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Database: UniProt
Entry: A0A0V0Y5K0_TRIPS
LinkDB: A0A0V0Y5K0_TRIPS
Original site: A0A0V0Y5K0_TRIPS 
ID   A0A0V0Y5K0_TRIPS        Unreviewed;      1924 AA.
AC   A0A0V0Y5K0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Myosin-4 {ECO:0000313|EMBL:KRX94937.1};
GN   Name=unc-54 {ECO:0000313|EMBL:KRX94937.1};
GN   ORFNames=T4E_6285 {ECO:0000313|EMBL:KRX94937.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX94937.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX94937.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX94937.1};
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:KRX94937.1}.
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DR   EMBL; JYDU01000064; KRX94937.1; -; Genomic_DNA.
DR   Proteomes; UP000054815; 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; -; 3.
DR   Gene3D; 1.20.5.370; -; 5.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 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; 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   InterPro; IPR014751; XRCC4-like_C.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF7; MYOSIN-3; 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; 5.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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:UP000054815};
KW   Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT   DOMAIN          31..80
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          84..777
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          652..674
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          870..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          901..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          941..964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        870..893
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         177..184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1924 AA;  223922 MW;  A02A767213A3C04A CRC64;
     MSYVNPEDDP GWQYLRQKAE QALQDQMKAY DSKKNCWIPD ATEGFIAAEI KSTKGDMITV
     MSAKGNEVTL KKEMVQEMNP PKFEKTEDMA NLTFLNEASV LHNLRQRYYS MMIYTYSGLF
     CVVINPYKRL PIYTESVIKL YMGRRRNEMP PHLFATSDEA YRNMVQDRAN QSMLITGESG
     AGKTENTKKV IAYFAIVGAT QAAMASGDKK PQQATLEEQI VQTNPVLEAF GNAKTVRNNN
     SSRFGKFIRV HFNKLGKLTG GDIEHYLLEK SRVIRQAPGE RCFHIFYQMM SGQLKGLRES
     LRLTKDLRYY HFVSQAELTI DGVDDKEEMK VTDYSFDVMG FEQEEKDNLY KLCAAIMHMG
     EMKFKQRPRE EQAEVDTLED AENACHCFGV NHEEFAKALI KPRVRVGTEW VNKGQNLDQA
     IYSRMFHWLI VRCNKTLSMK DMEKAFFIGV LDIAGFEIFD LNSFEQLWIN FVNERLQQFF
     NHHMFVLEQE EYQREGIKWE FIDFGLDLQA CIDLLEKPLG IVSMLDEECI VPKATDMTYV
     QKLNDQHLGK HPNYQKAKPP KAKQAEAHFA LVHYAGTVRY NVNGWLEKNK DPLNDTAVNV
     LKHANGNQLL LDIWKDYQTQ EEALEASKTG SSKKKGKSSS FMTVSMMYRE SLNNLMNMLN
     STHPHFIRCI IPNEQKKSGL IEASLVLNQL TCNGVLEGIR ICRKGFPNRV QYPDFKHRYA
     ILASDEAHSS EDAKVASEKM VDRMVVEKVF SEEEHRIGLT KIFFKAGVLA RLEEIRDQKL
     SDILTGFQAQ ARWYLGKIDA KRREEQRTGL LIIQRNIRTW LKLRNWHWFK LYGKELEGSL
     NNEEKTRKDL EGQLAKLIQE KNDLFTQLQS EKGNLSSSEE KIQKLTSQKS DLERQVNDLS
     DRLNNQEERG AELQKAKKKV ESECENLNRK IQDLELSLRK AESEKQSRDN QIRSLQDEMT
     SQDELAGKLN KEKKHQEEVN RKLMEDLQAE EDKVNHLNKL KSKLEQQLDD LEDSLEREKR
     ARQDVEKGKR KVEGDIRVAH ENIDEINKQK HDLESNLKKK EQEMQALSSK LEDEQGLVAK
     MQRQIKELQT RIQELEEELE QERQARSKSE KVRNDLQRQL EELSERLDEA GGATQAQLEM
     NKKREAELAK LRRDLEEANM NHEGQLASLR KKHNDAVAEM SDQLDQEKVA YQRELEDLHA
     AMDQENKAKQ DADRFSKQLE LQLAELQAKN DEQTRQLHDY TNMKNRINSE NADLMRQLED
     AESQLNSLNR LKSQYQTQLE EAKRTADEET RERHNLAAQL KNMEHENQSL REQLEEEAES
     KTEMQRHISK LNAEIQQWKA KFESEGLARV DEIEEAKRKL TQKVQEMQEA FEAANGKIAS
     LEKIRHKLLG EIDDAQVDVE RANNYAAQLE KKQKGFDKIV DEWKKKCDDL SSELDASQRE
     NRHLSTECFK LKNSQDELIE QIEAVRRENK NLVQEIKDIT DQLGEGGRSV HELQKVVRRL
     ELEKEELQQA LDEAESALEA EESKVMRAQV EVSQIRQEIE KRIREKEEEF ENTRKNHQRA
     LDSMQATLES EAKGRAEALR LKKKLESDIN ELEIALDHAN KANADAQKNI KMYQDQVKEL
     QMHIEDEQRQ REEIREQFHA SEKRCAMLQS EKEEYMTASE QAERARRQAE AELYELREQV
     NELSSTNASL SAIKRKLEGE LQALHAELDD TLNELKKVDE QCKKAMTDAA RLAEELRQEQ
     EHSMHVERMR KGLEQQVKEM QVRLDEAEQA ALKGGKKIIQ KLEQRIRELE QELDLEQRRH
     QETDKNMRKQ DRRIKETEFQ LEEDKKNAER MQDLIDKLQQ KLKTYKRQIE EAEELAATNL
     SKYRQLQQQL EDAEERADIA ENSLAKLRAK NRSSTSVGGN MAISHSASGI LRSASRARMT
     NNMD
//
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