instruction stringlengths 5 30.7k | sequence stringlengths 2 35.2k |
|---|---|
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 100 family. | MVRLFYNPIKYLFYRRSCKKRLRKALKKLNFYHPPKECCQIYRLLENAPGGTYFITENMTNELIMIAKDPVDKKIKSVKLYLTGNYIKINQHYYINIYMYLMRYNQIYKYPLICFSKYSKIL |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 100 family. | MVRLFHNPIKCLFYRGSRKTREKKLRKSLKKLNFYHPPGDCCQIYRLLENVPGGTYFITENMTNELIMIVKDSVDKKIKSVKLNFYGSYIKIHQHYYINIYMYLMRYTQIYKYPLICFNKYSYCNS |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 100 family. | MVRLFRNPIKCIFYRRSRKIQEKKLRKSLKKLNFYHPPEDCCQIYRLLENVPGGTYFITENMTNDLIMVVKDSVDKKIKSIKLYLHGSYIKIHQHYYINIYMYLMRYTQIYKYPLICFNKYYNI |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 100 family. | MVRLFRNPIKCIFYRRSRKIQEKKLRKSLKKLNFYHPPEDCCQIYRLLENVPGGTYFITENMTNDLIMVVKDSVDKKIKSIKLYLHGSYIKIHQHYYINIYMYLMRYTQIYKYPLICFNKYYNI |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. | MGNKESKYLEMCSEEAWLNIPNIFKCIFIRKLFYNKWLKYQEKKLKKSLKLLSFYHPKKDFVGIRDMLHMAPGGSYFITDNITEEFLMLVVKHPEDGSAEFTKLCLKGSCIVIDGYYYDTLHIFLSETPDIYKYPLIRYDR |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. | MGNKESKYLEMCSEEAWLNIPNIFKCIFIRKLFYNKWLKYQEKNLEKRLKLLSFYHPKKDFMGIRDMLDMAPGGSYFITDNVTEEFLMLVVKHPEDGSAEFTKLCLKGGCIVIDGFYYDDLHIFITENPNLYKYPLIHYDR |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. | MGNKESKYLEMCSDEAWLNIPNVFKCIFIRKLFYNKWLKYQEKKLEKRLRLLSFYHAKKDFIGIRDMLQTAPGGSYFITDNITEEFLMLVLKHPEDGSAEFTKLCLKGSCIMIDGYYYDNLDIFLAESPDLYKYPLIRYDR |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. | MGNKESRYLEMCSEEAWLNIPNIFKCIFIRKLFYNKWLKFQEKKLKKSLKLLSFYHPKKDFVGIRDMLQMAPGGSYFITDNITEEFLMLVVKHPEDGSAEFTKLCLKGSCIVIDGYYYDNLHIFISETPDIYKYPLIRYDR |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. | MGNKESRYLEMCSEEAWLNIPNIFKCIFIRKLFYNKWLKYQEKKLKKSLKLLSFYHPKKDFVGIRDMLQMAPGGSYFITDNMTEEFLMLVVKHPEDGSAEFTKLCLKGSCIVIDGYYYDNLHIFISETPDIYKYPLIRYDR |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. | MGNRLIRSYLPNTVMSIEDKQNKYNETIEDSKICNKVYIKQSGKIDKQELTRIKKLGFFYSQKSDHEIERMLFSMPNGTFLLTDDATNENIFIVQKDLENGSLNIAKLEFKGKALYINGKDYYSLENYLKTFEDFYKYPLIYNKNK |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. | MGNHLDGSYLPNTVMSIEDKQNTYNEAKEDSKICNKIYIKQSGKIDKKELKRIKKLDFFYSQKNDDEIERMFMNKPNGTFLLTDDATDENLFLVQKDLENGSLNIAKLDFNGKALYINGKNYFSLENYLKTVEDFYKYPLIYDENK |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. | MGNHLDGSYQPNMVMSIEDKQNKYNEAKERSKVCNKVYINQSGKIDKKELKRIKKLDFFYSQKNDDEIERMFFNMPNGTFLLTDDVTHENIYIAQKDLENGSLNIAKLEFKGEALYINGKNYFFLENYLKTFEDIYKYPLTNFNENK |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. | MGNRLNGSYLSNTDMSIEDEQNKYNEAIEDCKICNKVYIKQSGKIDKKELNRIKKLDFFYSQKTDYEIERMFFNVPNGTFLLTDDATNENLFIAQKDLENGSLNIAKLEFKGKALYIDGKDYFSLENYLKTFEDFYKYPLIYNKNE |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 100 family. | MGNRLNGSYLSNTDMSIEDKQNKYNEAIEDCKICNKVYIKQSGKIDKKELTRIKKLDFFYSQKSDHEIERMFFNVPNGTFLLTDDATNENLFIAQKDLENGSLNIAKLEFKGKALYIDGKDYFSLENYLKTFEDFYKYPLIYNKNE |
In microneme/rhoptry complexes. | MKFLVLLFNILCLFPILGADELVMSPIPTTDVQPKVTFDINSEVSSGPLYLNPVEMAGVKYLQLQRQPGVQVHKVVEGDIVIWENEEMPLYTCAIVTQNEVPYMAYVELLEDPDLIFFLKEGDQWAPIPEDQYLARLQQLRQQIHTESFFSLNLSFQHENYKYEMVSSFQHSIKMVVFTPKNGHICKMVYDKNIRIFKALYNEYVTSVIGFFRGLKLLLLNIFVIDDRGMIGNKYFQLLDDKYAPISVQGYVATIPKLKDFAEPYHPIILDISDIDYVNFYLGDATYHDPGFKIVPKTPQCITKVVDGNEVIYESSNPSV... |
In microneme/rhoptry complexes. Sporozoite antigen. | MKFLILLFNILCLFPVLAADNHGVGPQGASGVDPITFDINSNQTGPAFLTAVEMAGVKYLQVQHGSNVNIHRLVEGNVVIWENASTPLYTGAIVTNNDGPYMAYVEVLGDPNLQFFIKSGDAWVTLSEHEYLAKLQEIRQAVHIESVFSLNMAFQLENNKYEVETHAKNGANMVTFIPRNGHICKMVYHKNVRIYKATGNDTVTSVVGFFRGLRLLLINVFSIDDNGMMSNRYFQHVDDKYVPISQKNYETGIVKLKDYKHAYHPVDLDIKDIDYTMFHLADATYHEPCFKIIPNTGFCITKLFDGDQVLYESFNPLIHC... |
Causes the redistribution of lumenal ER protein to an enlarged ERGIC compartment. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. | MLVIFLGILGLLANQVLGLPTQAGGHLRSTDNPPQEELGYWCTYMESCKFCWECAHGICKNKVNTSMPLIIENSYLTSCEVSRWYNQCTYSEGNGHYHVMDCSDPVPHNRPHQLLRKIYEKEDL |
Causes the redistribution of lumenal ER protein to an enlarged ERGIC compartment. Belongs to the asfivirus MGF 110 family. | MLVIFLGILGLLANQVLGLPTQAEGHLRSTDNPPQEELGYWCTYMESCKFCWECEHGICKNKVNRSMPWIIENSYLTSCEVSRWYNQCTYDEGNGHYHVMDCSNPVPHNRPHRLGRKIYEKEDL |
Causes the redistribution of lumenal ER protein to an enlarged ERGIC compartment. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. | MLVVFFLGILGLLANQILGLPTQAGGHLRSTDNPPQEELGYWCTYMESCKFCWECAHGICKNKVNKSMPLIIENSYLTSCEVSRWYNQCTYSEGNGHYHVMDCSDPVPHNRPHQLLKKIYEKEDL |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. | MLVIFLGILGLLANQVSSQLVGQLHPTENPSENELEYWCTYMECCQFCWDCQNGLCVNKLGNTTILENEYVHPCIVSRWLNK |
Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. | MLVIFLGILGLLANQVSSQLVGQLHSTENPSENELEYWCTYMECCQFCWDCQNGLCVHKLGNTTILENEYVHPCIVSRWLNKCMYDLGQGIDHVMVCSQPKHWNPYKILKKEWKENNSQNI |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. | MLVIFLGILGLLANQVSSQLVGQLHPTENPSENELEYWCTYMECCQFCWDCQDGLCVNKLGNTTILENEYVHPCIVSRWLNKCMYDLGQGIDHVMVCSQPKYWNPYKILKKEWKENNSQN |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. | MLVIFLGILGLLANQVSSQLVGQLHPTENPSENELEYWCTYMECCQFCWDCQNGLCVNKLGNTTILENEYVHPCIVSRWLNKCMYDLGQGIDHVMVCSQPKYWNPYKILKKEWKENNSQNK |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 110 family. | MLVIILGVIGLLANQVLGLPTQAGGHLRSTDNPPQEELGYWCTYMESCKFCWECAHGICKNKVNESMPLIIENSYLTSCEVSRWYNQCTYSEGNGHYHVMDCSDPVPHNRPHRLLMKIYEKEDL |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. Belongs to the asfivirus MGF 110 family. | MLVIFLGILGLLANQVSSQLVGQLHPTENPSENELEYWCTYMECCQFCWDCQNGLCVNKLGNTTILENEYVHPCIVSRWLNKCMYDLGQGIDHVMVCSQPKYWNPYKILKKEWKENNSQNK |
Expressed in the early phase of the viral replicative cycle. N-glycosylated. Belongs to the asfivirus MGF 110 family. | MLVIFLGILGLLASQVSSQLVGQLRPTEDPPEEELEYWCAYMESCQFCWDCQDGTCINKIDGSAIYKNEYVKACLVSRWLDKCMYDLDKGIYHTMNCSQPWSWNPYKYFRKEWKKDEL |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. N-glycosylated. Belongs to the asfivirus MGF 110 family. | MLVIFLGILGLMASQVLGLPSNQPTGQLRPTEDPPEEELEYWCAYMESCQFCWDCQDGNCINKIDGSVIYKNEFVRPCSVSRWMDKCMYDLNKGIYHTMNCSQPQSWNPYKYFRKEWKKDEL |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. N-glycosylated. Belongs to the asfivirus MGF 110 family. | MLVTFLGILGLLASQVSSQLVGQLRPTEDPPEEELEYWCAYMESCQFCWDCQDGNCINKIDGSVIYKNEYVRPCSVSRSMDKCMYDLNKGIYHSMSCSDPKAWNPYKYFRKEWKKDEL |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. N-glycosylated. Belongs to the asfivirus MGF 110 family. | MLVIFLGILGLLASQVSSQLVGQLRPTEDPPEEELEYWCAYMESCQFCWDCQDGTCINKIDGSVIYKNEYVKSCLVSRWLDKCMYDLDKGIYHTMNCSQPWSWNPYKYFRKEWKKDEL |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Expressed in the early phase of the viral replicative cycle. N-glycosylated. Belongs to the asfivirus MGF 110 family. | MLVIFLGILGLLASQVSSQLVGQLRPTEDPPEEELEYWCAYMESCQFCWDCQDGTCINKIDGSVIYKNEYVKSCLVSRWLDKCMYDLDKGIYHTMNCSQPWSWNPYKYFRKEWKKDEL |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 110 family. | MLVIILGVIGLLASSNLVSSSTSTRVGGHLPLTFDPPENELGYWCTYVESCRFCWDCEDGVCTSRIWGNNSTSIVENSYIKYCEVSRWGDQCRYDVEEHIYYTMNCSDPKPWNPYKIARKEWKKNEHFRKDLKKDEF |
Belongs to the asfaviruses V110 family. | MLVIILGVIGLLASSNLVSSSTSTRVGGHLPLTFDPPENELGYWCTYVESCRFCWDCEDGICTSRVWGNNSTSIIENDYVKYCEVSRWGDLCRYDVEEHIYHSMNCSDPKPWNPYKIARKEWKKDKHFRKELKKDEF |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 110 family. | MLVIILGVIGLLASSNLVSSSTSTRVGGHLPLTFDPPENELGYWYTYVESCRFCWDCEDGVCTSRVWGNNSTSIVENDYVKYCEVSRWGDQCRYDVEEHIYYTMNCSDPKPWNPYKIAKEGVEKG |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 110 family. | MLVIILGIIGLLASSNLVSSSTSTRVGGHLPLTFDPPENELGYWCTYVESCRFCWDCEDGICTSRVWGNNSTSIVENDYVKYCEVSRWGNLCRYDVEEHIYYSMNCSDPKPWNPYKIARKEWKKNEYLRKDLKKDEF |
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 110 family. | MLVIILGIIGLLASSNLVSSSTSTRVGGHLPLTFDPPENELGYWCTYVESCRFCWDCEDGICTSRVWGNNSTSIVENDYVKYCEVSRWGNLCRYDVEEHIYHSMNCSDPKPWNPYKIARKEWKKNEHPRKDLKKDEF |
Belongs to the 14-3-3 family. | MIEDIKTLREEHVYRAKLAEQAERYDEMAEAMKNLVENCLDQNNSPPGAKGDELTVEERNLLSVAYKNAVGARRASWRIISSVEQKEANRNHMANKALAASYRQKVENELNKICQEILTLLTDKLLPRTTDSESRVFYFKMKGDYYRYISEFSNEEGKKASAEQAEESYKRATDTAEAELPSTHPIRLGLALNYSVFYYEILNQPQKACEMAKLAFDDAITEFDSVSEDSYKDSTLIMQLLRDNLTLWTSDLQTQEQQQQPVGEGAEAPKVEATEQQ |
Expressed in late sporogonial stages. Belongs to the 14-3-3 family. | MASKQYEEALQKANLSDMAERYDDMAKEMRLAVTLAHEDKHILNVMARNLFSVAYKNLVSSRRSSWRMLCSERQKLEGKDPSVVHVINEKIKVVEEELLRFCDEVLDIITTYILSLEEAQKNIEYNIFFLKMKGDYYRYKAEVVTGPEHSEVSKHAAESYKEATEKAKTLPPTNPIKLGLALNYSVFHYEILNDSEKACSIAKGAFDEAIKELDTLSEEHYRDSTLIMQLLRDNLTLWTSREEGNVMGDEGKGDPDEN |
Belongs to the 14-3-3 family. | MASRDDLVYMAKLAEQAERFDEMVDHMKAVAQQPKELSVEERNLLSVAYKNVIGSRRASWRVISSIEGKDTVSDQLPLIRDYKSKIETELTDICADILKIIEAELIPNSTSEEGKVFYYKMKGDYHRYLAEFQSADERKTSASDALDAYQLASDHANQDLPPTHPIRLGLALNFSVFYYEILNSPDRACGLAKAAFDDAIAELDTLSEESYKDSTLIIMQLLRDNLTLWTSDQGEAEEAPGNADGTVVEDL |
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity... | MAEAFTREDYVFMAQLNENAERYDEMVETMRKISGMEGELSDKERNLLSVAYKNVIGPRRAAWRIVSSIEAKEKGRQKPNAKRIEQIRVYRQKIEKELSDICNDILKLLQEQFVPRSTNADAKVFYYKMQGDYYRYLAEYSSGEDKEKIAGSALNAYNSAFEISQQLPPTHPIRLGLALNFSVFYYEILASPDRACELARKAFDAAITDLDKLTEESYKDSTLIMQLLRDNLNLWVTDSAGDDNAEEK |
