ID A0A0A0LG65_CUCSA Unreviewed; 1530 AA.
AC A0A0A0LG65;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Myosin XI {ECO:0008006|Google:ProtNLM};
GN ORFNames=Csa_2G010140 {ECO:0000313|EMBL:KGN60778.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN60778.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN60778.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. Plant myosin class XI subfamily.
CC {ECO:0000256|ARBA:ARBA00008049}.
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DR EMBL; CM002923; KGN60778.1; -; Genomic_DNA.
DR RefSeq; XP_004139250.1; XM_004139202.2.
DR EnsemblPlants; KGN60778; KGN60778; Csa_2G010140.
DR GeneID; 101206606; -.
DR Gramene; KGN60778; KGN60778; Csa_2G010140.
DR KEGG; csv:101206606; -.
DR eggNOG; KOG0160; Eukaryota.
DR OMA; DMTALWL; -.
DR OrthoDB; 5489458at2759; -.
DR Proteomes; UP000029981; Chromosome 2.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0009860; P:pollen tube growth; IBA:GO_Central.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd15475; MyosinXI_CBD; 1.
DR CDD; cd01384; MYSc_Myo11; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 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; IPR002710; Dilute_dom.
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; IPR037975; MyosinXI_CBD.
DR InterPro; IPR036018; MYSc_Myo11.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF792; MYOSIN-9; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 5.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 6.
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:UP000029981}.
FT DOMAIN 9..58
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 63..733
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1160..1473
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 614..636
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 990..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1530 AA; 173435 MW; 08ECA4F9D7605775 CRC64;
MQGTPVNIIV GSHVWIEDPE DAWLDGQVSK ITGQEAEIEA SNGKKVVAKL SKIYPKDMEA
PAGGVDDMTK LSYLHEPGVL QNLKIRYELN EIYTYTGNIL IAINPFQRLP HLYDGHMMQQ
YKGAPFGELS PHVFAVADVA YRAMINEGKS NSILVSGESG AGKTETTKML MRYLAFLGGR
AATEGRTVEQ QVLESNPVLE AFGNAKTVRN NNSSRFGKFV EIQFDKHGRI SGAAIRTYLL
ERSRVCQVSD PERNYHCFYL LCAAPQEEIE KYKLGNPRSF HYLNQSNCYE LVDVSDAHDY
LATRRAMDVV GISAKEQEAI FRVVAAILHL GNIVFTKGKD VDSSIPKDDK AKFHLKMTSE
LLMCDNAGLE DALCKRVMIT PEEVIKRSLD PQSAAVSRDG LAKTIYSRLF DWLVDKINVS
IGQDPKSKSL IGVLDIYGFE SFKANSFEQF CINFTNEKLQ QHFNQHVFKM EQEEYTKEEI
DWSYIEFVDN QDVLDLIEKK PGGIVALLDE ACMFPKSTHE TFANKLYQTF KAHKRFIKPK
LSRTDFTIAH YAGEVLYQSD QFLDKNKDYV VPEYQDLLGA SKCPFVAGLF PPLKEESAKS
SKFSSIGSRF KLQLQQLMET LNSTEPHYIR CVKPNNLLKP AIFENVNIMQ QLRCGGVLEA
IRISCAGYPT RRAFFEFINR FGILAQESLE GNYDEKTVCK KILEKQGLKG FQIGKTKVFL
RAGQMAELDA RRAEVLSNAA KTIQRRTRTH IARKQFIALR KATIYVQSRW RGKLACKLFK
NLKREAAAVK IQKSARRFHA RKTYKKLQAS VLYVQTGLRA MAARNEFRFR KQTKAAIIIQ
ARWRCHKAAS YYKKLQRGSI VAQCRWRGKV ARKELRKLKL AARETGALKE AKDKLEKKVE
ELTWRIQLEK RLRTDLEEAK AQEIGKLQNS LQELQTKVDE TNSLLVKERE AVKKAVEEAP
PVIQETQVLV EDTKKIDDLT TEVENLKTSL ETEKSRADES EKKCSEIEKS REEQRKKLED
TEKKAHQLQE SLTRLEEKLS NLESENQVLR QQALSMAPNK ILSGRSRSIL QRGAESGHYG
GEGRTPLDLH SPSINQRDSE VEDKPQKSLN DKQQENQDLL IRCIAQHLGF AGNRPIAACI
IYKCLLQWRS FEVERTSVFD KIIQTIGHAI ESQDNNDVLA YWLSNASTLL LLLQRTLKAS
GAAGMAPQRR RSSSATIFGR MTQSFRGAPQ GVNLSLINGG TSGGVDTLRQ VEAKYPALLF
KQQLTAYVEK IYGMIRDNLK KEISPLLGLC IQAPRTSRAS LVKGSSRSVA NTEAQRALIA
HWQGIVKSLG NFLNTLKANH VPPFLVRKVF IQIFSFINVQ LFNSLLLRRE CCSFSNGEYV
KAGLSELEHW CYKATDEYAG SAWDELKHIR QAIGFLVIHQ KPKKTLDEIS HDLCPVLSIQ
QLYRISTMYW DDKYGTHSVS PDVISNMRVL MTEDSNHAIS NSFLLDDDSS IPFSVDDLSK
SMEQIDIGDI EPPPLIRENS GFSFLLPRTD
//