ID A0A0V1LUJ4_9BILA Unreviewed; 2002 AA.
AC A0A0V1LUJ4;
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:KRZ63108.1};
GN Name=zip {ECO:0000313|EMBL:KRZ63108.1};
GN ORFNames=T02_14552 {ECO:0000313|EMBL:KRZ63108.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ63108.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ63108.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ63108.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ63108.1}.
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DR EMBL; JYDW01000003; KRZ63108.1; -; Genomic_DNA.
DR Proteomes; UP000054721; 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:UP000054721};
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 1962..2002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 844..1458
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1487..1819
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1853..1936
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1985..2002
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 2002 AA; 232010 MW; 6306781EE066235E 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 KKMLEEEATL
REQLLQENKQ KYMMQIEAIS DTVEQLRKGK QQAEKTKSVL ESEVAGLTAD LNNAQMAKQE
SDRRRKQVEA QLMEANGRLG DLERLKAENS DQLAKYQTEL ENAQKTAEDT ETKLTSATKE
LALVQLQSAE LQDLLQEETR AKLLLQNKLR NLENDCALVK EQKEELEESK QNAEKTIQAL
QLQMVELKKK NEEVSVEIME EAKKKAQKEI EIVQKKLQEV MVEKDRVERS KKKIQQEVED
LKVEFENLKA SHSEMEKKQR KFDQQLADER SHSAKLNCEL DVATQDIRER ETKILSLTKE
LEELREQLSE ADRVKRCMQL ELNDFISSKD NAGKNVHELE KAIRALDDTV ASQKIHITEL
EDALQLTEDA RLRLEVNLQA LRTEHERTLQ TKESDANEKR KQLLKQISEL EEELESERHV
KTTALNNKRK LEVQLRELEV QLEASNRVKE DSGKQLKKIM QQWKEVCREL EETRQLRDDG
LATIRELEKR IRTAESDAAA AQSQLESAVS ARKVAESERD ELFDQLHEVN ARGALATEER
RRFEEKIRAL EEELEDEGSS LELSNEKLRK AHMQLDHLTS ELASEKANSN NLESVRDTLE
RANRELKEKL VALETGQRNK IKTLTSALEL KIADLESKLS TESSERAVMS RVLKKTERRF
ADLSAQVDED RRQFEQLKDE REQNLNRIKQ MKRQLAENDD EIAKMHTKCR KAVRDVEELT
IANEALLKEN SNLRSRLRRV PDQSIKPAAY GFRGSGMLNR TGSTDLLDMS DGSLASREGS
LPDESVQPLP SNGNASDSGK FE
//
