ID A0A0B2VQF3_TOXCA Unreviewed; 1055 AA.
AC A0A0B2VQF3;
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=Unconventional myosin-Ie {ECO:0000313|EMBL:KHN83240.1};
GN Name=MYO1E {ECO:0000313|EMBL:KHN83240.1};
GN ORFNames=Tcan_14869 {ECO:0000313|EMBL:KHN83240.1};
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:KHN83240.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN83240.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN83240.1};
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 -!- 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:KHN83240.1}.
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DR EMBL; JPKZ01001209; KHN83240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2VQF3; -.
DR STRING; 6265.A0A0B2VQF3; -.
DR OMA; GCHEHFN; -.
DR Proteomes; UP000031036; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 1.10.10.820; -; 1.
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; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR13140:SF729; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 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 Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
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 SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 56..732
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 692..904
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1003..1055
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 609..631
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 902..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1055 AA; 119630 MW; A6BF8768C39E1FEB CRC64;
MSIDMCVCWW YTGESNSVEL KCCSGSGLRG APLLSPPMPP PQLAFHWQSK TNVQQVGVDD
MVLLSKLNEE AIVENLRKRL MANSIFTYIG PVLISVNPFK EMPYFTEREM EIYQGAAQYE
NPPHIYALAD NMFRNMIIDN ENQCVIISGE SGAGKTVDAK YIMSYISRIS GGGQRVQHVK
DVILQSNPLL ESFGNSATVR NWNSSRFGKY VEIVFSRGGE PIGGKISNFL LEKSRVVYQN
QGERNFHIFY QLCAGADDSL KNNLGIGSLD YYNYLNHSGC YKIDGTDDAR DFKQTLHAMS
VIGISNEMQL EVLQLVAAIM HIGNITFVEQ NNYAAVYDEQ FLEFPAFLLG LTTSAIKEKL
TSRHMESKWG RQTEQIDVTL NVQQAEFTRD AWVKELYARL FDFLINSVNE GMKVNTRLSG
TPLSIGILDI YGFEIFDNNG FEQFCINFVN EKLQQIFIEL TLKAEQEEYV NEGIRWNEID
YFNNKVVCDL IEGRKPPGIM CILDDTCSQI HGQSEGADSK FLMKLNQLLS TNEHYRSGAE
SFVIRHYAGE VVYNVDCFCE KNRDVLYQDL ISLMQQSQRP FLVQMFPEMV SSGAKSKPTS
FSSKIRTQAN DLVESLTKCA PHYVRCIKPN ETKRPLDWDD KRVLHQVEYL GLKENIRVRR
AGFAYRRTFE RFIYRYAILS KETWPNYHGD PRKGIQIICR SVNMDADQYQ LGKTKIFIKN
PESLFLLEEM RERKYDGYAR IIQKAFRKFN AQKHYMKVKT SKLDLLVTSK ELLLIGRELV
KSGPNKGKLV EVVKRTIGYN ELLSIGLSPY QDNFFVLNVR DSYTSLLETP LKTEFVTAVS
KRYAQLTNGA VLPLEFRNSY QIVLKKTRFG GGVRTVMFSL NPSGSDSTQL VPKGKTLTVY
IGPGLPTNSR PSAQRTTIGG YKMNPTRQTQ PHRAAPSPMQ HAPPPAPHHA GPTSSNRVYP
AQANGNVANS NAYRHNQNGI AGVPSPFVQA QSPRKPKPPV KPKPMPLVEA LYPYEAQDTD
ELSFAVGDKF ELINKGQQLI FIIPEDLSLE CHNNE
//