Belongs to the 14-3-3 family. | MAAASSPREENVYLAKLAEQAERYEEMVEFMEKVVAAADGGEELTIEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEGHVSTIRDYRSKIESELSSICDGILKVLDSKLIGSASGGDSKVFYLKMKGDYYRYLAEFKTGDERKLAAENTLSAYKAAQDIANAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEDSYKDSTLIMQLLRDNLTLWTSDMQDDTAEEVKEAPKPDDQ |
Belongs to the 14-3-3 family. | MSPAEPSREENVYMAKLAEQAERYEEMVEFMEKVARTVDTEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDHVALIKDYRGKIEAELSKICDGILKLLDSHLVPSSTAPESKVFYLKMKGDYHRYLAEFKSGAERKEAAESTLLAYKSAQDIALAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAISELDTLGEESYKDSTLIMQLLRDNLTLWTSDINEEAGDEIKEASKAVEGQ |
Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes. Belongs to the 14-3-3 family. | MSSESSREENVYMAKLAEQAERYEEMVEFMEKVAKMTDTEELSVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDHVSTIKEYRGKIETELSKICDGILNLLESHLIPSASTAESKVFYLKMKGDYHRYLAEFKTGAERKEAAENTLLAYKSAQDIALAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAISELDTLGEESYKDSTLIMQLLRDNLTLWTSDNAEEGGDEIKEAAAKRESGEEKPQQ |
Belongs to the 14-3-3 family. | MAEEIKNLRDEYVYKAKLAEQAERYDEMAEAMKNLVENCLDEQQPKDELSVEERNLLSVAYKNAVGARRASWRIISSVEQKELSKQHMQNKALAAEYRQKVEEELNKICHDILQLLTDKLIPKTSDSESKVFYYKMKGDYYRYISEFSGEEGKKQAADQAQESYQKATETAEGHSPATHPIRLGLALNYSVFFYEILNLPQQACEMAKRAFDDAITEFDNVSEDSYKDSTLIMQLLRDNLTLWTSDLQADQQQQEGGEKPAEQADQ |
Belongs to the 14-3-3 family. | MATAPSPREENVYLAKLAEQAERYEEMVEFMEKVCAAADSEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNDDHVSTIRDYRSKIETELSNICGGILKLLDSRLIPSAASGDSKVFYLKMKGDYHRYLAEFKTGAERKEAAESTLSAYKAAQDIANAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLANEAFDEAIAELDTLEEESYKDSTLIMQLLRDNLTLWTSDMQDDGGDEIKEAAPKPDEQY |
Belongs to the 14-3-3 family. | MAAAHTPREENVYMAKLAEQAERYEEMVEFMEKVSANADSEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDHVAVIRDYRSKIESELSNICDGILKLLDTRLIPSASSGDSKVFYLKMKGDYHRYLAEFKTGAERKEAAESTLTGYKSAQDIANAELPPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQDDGADEIKEAAPKADEQQ |
Is associated with a DNA binding complex to bind to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes. Belongs to the 14-3-3 family. | LAEQAERYEEMVEFMEK |
Belongs to the 14-3-3 family. | RNLLSVAYKNVVGARRASWRIISSIEQKEESRGNEDHVSVIRDYRSRIEKELSDNCDGILKLLDTKLVPAASSGDSKVFYLKMKGDYHRYLAEFKTGAQRKEAAESTLTAYKAAQDIANAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFVEAIAELDTLGEDSYKDSTLIMQLLRDNLTLWTSDMQDEAADEITEEAAKQQKAVNNNKIAY |
Most abundant in roots and flowers. Belongs to the 14-3-3 family. | MDKEREKQVYLARLAEQAERYDEMVEAMKTVAKMDVELTVEERNLVSVGYKNVIGARRASWRILSSIEQKEESKGHDQNVKRIKTYQQRVEDELTKYALTLSVIDEHVVPSSTSGESTVFYYKMKGDYYRYLAEFKSGDDRKEAADQSLKAYEAATATASADLAPTHPIRLGLALNFSVFYYEILNSPERACHLAKQAFDEAIAELDSLSEESYKDSTLIMQLLRDNFTLWTSDLEEGGEHSKGDERQGEN |
Highest expression during the active growth period 10-12 hours after germination. Belongs to the 14-3-3 family. | MGHEDAVYLAKLAEQAERYEEMVENMKIVASEDRDLTVEERNLLSVAYKNVIGARRASWRIVTSIEQKEESKGNSSQVTLIKEYRQKIENELAKICDDILEVLDQHLIPSAKSGESKVFYHKIKGDYHRYLAEFAIGDRRKDSADKSLEAYKAATEVAQTELPPTHPIRLGLALNFSVFYYEILNAPDQACHLAKQAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSSEAETPARLMPLLRRRPLLRLPSRRRRAQG |
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Belongs to th... | AKLSEQAERYDDMAASMKAVTELGAELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNDKRQQMAREYREKVETELQDICKDVLDLLDRFLVPNATPPESKVFYLKMKGDYYRYLSEVASGDSKQETVASSQQAYQEAFEISKSEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKSAFDEAIRELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGEEADNVEGDN |
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity... | MDKNDLVQKAKLAEQAERYDDMAAAMKAVTEQGGELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNEKKQQMAREYREKIEAELQDICKDVLALLDNYLIANATQAESKVFYLKMKGDYYRYLSEVASGDSKKTTVENSQQAYQEAFDISKKDMQPTHPIRLGLALNFSVFYYEILNSPEQACSLAKAAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN |
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity... | MDKNDLVQKAKLAEQAERYDDMAGAMKSVTEQGGELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNEKKQAMAKEYREKIETELQDICNDVLGLLDKYLIANATAAESKVFYLKMKGDYYRYLSEVAAGDAKKTTVDNSQQAYQDAFDISKKEMQPTHPIRLGLALNFSVFFYEILNNPEKACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLKGHLTLWTSENQGDEGETGEGEN |
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity... | MDKSDLVQKAKLAEQAERYDDMAASMKAVTEGGVELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNEKKQQMAREYREKIEAELQEICNDVLGLLEKYLIPNASQAESKVFYLKMKGDYYRYLSEVASGDSKRTTVENSQKAYQDAFEISKKEMQPTHPIRLGLALNFSVFYYEILNTPEQACSLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN |
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity... | MDKSELVQKAKLSEQAERYDDMAASMKAVTELGAELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNDKRQQMAREYREKVETELQDICKDVLDLLDRFLVPNATPPESKVFYLKMKGDYYRYLSEVASGDSKQETVASSQQAYQEAFEISKSEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKSAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGEEADNVEGDN |
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity... | MDKSDLVQKAKLAEQAERYDDMAAAMKAVTEGGVELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNEKKQQMAREYREKIETELQDICSDVLGLLEKYLIANASQAESKVFYLKMKGDYYRYLSEVASGDSKATTVENSQKAYQDAFDISKKDMQPTHPIRLGLALNFSVFYYEILNSPENACQLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSENQGEEAGENEN |
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desul... | MNLQRFPRYPLTFGPTPIQPLARLSKHLGGKVHLYAKREDCNSGLAFGGNKTRKLEYLIPEALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRILGADVRLVPDGFDIGFRRSWEDALESVRAAGGKPYAIPAGCSDHPLGGLGFVGFAEEVRAQEAELGFKFDYVVVCSVTGSTQAGMVVGFAADGRADRVIGVDASAKPAQTREQITRIARQTAEKVGLERDIMRADVVLDERFAGPEYGLPNEGTLEAIRLCARTEGMLTDPVYEGKSMHGMIEMVRNGEFPEGSRVLYA... |
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Belongs to the ACC deaminase/D-cysteine desulfhydrase family. | MHPKVDALLSRFPRITLIPWETPIQYLPRISRELGVDVYVKRDDLTGLGIGGNKIRKLEFLLGDALSRGCDTVITIGAVHSNHAFVTALAAKKLGLGAVLILRGEEVLKGNYLLDKLMGIETRIYEADNSWELMKVAEEVAEELKGEGKKPYIIPPGGASPVGTLGYIRGVGELYTQVKKLGLRIDTVVDAVGSGGTYAGLLLGSAIVNAEWSVVGIDVSSATEKAKERVKNLVEKTKELLGINVKVQEPRIYDYGFGAYGKIVKEVAKLIKSVGTMEGLLLDPVYTGKAFYGLMDLAKKGDLGESVLFIHTGGLPGIFH... |
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Belongs to the ACC deaminase/D-cysteine desulfhydrase family. | MHPKVQSLLSKFPRVELIPWETPIQYLPNISKLVGADIYVKRDDLTGLGIGGNKIRKLEYLLGDAIIRKADVIITVGAVHSNHAFVTGLAAKKLGFDVVLVLRGKEELRGNYLLDKIMGIETRVYEAKDSFELMKYAEEVAKELEEKGRKPYIIPVGGASPVGTLGYVRASGEIAEQGNRIGVNFDSIVVATGSGGTLAGLSVGLAILRKETRAIGMAVGKFGETMVNKVEELAKATGEFIGVKNLKLKIELYDYSFGEYGKITREVAETIRLVGTKEGVILDPVYTGKAFYGLLDLAKKGELGEKILFIHTGGISGTFH... |
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Belongs to the ACC deaminase/D-cysteine desulfhydrase family. | MHPKIFALLAKFPRVELIPWETPIQYLPNISREIGADVYIKRDDLTGLGIGGNKIRKLEYLLGDALSKGADVVITVGAVHSNHAFVTGLAAKKLGLDAILVLRGKEELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIPPGGASPIGTLGYVRAVGEIATQSEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLIKEAAELLGVKVEVRPELYDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGELGEKILFIHTGGISGTFHYGDK... |
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desul... | MNLQRFPRYPLTFGPTPIQPLKRLSAHLGGKVELFAKREDCNSGLAFGGNKTRKLEYLIPEALEGGYDTLVSIGGIQSNQTRQVAAVAAHLGLKCVLVQENWVNYSDAVYDRVGNIEMSRIMGADVRLDSAGFDIGIRPSWEQAMDDVRKRGGKPFPIPAGCSEHPLGGLGFVGFAEEVRQQEAELGFKFDYIVVCSVTGSTQAGMVVGFAADGRADKVIGIDASAKPEQTRAQILRIAQHTAELVDLGRNITERDVVLDTRYGGPEYGLPNEGTLEAIRLCARQEAMLTDPVYEGKSMHGMIDMVRNGEFPAGSRVLYA... |
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desul... | MNLNKHPRHPLTFGPTPIQPLKRLSAHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLVPEVLAGGYDTLVSIGGIQSNQTRQVAAVAAHLGLKCVLVQENWVNYADAVYDRVGNIELSRILGADVRLDAAGFDIGIRPSWEQAMEDVRRAGGKPFPIPAGCSEHPLGGLGFVGFAEEVRQQEAEFGFRFDYIVVCSVTGSTQAGMVVGFAADGRADRVIGIDASAKPEQTREQILRIARDTAKLVELGRDITEDDVVLDTRYGGPEYGLPNEGTLEAIRLCARQEGMLTDPVYEGKSMHGMIDRVRGGEFPEGSRVLYA... |
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desul... | MLEKFERYPLTFGLTPIEKLDRLGKHLGGKVEIYAKREDCNSGLAFGGNKLRKLEYVIPDAIASDADTLVTVGGVQSNHTRMVAAVAAKIGMKCLLVHESWVPHEDVVYDRVGNILLSRILGAEVRLVDDGFDIGIRRSWEKALYEVKARGGRPYAIPAGASVHPNGGLGYVGFAEEVRAQEEQLGFAFDYMVVCTVTGSTHAGMLVGFAKDGRQRNVIGIDASATPAKTKAQVLSIARHTATLVELGSELAEDDVVLLEDYAHPRYGIPSEETKEAIRLCARLEGMITDPVYEGKSMQGMIDLVQKGFFPAGSRILYAH... |
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desul... | MSLLEKFERYPLTFGPTPIEHLPRLTAALGGKVDIYAKRDDCNSGLAMGGNKLRKLEYIVPDAIASGADTLVSIGGVQSNHTRMVAATAAKIGMKCVVIQEKWVPHYDAVYDRVGNILMTKLMGADSRLVEDGFDIGIRKSWEDAIQSVEDAGGKPYAIPAGASVHKFGGLGYVGFAEEVAAQEKDLGFIFDYIIVCVVTGSTQGGMIVGFAALDRADRVIGIDASGTLQQTRDQVRKIVDATSELVNLGRSVREDEIVINPDYAYPAYGVPSEETNEAIRLAARTEAMITDPVYEGKSMQGMIDLARKGFFPEGSKVLY... |
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desul... | MLEKFERYPLTFGATAIEYLPRLTEALGGDVEIWAKREDCNSGLAMGGNKLRKLEYIVPDAIASNADTLVSIGGVQSNHTRMVAAVAAKLGMKCRLVQESWVPHEDAVYDRVGNILMTRLMGADSRIVDDGFDIGIRQSWEDAIQSVIDEGGKPYAIPAGASVHKYGGLGYVAFAEEVARQEADLGFKFDYIIVCVVTGSTQAGMIVGFAAQDRADRVIGIDASGTPEQTRSQVRQIVDNTAELVELGRPVREDEIVILNDYAYPAYGVPSNETNEAIRLAARTEAMITDPVYEGKSMQGMIDLTRKGFFPKGSKVLYAH... |
