ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
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.
Ca... |
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.
Ca... |
Q8Y0K4 | MPAQGWLADTYGRRLHDLRISVTDRCNFRCIYCMPKDVFDKDYRFLQHSELLSFEEIERMVRLFIEHGVEKIRLTGGEPLLRKDIERLVEMLARLNTRDGKPLDLTLTTNGALLARKAQALKDAGLTRVTVSLDAIDDATFRRMNDVDFAVAEVLHGIEVAQRVGLAPLKINMVVKKGDNDDQIVPLARHFRNSGIILRFIEYMDVGVTNHWEMASVVPSAEVIRRLSAAFALEPLSANYAGETAERWRYADGAGEIGVISSVTQAFCHDCTRARLSTEGKLYLCLFATQGFDLRALLRGGASDLEVSNAIRTVWQARTD... | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Ca... |
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 ... |
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 ... |
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 ... |
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 ... |
P07112 | MAIYHLTAKTGSRSGGQSARAKADYIQREGKYARDMDEVLHAESGHMPEFVERPADYWDAADLYERANGRLFKEVEFALPVELTLDQQKALASEFAQHLTGAERLPYTLAIHAGGGENPHCHLMISERINDGIERPAAQWFKRYNGKTPEKGGAQKTEALKPKAWLEQTREAWADHANRALERAGHDARIDHRTLEAQGIERLPGVHLGPNVVEMEGRGIRTDRADVALNIDTANAQIIDLQEYREAIDHERNRQSEEIQRHQRVSGADRTAGPEHGDTGRRSPAGHEPDPAGQRGAGGGVAESPAPDRGGMGGAGQRVA... | 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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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... |
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
|
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
|
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
|
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
|
P37732 | MPADGIRARFRVDYAGFALDVDLTLPGHGVTALFGHSGSGKTTLLRCVAGLERAAEARLEINGELWQDSAAGVFLPTHRRALGYVFQEASLFPHLSVRRNLEYGMKRVDAASRQVSWERVLELLGIGHLLERLPGRLSGGERQRVGIARALLTSPRLLLMDEPLAALDLKRKNEILPYLERLHDELDIPMLFVSHLPDEVARLADHVVLLDQGRVTAQGSLQDIMARLDLPTAFHEDAGVVIESVVAEHDDHYHLTRLAFPGGAVLVARRPEAPGQRLRLRVHARDVSLANSRIEDSSITNVLPATVREVVEADTPAHVL... | 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: 3... |
Q89TQ9 | MGGFTKEAKKGYIEVAFNGSLASILLDTQFSVPAKGVTAIFGPPGCGKTTLARCIAGVQRLPNGFCAIDGEIWQDETTFRPPHLRRVAYVFQLPILSSHLSVRRTLLYNASNSEPTLIDFDGVVELLGLAPLLERTPSHLSKTERQRLALGSALLGQPRLLLLDDPLIVRDRSAKCEILPFLERILQSLALPMIYISHDITDIERLADHLVMMKDGTVTAAGPLNVTQSDPALASRSEAAICLDTMVGGYDGRYGLVKLRLKSARFLIPAVPLRPGARLRLRIAAGDVSIACEPPRASSILNVFRARITASLPHGDAEVT... | 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: 3... |
Q44538 | MPEQGIEAQLRLQRGAFRLDAHLQLPANGISVLLGRSGSGKTTLLRAIAGLERAEGFLQVGGQLWQDATCFRPPHQRSLGYVRQASELLPHLDVRANLEFGYRRIPRARRRLGLDEVIALFGLEDLLDQRAEWLPNGPRQRVAIACALLTSPDLLLLDAPLICLDRHSRAQILPALEQLRGQLRIPLLYVTHSQDEVTRLADHLILLDKGKTFASGPPGRLLSDPRLPLNHPDEAAVVLIGQVEHHDPHYRLSTVRVPGGTLSVSLSRLPPGAETRVRIFARDVSLSLDPPHNSSILNILRVRIADLFHEQDSARVMVRL... | 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: 3... |
Q89EW7 | MTADGRGRIDAAFRGRLGRFVLDASLSVPATGVTAIFGPSGCGKTTIARCIAGLQRLSDGFCAIDGEIWQDGMAFRPAHRRPVGYVFQEPSLFPHLSVRGNLLYGAPKAAATSIGFDEVVELLGLTALLGRSPHRLSGGERQRVAIGRALLSQPRLLLMDEPLAALDRTTKNEILPFLERLHERLSLPVLYISHDMAEIERFADYLVLMERGRVVGAGPLHILQSDPALPLAYSRDAAVSIDGLVEAYDERYGLLTLAVNGGLLHVPSHRIAVGARQRLRIAASDVSIVRARPSESSILNILPARIVTQSPPGAGEVTIV... | 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: 8... |
Q8UCD5 | MTLSVSARHRLGTFELDASFTSEGGVTALFGRSGSGKTSMIRIIAGLLRPDEGQISLDGEVLADSGKRLFLPAHKRRFGYVFQEARLFPHLSVAQNLRYGRWFTTGKDTNANDDRIIDMLGISHLLQRRPNRLSGGEKQRVAIGRALLSSPRLLLMDEPLASLDEQRKAEIIPYLERLRDETKIPIVYVSHSIQEVARLADRVVVMKDGKVEAEGKAAEVLSRPDFSTYLERREAGSILSGNIESFDERHGLAAVRLNAALLQVPAKKATAGTPARVLIPARDVMLALVKPEGLSALNILEGHVTGISESEDGMVTIQMD... | 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: 3... |
