ID A0A0R3RMH1_9BILA Unreviewed; 463 AA.
AC A0A0R3RMH1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Myosin motor domain-containing protein {ECO:0000313|WBParaSite:EEL_0000268101-mRNA-1};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000268101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000268101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC {ECO:0000256|ARBA:ARBA00004657}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR AlphaFoldDB; A0A0R3RMH1; -.
DR STRING; 1147741.A0A0R3RMH1; -.
DR WBParaSite; EEL_0000268101-mRNA-1; EEL_0000268101-mRNA-1; EEL_0000268101.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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}; Methylation {ECO:0000256|ARBA:ARBA00022481};
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}.
FT DOMAIN 7..56
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 60..463
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT BINDING 153..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 463 AA; 52698 MW; 53CFD2193778FC9F CRC64;
DQSKPYDSKK NVWIPDAEDG YVAAEIKSSK GDTVTVVSAR GNEITLKSEL VQEMNPPKFE
KTEDMSNLTF LNDASVLHNL RSRYSQMLIY TYSGLFCVVI NPYKRLPIYE PSVAEMYMGK
RRTEMPPHLF AVSDEAYRNM LIDHENQSML ITGESGAGKT ENTKKVIAYF ATVGASQIRQ
ETSKTSEEAA APDEPTKRKV TLEDQIVQTN PVLEAFGNAK TVRNNNSSRF GKFIRIHFSK
LGRVASCDIE HYLLEKSRVI RQAPGERCYH IFYQLYSDHI PTLKKDLLLD KPLKEYWFVA
QAELTIDGVN DKEEHQLTDE AFDILHFSLE EKTNCYKLMA AIMHMGNMKF KQRPREEQAE
PDGTDEAEKA SSMYGIGHED FLKALTKPKV KVGNEWVNKG QNIEQVTWAV GAMAKGLYSR
VFNWLVKKCN KTLDQKGISR DFFIGVLDIA GFEIFDVSCP IIF
//