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Belongs to the ACC deaminase/D-cysteine desulfhydrase family. | MGLEQFKKYPLTFGPTPITSMKRLSKTLGGKVEIFAKREDCNSGLAFGGNKIRKLEYLIPEAIDGGYDTLVSIGGIQSNQTRQVAAVAAHLGLDCVLIQEDWVDYKDTMYDRVGNIELSRIVNADVRLDSSKFDIGIRPSFKNALEELTKKGKKPFPIPAGCSEHPYGGLGFVGCVEEIYEQEKQLGFKFDKIVVCTVTGSSFAGIIVGMALTGRQKDVIGIDASATPEKTKAQVLRIAQNTAKLIGLEKELTESDVNIDTRFAHPAYGIPNEGTIEAIKLCGATEGVLTDPVYEGKSMQGLIHLVRNNEIAEGSKVLYI... |
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Belongs to the ACC deaminase/D-cysteine desulfhydrase family. | MRIDLSLKPTPVQFLKRLSEKYGFNIYVKRDDLTELVGSGNKIRKLEYLLWEALKKGATTVFTCGGLQSNHARATAYVSRRYGLKPVLFLRKGEKVLNGNLLLDILLGAEIVEVSPEEYERIDEIFDVHKKMREKKGEKVYVIPEGGSNSLGAFGYFNAVLEMKDQLNLESFDAIVCAVGSGGTIAGLSAGISFLEYHVPVVGVNVTTKNSDYFVGKVKRIISGMEEYGLRVNETVFEVVDDYRGPGYAIPSSEDVEILKEVASIEGIILDPVYTAKAFRGMIEMFRNSEKNVLFIHTGGIFGLFAQSRRLV |
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desul... | MNLKKFPRHVLTFGPTPIQPLKRLSAHLGGKVDLYAKREDCNSGLAFGGNKTRKLEYLIPEALEGGYDTLVSIGGIQSNQTRQVAAVAAHLGLKCVLVQENWVNYSDAVYDRVGNIEMSRIMGADVRLDAAGFDIGIRQSWEQAMADVRAAGGKPFPIPAGCSEHPRGGLGSVGFAEEVRQQEAELGFKFDYLVVCSVTGSTQAGMVVGFAADGRADRVIGIDASAKPQQTFEQILRIAKNTAELVELGRDITEKDVVLDRRFGGPEYGLPNEGTLEAIRLSARFEGMLTDPVYEGKSMHGMIEKVRLGEFPAGSKVLYA... |
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+) Homotrimer. Belongs to the ACC deaminase/D-cysteine desul... | MNLKKFPRHALTFGPTPIHPLKRLSAHLGGEVELYAKREDCNSGLAFGGNKTRKLEYLIPEALEGGYDTLVSIGGIQSNQTRQVAAVAAHLGLKCVLVQENWVNYSDAVYDRVGNIEMSRIMGADVRLDSAGFDIGIRKSWEEAMADVRKAGGKPFPIPAGCSEHPRGGLGFVGFAEEVRQQEAELGFKFDYIVTCSVTGSTQAGMVVGFAADGRADRVIGIDASAKPEQTFAQIVRIAKGTAELVELGRDITDKDVVLDRRFGGPEYGLPNEGTLESIRLCARLEGMLTDPVYEGKSMHGMIEKVRLGEFPAGSKVLYA... |
Does not catalyze the synthesis of 1-aminocyclopropane-1-carboxylate but is capable of catalyzing the deamination of L-vinylglycine. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Similar to plant 1-aminocyclopropane-1-carboxylate synthases but lacks a number of residues which are necessa... | MFTLPQKEFRMTTACPGSDSIQDLPSNKGDGLERECSRKPDQKLLKFYGVGDPAAELSSSSPYLSSRGSVIKWFWDSAEEGYRTYHMDEYDEDKNPSGIINLGTSENKLCFDLLSRRLSQSDMLQVEPALLQYPDWRGHLFLREEVARFLSFYCRSPAPLKPENVVVLNGCASLFSALATVLCEAGEAFLIPAPYYGAITQHVYLYGNVRLVCVYLDSEVTGLETRPFQLTVEKLEMALQGANSEGVKVKGLILINPQNPLGDIYSPGELQEYLEFAKRHELHVMVDEVYMLSVFEESAGYRSVLSLERLPDPQRTHVMW... |
Does not catalyze the synthesis of 1-aminocyclopropane-1-carboxylate but is capable of catalyzing the deamination of L-vinylglycine. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Similar to plant 1-aminocyclopropane-1-carboxylate synthases but lacks a number of residues which are necessa... | MFTLPQKDFRAPTTCLGPTCMQDLGSSHGEDLEGECSRKLDQKLPELRGVGDPAMISSDTSYLSSRGRMIKWFWDSAEEGYRTYHMDEYDEDKNPSGIINLGTSENKLCFDLLSWRLSQRDMQRVEPSLLQYADWRGHLFLREEVAKFLSFYCKSPVPLRPENVVVLNGGASLFSALATVLCEAGEAFLIPTPYYGAITQHVCLYGNIRLAYVYLDSEVTGLDTRPFQLTVEKLEMALREAHSEGVKVKGLILISPQNPLGDVYSPEELQEYLVFAKRHRLHVIVDEVYMLSVFEKSVGYRSVLSLERLPDPQRTHVMWA... |
Does not catalyze the synthesis of 1-aminocyclopropane-1-carboxylate but is capable of catalyzing the deamination of L-vinylglycine. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Similar to plant 1-aminocyclopropane-1-carboxylate synthases but lacks a number of residues which are necessa... | MFCLPQQESTAPTTCTGSASTQDMDSGYGDGLQGECLRKPDQTQPKLYGVGDPTATFSSDSSCLSSRGRVIKWFWDSAEEGYRTYHMDEYDEDKNPSGIINLGTSENKLCFDLLSWRLTQGDMLHVEPSLLQYPDWRGHLFLREEVAKFLSFYCKSPAPLKPENVVVLNGCASLFSALATVLCEAGEALLIPTPYYGAITQHIYLYGNVRLAYVYLDSKVTGLNTRPFQLTVEKLEMVLQGVSSEGVKVKGLILINPQNPLGDVYSPEELQDFLRFAMRHKLHVIMDEVYMLSVFEESLGYRSVLSLERLPDPQRTHVMW... |
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Similar to plant 1-aminocyclopropane-1-carboxylate synthases but lacks a number of residues which are necessary for activity. | MLTEALVAVRQGTQTPAAQTTCAPSTMSSSSRPPLETLQAQSVSADETPGSALPACAQPCETARSATPTGGETPNRSRYLSHRGNSIRQQQGILQEGFLLYSLDKFHETDKPDGIINLGTSENKLCHDLLHERLTRPDMLLLDPPLLQYPDWSGHQFLREEVAKFLTDYCCSPKPLKAENVVVMNGCASLFSCIASVICDPKDAILISTPFYGAITEHLGLYSDVKLYHIHLDCEASGEDGRLFHLTVDKLEEGLRRAEHEGFIVRGLVLMNPHNPLADIYTPKEMVGFLEFAKRNELHTIVDEVYMLSVFDESVTFDSV... |
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. While belonging to the class-I pyridoxal-phosphate-dependent aminotransferase family, it lacks a number of residues which are necessary for activity thus suggesting that it lacks enzymatic activity. | MSHRSDTLPVPSGQRRGRVPRDHSIYTQLLEITLHLQQAMTEHFVQLTSRQGLSLEERRHTEAICEHEALLSRLICRMINLLQSGAASGLELQVPLPSEDSRGDVRYGQRAQLSGQPDPVPQLSDCEAAFVNRDLSIRGIDISVFYQSSFQDYNAYQKDKYHKDKNTLGFINLGTSENKLCMDLMTERLQESDMNCIEDTLLQYPDWRGQPFLREEVARFLTYYCRAPTRLDPENVVVLNGCCSVFCALAMVLCDPGEAFLVPAPFYGGFAFSSRLYAKVELIPVHLESEVTVTNTHPFQLTVDKLEEALLEARLEGKKV... |
