ID A0A061GBG7_THECC Unreviewed; 1524 AA.
AC A0A061GBG7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Myosin family protein with Dil domain isoform 1 {ECO:0000313|EMBL:EOY27185.1};
GN ORFNames=TCM_029097 {ECO:0000313|EMBL:EOY27185.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY27185.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY27185.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001884; EOY27185.1; -; Genomic_DNA.
DR STRING; 3641.A0A061GBG7; -.
DR EnsemblPlants; EOY27185; EOY27185; TCM_029097.
DR Gramene; EOY27185; EOY27185; TCM_029097.
DR eggNOG; KOG0160; Eukaryota.
DR InParanoid; A0A061GBG7; -.
DR OMA; MQQIEVA; -.
DR Proteomes; UP000026915; Chromosome 6.
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: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:SF772; MYOSIN-5; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 4.
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; 5.
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, ECO:0000256|SAM:Coils};
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:UP000026915}.
FT DOMAIN 8..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 62..732
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1156..1467
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 613..635
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 877..943
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 979..1051
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1524 AA; 172486 MW; EAF664BC60524C11 CRC64;
MAGPDNIIIG SQGWVEDPNL AWIDGEVVRI NGNEVHVKTT NGKTVVTNIS KAFPKDTEAP
PGGVDDMTKL SYLHEPGVLQ NLATRYELNE IYTYTGNILI AVNPFQRLPH LYDTHMMEQY
KGATFGELSP HVFAVGDAAY RAMINEGKSN SILVSGESGA GKTETTKMLM RYLAFLGGRS
GVEGRTVEQQ VLESNPVLEA FGNAKTVRNN NSSRFGKFVE IQFDKTGRIS GAAIRTYLLE
RSRVCQISNP ERNYHCFYLL CAAPPEDIER YKLGSPKTFH YLNQSNCYEL DGVNDAHEYL
ATRRAMDIVG INDQEQEAIF RVVAAILHLG NINFAKGKEI DSSVIKDEKS RFHLNMTAEL
LRCDAQSLED ALIKRVMVTP EEIITRTLDP ENAVASRDAL AKTVYSRLFD WLVDKINISI
GQDPNSKSII GVLDIYGFES FKCNSFEQFC INFTNEKLQQ HFNQHVFKME QEEYTKEEIN
WSYIEFVDNQ DVLDLIEKKP GGIIALLDEA CMFPKSTHET FAQKLYQTFK NNKRFIKPKL
SRTDFTISHY AGEVTYQANQ FLDKNKDYVV AEHQALLTAS ECSFVASLFP PLPEESSKSS
KFSSIGSRFK LQLQSLMETL SATEPHYIRC VKPNNVLKPA IFENFNIIQQ LRCGGVLEAI
RISCAGYPTR RTFYDFLNRF GLLAPDVLEG NYDDKTACQM ILDKKGLKGY QIGKTKIFLR
AGQMAELDAR RAEVLGNAAR TIQRQIRTYV ARKEFISLHG AAINLQSYLR GNMARKIYEE
LRKEAGALKI QKNFRRHIDR KSYLTMRKSA ITLQTGLRTM TARNEFRFRK QTKAAIIIQA
HWRCHQAYSY YQSLQKAVLV SQCGWRCRVA RRELRKLKMA ARETGALKAA KDKLEKRVEE
LTWRLQLEKR LRTDLEEAKA QEIAKLQDAL HEKQLQVEEA NSMVIKEREA ARKAIEEAPP
VIKETPVIVQ DTERINSLIS EVEKLKALLL AEKQTAEEAK QAHAATQAKN GELTKKLEDA
EKRAEHLQDS VHRLEEKLSN LESENQVLRQ QALTMSPTGK ALTARPRTTI IQRSPENGNV
LNEEIKKALP KPQVPETEEK PQKFLNEKQQ ENQELLIKCI SQDLGFSGGK PVAACLIYKC
LLHWRSFEVE RTSIFDRIIQ AIGISIEAPD NNDLLSYWLS NSSTLLLLLQ RTLKASGAAS
LTPQRRRSTS ASLFGRMSQG LRGSPQSAGF SFLNGRVLGG LDDLRQVEAK YPALLFKQQL
TAFLEKIYGM IRDNLKKEIA PVLASCIQAP RTSRASLVKG RSQANAVAQQ ALIAHWQSIV
KSLNNYLKTM RANYVPSFLV CKVFTQTFSF INVQLFNSLL LRRECCSFSN GEYVKAGLAE
LEHWCHDATE EFAGSAWDEL KHIRQAVGFL VIHQKPKKTL KEITNDLCPV LSIQQLYRIS
TMYWDDKYGT HSVSSDVIAS MRVMMTEDSN NAVSSSFLLD DDSSIPFSVD DISKSMQQIE
VAEIDPPPLI RGNSGFTFLL QHSE
//
