GenomeNet

Database: UniProt
Entry: A0A0D2R8S7_GOSRA
LinkDB: A0A0D2R8S7_GOSRA
Original site: A0A0D2R8S7_GOSRA 
ID   A0A0D2R8S7_GOSRA        Unreviewed;      1128 AA.
AC   A0A0D2R8S7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B456_004G219700 {ECO:0000313|EMBL:KJB25981.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB25981.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB25981.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. Plant myosin class XI subfamily.
CC       {ECO:0000256|ARBA:ARBA00008049}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001743; KJB25981.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2R8S7; -.
DR   STRING; 29730.A0A0D2R8S7; -.
DR   EnsemblPlants; KJB25981; KJB25981; B456_004G219700.
DR   Gramene; KJB25981; KJB25981; B456_004G219700.
DR   eggNOG; KOG0160; Eukaryota.
DR   Proteomes; UP000032304; Chromosome 4.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030048; P:actin filament-based movement; IEA:UniProt.
DR   CDD; cd01384; MYSc_Myo11; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR036018; MYSc_Myo11.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF864; MYOSIN-11 ISOFORM X1; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 3.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000032304}.
FT   DOMAIN          6..55
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          60..747
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          628..650
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          834..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          998..1019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1045..1128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..925
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        936..956
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1067..1096
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         161..168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1128 AA;  126913 MW;  F84EAF640C1D09C4 CRC64;
     MPQEITVGSH VWVEDQELAW VDGVVTSVNG NEAEVETING NQVTTKLSKL YPKDMEAPDT
     GVDDMTKLSY LHEPAVLHNL ATRYGIKEIY VRSTSFLTYC GNILIAINPF QAISHLYDTE
     LMDSYKGAQL GDRSPHVFAI TDVAYRAMNN EGKSNSILVS GESGAGKTET TKMIMRYLAY
     LGGHAAAEAR TVERKVLESN PVLEAFGNAK TVRNNNSSRF GKFVEIQFDA CGQISGAAIR
     TYLLEKSRVC QISEPERNYH CFYLLCAAPP KEIEKYKLGD PKSFHYLNQS SCYELVGVDD
     SHDYLATKKA MDIVGISVEE QDAIFRIVAA ILHLGNIAFA LEGEDSSVLE DDKAKFHLQV
     AAELLMCDLE ALETALCKRN MVTPEEVIKR SLDPLGAAIS RDGLAKTIYA RLFDWLVKKI
     NVSIGQDPDS KCLIGVLDIY GFESFKTSSF EQFCINFTNE KLQQHFNQHV FKMEQSVYQE
     EEIDWSYIDF VDNQDVLDLI EKKPGGIISL LDETCMFPKS THETFAQKLY QTFKDHKRFV
     KPKLARTEFT IVHYAGEVQY QCDQFLDKNK DYIVPEHQEL LSTSKCSFIA SLFPSLNAET
     PKSGKFSSIG SRFKVKSYVL ASLLQLQLQQ LMDILNSTEP HYIRCIKPNS DLRPEIFENV
     SVLQQLRSGG VLEAIRVKCE GYPTNRIFSE FLERFSILVP EVLKENVEEN VACKSIMEKV
     GLSNYQIGKT KIFLRAGQMA ELDGRKAKLL GESAKVIQKQ VRSRIARKRY VRIQTASICI
     QTVLRGEKRT AAAVKIQKSA RRKSASRKYT NIKSSAIVVQ TGIRAMVARN EFRSKMQNHS
     ATIKAATEEE EKDSGKEEKD IGKEEKDNGK EEKDIGKEEK DVGKEEKDVG KEEKDSGKEV
     EEPEDKEPEK QPTVEVQEKE ELPDPPVAVL EQNKPDKTDV SPDKEQEVTE ESNEPYHIVE
     EISSPIQDVL TAEELPSEVE QLKVLLIGEK KRADEYQKKH AEAQELSEQR RKKLEETEKK
     VHQLQESLNR LLFSMSEQFS QLKTILQTPS SSKPASPPIA RVDYFDNSDN SDASSTGSDF
     AFPASGRDSA NNSCPRPKAP QVHVKDATAT EITGTADSDK EGAFDDYF
//
DBGET integrated database retrieval system