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. While belonging to the class-I pyridoxal-phosphate-dependent aminotransferase family, it lacks a number of residues which are necessary for activity thus suggesting that it lacks enzymatic activity. | MSENRNEGSSQAAKANSDTQTPSHFKVTHPRLRDQLKKKSSKKKGFKFVQEKMLKFQHVIRNQFLQQISQQMQCVPPGDQQCTQTSRKRKKMGYLLSQMVNFLWSNTVKKLKFKVPLPCLDSRCGIKVGHQTLSPWQTGQSRPSLGGFEAALASCTLSKRGAGIYESYHLSFQSYEAYQADKYHKDKNPSGYINLSTSENKLCLDLITARLTQSDMNLLDEAQLQYSDWKGQPFLREELASFLTHYCKAPTPLDPENVVVLNGCSSVFASLAMVLCDPGDALLIPTPCYNGFVFSSHLYSKIELIPVHLESQVPRSNLDS... |
Transcription factor that promotes early floral meristem identity in synergy with LEAFY. Displays a redundant function with CAULIFLOWER in the up-regulation of LEAFY. Required subsequently for the transition of an inflorescence meristem into a floral meristem, and for the normal development of sepals and petals in flow... | MGRGRVQLKRIENKINRQVTFSKRRAGLFKKAHEISVLCDAEVALVVFSHKGKLFEYSTDSCMEKILERYERYSYAERQLIAPESDVNTNWSMEYNRLKAKIELLERNQRHYLGEDLQAMSPKELQNLEQQLDTALKHIRSRKNQLMYDSVNELQRKEKAIQEQNSMLSKQIKEREKVLMAQQEQWDQQNHGQNMPSPPPPQQHQIQHPYMLSHQPSPFLNMGGLYQEEDPMAMRRNDLDLSLEPVYNCNLGCFAA |
The A subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Seems to act as a positive regulator of PP2A catalytic activity. Confers resistance to phosphatase inhibitors such as okadaic acid and cantharidin. Involved d... | MAMVDEPLYPIAVLIDELKNDDIQLRLNSIRRLSTIARALGEERTRKELIPFLSENSDDDDEVLLAMAEELGVFIPFVGGIEFAHVLLPPLESLCTVEETCVREKAVESLCKIGSQMKENDLVESFVPLVKRLAGGEWFAARVSACGIFHVAYQGCTDVLKTELRATYSQLCKDDMPMVRRAAASNLGKFATTVESTFLIAEIMTMFDDLTKDDQDSVRLLAVEGCAALGKLLEPQDCVARILPVIVNFSQDKSWRVRYMVANQLYELCEAVGPDCTRTDLVPAYVRLLRDNEAEVRIAAAGKVTKFCRLLNPELAIQHI... |
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT. Required for proper chromosome segregation and for centr... | MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELHKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCREN... |
Acts as a scaffolding protein for phosphatase let-92 and its regulatory subunits (Probable). Probably together with let-92 and regulatory subunit sur-6, regulates centriole duplication, microtubule outgrowth and mitotic spindle stability during early embryonic cell division by preventing the degradation of sas-5 and ki... | MSVVEEATDDALYPIAVLIDELRNEDVTLRLNSIRKLSTIALALGVERTRNELIQFLTDTIYDEDEVLLVLAEQLGNFTPLVGGPDHVHCLLLPLENLATVEETVVRDKAVESLRKIADKHSSASLEEHFVPMLRRLATGDWFTSRTSACGLFSVVYPRVSPAIKSELKSMFRTLCRDDTPMVRRAAAAKLGEFAKVFEKTAVIEGLHSSLTDLHVDEQDSVRLLTVESAIAFGTLLDKANKKKLIEPILIELFDDKSWRVRYMVAEKLIEIQNVLGEDMDTTHLVNMYTNLLKDPEGEVRCAATQRLQEFALNLPEDKR... |
Scaffolding molecule which may coordinate the assembly of the catalytic subunit and a variable regulatory B subunit (PubMed:20493808). Component of the Sca1 complex, a regulator of cell motility, chemotaxis and signal relay (PubMed:20493808). The Sca1 complex is recruited to the plasma membrane in a chemoattractant- an... | MASINTESDDYHPIVILIDELKNEDIQLRLNSIKKLQSIAKALGPERTRTELIPYLQDSVLEDEDEVLVVLSEELGNLIEFVGGAEHAVCLLPPLQILAGAEELVVREKAVESLCKIAKEIPTSSFEESFLPLLFSLSKADWFTSRTSACGLFTVSYPRANAEMKKSLRKTFGGLCHDDTPMVKRAAATNLGSFAKQIEKESVKSEILPLFQSLSTDEQDSVRLLGVENCALLGSMLTNEENIQFILPTIKASSLDKSWRVRYMVARLLKELCESMGTEITKTELIGAFVKLLKDTEAEVRTEASLRIADVCSLLTKEMN... |
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. PP2A exists in several trimeric forms, all of which consist of a core composed of a catalytic subunit associated with a 65 kDa regulatory subunit (PR65) (s... | MAASDKSVDDSLYPIAVLIDELKNEDVQLRLNSIKKLSTIALALGEERTRSELIPFLTETIYDEDEVLLALADQLGNFTSLVGGPEFAMYLIPPLESLATVEETVVRDKAVESLRTVAAEHSAQDLEIHVVPTLQRLVSGDWFTSRTSACGLFSVCYPRVTQPVKAELRANFRKLCQDETPMVRRAAANKLGEFAKVVETEYLKSDLIPNFVQLAQDDQDSVRLLAVEACVSIAQLLPQDDVEHLVLPTLRQCASDSSWRVRYMVAEKFVDLQKAVGPEITRVDLVPAFQYLLKDAEAEVRAAVATKVKDFCANLDKVNQ... |
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (PubMed:15525651). Required for proper chromosome segrega... | MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCREN... |
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit (PubMed:10100624). Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (By similarity). Required for proper ch... | MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCREN... |