Q21UI2 | MNTRPEQASKDTSGLTLQVALQRQDFRLEIDLELAGHGITALFGPSGSGKTTALRVLAGLEPAAQGRVCVQGDMWQDSAQGVFKPVHQRALGYVFQEASLFDHLNVQENLQYGFKRTPASERFRNWDHTLDLLGIAHLLKRWPHELSGGERQRVAIARALAASPRLLLLDEPMAALDAPRKAEILPYLERLQSRLEIPVIYVTHAIDEVARLADQLVLLEAGQVTAHGPTAELLTRLDLPLAHGDSAGAVLHCSVVSHDEADHLTLTRFAGIDLVVPRQNAAVGQTLRVRVAARDASLTLQRQTDTSILNILPASVLALS... | 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: 3... |
Q0VQ44 | MSLALSISGRRGAFQLQVDATLQPEGVTVLFGASGAGKSSLLRMVAGLDPCEGTIRFADQLWRSSGLSSERKNDVDLAVWQRPIGMMFQQPTLFHHLTVQGNLNYVARRRRSPIGQVEQVIKQTGIAPLLSRRVDGLSGGESQRVALARALLGTPRLLLLDEPLSALGEEHKQGLLDLIALAAQTVPVLYVTHNMDELLRLADQVWLMEQGRVVAQGPVGQELSRLDGVLAQRADATALLAGEVGSYVREDHLQGIRVGSHTLWLPGLQRLTPGEPVRLRIAARDVSLCLSAPNDSSILNILPAQVVGLRDVGPGQCLVQ... | 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: 3... |
Q5E0T4 | MLLIDIKKQLGDLLLDVKLSLPSSGISAIFGRSGAGKSSLANVISGLTSPEEGRITLNNRVLFDSESKVSMPPEKRNIGYVFQDARLFPHYKVEGNLLYGCGGKRTPHFNDVVKLLDIESLLTRYPHSLSGGEKQRVAIGRAILSEPALLIMDEPLASLDLPRKHEVMPYLERLAKEIKIPILYVSHSLDEILRLADNMVLLNQGSVSLSGDITSVWGSPLMRPWLNASEHSALLEGTISELHSDHPMTKVTLNNSQQGIWVKSPCDCVEEGKKIRLRIRANDVSLIKQQPQHSSIRNILPVVIEDLSEDKENDVVAVKL... | 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: 3... |
Q5P4W2 | MSGAVPFGAGAVRTGAITGDEAIRARFGLGWPGFRLDVDLALPGRGVIALFGHSGSGKTTLLRCLAGLERAADGYLAVRGELWQDEAQRLFVPTHRRPLGYVFQEASLFAHLTVRRNLEFGLKRVPAASRRIPLDQAIALLGIEPLLDRMSGRLSGGERQRVAIARALATSPRLLLMDEPLAALDVKRKQEILPYLERLHAELDIPVVYVSHAPEEVARLADHVVLLADGRALAAGPIGEVMARLDLPFAHDEDAFVVIDARVAAHDEAYALTRLEFAGLPLWITGLDMPLASRVRARVLARDVSLALTERHDSSILNVL... | 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: 3... |
O02193 | MSEAELEQTPSAGHVQEQPIEEEHEPEQEPTDAYTIGGPPRTPVEDAAAELSASLDVSGSDQSAEQSLDLSGVQAEAAAESEPPAKRQHRDISPISEDSTPASSTSTSSTRSSSSSRYDDVSEAEEAPPEPEPEQPQQQQQEEKKEDGQDQVKSPGPVELEAQEPAQPQKQKEVVDQEIETEDEPSSDTVICVADINPYGSGSNIDDFVMDPDAPPNAIITEVVTIPAPLHLKGTQQLGLPLAAPPPPPPPPAAEQVPETPASPTDDGEEPPAVYLSPYIRSRYMQESTPGLPTRLAPRDPRQRNMPPPAVVLPIQTVLS... | 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 t... |
Q7X7A4 | MRRERDATQIPENPMEGIPQTAAAAAAAAAAEASEPPRKRARVDGGGGGAGEEEEDRLSDLPDCLLEDILAHLGSRQAVQTSVLSRRWRNLWRGVRVVVIDVGSFRLPGADGDPPRFRLDRIEDFADGVLSPSLHPGAARELDALRMRLDEDAVTTNFQRWIRRALWRRPATVDLYYLPRRSFSWPPAVPLTPVTAVSRLKTLRIFGLRPTVVFGADEFPALEDLHIERCSYAHGTIASPTLKRLALVSPINGCFVREQRLTAPGLTSLRLVLPYSREEGVRVITDAPLTSLVDASITIVDTDPGDPRNRRVNQFKVDFL... | 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... |
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... |
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 RA... |
Q14149 | MAAQPPRGIRLSALCPKFLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGSMRLGKDAIVFTKNGESMSVGLLSQTYLEVIKAEHVVVPIVAFNKHRQMINLAESKASLAAILEHSLFSTEQKLLAELDAIIGKKGTRIIIWNLRSYKNATEFDFEKDKYDIRIPEDLDEITGKKGYKKQERMDQIAPESDYSLRAYCSILYLKPRMQIILRGQKVKTQLVSKSLAYIERDVYRPKFLSKTVRITFGFNCRNKDHYGIMMYHR... | 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 IF... |
F4KAF2 | MEPIVKQENPVTTSTLSTWKPAARNKTIPPPESVIELSSSNEGSELGENLDEIAEIQSVDRTGGDDVSGTKRARSDSIASPAKRLAVMIPDDDEEFLLSTTSGQAILALPATPCNVVAAPSSWGSCKQFWKAGDYEGTSGGDWEVSAGGFDHVRVHPKFLHSNATSHKWSLGAFAELLDNALDEVRSGATFVNVDMIQNRKDGSKMILIEDNGGGMNPEKMRHCMSLGYSAKSKLADTIGQYGNGFKTSTMRLGADVIVFSRCLGKDGKSSTQSIGLLSYTFLKSTGKEDIVVPMLDYERRDSEWCPITRSSVSDWEKNV... | 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 archit... |
Q8TE76 | MLLYRGAPAGPGAPGCGLARPGGGPQAFGIRLSTMSPRYLQSNSSSHTRPFSAIAELLDNAVDPDVSARTVFIDVEEVKNKSCLTFTDDGCGMTPHKLHRMLSFGFTDKVIKKSQCPIGVFGNGFKSGSMRLGKDALVFTKNGGTLTVGLLSQTYLECVQAQAVIVPIVPFNQQNKKMIITEDSLPSLEAILNYSIFNRENDLLAQFDAIPGKKGTRVLIWNIRRNKNGKSELDFDTDQYDILVSDFDTEEKMTGGVTSELPETEYSLRAFCGILYMKPRMKIFLRQKKVTTQMIAKSLANVEYDTYKPTFTNKQVRITF... | 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-TYP... |
