ID A0A0V1AGE7_9BILA Unreviewed; 1999 AA.
AC A0A0V1AGE7;
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:KRY23912.1};
GN Name=zip {ECO:0000313|EMBL:KRY23912.1};
GN ORFNames=T12_6589 {ECO:0000313|EMBL:KRY23912.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY23912.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY23912.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY23912.1};
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:KRY23912.1}.
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DR EMBL; JYDQ01000001; KRY23912.1; -; Genomic_DNA.
DR Proteomes; UP000054783; 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:UP000054783};
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 1959..1999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 844..1035
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1061..1455
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1484..1816
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1850..1933
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1982..1999
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 1999 AA; 231692 MW; 49E30F0DF69B5CBF 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 VFFAFLARCD IEKLKRKLEA EVNDLKDHLS
EKRHLLDELQ QQLARREEEL AHALAKVDEE NASKQNFAKR LREYEGQVNE LQEDLESEKV
LRVKAEKQKR DLAGELESLK AELEETHDHS TIQQELRTKR EEEVAHLKKM LEEEATLREQ
LLQENKQKYM MQIEAISDTV EQLRKGKQQA EKTKSVLESE VAGLTADLNN AQMAKQESDR
RRKQVEAQLM EANGRLGDLE RLKAENSDQL AKYQTELENA QKTAEDTETK LTSATKELAL
VQLQSAELQD LLQEETRAKL LLQNKLRNLE NDCALVKEQK EELEESKQNA EKTIQALQLQ
MVELKKKNEE VSVEIMEEAK KKAQKEIEIV QKKLQEVMVE KDRVERSKKK IQQEVEDLKV
EFENLKASHS EMEKKQRKFD QQLADERSHS AKLNCELDVA TQDIRERETK ILSLTKELEE
LREQLSEADR VKRCMQLELN DFISSKDNAG KNVHELEKAI RALDDTVASQ KIHITELEDA
LQLTEDARLR LEVNLQALRT EHERTLQTKE SDANEKRKQL LKQISELEEE LESERHVKTT
ALNNKRKLEV QLRELEVQLE ASNRVKEDSG KQLKKIMQQW KEVCRELEET RQLRDDGLAT
IRELEKRIRT AESDAAAAQS QLESAVSARK VAESERDELF DQLHEVNARG ALATEERRRF
EEKIRALEEE LEDEGSSLEL SNEKLRKAHM QLDHLTSELA SEKANSNNLE SVRDTLERAN
RELKEKLVAL ETGQRNKIKT LTSALELKIA DLESKLSTES SERAVMSRVL KKTERRFADL
SAQVDEDRRQ FEQLKDEREQ NLNRIKQMKR QLAENDDEIA KMHTKCRKAV RDVEELTIAN
EALLKENSNL RSRLRRVPDQ SIKPAAYGFR GSGMLNRTGS TDLLDMSDGS LASREGSLPD
ESVQPLPSNG NASDSGKFE
//