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. PP2A exists in several trimeric forms, all of which consist of a core composed of a catalytic subunit associated with a 65 kDa regulatory subunit (PR65) (s... | VEAAHLKTDIMSVFDDLTQDDQDSFRFLAVEGCAALGKLLEPQDCLAHILPVIVNFSQDKSWRVRYMVANQLYELCEAVGPDSTKTELVPAYVRLLRDNVAEVRIAAAGKVSKFSRILSPELAIQHILPCVKELSTDSSQHVRSALASVIMGMAPVLGKDATIEQLLPIFLSLLKDEFPDVRLNIISKLDQVNQVIGIDLLSQSLLPAIVELAEDRHWRVRLAIIEYIPLLASQLGVGFFDDKLGALIMQWLKDKEYSIRNAAANNVKRLAAEEFGPEWAMQHIIPQVLDMINDPHYLYRMTILHAISLLAPVLGSEITS... |
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT. Required for proper chromosome segregation and for centr... | MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCREN... |
Phosphatase 2A affects a variety of biological processes in the cell such as transcription, cell cycle progression and cellular morphogenesis, and provides an initial identification of critical substrates for this phosphatase. The regulatory subunit may direct the catalytic subunit to distinct, albeit overlapping, subs... | MQTENQVNDLYPIAVLIDELKHDEITYRLNALERLSTIALALGPERTRDELIPFLDESIDDEDEVLSALADQLGNFVDYVGGPEYAHVLLSPLENLAATEETVVRDKAVDSLNKVCICLSQEQLEQYFVPLVQRLSTAEWFTSRASSAGLYCAAYSQSENPAVKVSLRQSFSHLCHDEAPMVRRPAATNCAKFVFLVTKQEAIDEFIPLFNSLSNDDQDSVRLLSFDIMVSLAEVLKSDSEIRHYLLQPLRSFVSDSSWRTRYMVAANFVKLAKVVGPSLIKDELIKPFVLLMKDTEQEVRRAIATQIPGFCELLDKRIV... |
Phosphatase 2A affects a variety of biological processes in the cell such as transcription, cell cycle progression and cellular morphogenesis, and provides an initial identification of critical substrates for this phosphatase. The regulatory subunit may direct the catalytic subunit to distinct, albeit overlapping, subs... | MSGARSTTAGAVPSAATTSTTSTTSNSKDSDSNESLYPLALLMDELKHDDIANRVEAMKKLDTIALALGPERTRNELIPFLTEVAQDDEDEVFAVLAEQLGKFVPYIGGPQYATILLPVLEILASAEETLVREKAVDSLNNVAQELSQEQLFSDFVPLIEHLATADWFSSKVSACGLFKSVIVRIKDDSLRKNILALYLQLAQDDTPMVKRAVGKNLPILIDLLTQNLGLSTDEDWDYISNIFQKIINDNQDSVKFLAVDCLISILKFFNAKGDESHTQDLLNSAVKLIGDEAWRVRYMAADRFSDLASQFSSNQAYIDE... |
The A subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Involved during developmental process such as seedling and floral developments. Seems to act as a negative regulator of PP2A catalytic activity. Associates wi... | MSMIDEPLYPIAVLIDELKNDDIQLRLNSIRRLSTIARALGEERTRKELIPFLSENNDDDDEVLLAMAEELGVFIPYVGGVEYAHVLLPPLETLSTVEETCVREKAVESLCRVGSQMRESDLVDHFISLVKRLAAGEWFTARVSACGVFHIAYPSAPDMLKTELRSLYTQLCQDDMPMVRRAAATNLGKFAATVESAHLKTDVMSMFEDLTQDDQDSVRLLAVEGCAALGKLLEPQDCVQHILPVIVNFSQDKSWRVRYMVANQLYELCEAVGPEPTRTELVPAYVRLLRDNEAEVRIAAAGKVTKFCRILNPEIAIQHI... |
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or s... | MAGASELGTGPGAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLENLATVEETVVRDKAVESLRQISQEHTPVALEAYFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQQFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKSEIVPLFTSLASDEQDSVRLLAVEACVSIAQLLSQDDLETLVMPTLRQAAEDKSWRVRYMVADRFSELQKAMGPKITLNDLIPAFQNLLKDCEAEVRAAAAHKVKE... |
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or s... | MAGAAGPGSGPGAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRTELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLESLATVEETVVRDKAVESLRQISQEHTPVALEAHFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQHFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKTEIVPLFTNLASDEQDSVRLLAVEACVSIAQLLSQEDLEALVMPTLRQAAEDKSWRVRYMVADKFSELQKAVGPKIALSDLIPAFQSLLRDCEAEVRAAAAHKVRE... |
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. PP2A exists in several trimeric forms, all of which consist of a core composed of a catalytic subunit associated with a 65 kDa regulatory subunit (PR65) (s... | NSAGAAAPGTGPVAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRTELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLESLATVEETVVRDKAVESLRQISQEHTPVALEAHFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQHFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKSEIVPLFTNLASDEQDSVRLLAVEACVSIAQLLSQDDLEALVMPTLRQAAEDKSWRVRYMVADKFSELQRAVGPKITLNDLIPAFQNLLKDCEAEVRAAAAHKVK... |
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or s... | MAGAAGPGTVPGAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRTELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLESLATVEETVVRDKAVESLRQISQEHTPVALEAHFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQHFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKTEIVPLFTNLASDEQDSVRLLAVEACVSIAQLLSQDDLEALVMPTLRQAAEDKSWRVRYMVADKFSELQKAVGPKIALSDLIPAFQSLLRDCEAEVRAAAAHKVRE... |