F4K2G3 | MAESGSTNPKSPSVVPDSTLGGLKRDLRNYHDGDDSNNLSIKKSKTTKMENNCREIVPLDVTPLSIVPPDTPKLSRQFWKAGDDDEAAPVPLYCSNDAAVRVHPQFLHANATSHKWALGALAELLDNSLDEVSNGATYVHVDSTINKRDGKSSILIVEDNGGGMNPSTFRECLSLGYSRKRNMANRVGQYGNGFKTSTMRLGADAIVFSRSRGINGNNPTQSIGMLSYTFLYETRKCEAIVPTVDYELVDNKWKEIVYNSTNEWLDNLETILRWSPYLSQQDLLDQFNHLEEQGTRIVIYNLWEDDEGKMELDFDTDPHD... | 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 archit... |
Q56Y74 | MSHDRSVNVSHDAVIAKPERGTMLQSFSPRSHGSKGYSLPQDSEENRGSVGQSAGQSSTSVVDQVRSPADDAGVTSSSTICPAPVCRQFWKAGSYNDELSSKSQQPNGKNYLHVHPMFLHSNATSHKWAFGAVAELLDNAVDEIQNGATFVIVDKTTNPRDGATALLIQDDGGGMDPQAMRHCMGFGFSDKKSDSAIGRYGNGFKTSTMRLGADVIVFSRHSKNQTLTQSIGLLSYTYLTRTGHDRIVVPILDYEFNASAGEFKTLQDREHFISSLSILLEWSPFSTEAELLQQFDDVGPHGTKVIIYNMWLNSDAKLEL... | 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/conden... |
F4JRS4 | MDNSIHVKREIQLPSTSPAGFPGRESVTVVDLCSSDDDSDIGEVAGGLEKVGNNFVGLKRGRDTFGGSSEVDRNNVKKVTTLAELGVGLPEGFGQSNPPESLTHPIPANPCNVFRPVPPPPPPPYAGTSGKIGGCKQFWKAGDYEGAAGDNWDLSSGGFDHVRVHPKFLHSNATSHKWALGAFAELLDNALDEVASGATYVKVDMLENNKGGNRMLLIEDNGGGMDPEKMRQCMSLGYSAKSKLANTIGQYGNGFKTSTMRLGADVIVFSRCPGKDGKSSTQSIGLLSYTFLRSTGKEDIVVPMLDYERRDPEWSKIIRS... | 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 archit... |
A0A0R8YXT5 | MISPVSSILASIWDNSKLLLDHTSVLSIALIGVACAISIRSILYVRLACANYSILLLTHAQRLRLAYSTPLRHVPGPWYAKFTALGLRANDVAGNRWYYVQGLHKKYGSIVRIAPEEVAISDPKVVSKVHALGTEFRKRQQPGTPFNIFSISDPKAHRTRQRFYAKAFSDETLKASTEPAVRQLIKTAVASIKRDAALRKDHTADVYKWCMLFGSDVAFQVIYGNSNTEGLMATQKTTDEVIMGAYLQRMNAWAQFCFPVFLLGRWLSPLSPTLHNIFRVEEKYGDFWQEGQRQREIAARTVFVQNTKYSKNDGVFSVSD... | 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 methylphl... |
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 | MSTELFSSTREEGSSGSGPSFRSNQRKMLNLLLERDTSFTVCPDVPRTPVGKFLGDSANLSILSGGTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSPAQLLCSTPNGLDRGHRKRDAMCSSSANKENDNGNLVDSEMKYLGSPITTVPKLDKNPNLGEDQAEEISDELMEFSLKDQEAKVSRSGLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVKKKYFSGQGKLRKGLCLKKTVSLCDITITQMLEEDSNQGHLIGDFSKVCALPTVSGKHQDLKYVNPETVAALLSGKFQG... | 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 MA... |
P48968 | MSTGPFPSSRREESSVSAPSFRFSQRKMLNLLLERNTSFTQDFPRSPGDKLLDSTNLSILSGGTPKRCLDLSNLSNGEMSASPLITSADFDDTGSLDSSGPQDVQLTEKNHHQDPMKGIPVQLLCSTPNALDHSHRKKDAVRGLSANKENINTNLKTLQWESPRIPRFQNTPGDPLASPLPLLGNGVSMDTEVRSLGSPITAVPKLSKNLNLEDQEEISEEPMEFSLEDHDTKECVLPTVSGKHQDLKYITPDTVAALLSGKFQGLIEKFYIIDCRYPYEYLGGHILGAINLCSQKELHEFFLKKPIVPLDIQKRVIIVF... | 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... |
P48967 | MSTGPIPPASEEGSFVSAPSFRSKQRKILHLLLERNTSFTIRSDFPESPKDKLHDSANLSILSGGTPKCCLDLSNLSSGEMSASPLTTSADLEDNGSLDSSGPLDRQLTGKDFHQDLMKGIPVQLLCSTPNAMNHGHRKKIAKRSTSAHKENINTSLKALEWEAPRTPRFRKMPGGPLTSPLCELEMKHLGSPITTVPKLSQNVKLEDQERISEDPMECSLGDQDAKGLSLRKMVPLCDMNAIQMEEEESGSELLIGDFSKVCVLPTVPGKHPDLKYISPDTVAALLSGKFQSVIERFYIIDCRYPYEYLGGHILGALNL... | 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 ... |
Q29029 | MAEGGRPGSGPSFRSNHRKILNLLLERETSFSMSSDRPGTPLKKKLFGDSANLSILSGGTPKRCLDLSNLSSGEMSATQFTTSADLDETGHLDSTGSEEIQLAGMSYHQHLLKCSPAQLLCSTPNALDHGRRKKDAICSSSENKENENNTSKPLEWWAHRNLLFQKRPGGPYMSPLSLLDNGNLVEGEMKHLGSPITAVSKLDKNPERGEDQAEEISDELMEFSLEDQEEAKVSLNTSCLYRSFSLPDSLNSPGLKQVVKFKDHTLPDKVKKKYCSSHEELRKGLGVKKMVSLCNINMIQMLEEDSNQGPLIGDFSKVCA... | 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... |
P20483 | MLWETIVEENNCSMDCNISNNTSSSSSINKMSGSRRARRSLELMSMDQEELSFYDDDVVPQDQQRSASPELMGLLSPEGSPQRFQIVRQPKILPAMGVSSDHTPARSFRIFNSLSSTCSMESSMDDEYMELFEMESQSQQTALGFPSGLNSLISGQIKEQPAAKSPAGLSMRRPSVRRCLSMTESNTNSTTTPPPKTPETARDCFKRPEPPASANCSPIQSKRHRCAAVEKENCPAPSPLSQVTISHPPPLRKCMSLNDAEIMSALARSENRNEPELIGDFSKAYALPLMEGRHRDLKSISSETVARLLKGEFSDKVASY... | 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] + phospha... |
