ID A0A0S3S9C3_PHAAN Unreviewed; 1177 AA.
AC A0A0S3S9C3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Vigan.06G036100 {ECO:0000313|EMBL:BAT89413.1};
GN ORFNames=VIGAN_06036100 {ECO:0000313|EMBL:BAT89413.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT89413.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT89413.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; AP015039; BAT89413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3S9C3; -.
DR Proteomes; UP000291084; Chromosome 6.
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; -; 1.
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; 3.
DR Pfam; PF00063; Myosin_head; 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; 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, 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:UP000291084}.
FT DOMAIN 136..185
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 189..845
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 19..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..747
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1053..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 962..1017
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 19..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 280..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1177 AA; 134354 MW; B646383ED4E0F080 CRC64;
MVLSASPCSL ARSSLEEMLD SLRRRDEEEE KKKDAPPALP PRPTSRARLP PARRSLPNDF
KVSGSERRVV LENGVATNEE SEVKEMDLGQ KRRKCGFGSK RLKKDVESPY VAISSSDSSG
KVWELDGDDS ISYFIRKKLR VWCRQPRGQW ELGMVQSTSG EEAFVSLSNG NVMKVNRSEI
LPANPDVLEN VDDLIKLCYL NEPSVLHSLK LRYSQGMIYS KAGPILIALN PFKDLQMYGN
KYVSACSQRT MNGPHVYATV DAAYNKMMRD EVNQSIIISG ESGSGKTETA KIAMQYLAAL
GSGGNCAIEN EFLQINRILE AFGNAKTSRN NNSSRFGKLI EIHFGSSGKI SGAKIQTLLL
EKSRVVQLAR DERSYHIFYQ LCAGSSADLK EKLNLRAVSE YKYLVQSDCM SIDGVDDAKN
FDQLMEALDA VRVCKEDQEL IFKILAALLW LGNISFQVDR ENHIEVVEDE AVNSAAQLMG
CSSQDLMTAL CTHKIQADED TIAKNLTLKQ AIERRDAIVK FIYASLFDWL LDQVNKSLEV
GKKCTWKSIS ILDLYGFQTF QKNGFEQFYI NYANERIQQH YNRHLFKLEQ EDYELDGIDW
TKVDFEDNQG CLDLFEKKPQ GLLSLLDEES NLPNASDLTF ANKLKHHLHP NPCFKGERGR
AFRIRHYAGE VLYDTNDFLE KNRDTMSSDC IQFLSSCNSE LLQLFSKMFN QSQKQSVATK
FKVQLFKLIH QLESTMPHFI RCIAPNTKQL PDIYDEGVVL RQLRCYGVPE ILRLSRAGYP
TRMTHQEFSR RYVFMLSEAN VSHDPLSISV AVLQKFNIPS EMYHVGYTKL YLRAGQIDAL
ENMRKQILQG IIGIQKCFRG HQARGCFCEL KNGVTTLQSF IRGENSRRKY GAMSKSSITI
YSRKLEEIHA IIRLQSVIRG WRVRKDASHV NRLKKYPENA KPRRKSFMKI IPEVQDLSKE
PVQNLLSALA ELQRQVDKAD AVVEQKEEEY IELREQLKQS ERKRIEYETK MKSMEEAWQK
QMASLQMSLV AARKSLASEN ATVQPVRHDF VLPRGYDSED TSMGSRTPGG STPMLSGNLS
ITDAGRQVNG NLTTISNLMK EFEQRTQDFD GEVKAMHDVK PGQCANTNSV EELRKLKQRF
EGWKKQYKIR LRDTKARLYK SESEKSWRAW WKLGSRA
//