The A subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Involved during developmental process such as seedling and floral developments. Seems to act as a negative regulator of PP2A catalytic activity. PP2A consists... | MSMVDEPLYPIAVLIDELKNDDIQRRLNSIKRLSIIARALGEERTRKELIPFLSENNDDDDEVLLAMAEELGGFILYVGGVEYAYVLLPPLETLSTVEETCVREKAVDSLCRIGAQMRESDLVEHFTPLAKRLSAGEWFTARVSACGIFHIAYPSAPDVLKTELRSIYGQLCQDDMPMVRRAAATNLGKFAATIESAHLKTDIMSMFEDLTQDDQDSVRLLAVEGCAALGKLLEPQDCVAHILPVIVNFSQDKSWRVRYMVANQLYELCEAVGPEPTRTDLVPAYARLLCDNEAEVRIAAAGKVTKFCRILNPELAIQHI... |
Probable regulatory subunit of serine/threonine phosphatase let-92. Together with let-92 and constant regulatory subunit paa-1, positively regulates centriole duplication during early embryonic cell divisions by preventing the degradation of sas-5 and kinase zyg-1 (PubMed:21497766). In addition, during vulva developmen... | MVMEVDEPAVAATTSQNQPQEHANDFDMDTSEGPIENDETFEPVDQINWKFNQVKGNIDADVHTEADVISCVEFSHDGEYLATGDKGGRVVIFQRDQSGKYVKGVRSREYNVYSTFQSHEPEFDYLKSLEIDEKINQIRWLKKKNAANFILSTNDKTIKLWKISERERKIGDDAWNLPRTNRINTSSFRGRLQIPSIVPMELIVEASPRRVYGNAHTYHVNSISVNSDQETFLSADDLRVNLWNLEITNESFNIVDIKPANMEELTEVITAAEFHPTQCNWFVYSSSKGSIRLCDMRDRALCDAYAKIFEEPEDPQSRSF... |
Regulatory subunit of type 2A protein phosphatase. Not involved in HMGR regulation in seedlings grown in standard medium, but negatively regulates root growth in response to salt. PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory sub... | MEIDGGNDVQILDPELLQLPGLSPVSLKENPHIAEELFSQWLSLPETGRLVKSLIDDTKSSTPVSVSKNCTSLNVACGSALPSVFLNSGTPPLSPRGSPGSPRFSRQKTSPSLQSPLKSVREPKRQLIPQFYFQHGRPPAKELREQCISMVDQFFSNYIDGLHMDEFKSITKEVCKLPSFLSSVLFRKIDTSGTGIVTRDAFIKYWVDGHMLAMDVASQIYNILRQPGCKYLRQADFKPVLDELLTTHPGLEFLRNTPEFQERYAETVIYRIFYYINRSGTGCITLRELKRGNLITAMQQVDEEDDINKVIRYFSYEHFY... |
Regulatory subunit of type 2A protein phosphatase. Involved in post-transcriptional regulation of HMGR but not in root growth regulation in response to salt. PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit ... | MVDTVIPGDMACLDADLLQLQEMSSFVLNSKPGFTQKLFDQWLSLPEAQRQVGSLLKDAVAGAPINVTGSASGSNSATIPSMFPAGSAPPLSPRSCGSPRTTKQRAPSNLGSTLKVVNEPVKEPIPQFYFQNGRPPPSEIKEQCMFRINHFFYGHMDGLQIQEFKLVTREICKLPSFFSTSLFRKIDLNNTGFVTRDAFIDFWVNGNMLIMDTTTQIFKILKQKDQSFIVKDDFKPLLKELLATHPGLEFLQSTPEFQERYAETVTYRIFYYINRSGNGRITFRELKRGNLIDAMLHADEEEDINKVLRYFSYEHFYVIY... |
3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH Amino-acid degradation; L-valine degradation. Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily. Extended N-terminus. | MSLRVMSPAMLNAWSQTLVRAMSTQGGAKNIGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDASYDEMTADGVNKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKITHCGVYGMGQAAKLCNNMMLAISMIGVSEAMNLAVRQGLDANVFAEIINSSTGRCWASEIYNPVPGVCPSAPANRDYAGGFSSALITKDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFSVVYDLMKKE... |
3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH Amino-acid degradation; L-valine degradation. Homodimer. Detected in skin fibroblasts. Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily. | MAASLRLLGAASGLRYWSRRLRPAAGSFAAVCSRSVASKTPVGFIGLGNMGNPMAKNLMKHGYPLIIYDVFPDACKEFQDAGEQVVSSPADVAEKADRIITMLPTSINAIEAYSGANGILKKVKKGSLLIDSSTIDPAVSKELAKEVEKMGAVFMDAPVSGGVGAARSGNLTFMVGGVEDEFAAAQELLGCMGSNVVYCGAVGTGQAAKICNNMLLAISMIGTAEAMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMDGVPSANNYQGGFGTTLMAKDLGLAQDSATSTKSPILLGSLAHQIYRMMCAKGYSK... |
3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH Amino-acid degradation; L-valine degradation. Homodimer. Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily. | TPVGFIGLGNMGNPMAKADRIITMLPSSMNSIEVYSGANGILKEVEKMGAVFMDAPVSGGVGAARICNNMLLAISMIGTAEAMNLGIRDLGLAQDSATSTKTPILLGSVAHQIYRDFSSVFQYLREEETF |
3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH Amino-acid degradation; L-valine degradation. Homodimer. Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily. | MAASLGFRGAASGLWYWSGRRRPVGSLAAVCSRSMASKTPVGFIGLGNMGNPMAKNLMKHGYPLILYDVFPDVCKEFKEAGEQVASSPAEVAEKADRIITMLPSSMNAVEVYSGANGILKKVKKGSLLIDSSTIDPSVSKELAKEVEKMGAVFMDAPVSGGVGAARSGNLTFMVGGVEDEFAAAQELLECMGSNVVYCGAVGTGQSAKICNNMLLAISMIGTAEAMNLGIRSGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMHGVPSSNNYQGGFGTTLMAKDLGLAQDSATSTKTPILLGSLAHQIYRMMCSKGYSKK... |
3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH Amino-acid degradation; L-valine degradation. Homodimer. Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily. | MAASLRLLGAASGLRYWSRRLRPAAGSFAAVCSRSVASKTPVGFIGLGNMGNPMAKNLMKHGYPLIIYDVFPDACKEFQDAGEQVVSSPADVAEKADRIITMLPTSINAIEAYSGANGILKKVKKGSLLIDSSTIDPAVSKELAKEVEKMGAVFMDAPVSGGVGAARSGNLTFMVGGVEDEFAAAQELLGCMGSNVVYCGAVGTGQAAKICNNMLLAISMIGTAEAMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMDGVPSANNYQGGFGATLMAKDLGLAQDSATSTKSPILLGSLAHQIYRMMCAKGYSK... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.