ID   MYO3_CAEBR              Reviewed;        1969 AA.
AC   Q60LV4; A8Y3Z1;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Myosin-3;
DE   AltName: Full=Myosin heavy chain A;
DE            Short=MHC A;
GN   Name=myo-3 {ECO:0000250|UniProtKB:P12844}; ORFNames=CBG23416;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Essential for muscle contraction. Involved in ovulation
CC       likely by regulating the contraction of gonadal myoepithelial sheath
CC       cells. {ECO:0000250|UniProtKB:P12844}.
CC   -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC       chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC       regulatory light chain subunits (MLC-2).
CC       {ECO:0000250|UniProtKB:P12844}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC       {ECO:0000250|UniProtKB:P12844}. Cytoplasm, myofibril, sarcomere, A band
CC       {ECO:0000250|UniProtKB:P12844}. Note=In myoepithelial sheath cells,
CC       forms filaments assembled in a nonstriated meshwork. Colocalizes with
CC       unc-15/paramyosin and with unc-89 to M line-like structures. Does not
CC       colocalize with beta integrin pat-3. {ECO:0000250|UniProtKB:P12844}.
CC   -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC       of a 28-residue repeat pattern composed of 4 heptapeptides,
CC       characteristic for alpha-helical coiled coils. {ECO:0000255}.
CC   -!- MISCELLANEOUS: MHC A and MHC B are found exclusively in the body wall
CC       muscle. They co-assemble into body wall thick filament.
CC       {ECO:0000250|UniProtKB:P12844}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000305}.
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DR   EMBL; HE601533; CAP39610.1; -; Genomic_DNA.
DR   RefSeq; XP_002636698.1; XM_002636652.1.
DR   AlphaFoldDB; Q60LV4; -.
DR   SMR; Q60LV4; -.
DR   STRING; 6238.CBG23416; -.
DR   GeneID; 8578694; -.
DR   KEGG; cbr:CBG_23416; -.
DR   CTD; 8578694; -.
DR   WormBase; CBG23416; CBP46195; WBGene00041777; Cbr-myo-3.
DR   eggNOG; KOG0161; Eukaryota.
DR   HOGENOM; CLU_000192_8_0_1; -.
DR   InParanoid; Q60LV4; -.
DR   OMA; TDTTQDK; -.
DR   OrthoDB; 47111at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
DR   GO; GO:0031672; C:A band; ISS:UniProtKB.
DR   GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR   GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; ISS:UniProtKB.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR   GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR   GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR   Gene3D; 1.20.5.370; -; 5.
DR   Gene3D; 2.30.30.360; -; 1.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
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   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; SSF52540; SSF52540; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding; ATP-binding; Coiled coil; Cytoplasm; Methylation;
KW   Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW   Reference proteome; Thick filament.
FT   CHAIN           1..1969
FT                   /note="Myosin-3"
FT                   /id="PRO_0000306245"
FT   DOMAIN          33..82
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT   DOMAIN          86..791
