDEKFIQDNQDWNSVLLGTFYIKPNYAPRCSHNCNAGFLVNGAHRGQKVGYRLAQVYLNWAPLLGYKYSIFNLVFVTNQASWKIWDKLNFQRIGLVPHAGILNGFSEPVDAIIYGKDLTKIEPEFLSME | Function: N-acetyltransferase involved in oxidative stress resistance. Acetylates the toxic proline metabolism intermediate (S)-1-pyrroline-5-carboxylate (P5C), or more likely its spontaneously forming tautomer glutamate-5-semialdehyde (GSA) into N-acetyl-GSA for arginine synthesis in the mitochondria. P5C has been shown to increase the levels of reactive oxygen species (ROS) in the cell by inhibiting the function of the respiratory chain in the mitochondria. The enzyme is able to reduce intracellular ROS levels under P5C-induced oxidative stress and protects cells from damage by oxidative stress . Also acetylates and thereby detoxifies the proline analog azetidine-2-carboxylate (AZC), however it is unlikely that AZC is a natural substrate as it occurs only in plants belonging to the Lilaceae family . Does not acetylate proline .
PTM: Not glycosylated.
Catalytic Activity: acetyl-CoA + L-glutamate 5-semialdehyde = CoA + H(+) + N-acetyl-L-glutamate 5-semialdehyde
Sequence Mass (Da): 26233
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.3.1.271
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Q801G2 | MATVVMEQIGRLFINAQQLRQIPRFLESAFPKLPCTVMVSDVPWVFRESHIITGYRPPDQNWRYYFLTLFQRHNESVNVWTHLLASLIILVKFQELSETVDFLRDPHAQPMFILLLAAFTYLGCSALAHLLSAKSEISHYTFYFLDYVGVAVYQYGSALAHFYYVVEEEWHAQVRTFFLPASAFLAWLSCTGCCYGKYASPKLPKFVHKLFQVVPSGLAYCLDISPVLHRIYRCYSSEHWCADQAVVYHCYQVLFFLISAYFFSYPHPERWFPGRCDFIGQGHQIFHVFLVLCTLVQIEAVRLDYTERRRLYEHLHGDLAHDAVALFIFTACCSALTAFYVRKRVKTYLEEKQE | Function: Steroid membrane receptor. Signals upon progestin binding, resulting in rapid activation of MAPK and down-regulation of adenylyl cyclase activity. Interacts with steroids with varying degrees of affinity, showing specificity for activation by the maturation-inducing steroid (MIS) 4-pregnen-17,20beta-diol-3-one (17,20beta-DHP). Capable of mediating progestin-induced oocyte maturation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41383
Sequence Length: 354
Subcellular Location: Cell membrane
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Q801D8 | MATVVMEQIGRLFINAQQLRQIPQLLESAFPTLPCTVKVSDVPWVFRERHILTGYRQPDQSWRYYFLTLFQRHNETLNVWTHLLAAFIILVKWQEISETVDFLRDPHAQPLFIVLLAAFTYLSFSALAHLLSAKSELSYYTFYFLDYVGVAVYQYGSALAHYYYAIEKEWHTKVQGLFLPAAAFLAWLTCFGCCYGKYASPELPKVANKLFQVVPSALAYCLDISPVVHRIYSCYQEGCSDPVVAYHFYHVVFFLIGAYFFCCPHPESLFPGKCDFIGQGHQLFHVFVVVCTLTQVEALRTDFTERRPFYERLHGDLAHDAVALFIFTACCSALTAFYVRQRVRASLHEKGE | Function: Steroid membrane receptor. Binds progesterone, progestin and 17-hydroxyprogesterone in vitro. Capable of mediating progestin-induced oocyte maturation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40585
Sequence Length: 352
Subcellular Location: Cell membrane
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Q7U0X4 | MSVRILVVDDDRAVRESLRRSLSFNGYSVELAHDGVEALDMIASDRPDALVLDVMMPRLDGLEVCRQLRSTGDDLPILVLTARDSVSERVAGLDAGADDYLPKPFALEELLARMRALLRRTKPEDAAESMAMRFSDLTLDPVTREVNRGQRRISLTRTEFALLEMLIANPRRVLTRSRILEEVWGFDFPTSGNALEVYVGYLRRKTEADGEPRLIHTVRGVGYVLRETPP | Function: Member of the two-component regulatory system MprB/MprA which contributes to maintaining a balance among several systems involved in stress resistance and is required for establishment and maintenance of persistent infection in the host. Functions as a transcriptional regulator that recognizes a 19-bp nucleotide motif comprizing two loosely conserved 8-bp direct DNA-binding motif repeats separated by a 3-bp spacer region (By similarity). MprB/MprA up-regulates expression of mprA and pepD.
PTM: Phosphorylated and dephosphorylated by MprB.
Sequence Mass (Da): 25924
Sequence Length: 230
Subcellular Location: Cytoplasm
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P53159 | MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHKEEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKNKNTEGAGISTPRKKLTESPIKLLSRNNIGKALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQKAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALLAGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI | Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 44585
Sequence Length: 387
Subcellular Location: Nucleus membrane
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C5E006 | MDFDKSSSSLVLDLAWNQVDKKNQDFIYAKDFPALIMSIEEILSRGQQTPLAFLSNTGKSVIDTFAREKEFFKIYRDEFKEIFHGLVGKTFKDTIEGTNVSRSVLDEQGQEPDVSTTPTRQQRSSPRKVNRLLKNLETRVASMKDELKFKDEILAEKDRELIQLTRKLSDYKDKYEFVQRQFSFYKDHGESPRRNSSESEQLNLEQNASTKHEFIISELKRKLQEQTLAISNLKEQLQRGEGAGVLYTNYSKRYNPLHNDGPMVLVLATLVFLTIILLIGSMIWVTGGKDDSNSFSQYSWWENNSLLSRIGWFFRDWSDTGVDYVNFEPSSDAYERIMGIRRI | Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 39859
Sequence Length: 343
Subcellular Location: Nucleus membrane
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P47069 | MNNSNEHRREEAGAANEQMPYNKAVKSAYADVLKDKMNREQEISLRAIKKGIYTDGGETDNYDMDKENDSAYEMFKKNLDFPLDQHNDDDDDDPYIEDNGQETDGYSDEDYTDEADKSFIEDSDSDSYDLESNSDFEENLESSGEAKKLKWRTYIFYGGLFFVFYFFGSFLMTTVKNNDLESHSSGATSSPGKSFSNLQKQVNHLYSELSKRDEKHSSELDKTVKIIVSQFEKNIKRLLPSNLVNFENDINSLTKQVETISTSMSELQRRNHKFTVENVTQWQDQLVKQLDTHLPQEIPVVINNSSSLLIIPELHNYLSALISDVIESPGIGTAGSAESRWEYDLNRYVKEILSNELQYIDKDYFIQEMNRRLQSNKQEIWEEITNRLETQQQQQQQQVQQDYSNVPQQYSSILMKRLIHQIYNSNQHQWEDDLDFATYVQGTKLLNHLTSPTWRQGSGVQPIELLTDSKQSSSTYWQCENEPGCSWAIRFKTPLYLTKISYMHGRFTNNLHIMNSAPRLISLYVKLSQTKEIKALQTLANQYGFGQHHKRDRNYIKIAKFEYRLTDSRIRQQMYLPPWFIQLKPLVRSIVFQVDENYGNKKFISLRKFIINGVTPQDLQIIENNEFPVLLGDTPEYGVTQNTDEGKRKVLLSKPPYASSSTSTKFHPASNVPSFGQDELDQ | Function: Component of the linker nucleocytoskeleton and cytoskeleton (LINC) complex that regulates telomere movement and meiotic recombination during meiosis . Connects the spindle pole body with the nuclear envelope through its interaction with MPS2 and mediates meiotic bouquet formation and rapid chromosome movements in meiotic prophase . Functions as an integral membrane anchor for telomeres and is a nuclear receptor for the SIR4 pathway of telomere tethering and gene inactivation . Essential for nuclear division and fusion and required for the first step of spindle pole body duplication in G1 . Functions in sister chromatid cohesion establishment . Recruits double-strand breaks (DSBs) to the nuclear periphery for chromosome healing .