P30303 | MEHSSPLAAMQPPSVMLGHCFRSDAPTSYHGFSPLPGLGPGGFNFKDLSMKRSNGDYFGTKVVRGSSPTASLAADLSQNFHIDQSPQVATPRRSLFSACLLGNGNRRGVDDAMTTPPLPSSSPAPAMDIMDMSPLPHKPPFISTPEIELDSPTLESSPMDTTMMSTDGLVPDSPTVLPKDGKQERRRPTFLRPSLARSKAQSFQVGMTRPAPESQGPPFKFQTNGINKTSSGVAASLEDMFGESPQRERPMMRINSTSGLNSRLRPPLGSGSHVRGNGSPSAASVRKSAHPNMRPRKQCRRSLSMYEHPEDVIADSEVSY... | 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-[p... |
P06652 | MDSPLSSLSFTNTLSGKRNVLRPAARELKLMSDRNANQELDFFFPKSKHIASTLVDPFGKTCSTASPASSLAADMSMNMHIDESPALPTPRRTLFRSLSCTVETPLANKTIVSPLPESPSNDALTESYFFRQPASKYSITQDSPRVSSTIAYSFKPKASIALNTTKSEATRSSLSSSSFDSYLRPNVSRSRSSGNAPPFLRSRSSSSYSINKKKGTSGGQATRHLTYALSRTCSQSSNTTSLLESCLTDDTDDFELMSDHEDTFTMGKVADLPESSVELVEDAASIQRPNSDFGACNDNSLDDLFQASPIKPIDMLPKIN... | 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 ... |
P23748 | MNNIFHGTEDECANEDVLSFQKISLKSPFGKKKNIFRNVQTFFKSKSKHSNVDDDLINKENLAFDKSPLLTNHRSKEIDGPSPNIKQLGHRDELDENENENDDIVLSMHFASQTLQSPTRNSSRRSLTNNRDNDLLSRIKYPGSPQRSSSFSRSRSLSRKPSMNSSSNSSRRVQRQDGKIPRSSRKSSQKFSNITQNTLNFTSASSSPLAPNSVGVKCFESCLAKTQIPYYYDDRNSNDFFPRISPETLKNILQNNMCESFYNSCRIIDCRFEYEYTGGHIINSVNIHSRDELEYEFIHKVLHSDTSNNNTLPTLLIIHC... | 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 | MPPVPLLRLQCGVNSYDWGKVGHESAAAKYAATTAASDFSIQSDKPYAELWMGTHPSLPSKDLETQRTLLDMVQDNQALISQEVSERYGGKLPFLFKVLSIRKALSIQAHPNKKLAEKLHARDPRNYPDDNHKPEMTIAITPFEGLCGFRPLVEIIHFLKAVAPLRQLVGERAASEFENTVKGSEESEDPAVTEKNKQALRTLFTSLMRSSPESIEAATKELVAIAQNSPETFTTSSSTPETNPTNPAELAAITVRLNGQFPNDIGSFVFFFLNFVKLEPGEAMFLKADDIHAYISGDIIECMASSDNVVRAGFTPKFKD... | 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: Nucleoti... |
P34650 | MLLKLKCTVNNYAWGPKGNSSMAGSLALDGGHIPNLDKDKPYAEFWVGTHANGPAHVIEKDIALKQLLATSPELQGKHEKGNLSFLFKVLSVLGPLSIQIHPTKEQGKLLHATDPKNYPDDNHKPEIAIALTEFELLSGFRQHSQISEYLKLYSEIQELLTEEEKSQIDSLGSYGESSAQVLKKIFSRIWRTPKEKLQIVVDKLARRIQGHENKTALDEIIVYLFTLYPGDVGVFAPIFLNYFKLQPGEATFLEPNMPHAYLKGDCVECMADSDNTIRAGLTPKYIDVESLVEMLNYDETLLPKYIPNELDDGSLLFTPR... | 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: Nucleoti... |
Q9HFU4 | MSPSVFKISPGINSYDWGKKGSASLAAQLATTSIPDFSIDEDKAYAELWMGTHPNNPSRLSDNTLLSEHLKSHPELIGSSVSSKFEDCKDGSLPFLFKVLSIGTALSIQAHPDKPLAKKLFDEKPDVYKDPNHKPEMAIALTPFLAFLNFLPLSVLLLHLLTVPELQEFVDSSLTESLASSLGLPTSQPPDTSLFKPTESPATAEQKDILKQIFAALMSADKKLVEEAISKLIKRYQAKRDIKENEKSLVDLALRLNDQYPGDVGVLCVFLLNVVELKRGEAAFLGANEPHAYIEGDIIECMATSDNVVRAGLTPKLRDV... | 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: Nucleoti... |
Q643C8 | MSTEVSEAQARRAVADIFNSTLASSAIGAAWELGALDELRENGKLDVSDFAVRHDLHEPAVVGMFTALASVGIVRREGATVVVGPYFDEANHHRSLFHWLNQGSGELFRRMPQVLPNENRTGKFYQRDAGAISYACREISERYFDPAFWAAVDGLGYTPTTVADLGSGSGERLIQIARRFPGVRGLGVDIADGAIAMAEKEVAAKGFGDQISFVRGDARTIDQVSARGEFAEVDLLTCFMMGHDFWPRENCVQTLRKLRAAFPNVRRFLLGDATRTVGIPDRELPVFTLGFEFGHDMMGVYLPTLDEWDGVFEEGGWRCV... | 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-... |
Q643C1 | MLTLHLQDDDVAAIDAVADELSRRYDSVESTEFQAESRLYADELPRRVRRALHEYRSTEKSGILVVTGLPVDDSALGATPADRRHKPVPSTSLRQDIAFYLIANLLGDPIGWATQQDGFIMHDVYPVQGFEHEQIGWGSEETLTWHTEDAFHPLRTDYLGLMCLRNPDGVETTACDIADVEIDDETRETLSQERFRILPDDAHRIHGKAPGDESARESALRERSRQRVASALESPDPVAVLFGDRDDPYLRIDPHYMQGVQGETEQRALETIGAAIDDAMSGVVLSPGDIVFIDNYRVVHGRKPFRARFDGTDRWLRRLN... | 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-enduracidi... |
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 sho... |
