ID A0A0V0U9N5_9BILA Unreviewed; 2006 AA.
AC A0A0V0U9N5;
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:KRX47970.1};
GN Name=zip {ECO:0000313|EMBL:KRX47970.1};
GN ORFNames=T05_12782 {ECO:0000313|EMBL:KRX47970.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX47970.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX47970.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX47970.1};
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:KRX47970.1}.
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DR EMBL; JYDJ01000035; KRX47970.1; -; Genomic_DNA.
DR Proteomes; UP000055048; 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:UP000055048};
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 1966..2006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 844..1035
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1059..1460
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1489..1821
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1857..1940
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1989..2006
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 2006 AA; 232431 MW; 39DF17B12A850653 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 SFIGILDIAG 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 VFFAFLVSLV SARCDIEKLK RKLEAEVNDL
KDHLSEKRHL LDELQQQLAR REEELAHALA KVDEENASKQ NFAKRLREYE GQVNELQEDL
ESEKVLRVKA EKQKRDLAGE LESLKAELEE THDHSTIQQE LRTKREEEVA HLKKMLEEEA
TLREQLLQEN KQKYMMQIEA ISDTVEQLRK GKQQAEKTKS VLESEVAGLT ADLNNAQMAK
QESDRRRKQV EAQLMEANGR LGDLERLKAE NSDQLAKYQT ELENAQKTAE DTETKLTSAT
KELALVQLQS AELQDLLQEE TRAKLLLQNK LRNLENDCAL VKEQKEELEE SKQNAEKTIQ
ALQLQMVELK KKNEEVSVEI MEEAKKKAQK EIEIVQKKLQ EVMVEKDRVE RSKKKIQQEV
EDLKVEFENL KASHSEMEKK QRKFDQQLAD ERSHSAKLNC ELDVATQDIR ERETKILSLT
KELEELREQL SEADRVKRCM QLELNDFISS KDNAGKNVHE LEKAIRALDD TVASQKIHIT
ELEDALQLTE DARLRLEVNL QALRTEHERT LQTKESDANE KRKQLLKQIS ELEEELESER
HVKTTALNNK RKLEVQLREL EVQLEASNRV KEDSGKQLKK IMQQWKEVCR ELEETRQLRD
DGLATIRELE KRIRTAESDA AAAQSQLESA VSARKVAESE RDELFDQLHE VNARGALATE
ERRRFEEKIR ALEEELEDEG SSLELSNEKL RKAHMQLDHL TSELASEKAN SNNLESVRDT
LERANRELKE KLVALETGQR NKIKTLTSAL ELKIADLESK LSTESRLAER AVMSRVLKKT
ERRFADLSAQ VDEDRRQFEQ LKDEREQNLN RIKQMKRQLA ENDDEIAKMH TKCRKAVRDV
EELTIANEAL LKENSNLRSR LRRVPDQSIK PAAYGFRGSG MLNRTGSTDL LDMSDGSLAS
REGSLPDESV QPLPSNGNAS DSGKFE
//