PTM: Phosphorylation at Ser-189 and Ser-190 by CDC7 and CDC28 during meiosis regulates of the localization on nuclear envelope for meiotic chromosome motion and nuclear envelope remodeling.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 79175
Sequence Length: 682
Domain: The SUN domain is involved in the binding to MPS2 and is important for modulating chromosome motion events that act in meiotic chromosome juxtaposition and by extension, promoting proper morphogenesis of the synaptonemal complex.
Subcellular Location: Nucleus inner membrane
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K2RYB6 | MTSSTESKHSNDESTDLEKQDAEESHGLPEERKQDIAAQLSSSDVQDPNLVDWDGPDDPANPMNWPKSKRLGHVVMASLTTLFANITSTAFAPAASSLEAEFGITSSITAALTVSIYLLGFAFGPLVIAPLSEHFGRLPVYRVCTVITVAFLIGCAQAKNLGMFLVFRLITGIAGSGPGTIGGGTIADVMAPENRGKAMGAFAMGPLMGPVLGPLMSGFIAQYLDWRWVFRVLCIATGVMTIVLYFVMTETYGPVLLKRKAARLRKETGNPDLHTKLEASGVSPLASLWMALQRPTKMLIFSPITLLLSLYCAFVFGLLILLFTTFSAVYRQQYGFNVSMGGLSYLGLGFGLAIGLVLFGMLSDKVAKKDSARSSEWKPEARLLLMVWFAPVIPGGFFWYGWTAYYKVHWILPMMGTSLIGMGALMVMMPIQVYLVDAFGPRVAASALAANTLLRSLAGCFLPLAGPSLYEALGLGWGNTLLGFIAIGFTCLPILFYRFGGKLRLRFPVTF | Function: MFS-type transporper; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities . Efflux pump that might be required for efficient secretion of macrophasetins (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55336
Sequence Length: 511
Subcellular Location: Membrane
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K2SE88 | MAHPQSPGEFQILAAEGPTAGAAWTRHSNDAYPKYSALSKTHWEMWMLEGIEQTGNAGVTVTFFIDGSQTFHGNDPLHITFHALLPDGAIEKHHLIAAAVRVRETDASIVLEWPSKENGDGTEANSFSRIEVAQDHSSATATFNVPGAVQGSLALTSYTRSPDPTAGALGPAVSHRQIMTGAHAESDLSFPGSGRRLRFAGKGGHDRCWMEAAFPAILSDTTYVRGHAGPYTFASLGVVSRMGESRGRNCQKFRLLRDGVEVFASKSDTVSLTEDYFVLRSSHGGPVKGPFLDTTTGYRLDFVRPRAGKHWAFEIAHEKVWWSMPLGPPPLVREGNSGFVSKVRGGEVGGDADGETFEGAGDIGQIQMPELSTLVELKTLKAKAAAAATAPAPAEQ | Function: Diels-Alderase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities . The PKS-NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins . Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B . Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo-IMDA reaction in a regioselective and stereoselective manner . Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C .
Sequence Mass (Da): 42424
Sequence Length: 396
Pathway: Secondary metabolite biosynthesis.
EC: 5.5.1.-
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P0DTN5 | MADLPAKQTALTFQDDGTLGISHDAPVAELKPDMIIVKTAAVSVNPVDTKMESGFAKAGSIGGCDFAGTVVAVGAAVRRPVKVGDRVTGAVMGSDPNDPSSGSFATYVSAPADITLTLPESVPWAVGTSLSTVWFTVGQALFHHLLPDLAVTPSSPYAGDKPITVLVYGGSTSVGTAAIQLLKLAGLRPVTTCSPRNFDLVKSYGAEEAYDYRSPTCAADIKAATKSNLKYALDCITTKDSIAICYAALGRAGGRYTALDPYWEATAATRKTVKANWTLGITMLGKDIAWPAPYGRPGSEDARAFGAKWAAELQALLESGKMRPHPLRAKEGASWEDVLAGLKEVKEGKVSGEKLVFVF | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities . The PKS-NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins . Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B . Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo-IMDA reaction in a regioselective and stereoselective manner . Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C .
Sequence Mass (Da): 37659
Sequence Length: 359
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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Q9RW45 | MRFSAVSRHHRGASIDPMTFSEATTPDALTPDAHTPRLLTCDVLYTGMGGAQSPGGVVVVGETVAAAGHPDELRRQYPHAAEERAGAVIAPPPVNAHTHLDMSAYEFQALPYFQWIPEVVIRGRHLRGVAAAQAGADTLTRLGAGGVGDIVWAPEVMDALLAREDLSGTLYFEVLNPFPDKADEVFAAARTHLERWRRLERPGLRLGLSPHTPFTVSHRLMRLLSDYAAGEGLPLQIHVAEHPTELEMFRTGGGPLWDNRMPALYPHTLAEVIGREPGPDLTPVRYLDELGVLAARPTLVHMVNVTPDDIARVARAGCAVVTCPRSNHHLECGTFDWPAFAAAGVEVALGTDSVASGETLNVREEVTFARQLYPGLDPRVLVRAAVKGGQRVVGGRTPFLRRGETWQEGFRWELSRDL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of aminodeoxyfutalosine (AFL) into futalosine (FL). To a lesser extent, can also deaminate 5'-deoxyadenosine, 5'-methylthioadenosine, 2'-deoxyadenosine, adenosine, 1-(6-amino-9H-purin-9-yl)-1-deoxy-N-ethyl-beta-D-ribofuranuronamide (NECA), and S-adenosylhomocysteine.
