ID A0A0V1DDF5_TRIBR Unreviewed; 1987 AA.
AC A0A0V1DDF5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Myosin heavy chain, non-muscle {ECO:0000313|EMBL:KRY59396.1};
GN Name=zip {ECO:0000313|EMBL:KRY59396.1};
GN ORFNames=T03_7165 {ECO:0000313|EMBL:KRY59396.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY59396.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY59396.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY59396.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY59396.1}.
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DR EMBL; JYDI01000013; KRY59396.1; -; Genomic_DNA.
DR Proteomes; UP000054653; Unassembled WGS sequence.
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; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.10.250.2420; -; 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}; Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 34..84
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 88..783
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 661..683
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1947..1987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 844..1443
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1472..1804
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1838..1921
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1970..1987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1987 AA; 230487 MW; 2CA46C5392D67C1A CRC64;
MNDRWRQLCP EEDLKYLVAS QDGREEQILQ PEWGRQRMVW VPHETAGFVA ARIVEEKGDM
VVVEIVDTGK KLEISEEMVE KMNPPKYEKV PDMADLTCLN EACVLHNLKA RYYSGMIYTY
SGLFCVVINP YEKLPIYTEA IIEMYKGQKR HEVPPHVFAI ADTAYRNMLQ ERDDQSILCT
GESGAGKTEN TKKVIQYLTY VAGTSRTPKC GTSQAVNTRG ELEQQLLQAN PILEAFGNAK
TVKNDNSSRF GKFIRINFDM SGFICGANIE SYLLEKSRAN RQAKDERSFH IFYQFLQGTT
EEEKKAFVLN KVDQYRFLAN GYIALPGVDD AAEFHNTVRS MRIMNFLDDE ISAILRVVSA
VLHFGNLEFI QDKKSDQAML PDDTVYQKVC RLLGLSVSEL SKALIRPRIK VGRDYVHKSQ
SKEQAEFSVE AISKACYERL FKWLVHRINK SLDRTKRQSA SFIGILDMAG FEIFNLNSFE
QLCINYTNEK LQQLFNHTMF ILEQEEYQKE GIDWQFIDFG LDLQPTIDLI EKPMGILSLL
DEDCWFPKAT DKSYTEKLKA NHSKHPKFII PDFKAASDFA LLHYAGRVDY STKQWLMKNM
DPLNENVVAL LQNSSDPFVV SIWKDAEFAG IGATEVNETT FGVRTKKGMF RTVSQLYKEQ
LNRLMGLLRN STPHFVRCII PNYEKKNGKL DAMLVLEQLR CNGVLEGIRI CRAGFPNRIP
FQEFRHRYEI LCPNVISRGF MDGKEAVKKM VDYLDLEPVL YRIGQSKIFF RAGILAELED
ERDRQLSGLI AKFQAICRGV LSRRYYHKRV QQFNAIRVIQ RNGLAYLKLR HWKWWRLFTK
VKPLLQVTNQ EERLQHKEEE LQRLKDHMQR QDVDIRELEK KLQQLIEEKA VLVEQLQAET
EACVEADDAR LRILQKKNEL EEHVNELTAR LEEEEEKIQN AFTEKKRFMM NISDLENQLE
CEEASRQKLE LEKTQIENKL KKAEEALAVL DDSHSKVYTY RFCMYLLKEK KYAEERCADV
SKKLSEEEDR SKSLQKLKVK YETQARCDIE KLKRKLEAEV NDLKDHLSEK RHLLDELQQQ
LARREEELAH ALAKVDEENA SKQNFAKRLR EYEGQVNELQ EDLESEKVLR VKAEKQKRDL
AGELESLKAE LEETHDHSTI QQELRTKREE EVAHLKKMLE EEATLREQLL QENKQKYMMQ
IEAISDTVEQ LRKGKQQAEK TKSVLESEVA GLTADLNNAQ MAKQESDRRR KQVEAQLMEA
NGRLGDLERL KAENSDQLAK YQTELENAQK TAEDTETKLT SATKELALVQ LQSAELQDLL
QEETRAKLLL QNKLRNLEND CALVKEQKEE LEESKQNAEK TIQALQLQMV ELKKKNEEVS
VEIMEEAKKK AQKEIEIVQK KLQEVMVEKD RVERSKKKIQ QEVEDLKVEF ENLKASHSEM
EKKQRKFDQQ LADERSHSAK LNCELDVATQ DIRERETKIL SLTKELEELR EQLSEADRVK
RCMQLELNDF ISSKDNAGKN VHELEKAIRA LDDTVASQKI HITELEDALQ LTEDARLRLE
VNLQALRTEH ERTLQTKESD ANEKRKQLLK QISELEEELE SERHVKTTAL NNKRKLEVQL
RELEVQLEAS NRVKEDSGKQ LKKIMQQWKE VCRELEETRQ LRDDGLATIR ELEKRIRTAE
SDAAAAQSQL ESAVSARKVA ESERDELFDQ LHEVNARGAL ATEERRRFEE KIRALEEELE
DEGSSLELSN EKLRKAHMQL DHLTSELASE KANSNNLESV RDTLERANRE LKEKLVALET
GQRNKIKTLT SALELKIADL ESKLSTESSE RAVMSRVLKK TERRFADLSA QVDEDRRQFE
QLKDEREQNL NRIKQMKRQL AENDDEIAKM HTKCRKAVRD VEELTIANEA LLKENSNLRS
RLRRIPDQSI KPAAYGFRGS GMLNRTGSTD LLDMSDGSLA SREGSLPDES VQPLPSNGNA
SDSGKFE
//
