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Database: UniProt
Entry: A0A2T7D5P1_9POAL
LinkDB: A0A2T7D5P1_9POAL
Original site: A0A2T7D5P1_9POAL 
ID   A0A2T7D5P1_9POAL        Unreviewed;      1530 AA.
AC   A0A2T7D5P1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GQ55_6G109100 {ECO:0000313|EMBL:PUZ50892.1};
OS   Panicum hallii var. hallii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC   Panicum sect. Panicum.
OX   NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ50892.1, ECO:0000313|Proteomes:UP000244336};
RN   [1] {ECO:0000313|EMBL:PUZ50892.1, ECO:0000313|Proteomes:UP000244336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA   Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA   Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA   Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA   Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT   "WGS assembly of Panicum hallii var. hallii HAL2.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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; CM009754; PUZ50892.1; -; Genomic_DNA.
DR   STRING; 1504633.A0A2T7D5P1; -.
DR   EnsemblPlants; PUZ50892; PUZ50892; GQ55_6G109100.
DR   Gramene; PUZ50892; PUZ50892; GQ55_6G109100.
DR   Proteomes; UP000244336; 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:0007015; P:actin filament organization; IEA:InterPro.
DR   GO; GO:0030048; P:actin filament-based movement; IEA:UniProt.
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; 3.
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, 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:UP000244336}.
FT   DOMAIN          8..57
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          62..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          613..635
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          982..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1059..1112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          885..951
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        988..1017
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1059..1094
FT                   /note="Polar residues"
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         156..163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1530 AA;  173671 MW;  2C7C21395E32F77C CRC64;
     MGTKVNIIVG SHVWAEDPAI CWVDGEVVKI NGEEAEIQAT NGKMIVANLS KLYPKDMEAA
     AGGVDDMTKL SYLHEPGVLQ NLAIRYELNE IYTYTGNILI AVNPFQRLPH LYDPHMMQQY
     KGAPFGELSP HVFAVADVAY RAMINENKSN AILVSGESGA GKTETTKMLM RYLAYLGGRA
     ATEGRTVEQQ VLESNPVLEA FGNAKTVRNN NSSRFGKFVE IQFDKHGRIS GAAIRTYLLE
     RSRVCQISDP ERNYHCFYLL CAAPQEEVEK YKLGSPKTFH YLNQSNCYEL VGVSDAHEYL
     ATRRAMDIVG ISTQEQDAIF RVVAAILHIG NIEFSKGKEV DSSVLKDEKS KFHLETTAEL
     LMCNPGALED ALCKRVMVTP EEVIKRSLDP YNATVSRDGL AKTIYSRLFD WLVDKINSSI
     GQDASSKCLI GVLDIYGFES FKSNSFEQFC INYTNEKLQQ HFNQHVFKME QEEYTKEQID
     WSYIEFVDNQ DVLDLIEKKP GGVIALLDEA CMFPKSTHET FAQKLYQTFQ RHKRFVKPKL
     SRTDFTICHY AGEVLYQSDQ FLDKNKDYVV AEHQELLSAS KCSFISGLFP PLPEETSKSS
     KFSSIGARFK QQLQALMDTL NSTEPHYIRC VKPNNVLKPA IFENVNVMQQ LRCGGVLEAI
     RISCAGYPTR RTFYEFLHRF GILAPEALEG NSSDEKAACK KILEKKGLAG FQIGKTKVFL
     RAGQMAELDA RRTEVLSAAA KTIQGKMRTH IMRKKFLSLR KASVCVQAIW RGRLACKLYD
     NMRREAAAIK VQKNQRRHQA RRSYKLQYAS VLVVQTALRA MAARNEFRFK KQSKAAVTIQ
     ARYRCHKAHS YHRKLKCAAI VAQCRWRGRI ARKELKKLKM EARETGALKE AKDKLEKKVE
     ELTWRVQLEK RLRTDLEEAK AQEVSKLQSS MEALQAKLEE ANTMLVKERE AAKTIVEAPP
     VVQETQVVVQ DTEKVDSLTT EVQELKTSLQ SEKQRADDLE KKRSEKEQAN EEKQKRLEET
     EIKMRQFQDY LRRLEEKLAN VESENKVLRQ QAVSMAPSKI LSGRSKSNLQ RSSENVQVSS
     NDPKLILESN NTSSPKKEYD IDDKPQKSLN EKQQENQDLL IRCITQHLGY AGNRPVAACI
     IYKCLLHWRS FEVERTSVFD RIIQTIGHAI ETQDNNEVLA YWLSNASTLL LLLQRTLKAS
     GSTGMAPQRR RSSSATLFGR MTQSFRGTPQ GVNLSLINGS MVSGVETLRQ VEAKYPALLF
     KQQLTAYVEK IYGMIRDNLK KEISPLLGLC IQAPRTSRAS LMKGSSRSNT NTAAQQALIA
     HWQGIVKSLG NFLNILKVNN VPPFLVRKVF TQIFSFINVQ LFNSLLLRRE CCSFSNGEYV
     KAGLAELEHW CYRATDEYAG SAWDELKHIR QAIGFLVIHQ KPKKTLDEIS HDLCPVLSIQ
     QLYRISTMYW DDKYGTHSVS PEVISNMRVL MTEDSNNPVS NSFLLDDDSS IPFSVDDISK
     SMQQIDISDI EPPPLIRENS GFVFLLPPPE
//
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