Catalytic Activity: 6-amino-6-deoxyfutalosine + H(+) + H2O = futalosine + NH4(+)
Sequence Mass (Da): 45524
Sequence Length: 418
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
EC: 3.5.4.40
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A6Q234 | MRIIKPFAILTPQTIIQDKAVAFDKKIEAIDTVENLIKKYPNAAVEHDENSLLLPGFANPHLHLEFSANKATLQYGDFIPWLYSVIRHREDLLPLCDGACLEQTLSSIIQTGTTAIGAISSYGEDLQACIDSALKVVYFNEVIGSNAATADVMYASFLERFHQSKKHENERFKAAVAIHSPYSVHYILAKRALDIAKKYGSLVSVHFMESRAEREWLDKGSGEFAKFFKEFLNQTRPVNDTKSFLELFKELHTLFVHMVWANEEEIQTIASYNAHIIHCPISNRLLGNGVLDLEKIKSIPYAIATDGLSSNYSLNMYEELKAALFVHPNKEATTFAKELIIRATKAGYDALGFEGGEIAVGKDADMQLIDLPEGLTNVEDLYLHVILHTTKPKKVYIQGEEHVRE | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Catalyzes the deamination of aminodeoxyfutalosine (AFL) into futalosine (FL), a step in the biosynthesis of menaquinone (MK, vitamin K2). To a lesser extent, can also deaminate 5'-methylthioadenosine.
Catalytic Activity: 6-amino-6-deoxyfutalosine + H(+) + H2O = futalosine + NH4(+)
Sequence Mass (Da): 45532
Sequence Length: 405
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
EC: 3.5.4.40
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Q82K09 | MTEHFDARGTRDAQTGRDLHSFIAGLPKAELHVHHVGSASPRIVSELAARHPDSSVPTDPEALADYFTFTDFAHFIKVYLSVVDLIRTPEDVRLLTYEVARELARQQVRYAELTITPFSSTRRGIDERAFMDAIEDARKSAEAEFGTVLRWCFDIPGEAGLESAEETVRLATDDRLRPEGLVSFGLGGPEIGVPRPQFKPYFDRAIAAGLRSVPHAGETTGPETVWDALTDLRAERIGHGTSSAQDPKLLAHLAEHRIPLEVCPTSNIATRAVRTLDEHPVKEFVRAGVVVTINSDDPPMFGTDLNNEYAIAARLLDLDERGLAGLAKNSVEASFLDAAGKARIAAEIDTYTAAWLAP | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of aminodeoxyfutalosine (AFL) into futalosine (FL), a step in the biosynthesis of menaquinone (MK, vitamin K2). To a lesser extent, can also deaminate adenosine, 5'-methylthioadenosine, 5'-deoxyadenosine, and 2'-deoxyadenosine.
Catalytic Activity: 6-amino-6-deoxyfutalosine + H(+) + H2O = futalosine + NH4(+)
Sequence Mass (Da): 39203
Sequence Length: 358
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
EC: 3.5.4.40
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O86737 | MRPAYDDPRTTDQPITRARPPPRAARGRRLGEEPLTEHLVDPDVPRDLHAFIAGLPKAELHVHHVGSASPRIVSELAARHADSKVPTDPEALVDYFTFTDFAHFIDVYLSVVDLIRTPEDVRLLTYEVARDMARQQVRYAELTITPFSSTRRGIDEGAFMDAIEDARKAAEAEFGTVLRWCFDIPGEAGLESAEETARLATDDRLRPEGLVSFGLGGPEIGVARPQFKPYFDRAIAAGLHSVPHAGETTGPQTVWEALIDLRAERIGHGTSSAQDPKLLAHLAERRIPLEVCPTSNIATRAVRTLDEHPIKEFVRAGVPVTINSDDPPMFGTDLNNEYAVAARLLGLDERGLADLAKNGVEASFLDAPGKARIADEIDTYTAAWLAS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of aminodeoxyfutalosine (AFL) into futalosine (FL), a step in the biosynthesis of menaquinone (MK, vitamin K2).
Catalytic Activity: 6-amino-6-deoxyfutalosine + H(+) + H2O = futalosine + NH4(+)
Sequence Mass (Da): 42430
Sequence Length: 387
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
EC: 3.5.4.40
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Q9HVF1 | MAQNDHETVDMLLVGAGIMSATLAVLLKELDPNLKMEVVELQESGAIESSNPWNNAGTGHAGLCELNYTPQSADGSIDIKKAVGINTMFEVSKQFWSHLVAKGTFGSPKTFINPVPHLSFVRGSEGIAYLKKRFESLTKHHAFETMVYSEDKATLAEWMPLMMPGRPADEAIAATRVEGGTDVNFGALTNQLLQHLAQQPGAQIRYNQKVTHLRRADNGWRVTVKDTRNGGDREIQARFVFLGAGGGALPLLQLSGIPEGKGFGGFPVSGQWLRCDNPEIVKQHQAKVYSQAEVGSPPMSVPHLDTRVVDGKKSLLFGPYAGFSTKFLRHGSFLDLPLSVRPGNILPMLSVARDNMDLTRYLIGQVMQSPEQRLEALRKFYPEARAEDWRLEVAGQRVQIIKKDPKKGGILQFGTELVAAHDGSIAALLGASPGASVTVSIMLGLIERCFPEQARSPEWSAKLKEIFPAREKELESDAELYRSVSSRCSEVLELTAKNDVQAPVNAE | Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Mass (Da): 55498
Sequence Length: 507
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
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Q9D159 | MANGTDASVPLTSYEYYLDYIDLIPVDEKKLKANKHSIVIALWLSLATFVVLLFLILLYMSWSGSPQMRHSPQPQPICSWTHSFNLPLCLRRASLQTTEEPGRRAGTDQWLTQQSPSASAPGPLALP | Function: Modulator of melanocortin receptors (MC1R, MC2R, MC3R, MC4R and MC5R). Acts by increasing ligand-sensitivity of melanocortin receptors and enhancing generation of cAMP by the receptors. Required both for MC2R trafficking to the cell surface of adrenal cells and for signaling in response to corticotropin (ACTH). May be involved in the intracellular trafficking pathways in adipocyte cells (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14170
Sequence Length: 127
Subcellular Location: Cell membrane
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A3DE29 | MKLNLPFNISPHVFVFILSFAFSLILGPVLIPMLTRLKFGQTVRDDGPKTHYKKTGTPTMGGMIFLIPVTVLAAFYAGHDRRILPLIFVTLGFGLIGFIDDFIKVVKKRKDGLYWNQKMFGLLLVAVTFAVYLSHTHTSDIIIPFMGMDKTVSLGWLFVPFVVLVLIASTNAVNITDGLDGLAAGVTLIVTVFFTIVAMTRSEWEYIKMFSAMVAGGCLGFLTFNAYPARIFMGDTGSLALGGAVGAIAILMKMPLILLIVGGIYVVEALSVMIQVLSFKLTGKRVFKMAPIHHHFELSGWKEVKVVLVFWTITVLLCILGFFALRLKFY | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36488
Sequence Length: 330