Q801G2 | MATVVMEQIGRLFINAQQLRQIPRFLESAFPKLPCTVMVSDVPWVFRESHIITGYRPPDQNWRYYFLTLFQRHNESVNVWTHLLASLIILVKFQELSETVDFLRDPHAQPMFILLLAAFTYLGCSALAHLLSAKSEISHYTFYFLDYVGVAVYQYGSALAHFYYVVEEEWHAQVRTFFLPASAFLAWLSCTGCCYGKYASPKLPKFVHKLFQVVPSGLAYCLDISPVLHRIYRCYSSEHWCADQAVVYHCYQVLFFLISAYFFSYPHPERWFPGRCDFIGQGHQIFHVFLVLCTLVQIEAVRLDYTERRRLYEHLHGDLA... | 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-on... |
Q801D8 | MATVVMEQIGRLFINAQQLRQIPQLLESAFPTLPCTVKVSDVPWVFRERHILTGYRQPDQSWRYYFLTLFQRHNETLNVWTHLLAAFIILVKWQEISETVDFLRDPHAQPLFIVLLAAFTYLSFSALAHLLSAKSELSYYTFYFLDYVGVAVYQYGSALAHYYYAIEKEWHTKVQGLFLPAAAFLAWLTCFGCCYGKYASPELPKVANKLFQVVPSALAYCLDISPVVHRIYSCYQEGCSDPVVAYHFYHVVFFLIGAYFFCCPHPESLFPGKCDFIGQGHQLFHVFVVVCTLTQVEALRTDFTERRPFYERLHGDLAHD... | 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 nucleot... |
P53159 | MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHKEEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKNKNTEGAGISTPRKKLTESPIKLLSRNNIGKALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQKAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL... | 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 membran... |
C5E006 | MDFDKSSSSLVLDLAWNQVDKKNQDFIYAKDFPALIMSIEEILSRGQQTPLAFLSNTGKSVIDTFAREKEFFKIYRDEFKEIFHGLVGKTFKDTIEGTNVSRSVLDEQGQEPDVSTTPTRQQRSSPRKVNRLLKNLETRVASMKDELKFKDEILAEKDRELIQLTRKLSDYKDKYEFVQRQFSFYKDHGESPRRNSSESEQLNLEQNASTKHEFIISELKRKLQEQTLAISNLKEQLQRGEGAGVLYTNYSKRYNPLHNDGPMVLVLATLVFLTIILLIGSMIWVTGGKDDSNSFSQYSWWENNSLLSRIGWFFRDWSDT... | 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 membran... |
P47069 | MNNSNEHRREEAGAANEQMPYNKAVKSAYADVLKDKMNREQEISLRAIKKGIYTDGGETDNYDMDKENDSAYEMFKKNLDFPLDQHNDDDDDDPYIEDNGQETDGYSDEDYTDEADKSFIEDSDSDSYDLESNSDFEENLESSGEAKKLKWRTYIFYGGLFFVFYFFGSFLMTTVKNNDLESHSSGATSSPGKSFSNLQKQVNHLYSELSKRDEKHSSELDKTVKIIVSQFEKNIKRLLPSNLVNFENDINSLTKQVETISTSMSELQRRNHKFTVENVTQWQDQLVKQLDTHLPQEIPVVINNSSSLLIIPELHNYLSA... | 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 movement... |
K2RYB6 | MTSSTESKHSNDESTDLEKQDAEESHGLPEERKQDIAAQLSSSDVQDPNLVDWDGPDDPANPMNWPKSKRLGHVVMASLTTLFANITSTAFAPAASSLEAEFGITSSITAALTVSIYLLGFAFGPLVIAPLSEHFGRLPVYRVCTVITVAFLIGCAQAKNLGMFLVFRLITGIAGSGPGTIGGGTIADVMAPENRGKAMGAFAMGPLMGPVLGPLMSGFIAQYLDWRWVFRVLCIATGVMTIVLYFVMTETYGPVLLKRKAARLRKETGNPDLHTKLEASGVSPLASLWMALQRPTKMLIFSPITLLLSLYCAFVFGLLI... | 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 secret... |
K2SE88 | MAHPQSPGEFQILAAEGPTAGAAWTRHSNDAYPKYSALSKTHWEMWMLEGIEQTGNAGVTVTFFIDGSQTFHGNDPLHITFHALLPDGAIEKHHLIAAAVRVRETDASIVLEWPSKENGDGTEANSFSRIEVAQDHSSATATFNVPGAVQGSLALTSYTRSPDPTAGALGPAVSHRQIMTGAHAESDLSFPGSGRRLRFAGKGGHDRCWMEAAFPAILSDTTYVRGHAGPYTFASLGVVSRMGESRGRNCQKFRLLRDGVEVFASKSDTVSLTEDYFVLRSSHGGPVKGPFLDTTTGYRLDFVRPRAGKHWAFEIAHEKV... | 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... |
P0DTN5 | MADLPAKQTALTFQDDGTLGISHDAPVAELKPDMIIVKTAAVSVNPVDTKMESGFAKAGSIGGCDFAGTVVAVGAAVRRPVKVGDRVTGAVMGSDPNDPSSGSFATYVSAPADITLTLPESVPWAVGTSLSTVWFTVGQALFHHLLPDLAVTPSSPYAGDKPITVLVYGGSTSVGTAAIQLLKLAGLRPVTTCSPRNFDLVKSYGAEEAYDYRSPTCAADIKAATKSNLKYALDCITTKDSIAICYAALGRAGGRYTALDPYWEATAATRKTVKANWTLGITMLGKDIAWPAPYGRPGSEDARAFGAKWAAELQALLESG... | 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 enoylre... |
Q9RW45 | MRFSAVSRHHRGASIDPMTFSEATTPDALTPDAHTPRLLTCDVLYTGMGGAQSPGGVVVVGETVAAAGHPDELRRQYPHAAEERAGAVIAPPPVNAHTHLDMSAYEFQALPYFQWIPEVVIRGRHLRGVAAAQAGADTLTRLGAGGVGDIVWAPEVMDALLAREDLSGTLYFEVLNPFPDKADEVFAAARTHLERWRRLERPGLRLGLSPHTPFTVSHRLMRLLSDYAAGEGLPLQIHVAEHPTELEMFRTGGGPLWDNRMPALYPHTLAEVIGREPGPDLTPVRYLDELGVLAARPTLVHMVNVTPDDIARVARAGCAV... | 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 ... |
