ID A0A0N5AQ97_9BILA Unreviewed; 1932 AA.
AC A0A0N5AQ97;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Myosin head {ECO:0000313|WBParaSite:SMUV_0000685101-mRNA-1};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000685101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000685101-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; 451379.A0A0N5AQ97; -.
DR WBParaSite; SMUV_0000685101-mRNA-1; SMUV_0000685101-mRNA-1; SMUV_0000685101.
DR Proteomes; UP000046393; 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; -; 5.
DR Gene3D; 1.20.5.370; -; 3.
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; 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 Gene3D; 4.10.270.10; Myosin, subunit A; 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; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014751; XRCC4-like_C.
DR PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR PANTHER; PTHR45615; 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 SUPFAM; SSF57997; Tropomyosin; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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 28..77
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 81..787
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 662..684
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1040..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1932 AA; 222999 MW; 06716E8403E10D50 CRC64;
MDYEQDPGWV YLRQSQEQLL AATTKKFDSK KNVWISDTEE GFIAAEIKST KGDTVVVVTS
KGTEKTLKKD DTQQMNPPKF EKTEDMANLT FLNDASVLHN LRQRYYSMMI YTYSGLFCVV
INPYKRLPIY TESVCKMYIG KRRSEMPPHL FAVSDEAYRN MINGRMNQSM LITGESGAGK
TENTKKVISY FATVGATQQA VKKGKTSSKK KATIEDQIVQ TNPVLEAFGN AKTVRNNNSS
RFGKFIRIHF NSVGKLAGAD IEHYLLEKSR VIKQAPGERS YHIFYQIMSG QIKGLKEKLF
LTKDIRSYRF VSQAEITIDG VNDKEEMQIT DESFGIMHFT EEEKMDLFKL TAGIMHMGEM
KFKQRPREEQ AECEDQAEGD LACKLWNVDQ DKFVTALLKP RVKVGTEWVN KGQNLEQVNW
AVGALAKAIF ARMFTWLIKR CNKTLDAQAL TRDFFIGVLD IAGFEIFDHN SFEQLWINFV
NEKLQQFFNH HMFVLEQEEY QIEGIKWEFI DFGLDLQACI ELIEKPLGII SMLDEECIVP
KATDMTLAQK LNDQHLGKHP NFQKPKPPKG KQGDAHMAIV HYAGTVRYNV KGWLEKNKDP
LNDTAVAVLK ANTGMKLMSE IWADYKTQED MAALVKEGKS TGKKKGKSAS FMTVSMMYRE
SLNNLMTMLY QTHPHFIRCI IPNEQKKSGV IEANLVLNQL TCNGVLEGIR ICRKGFPNRM
AYPDFKQRYS VLAADAAKAG KDPPESSRNI LDELSKKNLL KPEEFQAGKT KVFFKAGVLA
RLEEMRDEAL SKIITKLQSV CRYYYAQIDI RRRIQQRAGI LIVQRNVRSW CTLRSWHWFK
LYNRVKPLIQ GNKKDEEFEA LEKKYKEMEE TLNREAEMRK DADATIQRLN SERQALLLQL
EQERDVTAEG EERAAKMLAQ KADVEKQMSD LNEQLADQED KNASLQKVRR KLESDNDVLK
KTVSELETTI KKQESEKASK DNQIRTLQDE IASQDEMVAK INKEKKHQEE VNRKLLEDIQ
AEEDKVNHLN KMKVKLEQSL DDMEDGLERE RRSRQDVEKA KRKAEGELKI AQENIEELLR
QKHENENALK KKDAELHSLT SRIEDEQSLV GKLQRQIKDL LARIQELEET LEAERQSRHK
AEKARSEMQN ELEELGDRLD EAGGATQAQM EVNKKREAEL AKLRRDLEEA ALNSETALAA
MRKKHNDAVA ELSDQLDTLQ KARSKVEKDK LQMQKELEEL HAQLDAEIKQ RQNADRLSKQ
LEAQLTEMQL KGDEQARQAQ EVMAIKNKLQ TENADLNKQL EDTESQLGAI SRIKQQFSSQ
IEEMRRQLEQ ETRERHSLSS QAANYQMECQ QLRDALEEEQ DSKTELQRLI SKANAEAQQW
RTRYEGEGMS RAEELEDAKR KLQSKVQEMQ EQLESANSRV STLDKTRLRL AQELEDAQIE
ADRANSLANS LEKKQKGFDK IVEDWKRKCD SLVMELEASQ RDTRNAATEA FRLRNSLDES
AEQLEGVRRE NKALAQELKD VTDQLGEGGK SQALDDAEAA LEAEESKVLR AQVEISQIRS
EIEKRISEKE EEFENTRKNH QRSLESMQAT LETETRGRAE LMRMKKKLES DINELEIALD
HANKANVDAQ KNIKRHQDTI RELQTQMEEE QRQREELRDQ VNAVERRAQI LQSEKEDLAI
GFEQAERLRR QAELEAADAK ETATALTVNN GSLSAAKRKA ETELQQLHSE FDEALSELKN
TDDRCKKAMM DAAKLAEELR AEQEHSQNLE RQRKGYEQQI KEMQVRMDEA EAGAMKGGKR
MLAKLDQRVR ELEFELAEEN RKHTETQKNL RNKDRRVREL QFQVDEDKKS MERTYDLIEK
LQGKIKTYKR QVEEAEQLAS QNLGKYKQLQ HMLEDAEERA DIAENSLAKM RAKSRSVISF
ASSSRLSRSV SR
//