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 2.7.8.13
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P64258 | MLVWLAEHLVKYYSGFNVFSYLTFRAIVSLLTALFISLWMGPRMIAHLQKLSFGQVVRNDGPESHFSKRGTPTMGGIMILTAIVISVLLWAYPSNPYVWCVLVVLVGYGVIGFVDDYRKVVRKDTKGLIARWKYFWMSVIALGVAFALYLVGKDTPATQLVVPFFKDVMPQLGLFYILLAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAGGFALVAWATGNMNFASYLHIPYLRHAGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVLLRQEFLLVIMGGVFVVETLSVILQVGSFKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISLMLVLIGLATLKVR | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39903
Sequence Length: 360
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.8.13
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Q52952 | MLIWLVELADHFQFFNLFRYITFRTGAALFTSALIVFLFGPAMIASLRIRQGKGQPIRADGPQTHFKKAGTPTMGGLMILTGIVVSSLLWADLSSIYVVSTLLVTLGFGAIGFYDDYLKVTKQSEKGFSGKARLGIEFVIAAVAVFFMMQAALSAGAAGSTFGSSVTFPFFKDLMLNLGYFFVLFGGFVIVGAGNSVNLTDGLDGLAIVPVMIASAAFGLIAYLAGNAVFANYLQIHFVPGTGELAVILGAVIGAGLGFLWFNAPPAAIFMGDTGSLALGGLIGTVAVATKHEIVMIIIGGLFVIETLSVIIQVFWFKRTGHRVFLMAPIHHHFEKKGWTESQVVIRFWIIAVILAMVGLSTLKLR | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39266
Sequence Length: 366
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.8.13
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Q73G61 | MILATKVFFTSFVFGFILFPYFIKLLKKISKDGQPIRSCGPESHLITKKNVPPMGGIIILISSLLPILLWAQLTPEILLLILITLFFALLGFIDDYLKLKTNHYRGLSAKTKILIQFIVALVGVFILKLYSAECFTKTSLFKGVIIDFGYLYVPFAAFVIVGSSNAVNLTDGLDGLAATQVITSFAFLGLIAYITQADMNITLFCIAFIGAILSFLWFNTHPAKIFMGDVGSLSVGAALGLTSVLIKREMLFAIIGIIFVIETLSVIIQISYFKYTKFKYGEGKRVFLMAPIHHHFEKKRWSENVIVMKFWIISIICSVFTITFLL | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36491
Sequence Length: 326
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 2.7.8.13
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Q9P7T4 | MASLDENADELHRMDSSDEASINDDQEDILDTPRTRVRKMLASVDMQLSSNAVSEASLDKESTVGNLENQKNRSYSSEIYLHSDTNFLSNFDSAYERVRRLLNQQGGKSSLQKKEVEQIETQEGGDNAKGSPSSENKDSDRNSRLQQLIEKKRNALKKEQEDLIQNSATSHSKSDNLDSESADDSDLADESELSKKYTSDRKIRNASKKALLELHRNTARLTRETALKPEVVVKKKVTLREFFQKIGFKNDNQLENKAISEEEANSTEPPNVEKEEPKPSVDRSTGIVNSEDIKELSVEDDSLELKEITPEALDIGQTSLFTTLNQTQVKKEDNKKFLLKEINAKLNEDDIDSELEIEVKPKTTALDNIEKSKLSEENEHGIKGKLKQLAEIKLSKDGKPFENEFNIKSFNRNLVKRAAVMAKLQRNQLEEELKAKGIYKPTIQGEKEEEEDPLERARNDAEKIRQLEKASGNASDEGELNDEEEVISSSNTPSTKAKTTNKVIISDVIIEATQAEPKRRQKNSRVVFDEEDLTGDSHGSSNMKISESDDESNGDMIRDSFDRLSSESIKDSQKTEELHDSFGINDEVDQSTSLYVQNSQPSASQLTIVDATYSQPPPRWESSSRDDKTNTSSTQPSQVDSLVPTQLDSTIPTQIDSVQRNKDQDDEEILEERRESRRDSKTFLSRTMLYNKDTGKADSAWASDLIEEQAIESDDEYAGIGGLSDDGLSDSDAELEVQNMIDDETTIQKGEVASMAQFAKDQEMDRDEKLVKQLMKDVTTGALRKRNRNGFAALDDSDDEDYSNLRREKLKELRRQKLLEDGNLNVLEGDKRKAFLATVEDSLVSSKDNLTWLDATVEDSGVGSSDLGDEYLYSEQSLNHEEEEQMEEELSEIFSSGGPNVVDRVYLKKSSTRHTSDNNSLEEVLPIFPGVRKLVSNSQSEKIGDLSNDNSMGAKSYKTPIISSTQRPQGRKFRGLMNQSSKADISRTVDAGSIKVVPNSQSANPPRLLASLNNYSDFD | Function: Component of the replisome and is required for rad3-dependent activation of the checkpoint kinase cds1 in response to replication fork arrest. Phosphorylation allows it to mediate the activation of cds1.
PTM: Phosphorylated by rad3 and tel1.
Sequence Mass (Da): 114319
Sequence Length: 1019
Subcellular Location: Nucleus
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Q05648 | MLSFRSLTSTFGFVSRFQIRRLGTSLSIQNLEVQDGRWKGKLATEKKTNREHKSVDTNIKTMKMLKNPKNSTRYLRRSFVPNHRKQENGRDILEDSLSKDHLKVKSCITITTGEGYDLKRCMKLLTMQGLQPTNLIPDEIVSFSYQDNGNKGDVMILGQNGSIVSWGFSESSVRNCIVPIVKAASLNPLNGEDFETEDMDYVEIEGEQDFDKLSSLDNKVTPRIACESFLSGDLIIINSLDSDQGMLDKAAFSSGLSRSTNLAVLEEAMEKHISKTRTITENISKGTKLNLRSSDALKSIGRLFLIRGKLNLYSELIETPDLYWSEPQLEEIFKNVSRYLDIGPRINILNSKLDYSTDECRALISLLNERNSTFLEWIIIYLIAFELCFEIYHFYQKYSSYCSEPTNDDLDATK | Function: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47173
Sequence Length: 414
Subcellular Location: Mitochondrion inner membrane
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Q03079 | MTVMNLFFRPCQLQMGSGPLELMLKRPTQLTTFMNTRPGGSTQIRFISGNLDPVKRREDRLRKIFSKSRLLTRLNKNPKFSHYFDRLSEAGTVPTLTSFFILHEVTAILPLFLLWWLLYNLDLSDDFKLPNFLNGLMDSCHTAMEKFVGKRYQECLNKNKLILSGTVAYVTVKLLYPVRIFISIWGAPYFGKWLLLPFQKLKHLIKK | Function: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24166
Sequence Length: 207
Subcellular Location: Mitochondrion outer membrane
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P0DKT0 | MSNVTIYATDWCPYCRSLLKGLDGQEYDLIDVDQDEEAGEWVKSVNDGNRIVPTVRYSDGTHATNPLAAEVIAKIEALA | Function: Involved in defense against toxic arsenate. Involved in the mycothiol/myoredoxin redox pathway which uses a mycothioltransferase mechanism; functions as a monothiol mixed disulfide reductase and is recycled by a second mycothiol forming mycothione which in turn is reduced in a NADPH-dependent manner (By similarity).