A6Q234 | MRIIKPFAILTPQTIIQDKAVAFDKKIEAIDTVENLIKKYPNAAVEHDENSLLLPGFANPHLHLEFSANKATLQYGDFIPWLYSVIRHREDLLPLCDGACLEQTLSSIIQTGTTAIGAISSYGEDLQACIDSALKVVYFNEVIGSNAATADVMYASFLERFHQSKKHENERFKAAVAIHSPYSVHYILAKRALDIAKKYGSLVSVHFMESRAEREWLDKGSGEFAKFFKEFLNQTRPVNDTKSFLELFKELHTLFVHMVWANEEEIQTIASYNAHIIHCPISNRLLGNGVLDLEKIKSIPYAIATDGLSSNYSLNMYEEL... | 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(+) + H... |
Q82K09 | MTEHFDARGTRDAQTGRDLHSFIAGLPKAELHVHHVGSASPRIVSELAARHPDSSVPTDPEALADYFTFTDFAHFIKVYLSVVDLIRTPEDVRLLTYEVARELARQQVRYAELTITPFSSTRRGIDERAFMDAIEDARKSAEAEFGTVLRWCFDIPGEAGLESAEETVRLATDDRLRPEGLVSFGLGGPEIGVPRPQFKPYFDRAIAAGLRSVPHAGETTGPETVWDALTDLRAERIGHGTSSAQDPKLLAHLAEHRIPLEVCPTSNIATRAVRTLDEHPVKEFVRAGVVVTINSDDPPMFGTDLNNEYAIAARLLDLDE... | 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 Activi... |
O86737 | MRPAYDDPRTTDQPITRARPPPRAARGRRLGEEPLTEHLVDPDVPRDLHAFIAGLPKAELHVHHVGSASPRIVSELAARHADSKVPTDPEALVDYFTFTDFAHFIDVYLSVVDLIRTPEDVRLLTYEVARDMARQQVRYAELTITPFSSTRRGIDEGAFMDAIEDARKAAEAEFGTVLRWCFDIPGEAGLESAEETARLATDDRLRPEGLVSFGLGGPEIGVARPQFKPYFDRAIAAGLHSVPHAGETTGPQTVWEALIDLRAERIGHGTSSAQDPKLLAHLAERRIPLEVCPTSNIATRAVRTLDEHPIKEFVRAGVPV... | 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
Path... |
Q9HVF1 | MAQNDHETVDMLLVGAGIMSATLAVLLKELDPNLKMEVVELQESGAIESSNPWNNAGTGHAGLCELNYTPQSADGSIDIKKAVGINTMFEVSKQFWSHLVAKGTFGSPKTFINPVPHLSFVRGSEGIAYLKKRFESLTKHHAFETMVYSEDKATLAEWMPLMMPGRPADEAIAATRVEGGTDVNFGALTNQLLQHLAQQPGAQIRYNQKVTHLRRADNGWRVTVKDTRNGGDREIQARFVFLGAGGGALPLLQLSGIPEGKGFGGFPVSGQWLRCDNPEIVKQHQAKVYSQAEVGSPPMSVPHLDTRVVDGKKSLLFGPY... | 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... |
A3DE29 | MKLNLPFNISPHVFVFILSFAFSLILGPVLIPMLTRLKFGQTVRDDGPKTHYKKTGTPTMGGMIFLIPVTVLAAFYAGHDRRILPLIFVTLGFGLIGFIDDFIKVVKKRKDGLYWNQKMFGLLLVAVTFAVYLSHTHTSDIIIPFMGMDKTVSLGWLFVPFVVLVLIASTNAVNITDGLDGLAAGVTLIVTVFFTIVAMTRSEWEYIKMFSAMVAGGCLGFLTFNAYPARIFMGDTGSLALGGAVGAIAILMKMPLILLIVGGIYVVEALSVMIQVLSFKLTGKRVFKMAPIHHHFELSGWKEVKVVLVFWTITVLLCIL... | 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 ... |
P64258 | MLVWLAEHLVKYYSGFNVFSYLTFRAIVSLLTALFISLWMGPRMIAHLQKLSFGQVVRNDGPESHFSKRGTPTMGGIMILTAIVISVLLWAYPSNPYVWCVLVVLVGYGVIGFVDDYRKVVRKDTKGLIARWKYFWMSVIALGVAFALYLVGKDTPATQLVVPFFKDVMPQLGLFYILLAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAGGFALVAWATGNMNFASYLHIPYLRHAGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVLLRQEFLLVIMGGVFVVETLSVILQVGSFKLRGQRIFR... | 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 ... |
Q52952 | MLIWLVELADHFQFFNLFRYITFRTGAALFTSALIVFLFGPAMIASLRIRQGKGQPIRADGPQTHFKKAGTPTMGGLMILTGIVVSSLLWADLSSIYVVSTLLVTLGFGAIGFYDDYLKVTKQSEKGFSGKARLGIEFVIAAVAVFFMMQAALSAGAAGSTFGSSVTFPFFKDLMLNLGYFFVLFGGFVIVGAGNSVNLTDGLDGLAIVPVMIASAAFGLIAYLAGNAVFANYLQIHFVPGTGELAVILGAVIGAGLGFLWFNAPPAAIFMGDTGSLALGGLIGTVAVATKHEIVMIIIGGLFVIETLSVIIQVFWFKRT... | 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 ... |
Q73G61 | MILATKVFFTSFVFGFILFPYFIKLLKKISKDGQPIRSCGPESHLITKKNVPPMGGIIILISSLLPILLWAQLTPEILLLILITLFFALLGFIDDYLKLKTNHYRGLSAKTKILIQFIVALVGVFILKLYSAECFTKTSLFKGVIIDFGYLYVPFAAFVIVGSSNAVNLTDGLDGLAATQVITSFAFLGLIAYITQADMNITLFCIAFIGAILSFLWFNTHPAKIFMGDVGSLSVGAALGLTSVLIKREMLFAIIGIIFVIETLSVIIQISYFKYTKFKYGEGKRVFLMAPIHHHFEKKRWSENVIVMKFWIISIICSVF... | 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 ... |
Q9P7T4 | MASLDENADELHRMDSSDEASINDDQEDILDTPRTRVRKMLASVDMQLSSNAVSEASLDKESTVGNLENQKNRSYSSEIYLHSDTNFLSNFDSAYERVRRLLNQQGGKSSLQKKEVEQIETQEGGDNAKGSPSSENKDSDRNSRLQQLIEKKRNALKKEQEDLIQNSATSHSKSDNLDSESADDSDLADESELSKKYTSDRKIRNASKKALLELHRNTARLTRETALKPEVVVKKKVTLREFFQKIGFKNDNQLENKAISEEEANSTEPPNVEKEEPKPSVDRSTGIVNSEDIKELSVEDDSLELKEITPEALDIGQTSL... | 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 Locatio... |
