ID A0A2T7DHM1_9POAL Unreviewed; 2275 AA.
AC A0A2T7DHM1;
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_5G183100 {ECO:0000313|EMBL:PUZ55082.1};
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:PUZ55082.1, ECO:0000313|Proteomes:UP000244336};
RN [1] {ECO:0000313|EMBL:PUZ55082.1, 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; CM009753; PUZ55082.1; -; Genomic_DNA.
DR EnsemblPlants; PUZ55082; PUZ55082; GQ55_5G183100.
DR Gramene; PUZ55082; PUZ55082; GQ55_5G183100.
DR Proteomes; UP000244336; Chromosome 5.
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:SF737; MYOSIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01843; DIL; 1.
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; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 4.
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..731
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1915..2218
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 612..634
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1779..1867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 876..1123
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1159..1361
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1390..1515
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1600..1683
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1779..1796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1818..1839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1841..1857
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 2275 AA; 258802 MW; 7A0BD278DB664902 CRC64;
MASMLNIVKG SHVWVEDKDL AWVDGEVFGI DGQNAHVRTT KGKTVTAKIS DIHPKDTEAP
PDGVDDMTRL SYLHEPGVLD NLAVRYAKNI IYTYTGNILI AINPFQRLPN LVDACTMEKY
KGANLGDLDP HVFAIADVSY RQMINEGKSN SILVSGESGA GKTETTKLLM RYLAFLGGRS
GTGERTVEQQ VLESNPVLEA FGNAKTVRNN NSSRFGKFVE IQFDKSGKIS GAAIRTYLLE
RSRVCQINSP ERNYHCFYFL CAAPSEDLKK YKLGDPSSFH YLNQSACIKV DGINDAEEYL
ATRNAMDTVG ITEQEQEAIF RVVAAVLHLG NINFAKGREV DSSVIKDDKS RFHLNTAGEL
LMCDCEKLEN ALINREINTP EGVITTTVGP NSATISRDGL AKQIYSRLFD WLVNRINASI
GQDPDSNKLI GVLDIYGFES FKTNSFEQLC INFTNEKLQQ HFNQNVFKME QEEYTREQIN
WSYIEFVDNQ DVLDLIEKKP GGIIALLDEA CMFPKSTHET LSQKLYEKFK NHKRFTKPKL
SRTAFTIQHY AGDVTYQSDQ FLDKNKDYVV SEHQELLNAS KCSFVSGLFP PATEENTKSS
KSSIATRFKM QLHELMETLS STEPHYIRCI KPNSVLKPAI FENTNVLQQL RCSGVLEAIR
ISCAGYPTRK LFHDFLHRFR VLAPEILKEK NDEKVACQKI LDKIGLQGYQ IGRTKVFLRA
GQMADLDARR TEMRNYAARG VQSQYRTHVA REQFLLLRDA SICLQSFVRA RLACKQHEFL
RQQAAALRIQ KTTRWYFAWK TYCQLRLSAV TLQAGVRAMA ARNEFNFRKR NKASVRIQSQ
WRCHRDYSNY MKLKRAALTY QCAWRRRVAK KELRKLRMAA RDTQALKVAK EKLEERVEDL
TSRLGLEKKL RDDLEKSKAE EVAKLKTALR EMEQRVEEVK AMQEQESAKK AVEEALAQER
EKISLLTTEI EGLKELLVAE REENDIRKKA HANALETNEE LNKKVSDADE KIKQFSDTVQ
RLEGTIREGE ALLLTERQQN EAASATLAES QARNEALVSK LEDAVKQNDL LRETSQRFEE
AMKNLESSLI FEKQQHEASL LELAEAREKI EELQREVGDT DEKSTLLKTT IQSLEERSRE
KDALLTLERQ ESEATKKSLS DSEDRNQNLL MKIEVAEKEI AHFQETIQRY EQNMAALETS
LRSEKQQTDV IMKQLADSQG EIGELQRKLE DADGRNRLLQ DSLQRLEEGA TTTDALYLAE
KQEHDHTKKS LSEAQGINKE LLTKIEEAEK NIHQLLENVE RLEKDTAARE SILLTTKQSY
DETAKLLLEA QEKNRELMHK VEDSDSKIVL LEDSVKRLEE STADKDSLLA IERHENCETK
KELAGSQKKI EELLTEVQDA HVNIAELEES VRRLEGNLGV TEALLLTEKE QNASTLKLLS
EAQLRIEDLI KKLEGADRKS DSLQDTITRL EQDGTAKEAL LLTEKQAHEA TKKTLSEAQE
RNEELLKKIH DNDKNILQLQ FTIQRLEETT VANENLLLRE REQNDATTKA HIESQEKYEE
LLKKFVDVDR KIDLLQGTIE RFGENTTTKD ALLLSERHEK DAIKKALTEA DEKNEELLMK
VEDANEKIEH LQTMINKLED NIAAKDVSLE AATKENDTIR KSLAEAQERN DELLKKISDS
EYRIHLLQDT VQKLQVDAIS RLSSFVMEKQ ESDAAKRAVT EAHERNEDLL KRNEDLLKRN
DALIKKIEES SKIVTQLQEA LQRLEGKAAN LEAENQVLRQ QATATPPSTA KSPASRSKIT
RIHRSPENGH ILNGDIRQTE MKPSTSTSEA ITSSGNVPDL GDQKEFEHGE KLQRVPKQKY
QSSHHQQPQD DQQWLLTCIS QYLGFSGSKP VAALLIYQCL LHWKSFEAMK TGVFDSILHA
INTATEAQND MRTLAYWLSN LSTLTVLLQR SFKTTRTAIS TPQRRRFSSD RIFHGNQTSN
AGLAYLSGQS VVGSAGLPQV EAKYPALLFK QQLVDLIEKV YGMISDSVKK ELNPLLELCI
QDPRTSHSSL AKGHLNGMGQ QNQLTHWLGI VKILTSYLDV LKANHVPSVL VHKLFTQIFS
LIDVQLFNRL LLRRECCSFS NGEYVRAGLA ELKHWSDNAT REFAGSAWEA LRHIRQAVDF
LVISLKPMRT LREIRTDVCP ALSIQQLERI VSMYWDDVNG TNTISAEFTS SLKSAVREES
NMATSFSILL DDDSSIPFSL DDITKTLPVI EMADDDLLPF VHENPSFAFL LQRGE
//