Catalytic Activity: [mycoredoxin]-L-cysteine + arseno-mycothiol + H(+) = [mycoredoxin]-S-mycothiol-L-cysteine + arsenite
Sequence Mass (Da): 8717
Sequence Length: 79
Subcellular Location: Cytoplasm
EC: 1.20.4.3
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Q12467 | MTVLYTSASLKKMKCLAFNMGMNCVRTVSHARSGGAKFGGRNVFNIFDSKTPDSVRIKAFKNTIYQSAMGKGKTKFSAMEINLITSLVRGYKGEGKKNAINPLQTNVQILNKLLLTHRLTDKDILEGMNLAAGPVNVAIPRDITPQEEKKKVELRNRKAENMDLHPSRKMHIKELLHSLNLDMCNDEEVYQKISLYLQKNEESRTSVGASQQNHVDIDINSLKRYLQNIEKKARQKSAIDKQKKNQARIYQWNTQSFSEIVPLSAGNILFKREPNRLWKRLQNGISVFLGSNGGGKKSKTTKKVLQGNNILLHSLENNKDMTLSNNFDHSVFNINFTDLFGVINASGSPPDRVLNEINEIELKGWKCVGNLYDNNKIVVFQSSNPLLEDTKIPQKSFTNSKRFLISLSALLASFFAYYRYRLSQRQESKK | Function: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 48827
Sequence Length: 430
Subcellular Location: Mitochondrion
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Q05473 | MEQLCKRYVHTPAAFIQNIVANTKRTTLATQLSVEKAKKKVPKTALKKKLNSRPKERLPNWLKLNDVFNIHYEKPSNSDINKVNRFFNKAKVEFEWCAASFDDIPENPFLNKKSHKDILKDHGECGTTLIDTLPEVIFLGGTNVGKSSILNNITTSHVSRDLGSLARVSKTTGFTKTLNCYNVGNRLRMIDSPGYGFNSSKEQGKVTLQYLLERKQLVRCFLLLAGDKEINNTDNMIIQYIHEHGVPFEVVFTKMDKVKDLNKFKKKVMSSGLMDLPTLPRLVLTNSLTSSTSPKRFGIDLLRYVIFQSCGLIL | Function: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression.
PTM: Sumoylated upon ethanol stress.
Sequence Mass (Da): 35614
Sequence Length: 314
Subcellular Location: Mitochondrion
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Q07349 | MFKVPVGLASRTRELMNSVTLNSLNNGKGFNMYLPGILRAFPKPVPSAITSPAIPKYRGESFQFRKLSCISSNYCSTTHQFLSSLKSSTSRLVGKRAFHSSRRAEIKFIFSSKSPKNGNKPFVKVYKVSPFFIIFATASIFTFILTSTIVVIPLIFHFFFPLLIMFFFFKQFKKWQKNIFYKDVLTSLPKTKLKITLPTMRSLQLQPMVQSWKEISSRMGIPNEFAKGLNVDLVKQEETRKQFLSFLQKRVLESFTKNELGIRSYFLGDSVEKWIKESYDLELDIDNCRSELRKFQTFIFSSVRYKLYLDSMKNLPLNPSKKLEGKKHIADVYVIILDESFPAIMFNGGAYSKADFFKILQESETSNSSKTLNTIIAIKSVNTLLSKHFVITTNGDSGEFFSKYNISKINDKNTEYTLKE | Function: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48312
Sequence Length: 420
Subcellular Location: Mitochondrion
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Q750Q4 | MFRVTGIATARAVALQPFRAPLGVIRRFGISATASYEFQHGHDMQSRNGSRWDSRRQGDRRSSRWEGRGSDREDGERGSRGGMWRKPQGRRGRTDGAAREGFSLGPNTEVVRVADEAAGVESTPRTLVEEGVLSNELYEMLQSRGFDKLTPVQQKTLKPILQTEHDVVARAKTGTGKTLAFLMPLFQRLLEGPPSENVKAVVIAPTRDLAAQIFNEINEMRNANRKLRRFNAVVMMGGSSRTETFRSLERRRPNIVVATPGRLIDMLEACGPKYFTEVDFKVLDEADTLLEIGFKQALEQINDILNQLNQKGTTHIRTLLVSATLDDKVQSLANSIMNHAKCLFIDTVDPNEQATNENIAQKVVISKDFADNITASLYKIREEASANPKLKAIVFMPTIVAVEYWGELLQSQCRGTPVLLFHGGLSQGRRNSTMKRFRAMDSGILVCTDVAARGMDVSDVQHVYQVGVPTSPDNYIHRIGRTGRAGRKGSSTIFLAEHELCILDILRRKNNVVISDQETFDAAAQELSDVREAFSLDRDRLHDFLLKNLSFYRGSQGEYDFPLEAYISIARAYGTLLGDSNQRLTLSGRMLTTFVPNHPAVCSLFNIIGPVNSKSSYGFRDTNKRHRRGRLDDSGRLEYSKKRHSYARSYSPSISDGF | Function: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 73643
Sequence Length: 658
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Mitochondrion matrix
EC: 3.6.4.13
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Q4WRP2 | MMLGAVRRYGVVHALRASVPRTICRPSNSQLLRCQTSPVTACPQSVRLLHKSSPFFSSASAQAQAQPDDLQSAAPQEPLREFTDLAERGLVDPKIIRAIVKDMNIKTMTDVQSQTLREILQGDDVLAQAKTGTGKTLAFLTPVFQNIMKDPSLKGLNWRRSQASSSDIRAIIISPTRELAEQIAVEARRLAAHSGVIVQTAVGGTQKREGLRRIQREGCHVLIGTPGRLKDVLSDSYNGVTAPNLSTLVLDEADRLLDDGFSDAIIDIQRLLPDPMKVDRQTLMFSATVPREVMQMVRKTMKPNFKFVKTVRDDEVPTHLTVPQKYVILRGYENAMPALLEFVTKYVEGEKENPNQRPFKAIVYFNSTVQTNLVYETFRNIVEQRHHPLRRVRVYEIHSQLTQARRTRSSDFFRAAKSAILFSSDVTARGMDFPDVTHVIQVSIPRDRATYIHRLGRTARANKTGEGWVLTHRGELPEFLKQLEGIPLNLDKETFATATVDMTKPELDPKSPATRFIQEIKDAVREVPESLKRRAYTSLLGPLRGYFARKQDLIQAINNCVVHGYGLPVPPQLSPTLARNLGLDRVPGVRIANYRGSSDNMSTRPDYRGGDRDMWASNSRRGREFNSDRRESRFGNHRNADDFFGGRRRAYRDDY | Function: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 73931
Sequence Length: 655
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Mitochondrion matrix
EC: 3.6.4.13