Q05648 | MLSFRSLTSTFGFVSRFQIRRLGTSLSIQNLEVQDGRWKGKLATEKKTNREHKSVDTNIKTMKMLKNPKNSTRYLRRSFVPNHRKQENGRDILEDSLSKDHLKVKSCITITTGEGYDLKRCMKLLTMQGLQPTNLIPDEIVSFSYQDNGNKGDVMILGQNGSIVSWGFSESSVRNCIVPIVKAASLNPLNGEDFETEDMDYVEIEGEQDFDKLSSLDNKVTPRIACESFLSGDLIIINSLDSDQGMLDKAAFSSGLSRSTNLAVLEEAMEKHISKTRTITENISKGTKLNLRSSDALKSIGRLFLIRGKLNLYSELIETP... | 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 simil... |
Q12467 | MTVLYTSASLKKMKCLAFNMGMNCVRTVSHARSGGAKFGGRNVFNIFDSKTPDSVRIKAFKNTIYQSAMGKGKTKFSAMEINLITSLVRGYKGEGKKNAINPLQTNVQILNKLLLTHRLTDKDILEGMNLAAGPVNVAIPRDITPQEEKKKVELRNRKAENMDLHPSRKMHIKELLHSLNLDMCNDEEVYQKISLYLQKNEESRTSVGASQQNHVDIDINSLKRYLQNIEKKARQKSAIDKQKKNQARIYQWNTQSFSEIVPLSAGNILFKREPNRLWKRLQNGISVFLGSNGGGKKSKTTKKVLQGNNILLHSLENNKD... | 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 | MFKVPVGLASRTRELMNSVTLNSLNNGKGFNMYLPGILRAFPKPVPSAITSPAIPKYRGESFQFRKLSCISSNYCSTTHQFLSSLKSSTSRLVGKRAFHSSRRAEIKFIFSSKSPKNGNKPFVKVYKVSPFFIIFATASIFTFILTSTIVVIPLIFHFFFPLLIMFFFFKQFKKWQKNIFYKDVLTSLPKTKLKITLPTMRSLQLQPMVQSWKEISSRMGIPNEFAKGLNVDLVKQEETRKQFLSFLQKRVLESFTKNELGIRSYFLGDSVEKWIKESYDLELDIDNCRSELRKFQTFIFSSVRYKLYLDSMKNLPLNPS... | 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 | MFRVTGIATARAVALQPFRAPLGVIRRFGISATASYEFQHGHDMQSRNGSRWDSRRQGDRRSSRWEGRGSDREDGERGSRGGMWRKPQGRRGRTDGAAREGFSLGPNTEVVRVADEAAGVESTPRTLVEEGVLSNELYEMLQSRGFDKLTPVQQKTLKPILQTEHDVVARAKTGTGKTLAFLMPLFQRLLEGPPSENVKAVVIAPTRDLAAQIFNEINEMRNANRKLRRFNAVVMMGGSSRTETFRSLERRRPNIVVATPGRLIDMLEACGPKYFTEVDFKVLDEADTLLEIGFKQALEQINDILNQLNQKGTTHIRTLL... | 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 characteri... |
Q4WRP2 | MMLGAVRRYGVVHALRASVPRTICRPSNSQLLRCQTSPVTACPQSVRLLHKSSPFFSSASAQAQAQPDDLQSAAPQEPLREFTDLAERGLVDPKIIRAIVKDMNIKTMTDVQSQTLREILQGDDVLAQAKTGTGKTLAFLTPVFQNIMKDPSLKGLNWRRSQASSSDIRAIIISPTRELAEQIAVEARRLAAHSGVIVQTAVGGTQKREGLRRIQREGCHVLIGTPGRLKDVLSDSYNGVTAPNLSTLVLDEADRLLDDGFSDAIIDIQRLLPDPMKVDRQTLMFSATVPREVMQMVRKTMKPNFKFVKTVRDDEVPTHL... | 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 characteri... |
Q2UST1 | MKTGRTRPLRVFDILVPPWPPTVPHRIKLPRGKTNWFEFYSAITRNWNKLKGLKNCWQIWKDVQEIIRRIRKYQGESTVMQGPGNNDGAHPYATMAGKLDSKLLQALKVMEFEYMTPVQHRVLTELPSWRSDCLVQAKTGTGKTLAFLLPTLHCLLQGHSAPPRGQVAILIITPTRELAQQIAKSCDQLTSQLARPLECHIAVGGTARASALARFMKGAPSILVATPGRLKDYLSEPSTAEKLSNIQTLILDEADTMLESGFLADVKRILQLIPPKSTGWQGMCFSATVPPKVKDVVSVVLKPGYTSISTIEKNETPTHE... | 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 characteri... |
Q5APM7 | MLKQLSRSLGIRSSPIVANLIRSKQVCTRGFHISLVKQNTSSKVNEITDITSDSLKVKEDAAGSDLPSTKTDKKSKSESFQPVKFEDFKGKGYIHDSIINSLHKNDFKELTPIQQKSLVPIFNTEKGLVCRAKTGTGKTLAFAVPTLQYAYKNRGKGVSTVVLVPTRDLAFQIEEEYRKLISHLKYNERPNLELIIGGQRTSFNPRRPAEIVIATPGRLEKELQTDRKLAKCFSNVTYRIYDEADRLLDVGFESVLNEIDGLLYKVRTTPKPIKSLLFSATVDEAISEFSKKHIHPEYEFLNTVTKDDLEIPENIHQQLI... | 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 characteri... |
Q6FU81 | MLRHCSLGLVTTQISAIAPLRLVGSPLFCRSYQDFAGRDRRSSRSREDKPYNSRTRRFDDEGSSNYSSSRDDYRGQNTYGFRGKAPRKNFSSRDNYSSRDNFRSSNGFQERGYKNKFSKNTKSYSKGGNTSGSFIPEGKMAKMTHIGKSDSDIVVTLESLLEKNVISRDLYDSISRMGFEQLTPVQQKTIEPIITNSDSDIIARAKTGTGKTFAFLLPIFQHLLNTKIDSQNKVKSVIVAPTRDLALQIEDEVRKIHSKNRKLKAFECVSLVGGTNFDRSIRYIEKVSPSIVIGTPGRLIDVMEKFGNKFFKDVDFKVLD... | 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 characteri... |
Q6CQA1 | MLVLQRIPKRALQFNGVTGTVCSTRLFHHAFNLNLQQSFVPSEERRYRNSNRGFTRGSDSNSNNKYRNSSYDDNRSRSNYGGDKRNNRNNNNYGNNRNNGSRRRYQDENSDIEVFKSKSFNVTTLNPESFHEQVTIDSLLEESLLDANVHKAISAMKFESLTPVQQRTIKPILTTENDVVAKAKTGTGKTLAFLAPLFQHLISTKLQNPLAVKAVIVTPTRDLAIQIASEVKKLQQCNPSLKSYRSLTLIGGTNLDKSLKDLHTLNPNIIVGTPGRINDILDRVGAKYFKDVDFKVLDEADTLLQIGFQTELSLISRKLN... | 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 characteri... |
