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Database: UniProt
Entry: A0A3B6C3T7_WHEAT
LinkDB: A0A3B6C3T7_WHEAT
Original site: A0A3B6C3T7_WHEAT 
ID   A0A3B6C3T7_WHEAT        Unreviewed;      1088 AA.
AC   A0A3B6C3T7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS2B02G232300.2};
RN   [1] {ECO:0000313|EnsemblPlants:TraesCS2B02G232300.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS2B02G232300.2};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [2] {ECO:0000313|EnsemblPlants:TraesCS2B02G232300.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   AlphaFoldDB; A0A3B6C3T7; -.
DR   EnsemblPlants; TraesCS2B02G232300.2; TraesCS2B02G232300.2; TraesCS2B02G232300.
DR   Gramene; TraesCS2B02G232300.2; TraesCS2B02G232300.2; TraesCS2B02G232300.
DR   Gramene; TraesCS2B03G0558200.2; TraesCS2B03G0558200.2.CDS; TraesCS2B03G0558200.
DR   OMA; YVANSHE; -.
DR   Proteomes; UP000019116; Chromosome 2B.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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; cd01383; MYSc_Myo8; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 2.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.20.240.20; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 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; IPR036022; MYSc_Myo8.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 4.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 3.
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:UP000019116}.
FT   DOMAIN          191..240
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          244..914
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          27..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..816
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   COMPBIAS        68..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         335..342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1088 AA;  122839 MW;  342715FF1E8B74C7 CRC64;
     MLSAAAVMAP VPAAPKSSLE VLLETIKKRD ERPKDEPPAL PARPTCRGRL PRARRSPTPP
     RVHLEDGVAE GAVADTDKKP EAVADTDKKP EAVNENKPEI EKENTPEVKK EIGGQEAKEG
     KAVNGRIFGA KRKLCSVEVE LLDESPYVEN LHEERKDAMA CKEPPSPYFS SARSKRNGKP
     VFTDSMDYVL QKKLRVWCSA SDEKWELGQI QSISGDDVEI HLVNGEVLTL PPERLLPANP
     DILDGVDDLI QMSYLNEPSV LYNLQYRYSR DLIYTKAGPV LIAINPLKEV PLYGKDFIRK
     YRQKLTNDPH VYAIADIAFN EMLRDGINQS IIISGESGAG KTETAKIAMQ YLAALGGANG
     MESEVLQTNV ILEALGNAKT SRNDNSSRFG KLTEMHFSET GKICGAKIQT FLLEKSRVVR
     RASGERSYHI FYQLCSGASP LHRKKLLLRD ANYYNYLKQS ACLRIDGVDD AKRFSSLLGA
     LDIVQISGEN QMELFSMLAV VLWLGNISFS VIDNESHVEV DSNEGLVNAA KLLGCSVPQL
     VIALSTRKIQ AGKENIVQRL TLTQAIDARD ALAKSIYAHL FDWIVEQIND SLGTGRQRTR
     RSISILDIYG FESFNKNGFE QFCINYANER LQQHFNRHLF KLEQEEYLDD GIDWASVEFV
     DNTDCLSLFE KRPLGLLSLL DEESTFPKAT DLSFANKLKQ HLSGNPGFKG EQDGAFKICH
     YAGEVSYDTT GFLEKNRDPL HSESIQLLSS CKSDLPKDFA SVMIADSQNK STLSRHLFVD
     SQKQSVVNKF KAQLFKLMQQ LENTSPHFIR CIQPNNKQRP RQFEHDLVLH QLKCCGVFEV
     VRISRAGYPT RMTHQQFAER YGFLLSHSVA SQNPLSISVA VLQQFSIPPE MYQVGYTKLF
     LRTGQVAALE NAKNRMFHGA LRIQRNFRGL HTRREYHTLK KGATALQSFV RGEKARFRFD
     YLFKRWRAAV LIQKYTRRRL AATMFTDQLK NIVVLQSVIR GCLARKKFNC LQEEKESKVI
     NSKVKRDVRN NISQPRLCHV SSRSPDLYIL SVINLARPWL LLHTTFMQHQ MGSNLLLSPA
     PDGNYSIL
//
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