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Q2UST1 | MKTGRTRPLRVFDILVPPWPPTVPHRIKLPRGKTNWFEFYSAITRNWNKLKGLKNCWQIWKDVQEIIRRIRKYQGESTVMQGPGNNDGAHPYATMAGKLDSKLLQALKVMEFEYMTPVQHRVLTELPSWRSDCLVQAKTGTGKTLAFLLPTLHCLLQGHSAPPRGQVAILIITPTRELAQQIAKSCDQLTSQLARPLECHIAVGGTARASALARFMKGAPSILVATPGRLKDYLSEPSTAEKLSNIQTLILDEADTMLESGFLADVKRILQLIPPKSTGWQGMCFSATVPPKVKDVVSVVLKPGYTSISTIEKNETPTHERVPQYHVLIPSVADTFTTLASLLNLEIKNSSKIIVFGVTANMVALFAAAFSQGLTPLKVFEIHSRLSQSARTKTTALFKEAATGIMFASDVIGRGMDFPNVDLVIQVGLPSNGEQYVHRVGRTARAGNDGRAIILLTEAESFFMKVNRHLPIQPHPQTDAINAGASSCADAVTKAMYSIGEETKQRAYSSYIGFFAGSGLLKQVRLDKPGLVQLANELAIQGMGCPEPPPMDKKVVGKMGLKGVPGFNYATGNDLNGDRPARPRGRPGNKTRDVLSPGAGQGDRRGSVSKNRGGRRGGGRGGRGGRGGKPRAA | Function: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 68795
Sequence Length: 633
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Mitochondrion matrix
EC: 3.6.4.13
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Q5APM7 | MLKQLSRSLGIRSSPIVANLIRSKQVCTRGFHISLVKQNTSSKVNEITDITSDSLKVKEDAAGSDLPSTKTDKKSKSESFQPVKFEDFKGKGYIHDSIINSLHKNDFKELTPIQQKSLVPIFNTEKGLVCRAKTGTGKTLAFAVPTLQYAYKNRGKGVSTVVLVPTRDLAFQIEEEYRKLISHLKYNERPNLELIIGGQRTSFNPRRPAEIVIATPGRLEKELQTDRKLAKCFSNVTYRIYDEADRLLDVGFESVLNEIDGLLYKVRTTPKPIKSLLFSATVDEAISEFSKKHIHPEYEFLNTVTKDDLEIPENIHQQLIECTDGIDKVNVSLSELHGIMKQHNDYKVIVFLPTKTAVDWFYEYITNALDDELFELFSKPPRVFMLHGGRSVRQRSAALKGFKVAKKGILISTDVAARGIDVKDVTNVMQMFPSVEIADYIHKVGRTGRAGKKGKASLFATPAELPYVSLLKRKRKVKFQEVIQSEKLNSSNIIDQIESPLDSTKEFLATMVGYLQQLQSAHRLDYDSLVIENMELYRKLVRDDKAMLESRILSRIGKGISAHVKRRYFTRTRYQSHDDAEFDSYSDFSRSGMSQRPRSNDRSSKMTFNGRGKYGNNRNNDWSYQNKNRYNNNNNRQTERSYDSDRKSHNDWKYEKKFEHRRIRDHDE | Function: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 76701
Sequence Length: 668
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Mitochondrion matrix
EC: 3.6.4.13
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Q6FU81 | MLRHCSLGLVTTQISAIAPLRLVGSPLFCRSYQDFAGRDRRSSRSREDKPYNSRTRRFDDEGSSNYSSSRDDYRGQNTYGFRGKAPRKNFSSRDNYSSRDNFRSSNGFQERGYKNKFSKNTKSYSKGGNTSGSFIPEGKMAKMTHIGKSDSDIVVTLESLLEKNVISRDLYDSISRMGFEQLTPVQQKTIEPIITNSDSDIIARAKTGTGKTFAFLLPIFQHLLNTKIDSQNKVKSVIVAPTRDLALQIEDEVRKIHSKNRKLKAFECVSLVGGTNFDRSIRYIEKVSPSIVIGTPGRLIDVMEKFGNKFFKDVDFKVLDEADRLLEIGFKEDLSYINKMLNTLNTNSTEHIRTLLFSATLDHKVQSLSNDIMNKEECLYIDTIDENEPQAHEKIDQTLVVGETFADNLYAAIEHIREFGTKTPNYKSILFLPTVKFTKFMATILKRQVKLPIYEFHGQIDQKKRTRIVNEFKTMKKGLLVCTDVGARGMDFPNITEVLQIGLPSEIPNYIHRIGRTARSGKEGSSVTFISKEELPFFEILEDKHNVTIKNIRKFEAQPHVMADLSLRLHVSEDELQEIILSVISFYRACLKDYGINYKNMLPQIAHTYGTLLQNEDKRIPLAGNHILNRLGMDRDPIATKMFQIDEMPNQYNRRGPRSNYNRRRF | Function: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 76320
Sequence Length: 666
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Mitochondrion matrix
EC: 3.6.4.13
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Q6CQA1 | MLVLQRIPKRALQFNGVTGTVCSTRLFHHAFNLNLQQSFVPSEERRYRNSNRGFTRGSDSNSNNKYRNSSYDDNRSRSNYGGDKRNNRNNNNYGNNRNNGSRRRYQDENSDIEVFKSKSFNVTTLNPESFHEQVTIDSLLEESLLDANVHKAISAMKFESLTPVQQRTIKPILTTENDVVAKAKTGTGKTLAFLAPLFQHLISTKLQNPLAVKAVIVTPTRDLAIQIASEVKKLQQCNPSLKSYRSLTLIGGTNLDKSLKDLHTLNPNIIVGTPGRINDILDRVGAKYFKDVDFKVLDEADTLLQIGFQTELSLISRKLNEFNTQGEEHIRTLLFSATMDHNVQELAATIMNKKDCLFIDTVDKNDSEAHDSIDQKLVITKSFAESMVALIQSIESELLQKKNFKAILFLPTVKFVDFFSETLSESLTKRIDIIKFHGKIDQKKRTKLVDRFKKTNHGIFVCTDVGARGMHFPSVEHVYQLCVPTSLPNYIHRIGRTARAGESGAATIFLFREELKFVDELRRDTNVVIKNQEDYLNQDKENFDMISSIITNNPDFPEALKSIIGFYKGVQNEYRLNYKVAQNVLRSFSELHSDSSMLLRFRPSEINNFFSNRDMRFVSDLIDVKNPHSFGKDREFDDEDRYTSRSQNNYKSKQSSKSNRFEGRNDYSNSRRSHANQKRNFTFDD | Function: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 78559
Sequence Length: 685
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Mitochondrion matrix
EC: 3.6.4.13
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A5DTK7 | MMIARFGKQVLRKNVLVSNRIHFPVISRGFHNSFINKSDDLKSPPIDITKGQTEAKVETKKDKFAGFGLDLDELIGETAKGSQVTEQTELTKSEEEEKKKKNINTNTNKNDRKSVPAISLEDFNPSQFKDFKNTGLIDDVILRALDRAHFKDLTPIQQKSIVPLLETERGMVCRAKTGTGKTLTFLIPTLQSAVSRKIASGGRSSGVDTVIIVPTRDLALQIYDEYQKVLRGISGSRKPHISYVIGGMKNSFNPRNPSEIVIATPGRLEADLRSPLFASAFTDIKYRVYDEADRLLDVGFEPTLDSIDRSIKMIRSDDAEPLKSLLFSATVDARLDQFAKQHINKKYDYINTVPEDDPEVHENIHQVMYKCKDAIDKFGSFFNYVNQLVKDSPDMKMMVFLPTQTAVEFLYSYMSEACHKHDVDIDIFHLHGKRSASQRQRALSNFKRDDSGILITTDVAARGIDVKGVTHVVQLFPSSEIADYVHKVGRTGRAGKEGKAVLFITQPEMAYVRRLNSERGVTFEQVHESSEIDNSIDFFEGMRPDEQVANDFFYTLMSFLAQISSTYRLRADDLVAENVSLYRAILQKPDAKLSLRAASALIKRLNRDVVREFFEQGRGGNNGGYGGYGGYGGSSYGRSGGSNRYSGGGGNRSEKRFSFAGRGGNSGGHSGRGRGGRSGYSGGRSSQYSDWE | Function: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 77154
