ID A0A0R3S3V9_9BILA Unreviewed; 1988 AA.
AC A0A0R3S3V9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Myosin heavy chain, nonmuscle {ECO:0000313|WBParaSite:EEL_0000946201-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_0000946201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000946201-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}.
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DR STRING; 1147741.A0A0R3S3V9; -.
DR WBParaSite; EEL_0000946201-mRNA-1; EEL_0000946201-mRNA-1; EEL_0000946201.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0030017; C:sarcomere; IEA:UniProt.
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 CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 2.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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; 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; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF71; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Muscle protein {ECO:0000256|ARBA:ARBA00023179};
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}; Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 40..90
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 94..801
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 679..701
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 886..1940
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 187..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1988 AA; 232029 MW; 7A6B7674768C8A6C CRC64;
MVQWLPRRRR SLICRYLRNN LIIQVQKGIV ADPALQAEWA KKRLVWVPHE TEGFVSGSIK
EDRGDDAVVE LVDNGKRLTL SKDDLQKMNP PKFDKVEDMA ELTCLNEASV LHNLRERYFS
SLIYTYSGLF CVVVNPYKKL PIYSETLIEA FKGKKRHEMP PHIFAIADTA YRSMLQERED
QSILCTGESG AGKTENTKKV IQYLAYVAGA TRQGKGNSPS KQKQDLENVI GELEHQLLQA
NPILEAFGNS KTVKNDNSSR FGKFIRINFD MSGYISGANI EFYLLEKSRT LRQAADERSF
HVFYQFLRGT SAAEKGNFLL EDVDKYRFLN NGYINLPNVD DANEFHNTVR SMKIMGFQEE
EITCKMLFRE AVLRLVSAVL LFGNMEFFQE KKSDQAILPD DRVSQKLCHL LGLPLVDFTK
AFLRPRIKVG REFVHKAQNK EQAEFAVEAI SKACYEKMFR WLVGRLNKSL DRTRRQGASF
IGILDIAGFE IFELNSFEQL CINYTNEKLQ QLFNNTMFIL EQEEYQREGI DWKFIDFGLD
LQPTIDLIEK PMGILALLDE QCLFPKATDK SLVEKLLVNH SKHPKFVIPE MRAKSDFAVI
HYAGRVDYSA DQWLMKNMDP LNENVVALFQ NSSDPFVVSI WKDAEFAGIC ASEYSETAFG
VRTKKGMFRT VSQMHKEQLT RLMTTLRNTN PHFVRCIIPN HEKKAGKISS LLVLEQLRCN
GVLEGIRICR QGFPNRVPFQ EFRHRYEILT PNIIPKGFMD GKEAVRKMID ALEMENNLYR
VGQSKIFFRT GVLAHLEEER DLKLTGLIVS FQAQCRAFLA RRLYQKRMQQ SNAIRVLQRN
GLAWLKLRNW QWWRLFTKVK PLLQVTNQEA AIALKDEELK VVKDKLSKKE IEYGDIEKRL
KQLSEERNVL QEQLQQESEE RAEVEEMRER LSSKKVELED MLTELNAKLD EGEEQVEKLT
EEKKKLQETV RDLEEQLEEE EQARQKLMLD KVNVDQRWKK LEEKHAELAD SYEKLFKEKK
NIEERAAQLS NHLLEEEEKA KHVGKQRSRV EMQLQEQEQE LRKEKQIRTE VERLKRKLEV
EMEEQKELLE EKRNKLEELN SLLSKREEEL TTLLTKSDED SANNIVLQKQ IRELESALEE
LKEDLDNEKV LREKAEKIRR DLNDDLETLR TEYLEAADKT AISLEIQKKK DEELKELKRA
LESANSANDA KAEELKQKYL KQIEEFDEQV EQQKRIRSQV EKAKNALEIE KASLAAELTV
VQAAKAEADK KRKQAETACL ELNARIAELD SANSALTQHL AKAQSELDSV VKQKEEDEQN
VSALQRKITL LQQQLAEAQD QLQQETRSKL AMQTRVRQLE DDLIESHEMR DEVELKRKEL
EGQLDSARMA LAGAKKKADE GVLQQIEEMK KKAQRDLEVT QKTLAEMEVA RDRVERSKRK
LQQEVEDANI ELNNVRAYSR DLEKKQRRFD QQLAEERANL QKVINERDAL AQESRDRETR
ILSLNNELES LRCQLEESER VKRMLQMELD ESVSSKDDVG KNVHELEKAK RQLETELQEQ
RAQVEELEDA VQIAEDARLR LDVNLQALKS EQERVLAAKE QESEEKRRIL LKQIRDLENE
IENERRSRTG AISNRKKIES QLIEMGQQLE LANRLKDDYS RQLKKHQQII KDLQHDNEEL
RQSKEELSGS LRELERKLRT IDSENIRLLE TNELLLNQKR HLEAEKDELE DARGRGGGMN
VDERRRLEAK VTALEEEVEE EQSLAELALD KQRKAQMQVE QLTTELSVER STTQKLETEK
QAMERANREL KNKVSELETS AQARSRAQIA ALEAKIQFLE EQYNAESQER ANATRQYRRI
EKRLADAILQ LEDERRNTEQ NKELAEREKN RVRQIRRRLD EMEEELIREQ TKARNLQRMI
DDLNAANDTL ARDNNNLRGQ RRTMRESLLG GRRVHLRNSS PHDDLDSIGT EGSRYNYLNT
RILILIFV
//
