ID A0A0B2VPW3_TOXCA Unreviewed; 1799 AA.
AC A0A0B2VPW3;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Myosin-4 {ECO:0000313|EMBL:KHN83384.1};
GN Name=unc-54 {ECO:0000313|EMBL:KHN83384.1};
GN ORFNames=Tcan_05448 {ECO:0000313|EMBL:KHN83384.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN83384.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN83384.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN83384.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) 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:KHN83384.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPKZ01001199; KHN83384.1; -; Genomic_DNA.
DR STRING; 6265.A0A0B2VPW3; -.
DR OMA; IHIIEVM; -.
DR Proteomes; UP000031036; 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; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 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 Gene3D; 4.10.270.10; Myosin, subunit A; 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:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR PANTHER; PTHR45615; 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; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000031036};
KW Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 30..78
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 82..785
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 660..682
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1024..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1770..1799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 856..939
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1784..1799
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 175..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1799 AA; 207583 MW; 257BFE002762CB06 CRC64;
MALEYESDPG WQYLRRSREQ IAADQSAPYD SKKDVWIPDK EEGYIAAQIV STKGDEVVVK
VNGTEKTLKK ELCAQMNPPK FEKTEDMSNL TFLNDASVLH NLRARYAVML IYTYSGLFCV
VINPYKRLPI YTDSVAQMFM GKRRSEMPPH LFAVSDEAYR NMLQNHENQS MLITGESGAG
KTENTKKVIA YFASVGASQQ GQTANAPDGK KKVTLEDQIV QTNPVLEAFG NARTVRNNNS
SRFGKFIRIH FSKHGKVASC DIEHYLLEKS RVIRQAPGER CYHIFYQMTS DYKPELKPAL
LLDRPLRDYW FVAQAELTVD GMNDAEEFQL TDEAFDILHF SPEEKMNCYK LMSAHMHIGN
MKFKQRPREE QAEPDGTDEA EKAAQMYGVD TEELLKAFTH PRVKVGTEWV NKGQNVEQVN
WAVGAMGKAI YARVFNWLVK KCNITLDQKG IRRDYFIGVL DIAGFEIFDF NSFEQLWINF
VNEKLQQFFN HHMFVLEQEE YAKEGIQWKF IDFGLDLQAC IELIEKPMGI ISMLDEECIV
PKATDMTLAQ KLNEQHLGKH PNFEKPKPPK GKQSEAHFAM RHYAGLVRYN VMNWLEKNKD
PLNDTVAACL KASKGNALLN EIWADYTTQE EASHAAKSGG HRKGKSGSFM TVSMLYRESL
NNLMSMLYKT HPHFIRCIIP NEKKKSGLLD AALVLNQLTC NGVLEGIRIC RKGFPNRSPH
PDFVERYALL CAEESKSSND PKECAGKMLD KLVKDGSMKE EMFKIGLTKV FFKAGVLAHL
EDLRDARLAE LIAGLQARIR YYCQQIDLKE RREILAATKV IQYNVADWAH VMNWPWLLLF
IDTMPIVRAS KMEEIMEQLR TDIGSFEGKL NEKNRERKNL EEELEKVLAE KNAIMEEIKN
SRSGNTEVED QIDRLNVQKV ELETEIDNKL EKLKMEQQRT ADESQAVKKI EELMETIKRN
VQDVELGKRK SEAEKAAKEN QIRSLTEEVA QQEEMITKLN KERKAQDENA KKLAEDIKAQ
EEKNELANKT KTKLEKSVSE LEDEVDKEKR VRSENEKERR KVEGDLRVGQ EMLEELNKEK
KDLEMRARKK ESEFRSLDMQ LEQQQTLVSR LTKQVKDNEA KIAAFEEETD AEHEARAKSE
RARAVAHREL TELNDRLDEQ RSATAAQIEI GKRHEAEIAK LKHELEETKL KQQSMLAAMR
KKNSDNIAEL NDQIAELRKQ KMNSEKERNN LQNQVEEAMG RVDTATKLRV EIERKKKELE
TTLNDLQQKC DEQMRQIQES TTLKNRTITD NSELTHRIEE LQEDISVLTT TKAQIAQQLE
EMKRAVVDET GKKQSLNTTV RGLQVEIEQL RVTLEEEISG KDELNRQLNR ANTEASQLKA
QFEDANYVES KILEDEKKKY AIAISELEEA LDAANSKLLT LEKAKDRLST DVDDAQVEAE
KHIATIAQLE KKQKAFQQLV DDWKKKVDDA SNELDAAQKE CRICAADVFK EQALNDNLNI
QVEGLRHENG NLVDEIRDLQ SQLGEGGKNV HEMRKMMRRL EVEKEELHRA IDETEAMLES
EESKVTRFHV EIDQIRKTIE KRIEEKEEEF ENIRKNHQRS LDSIQAALEN EQKEKGELQR
MKKKLEMDVN SLENALMHAN MANEDAQRNI AKYSEQVGEL QQVLEEERTQ REQFKDDFAN
AEKRLAITQS EKEELAAKAL QAERLKKQME SEVNEARSQV EQLSIQSNDL SAVNKKIQEE
MLQAREETAT LNLQKYRRLH AQLQTAEERV EAAQNGLQKF RSKTKTENAN KRNSFTREQ
//