Sequence Length: 692
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Mitochondrion matrix
EC: 3.6.4.13
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Q2SIN5 | MSKVAKQYAGAQVYGRLLSYLKPLWKVFALAVLGNVIYALASAAMADATKYIVAAIETPSPEGRLLVPMLIIGIFALRGLGSFCGGYFMARVARGIVHRMRLELFRHLTVLPCRFFDSNSTGHLVSRITYNVDQVTGAATNAITVVLREGFTVIGLMGYMIYVSWKLTLLFLVLGPIIGVLIGYVSKRFRRISRRIQSSMGDVTHVASESIGGYRVMRTFGGEEYEFNRFMKASEYNITQALKMSLTQALSTPIIQLVISVFIALLVWLALSPEVRGNMSTGEFLAYITAATTCAKPIRQLTEVNAVIQRGISAAQDVFMQLDEPVEKDEGSYVADRVQGRLEFKSLGFAYSDEGKPALQEINLVIEPGETVALVGRSGSGKSTLVNLLPRFYDYEQGEILLDGKPLKDFALTSLRRQISIVTQQVVLFNDTVTNNIAYGALADATPEQVREAAKSADALGFIEQLEQGFDTLLGENGTRLSGGQRQRMVIARALLKDSPILILDEATSALDTHAERNIQSALETLMKGRTTLVVAHRLSTIENADKIVVMDQGRIVEVGSHRELIEKDGAYAALHKLQFSEADA | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-core oligosaccharideSide 1 = ADP + phosphate + lipid A-core oligosaccharideSide 2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64225
Sequence Length: 585
Domain: In MsbA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Subcellular Location: Cell inner membrane
EC: 7.5.2.6
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Q31FG2 | MFDRHTLSLYKRLLKYISGYKSAIFITLITIAIIAATEPLSAIILGNLVDESLIEKDPNSFLLLPLQLAAVFIVKGVAEYFSKVMSTWIAQKAIFNIRSELYDKMLCLPQAEHNQTSTGTLMSKVTYDVTQTGNALSEAWIVIARDSLTILALLATLIYYSWQLTLVMLIIGPIVAFFIDRAGKLMRTSSTDMQDNMGEMTHRLEEGLKGYQDIKIYGSEKYELDRFKASAESLRQNTMKVIKVSALNVPLVQVIAAIALSIVVYIAVQMVNAETMTAGNLITYVTAMGLIFEPIRRITNINATVQRGMAAAKSIFAILDTPSEANNGKIELSNVNGQIDFNNVSFSYLGTEKTALNNFSLSIPARKTTALVGQSGSGKTTLANLITRFYQVNHGTITIDGIALDEIELNNLRANIAFVSQNVVLFNDTIAANIAYGHEEYDEQAIMNAAKAAHAWEFIEKLPEGLNTIIGDNGTLLSGGQRQRLAIARAFLKNAPILIMDEATSALDNQSEKLIQEAMNSLRKNRTVIIIAHRLSTIENADKIVVLEEGSLKEQGTHAELMALNSIYSQLYKQGNLSEQV | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-core oligosaccharideSide 1 = ADP + phosphate + lipid A-core oligosaccharideSide 2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64038
Sequence Length: 581
Domain: In MsbA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Subcellular Location: Cell inner membrane
EC: 7.5.2.6
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Q5ZUH9 | MKNNLPIKSRLLYKRLLSYVKPFWPVLLLGVLANILYSGIDAGFTYMTKLFLDKSFITIDLNFVKQIPLIVLIGITLRGLVSSLGSYCMTWVARSVVKVLRQTVFSHIIHLPADYYDEATSGQLLSKILYDVEQVAQVSADALTDFIQNICLVIGLLTVMMVICWQLSLMFLLTIPFVGIIVNYTNKRVRRISHKVQKTMGEVTEIASEAIEGYRVVRIFGGERYEITKFNKATEYSRKNDMKVAISKAINVSGVQLVIAIGIATIIMAAIHLSTVITISAGSFLAIIAAMLQLIKPMKTLTTLNATIQRGLAGAESVFNLLDLPLERNNGLILKEKIRGEIEFKHVYHAYRQGQNILHDVNFVIEAGTSVALVGHSGSGKTTIASLLPRFYELSQGMITLDGMPIQQLSLESLRKQMSLVSQNVTLFNDTLANNIAYGRFDASREQIITAAKLAYADEFIKQLPDGYDTRVGENGVLLSGGQRQRIAIARAILKDAPILILDEATSALDSESEHYIQAALEQVMKGRTTLIIAHRLSTIKHAHKIIVLQHGRIVEQGSHQELLDMDGHYAQLYKVQQFGRINEEVVA | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-core oligosaccharideSide 1 = ADP + phosphate + lipid A-core oligosaccharideSide 2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65419
Sequence Length: 588
Domain: In MsbA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Subcellular Location: Cell inner membrane
EC: 7.5.2.6
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Q60AA3 | MKHSASESKPLSSGLAIYRRLLRYGFPYWRSFCVAVVAMIAYAAITPFFAKLIQPLIDGSFIDNDPTVLRQVSLMLIGLSVLRGIAGFLSEYCSGSVGRRVIADLRRDIFDQLLNLPCSFYDNASGGQLLSKLLYNTEQVSASLQQGIITCIREGFTVIGLMALMVYQNPVLSLVFLVLGPVLGLSVRFVSKRFRRLSMRIQESMGKVSHVTQEVIDAQRIVKVFNGKDYEAAKFATENDRNQKRQMKLIATDALGGGVIHLISVAGVAGILYVVSLDSVRQTITPGSLMAFIAAMAMMLSPIRRLSQVVSVMQRGIAAGDSIFAMLDLPRERDRGRISLKRARGSIEYRHVSLVYDDRHGAAVDDVSLVIPAGKTVALVGQSGSGKTSLVRLLPRLYEATAGEILIDGHDIRELTLESLRRQIAYVGQEVTLFNDTVASNIAYGCLDRVGLDAVREAARAANALDFIETLPQGFDTLVGQQGIVLSGGQRQRIAIARALLKNAPILILDEATSALDAESERYVQQALEVLMQNRTTLVIAHRLSTIQNADQICVMRGGRIIECGTHAQLMAARGGYADLYAMQFGYSSVPEAVAVHAVRR | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-core oligosaccharideSide 1 = ADP + phosphate + lipid A-core oligosaccharideSide 2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65686
Sequence Length: 601
Domain: In MsbA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Subcellular Location: Cell inner membrane
