ID   A0A0N4T540_BRUPA        Unreviewed;      1029 AA.
AC   A0A0N4T540;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Myosin motor domain-containing protein {ECO:0000313|WBParaSite:BPAG_0000332101-mRNA-1};
GN   ORFNames=BPAG_LOCUS3291 {ECO:0000313|EMBL:VDN84477.1};
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000332101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BPAG_0000332101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN84477.1, ECO:0000313|Proteomes:UP000278627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; UZAD01000850; VDN84477.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4T540; -.
DR   STRING; 6280.A0A0N4T540; -.
DR   WBParaSite; BPAG_0000332101-mRNA-1; BPAG_0000332101-mRNA-1; BPAG_0000332101.
DR   Proteomes; UP000038020; Unplaced.
DR   Proteomes; UP000278627; 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:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   Gene3D; 1.20.5.340; -; 3.
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   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF58; MYOSIN-4; 1.
DR   Pfam; PF00063; Myosin_head; 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; PS51456; MYOSIN_MOTOR; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW   Muscle protein {ECO:0000256|ARBA:ARBA00023179};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000278627};
KW   Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT   DOMAIN          1..346
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          221..243
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          529..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          681..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..546
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..652
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1029 AA;  118814 MW;  1369C2B810C315C1 CRC64;
     NKTLDQKGIS RDFFIGVLDI AGFEIFDFNS FEQLWINFVN EKLQQFFNHH MFVLEQEEYA
     REGIQWTFID FGLDLQACIE LIEKPLGILS MLDEECIVPK ATDLTLAQKL NDQHLGKHPN
     FEKPKPPKGK QGEAHFAMRH YAGTVRYNVS NWLEKNKDPL NDTVVSVMKH STGNLLLTEI
     WQDYTTQEEA AAAAKDGGGA GKKKGKSGSF MTVSMLYRES LNNLMTMLNM THPHFIRCII
     PNEKKQSGLL DAALVLNQLT CNGVLEGIRI CRKGFPNRTL HKDFKQRYSI LAANESISST
     DMRKCAEAML SKIVKENILT EENFRIGETK VFFKAGVLAH LEDVRDEALK TLLTKLQSQI
     KWYLGLTDKK RRIQQKAGLL ILQRNVRAWC SLRTWEWFKL YTKVRPMLKE GKIAEELEKL
     QEKLKSLEET LQKEENLRKN LDDSAKKMET EKAELFEKLE AVKNNLTKSE GNLSQMESAK
     SDADKKLEEL NEQLADVEDQ NTEIQRSKKK VEGEIDALKK QIQDLEMSAR KAEMEKQSKD
     HQIRSLQDEL QQQAESMAKL NKEIRHQEEL NKKITEDLQG EEDKTNHANK VKSKLEQTLN
     DLEDNLERER RAKADSEKSK RKLEGELKIT QESIDEATRQ RRDLENNMKR KEAELNALSS
     RLEDEQATIS KLQRQIKELQ SRAAELEDEV QNERQSRSKT DKARSDIQHE LEELNDRLDE
     QGGATAAQIE INKKREAELA KLRRDIEEAN MNHESQLAAL RKKHTDAVAE LTDQLDQIQK
     QKQKLEKDKM QYVRNTEDLA AQLDGESAAK VSNEKLVKQF ELQLNDLQAR ADEQSRQLHD
     YSSVRNRLGN ENSDMIRQLE DAEEQISTLQ RFKGQLTQQI EDIRSATDEE IRERQVLAAQ
     VKNLQIEAEQ AHNNLEEEIE SKNEVARQLS KANGEIQQWQ SRFEQDGMLQ TTELEEVRRK
     QGIKINELQE ALEQANQKII TLEKARSRLL GDLDDAQVDV ERANATASQL EKKQKGFDAK
     VEYFQLADH
//