ID A0A0V0X6T8_9BILA Unreviewed; 2016 AA.
AC A0A0V0X6T8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Myosin heavy chain, non-muscle {ECO:0000313|EMBL:KRX83589.1};
GN Name=zip {ECO:0000313|EMBL:KRX83589.1};
GN ORFNames=T06_3087 {ECO:0000313|EMBL:KRX83589.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX83589.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX83589.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX83589.1};
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:KRX83589.1}.
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DR EMBL; JYDK01000012; KRX83589.1; -; Genomic_DNA.
DR STRING; 92179.A0A0V0X6T8; -.
DR Proteomes; UP000054673; 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; -; 2.
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:UP000054673};
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 1976..2016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 844..1172
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1230..1472
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1501..1833
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1867..1950
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1999..2016
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 2016 AA; 233518 MW; AFAF815704FC970B 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 DDSHSKLLKE KKYAEERCAD VSKKLSEEED
RSKSLQKLKV KYETQVVEHE ESLTKERQAC VFFAFLVSLA RCDIEKLKRK LEAEVNDLKD
HLSEKRHLLD ELQQQLARRE EELAHALAKV DEENASKQNF AKRLREYEGQ VNELQEDLES
EKVLRVKAEK QKRDLAGELE SLKAELEETH DHSTIQQELR TKREEEVAHL KVRLSSSFDD
LLAAYKMLEE EATLREQLLQ ENKQKYMMQI EAISDTVEQL RKGKQQAEKT KSVLESEVAG
LTADLNNAQM AKQESDRRRK QVEAQLMEAN GRLGDLERLK AENSDQLAKY QTELENAQKA
AEDTETKLTS ATKELALVQL QSAELQDLLQ EETRAKLLLQ NKLRNLENDC ALVKEQKEEL
EESKQNAEKT IQALQLQMVE LKKKNEEVSV EIMEEAKKKA QKEIEIVQKK LQEVMVEKDR
VERSKKKIQQ EVEDLKVEFE NLKASHSEME KKQRKFDQQL ADERSHSAKL NCELDVATQD
IRERETKILS LTKELEELRE QLSEADRVKR CMQLELNDFI SSKDNAGKNV HELEKAIRAL
DDTVASQKIH ITELEDALQL TEDARLRLEV NLQALRTEHE RTLQTKESDA NEKRKQLLKQ
ISELEEELES ERHVKTTALN NKRKLEVQLR ELEVQLEASN RVKEDSGKQL KKIMQQWKEV
CRELEETRQL RDDGLATIRE LEKRIRTAES DAAAAQSQLE SAVSARKVAE SERDELFDQL
HEVNARGALA TEERRRFEEK IRALEEELED EGSSLELSNE KLRKAHMQLD HLTSELASEK
ANSNNLESVR DTLERANREL KEKLVALETG QRNKIKTLTS ALELKIADLE SKLSTESSER
AVMSRVLKKT ERRFADLSAQ VDEDRRQFEQ LKDEREQNLN RIKQMKRQLA ENDDEIAKMH
TKCRKAVRDV EELTIANEAL LKENSNLRSR LRRVPDQSIK PAAYGFRGSG MLNRTGSTDL
LDMSDGSLAS REGSLPDESV QPLPSNGNAS DSGKFE
//