EC: 7.5.2.6
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Q1GZI0 | MSKTALGKANASVQSARALYLRLLKYAARYWVAFLISIIALVTFSATNTGFLATIKLVTDAGFVNQDSTKLHLLPFMLFGLLAIRALAGFISNFAMRWVARRVVENLRQDTFRRLMSLPVSFFDAVSAGVVTSKLTYDTEQMAGAATKVAMSAVRDTLTILGMVGYMLYLDWQLTLIFAVVAPAMAWYLKSMTPKLRSSGKAVQQTMGEMTKVIEEAVSGQRMVKIFGGGDYEYQRFTKVAGKNRHMQIRLARFSGLNSMVVELLAGVALALVVFYAVGKFSAGEFAAFIGALLMLIGPVKTLTSLNEELQVGLAAAHSVFELIDSIPEVDEGHEEIGRAEGSIVFENVTLQYPSAQRPALLDLNFTVKPGEKIALVGRSGGGKTTLVNLLPRFYEVQQGRVLIDGVDVRNMSLKSLRQQFSLVSQDVILFNDTVFNNIAYGVLRNASEEDVIAAAKAAHAWDFIQQLPNGLQSEIGDRGVRLSGGQRQRLAIARAILKNAPILLLDEATSALDTESERHVQAALDELMQNRTSIVIAHRLSTIENADRIMVMEQGRIIEGGSHEELLALDGHYAKLYRKQFH | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-core oligosaccharideSide 1 = ADP + phosphate + lipid A-core oligosaccharideSide 2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64077
Sequence Length: 583
Domain: In MsbA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Subcellular Location: Cell inner membrane
EC: 7.5.2.6
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Q9JXR3 | MIEKLTFGLFKKEDARSFMRLMAYVRPYKIRIVAALIAIFGVAATESYLAAFIAPLINHGFSAPAAPPELSAAAGIISTLQNWREQFTYMVWGTENKIWTVPLFLIILVVIRGICRFTSTYLMTWVSVMTISKIRKDMFAKMLTLSSRYHQETPSGTVLMNMLNLTEQSVSNASDIFTVLTRDTMIVTGLTIVLLYLNWQLSLIVVLMFPLLSLLSRYYRDRLKHVISDSQKSIGTMNNVIAETHQGHRVVKLFNGQAQAANRFDAVNRTIVRLSKKITQATAAHSPFSELIASIALAVVIFIALWQSQNGYTTIGEFMAFIVAMLQMYAPIKSLANISIPMQTMFLAADGVCAFLDTPPEQDKGTLAPQRVEGRISFRNVDVEYRSDGIKALDNFNLDIRQGERVALVGRSGSGKSTVVNLLPRFVEPSAGNICIDGIDIADIKLDCLRAQFALVSQDVFLFDDTLFENVRYSRPDAGEAEVLFALQTANLQSLIDSSPLGLHQPIGSNGSNLSGGQRQRVAIARAILKDAPILLLDEATSALDNESERLVQQALERLMENRTGIIVAHRLTTIEGADRIIVMDDGKIIEQGTHEQLMSQNGYYTMLRNISNKDAAVRTA | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-core oligosaccharideSide 1 = ADP + phosphate + lipid A-core oligosaccharideSide 2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68903
Sequence Length: 621
Domain: In MsbA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Subcellular Location: Cell inner membrane
EC: 7.5.2.6
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Q3J7R8 | MTFTPSLNSGLAVYRRLLSYTRPYRWIFAASIITMAIYAATETGLAALMKPLMDGSFIERDPATIQIIPLLLIGLFVIRGGANFITQYGLKWVARRVVRDLREQMFCHLLALPARYYDQKASGQLLAKLIYDVEQVSNAATDAILTIIRDSLTILGLLAWMAYLNGLLTLIILVTAPLIALIIWWVSHRFRRISRKIQNSMGDVSQVAQETIEGHREVKIFGGQTYEAERFDQVNEQNRRQTMKMAATDAISQPVVQLIAVLGLAGVIHLATRESMLAQISVGTFISFITAMMLLLGPVKRLTKINGTLQRGIAAAQSIFGLLAETPEADRGQQSLRRARGAIRFEHLSFCYEPAKGPVLENIDLEIKPYQTIALVGHSGSGKSTLVSLLARFYETTSGRILIDEMDIQTLRLTELRRQIALVSQQIILFNDTIAHNIAYGSYQQTSKQDIIRAAEAAHAMEFINRLPDGLDTVIGEKGVLLSGGQRQRLAIARALLKDAPILILDEATASLDTEAERHIQAALETLMRQRTTLVIAHRLSTVENADQIIVLHQGQIIERGTHSQLLARESHYAGLYRLQFRHSHEHVSPLSANVGL | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-core oligosaccharideSide 1 = ADP + phosphate + lipid A-core oligosaccharideSide 2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66459
Sequence Length: 597
Domain: In MsbA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Subcellular Location: Cell inner membrane
EC: 7.5.2.6
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Q12C33 | MTQLSEPVPVSLAARRSLWQRVARVWPYFSGSRAGWALAIGATIVASATEPFVPALLKPLLDRGFQRDSFNLWLVPLALMLLFTVRGLSGFLAQFALAKVTNDGLLKLRGAMFDKLLSARLTLFADQSSSAIANTVVYEVFNGSSMLINAIMKLARDVLTLLALIGYLVYLNWKLMLVVALLFPAVAFVIQVLSKRLYRLTKESQTATDDLAYVVEENVMAHRDVRLHGAQAGQASRFNHLSNSLRRLSMKSTAAYAGMSAITQVLAAMALSAVISIALLQSAENTTTVGGFVAFVTAMLLLIAPVKSLSDAATPVTRGLAALERGLDLMNLTPDESGGSFVKARAHGDIEFADVSVIYKADAAAALDQFSLSIKAGETLAIVGASGSGKTTLVNLLPRFVEMSSGNIYLDGQDLRAWNLASLRAQFAFVSQHVVMLNNSIAVNVALGQPVDRARVTECLAAANLSGLLAELPGGIDTILGHNAMQLSGGQRQRLAIARALYKNAPILVLDEATSALDTESELAVQEAIKRLTASRTSLVIAHRLSTVQHADRIIMMEAGRMIESGTHAELLARNGAYAHLYRLGFRNT | Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Catalytic Activity: ATP + H2O + lipid A-core oligosaccharideSide 1 = ADP + phosphate + lipid A-core oligosaccharideSide 2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63309
Sequence Length: 589
Domain: In MsbA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Subcellular Location: Cell inner membrane
EC: 7.5.2.6
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