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Database: UniProt
Entry: A0A0S4JP47_BODSA
LinkDB: A0A0S4JP47_BODSA
Original site: A0A0S4JP47_BODSA 
ID   A0A0S4JP47_BODSA        Unreviewed;      1140 AA.
AC   A0A0S4JP47;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Myosin heavy chain, putative {ECO:0000313|EMBL:CUG90281.1};
DE   Flags: Fragment;
GN   ORFNames=BSAL_25900 {ECO:0000313|EMBL:CUG90281.1};
OS   Bodo saltans (Flagellated protozoan).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Eubodonida; Bodonidae; Bodo.
OX   NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG90281.1, ECO:0000313|Proteomes:UP000051952};
RN   [1] {ECO:0000313|Proteomes:UP000051952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; CYKH01001806; CUG90281.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4JP47; -.
DR   VEuPathDB; TriTrypDB:BSAL_25900; -.
DR   OMA; MIDHEFE; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000051952; 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; cd00124; MYSc; 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   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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|PROSITE-ProRule:PRU00782};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051952}.
FT   DOMAIN          63..727
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          611..633
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1035..1070
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1121..1140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          817..851
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          921..974
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         159..166
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   NON_TER         1140
FT                   /evidence="ECO:0000313|EMBL:CUG90281.1"
SQ   SEQUENCE   1140 AA;  131466 MW;  2D971AE19E2D2B33 CRC64;
     MENFVDGPVY AKCPKRSWII GKLESWDKSK NVGSVKAIND GGDTLANLKE QDVHPMRDGG
     AVEDVDDLLL LTELHDATLL HCIRHRYMKD VIYTNIGAIT VALNPFNFKI PRYMDTMMPT
     YLSEGEVIEK SLPHSWACAH NTYYEMKRDA KDQCILVSGE SGAGKTEASK IVMKYLAAVS
     CIRGEAAVRE EAALVGQKIN SSSPALEAFG NAKTVRNDNS SRFGKFMRVK FNDNSFLVGA
     HITKYLLEKS RIVTASPGER IYHSFYLIIR CKDRAKYLLG DDKQYRSLNA GQTLNNPEFN
     THEEFEEVCK SMTTMGISDA NIQSLWKAVA GILHFENVEF TAEGEGSIPT PASLAHINNG
     CQMWNIDQNS YLQEVRENTL TIMGNQVRKL LTPAMAQDAR SAVNKSIYDN AFSWLVSECN
     SNLDKEDCSN WIGLLDIFGF EDFKHNSFEQ LCINLTNETL QHHYNMYIFC KDVEECRGEG
     IDMSDVSFPD NTPCLKMISA SGGVMALLDE ECQLGSGSDA SFFSKVTGKF NGFPFFIVDK
     LSRTNFVIRH YAGDVSYDTT DFREKNLDTL KDAWKLLLRT SRDELIKELL PAPVDVKGPK
     PTVSVFFRRQ LQELMDLINS TSPHWIRCVK PHPAKKALMF DNISVMNQLS SSGVLGTVKI
     RKAGYAVRIP KDQFLGDFKI VSAAAGTPNT LDGIFQACGY SKNDAQIGTR RVFLRSHIYM
     DLEARKKKAL LNSTKVVQAF SHVVCAFQKA NKAMFASNRL LIDELRKHVR QLLAAQDKEM
     QARQKLMQDA ARLWKLLLGK EAQAAKAVKQ GEAEKRAKII RAMRIEHEEQ REQLEDQETS
     AREEFQIVLQ ELYIDMRFRW DISQRAAEER QARREHAEVE KALMIRRREA CERRREHDRQ
     HMFQQCSKRM EPTVAREDKT IRSLQRIQKQ KQLELEAAQR QMEKELHREE TVQKHRQEIQ
     HQREERAQEN LRKRLHTSQA VAMRDVAFER YYRVMREDFE WQKLERQMLK GQQLVLEEAR
     QAFLREKAES DKLRRKTLEE EDSKVRTQQR LVMEERRQRD EQQSKITAEK ALEDEKRQLV
     EERKQREAIH VRKREKEVER AIGWDNDRRE RILLQRPDIT KSDIDDSPLA MRVPAPTPFI
//
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