A5DTK7 | MMIARFGKQVLRKNVLVSNRIHFPVISRGFHNSFINKSDDLKSPPIDITKGQTEAKVETKKDKFAGFGLDLDELIGETAKGSQVTEQTELTKSEEEEKKKKNINTNTNKNDRKSVPAISLEDFNPSQFKDFKNTGLIDDVILRALDRAHFKDLTPIQQKSIVPLLETERGMVCRAKTGTGKTLTFLIPTLQSAVSRKIASGGRSSGVDTVIIVPTRDLALQIYDEYQKVLRGISGSRKPHISYVIGGMKNSFNPRNPSEIVIATPGRLEADLRSPLFASAFTDIKYRVYDEADRLLDVGFEPTLDSIDRSIKMIRSDDAE... | 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 characteri... |
Q2SIN5 | MSKVAKQYAGAQVYGRLLSYLKPLWKVFALAVLGNVIYALASAAMADATKYIVAAIETPSPEGRLLVPMLIIGIFALRGLGSFCGGYFMARVARGIVHRMRLELFRHLTVLPCRFFDSNSTGHLVSRITYNVDQVTGAATNAITVVLREGFTVIGLMGYMIYVSWKLTLLFLVLGPIIGVLIGYVSKRFRRISRRIQSSMGDVTHVASESIGGYRVMRTFGGEEYEFNRFMKASEYNITQALKMSLTQALSTPIIQLVISVFIALLVWLALSPEVRGNMSTGEFLAYITAATTCAKPIRQLTEVNAVIQRGISAAQDVFM... | 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-c... |
Q31FG2 | MFDRHTLSLYKRLLKYISGYKSAIFITLITIAIIAATEPLSAIILGNLVDESLIEKDPNSFLLLPLQLAAVFIVKGVAEYFSKVMSTWIAQKAIFNIRSELYDKMLCLPQAEHNQTSTGTLMSKVTYDVTQTGNALSEAWIVIARDSLTILALLATLIYYSWQLTLVMLIIGPIVAFFIDRAGKLMRTSSTDMQDNMGEMTHRLEEGLKGYQDIKIYGSEKYELDRFKASAESLRQNTMKVIKVSALNVPLVQVIAAIALSIVVYIAVQMVNAETMTAGNLITYVTAMGLIFEPIRRITNINATVQRGMAAAKSIFAILD... | 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-c... |
Q5ZUH9 | MKNNLPIKSRLLYKRLLSYVKPFWPVLLLGVLANILYSGIDAGFTYMTKLFLDKSFITIDLNFVKQIPLIVLIGITLRGLVSSLGSYCMTWVARSVVKVLRQTVFSHIIHLPADYYDEATSGQLLSKILYDVEQVAQVSADALTDFIQNICLVIGLLTVMMVICWQLSLMFLLTIPFVGIIVNYTNKRVRRISHKVQKTMGEVTEIASEAIEGYRVVRIFGGERYEITKFNKATEYSRKNDMKVAISKAINVSGVQLVIAIGIATIIMAAIHLSTVITISAGSFLAIIAAMLQLIKPMKTLTTLNATIQRGLAGAESVFN... | 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-c... |
Q60AA3 | MKHSASESKPLSSGLAIYRRLLRYGFPYWRSFCVAVVAMIAYAAITPFFAKLIQPLIDGSFIDNDPTVLRQVSLMLIGLSVLRGIAGFLSEYCSGSVGRRVIADLRRDIFDQLLNLPCSFYDNASGGQLLSKLLYNTEQVSASLQQGIITCIREGFTVIGLMALMVYQNPVLSLVFLVLGPVLGLSVRFVSKRFRRLSMRIQESMGKVSHVTQEVIDAQRIVKVFNGKDYEAAKFATENDRNQKRQMKLIATDALGGGVIHLISVAGVAGILYVVSLDSVRQTITPGSLMAFIAAMAMMLSPIRRLSQVVSVMQRGIAAG... | 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-c... |
Q1GZI0 | MSKTALGKANASVQSARALYLRLLKYAARYWVAFLISIIALVTFSATNTGFLATIKLVTDAGFVNQDSTKLHLLPFMLFGLLAIRALAGFISNFAMRWVARRVVENLRQDTFRRLMSLPVSFFDAVSAGVVTSKLTYDTEQMAGAATKVAMSAVRDTLTILGMVGYMLYLDWQLTLIFAVVAPAMAWYLKSMTPKLRSSGKAVQQTMGEMTKVIEEAVSGQRMVKIFGGGDYEYQRFTKVAGKNRHMQIRLARFSGLNSMVVELLAGVALALVVFYAVGKFSAGEFAAFIGALLMLIGPVKTLTSLNEELQVGLAAAHSV... | 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-c... |
Q9JXR3 | MIEKLTFGLFKKEDARSFMRLMAYVRPYKIRIVAALIAIFGVAATESYLAAFIAPLINHGFSAPAAPPELSAAAGIISTLQNWREQFTYMVWGTENKIWTVPLFLIILVVIRGICRFTSTYLMTWVSVMTISKIRKDMFAKMLTLSSRYHQETPSGTVLMNMLNLTEQSVSNASDIFTVLTRDTMIVTGLTIVLLYLNWQLSLIVVLMFPLLSLLSRYYRDRLKHVISDSQKSIGTMNNVIAETHQGHRVVKLFNGQAQAANRFDAVNRTIVRLSKKITQATAAHSPFSELIASIALAVVIFIALWQSQNGYTTIGEFMA... | 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-c... |
Q3J7R8 | MTFTPSLNSGLAVYRRLLSYTRPYRWIFAASIITMAIYAATETGLAALMKPLMDGSFIERDPATIQIIPLLLIGLFVIRGGANFITQYGLKWVARRVVRDLREQMFCHLLALPARYYDQKASGQLLAKLIYDVEQVSNAATDAILTIIRDSLTILGLLAWMAYLNGLLTLIILVTAPLIALIIWWVSHRFRRISRKIQNSMGDVSQVAQETIEGHREVKIFGGQTYEAERFDQVNEQNRRQTMKMAATDAISQPVVQLIAVLGLAGVIHLATRESMLAQISVGTFISFITAMMLLLGPVKRLTKINGTLQRGIAAAQSIF... | 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-c... |
Q12C33 | MTQLSEPVPVSLAARRSLWQRVARVWPYFSGSRAGWALAIGATIVASATEPFVPALLKPLLDRGFQRDSFNLWLVPLALMLLFTVRGLSGFLAQFALAKVTNDGLLKLRGAMFDKLLSARLTLFADQSSSAIANTVVYEVFNGSSMLINAIMKLARDVLTLLALIGYLVYLNWKLMLVVALLFPAVAFVIQVLSKRLYRLTKESQTATDDLAYVVEENVMAHRDVRLHGAQAGQASRFNHLSNSLRRLSMKSTAAYAGMSAITQVLAAMALSAVISIALLQSAENTTTVGGFVAFVTAMLLLIAPVKSLSDAATPVTRGL... | 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-c... |
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