(data stored in ACNUC7421 zone)

SWISSPROT: Q75C49_ASHGO

ID   Q75C49_ASHGO            Unreviewed;      1805 AA.
AC   Q75C49;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 101.
DE   SubName: Full=ACR068Wp {ECO:0000313|EMBL:AAS51294.2};
GN   ORFNames=AGOS_ACR068W {ECO:0000313|EMBL:AAS51294.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51294.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51294.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782,
CC       ECO:0000256|SAAS:SAAS00912437}.
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DR   EMBL; AE016816; AAS51294.2; -; Genomic_DNA.
DR   RefSeq; NP_983470.2; NM_208823.2.
DR   STRING; 33169.AAS51294; -.
DR   EnsemblFungi; AAS51294; AAS51294; AGOS_ACR068W.
DR   GeneID; 4619595; -.
DR   KEGG; ago:AGOS_ACR068W; -.
DR   HOGENOM; HOG000248744; -.
DR   InParanoid; Q75C49; -.
DR   KO; K10352; -.
DR   OMA; VYPDFKM; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0000142; C:cellular bud neck contractile ring; IEA:EnsemblFungi.
DR   GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR   GO; GO:0016460; C:myosin II complex; IEA:EnsemblFungi.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000915; P:actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR   GO; GO:0000916; P:actomyosin contractile ring contraction; IEA:EnsemblFungi.
DR   GO; GO:0000920; P:septum digestion after cytokinesis; IEA:EnsemblFungi.
DR   Gene3D; 2.30.30.360; -; 1.
DR   Gene3D; 3.40.850.10; -; 1.
DR   Gene3D; 4.10.270.10; -; 1.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR027401; Myosin_IQ_contain_sf.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75C49.
DR   SWISS-2DPAGE; Q75C49.
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS01238310};
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00875240};
KW   Coiled coil {ECO:0000256|SAAS:SAAS01033845, ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00874053};
KW   Myosin {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS01033784};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00874078};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          64..732
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   NP_BIND         157..164
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          612..634
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          929..954
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          998..1037
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          803..830
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1038..1104
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1112..1139
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1171..1201
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1216..1236
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1246..1266
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1356..1404
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1419..1453
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1521..1576
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1605..1639
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1702..1722
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1758..1778
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        929..945
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1030
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1805 AA;  209258 MW;  5B2E6B4BE5697288 CRC64;
     MSEQCQMIWV PDAEEVFVKG QLVSTKTIKN KQNKDEKVCL VRVNGKEREV LEVETAAVNP
     STFDKIDDMS ELTHLNEASV LYNLENRYKD DMIYTYSGLF LVALNPYSNI KVYTQDYVNL
     YHGSPKEDNE PHIFAVAEQA YRNLLTQRQD QSVLVTGESG AGKTENTKKI LQYLASITSD
     EKLAHTNLES FERKILQANP ILESFGNAQT VRNNNSSRFG KFIKIEFDEF GKINGAHIEW
     YLLEKSRIIQ QNIRERNYHV FYQLLSGMPA GKLKTLELVS NSITDYAYLR DSNPSIPGVD
     DAHDFSSLLS AFNVVGFKED EIHDIFQCIA IILHIGNVEF TSTRAEQATI KNDVAPLCKL
     IGVDEAAFKM AVLKPKSKAG KEWVSQSKNA AQSRFILNSL SRSLYEKLFA HIVRRINRSL
     DHGSMTENYI GLLDIAGFEI FKDNSFEQLC INYTNEKLQQ FFNHHMFVLE QREYVKEDIQ
     WDFIDYGKDL EYTIELIEKK NNPAGILSIL DEESILPKST DESFYSKLMS AWDGKSPKFK
     RSKLQQCFVL EHYAADVEYN VKDWLSKNKD PLNDHLLTLL SESSNKLISE FYTEQSRGHF
     SKTASNRHKE QLTLLLDQLS STDPHFVRCI VPNTKKKAKT FDRKLILDQL RCNGVLEGIR
     IAREGYPNRI FFREFFQRYK ILGADPKFSN NSKKNCEYLL SCISLDPSLY KVGNTKLFFK
     AGVLAQLETQ KEEKISGIVT GLNAIIHGKT VRTAINLQFQ KLQAAKVLST TFNLYSKLME
     DPWYSLYVKV KPMLGSSQFI AKSKKIAEQV KQLEKDLSAT KSERDDLATK NFNVEKELAE
     IRTALSKETE KLQNFERLYD TAKKREEELR SAYEEAVKLK DTLQSETTIN NEEYQKLQKE
     LQQLKESREQ SNTKIKELET EKSNLQKQID SMKRQVDSST KQAMAMKADK SDLESQLRKL
     KLELKSKEKR VKELEQKVDN SGEDLKLKLQ QVERAAATNN KRLEQLTSEN KLMKDQMEKS
     KKEQHESQRQ LSSRGSELIR LNERIEAERE QVSDLTRERD NLVAEHEQVV NQLAIARSEI
     AEYKKKIEAL KAEAENMKEN YAESSPASQA LVATVENRMR GLEDELTKER AMNRFLNEKL
     LSAFHNGGVH DAQYKESATK EDLIACYEEA KLKLRKTAFR LEKELEEKKE LISRLRFTET
     RLASASFDNQ TICMQLKKLK ELLRKSNKNI NMEKELEEVD IIEFNHEKLL LEIDYLKRQL
     EHERNARVNA EHVASSLHSK FRQIQRSDSI PDIYKLKYEA SEERVRALES KLMSSPLKDK
     TNTSNGEIFL HRESISKYED ELKLHKLENY KLQDYLKESN KQLSTLTHEL KVAKMAETAM
     HDQLVQLEQD LASTEKQKQL LQSSVRHHQT QYENCINDLH ATEAQMRDLV HSLKQSEEDI
     QTMTDLIQKL RSQSKQKDML IWDLEKTIGQ LEGKLGDRTR AESELKKELT TLTYKGNVLR
     AETASKIDDL LQQSTHYDAI IQDLVSQKEA AESLQTALQN KLNALTSQMD NMAKDLNSLA
     TEKLQLENDR EMLLSKLKTT NVDFEKSINE RTNIVNELEF LREQMVLQQR QNERNESLIE
     QIQEEALRIK SQLNDERNKN IELYEQNQSL GRTNMQLGQR LEMLEGGLAD GSEKRVWMKR
     IHELEMRLNE ESELKFEEMK RNQGLQRMLE ELKSATNNQE NIISIASKDR DVVEKQFAEV
     ASRVDGMEKY ISKQDGAFKK MEQENTYYKN RIAELEQEIF LWQERYKGLS THRRSLAQST
     EEVLI
//

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