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          794..823
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          667..689
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P12844"
FT   REGION          770..784
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P12844"
FT   REGION          943..967
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          993..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1134..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          853..1941
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1000..1029
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         179..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P12844"
FT   MOD_RES         130
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1969 AA;  225901 MW;  F4E140250CE57847 CRC64;
     MSGNPDAFEN DPGFPFLGMS REAKAASAAR PFDSKKNCWI PDPEDGFVAA EIQSTTGDQV
     TVVTVKGNQI TVKKDQCQEM NPPKFDKTED MANLTFLNEA SVLGNLKDRY KDLMIYTYSG
     LFCVVINPYK RLPIYSESVI KHFMGKRRNE MPPHLFAVSD EAYRNMVQDK ENQSMLITGE
     SGAGKTENTK KVISYFAIVG ATQAAAGGKK EEGKKGGTLE EQIVQTNPVL EAFGNAKTVR
     NNNSSRFGKF IRTHFSGSGK LAGGDIEHYL LEKSRVVRQA PGERCYHIFY QIMSGNDASL
     RGKLKLNNDI TYYHFCSQAE LTIEGMDDKE EMRLTQEAFD IMGFEDQETM DLYRSTAGIM
     HMGEMKFKQR PREEQAEPDG EEDALNAAAM LGINAEEFLK ALTKPRVRVG TEWVNKGQNL
     EQVSWAVSGL AKAIYARMFK WIINRCNKTL DAKEIERKHF IGVLDIAGFE IFDLNSFEQL
     WINFVNERLQ QFFNHHMFVL EQEEYKREGI AWTFIDFGLD LQACIELIEK PLGIISILDE
     ECIVPKATDM TYAQKLLDQH LGKHPNFQKP KPPKGKQGDA HFAIVHYAGT VRYNANNFLE
     KNKDPLNDTA VALLKHSVDN NLMLDIWQDY QTQEEAAEAA KAGQSGGGKR GKSSSFATVS
     MIYRESLNNL MNMLYQTHPH FIRCIIPNEK KASGVIDSAL VLNQLTCNGV LEGIRICRKG
     FPNRMLYPDF KHRYAILAAD AAKDSDPKKA SVGILDKIAN DGNLTDEEFK IGETKIFFKA
     GVLAKLEDLR DEILSRIVTM FQSRIRSYLA KAEVRRRYEQ QTGLLIVQRN VRAWCTLRTW
     EWFKLFGKVK PMLKAGKEQE AMGELAEKIQ KLEEAVQRGE IARSQLETQV ADLVEEKNAL
     FLSLETEKAN LADAEERNEK LNQLKATLES KLTDITGQLE DMQERHEDLT RQKKKTEQEL
     SDTKKHVQDL ELTLRKAEQE KQSRDHQIRS LQDEMANQDE SVAKLNKEKK HQEESNRKLN
     EDLQSEEDKV NHLEKIRNKL EQQMDELEET IDREKRSRSD IEKSKRKVEG DLKVAQENID
     EITKQKQDVE NTLKRKEDDL HHASTKLAEE QALAAKLQRQ IKELQARIAE LEEELESERN
     SRQKADRTRN ELQRELEEIS ERLEQQGGFS AAQLEANKKR EAEIAKLRRE KEEDALNHET
     AVSSLRKRQV DAVAELTEQL ETLQKLKAKG DAERAKLQRD LEEAQHATDS EVRARQEVEK
     SYKTIEVQFS ELQTKADEQS RQLQDFAALK NRLNNENGDL NRTLEEMDNQ VNSLHRLKST
     LQSQLDETRR NFEEESRERQ ALAATAKNLE HENEILREHL DEEAESKADL TRQISKLNAE
     IQQWKARFDS EGLNKLEEIE AAKKALQLKV QELSDTNEGL FAKIASQEKV RHKLMQDLDD
     AQSDVEKAAA QVAYYEKHRR QFEKIVEEWK KKTDDLASEL DAAQRDNRQL STDLFKAKTA
     NDELAEYLDS TRRENKSLAQ EVKDLTDQLG EGGRSVAELQ KIVRRLEVEK EELQKALDEA
     EAALEAEEAK VLRAQIEVSQ IRSEIEKRIQ EKEEEFENTR RNHQRALESM QATLEAETKQ
     KEEALRIKKK LESDINDLEI ALDHANRANA DAQKTIKKYM ETVRELQVQI EEEQRQKDEL
     REQFLASEKR NGILQAEKDE LAQQAEAAER ARRNAEADCI ELREQNNDLS NQVSSLTGWR
     RKLEGELLAV HAELEELVTE LKNAQEQGQK ASADAARLAE ELRQEQEHSM HIERIRKGLE
     LQIKEMQIRL DDAENAALKG GKKIIAQLEA RIRAIEQELD GEQRRHQDTE KNWRKAERRV
     KEVEFQVIEE KKNEERLTEL VDKLQTKLKI FKRQVEEAEE VAASNLNKYK VLQAQFEQAD
     ERAEIAENAL SKMRNKIRAS ASVIPPDGFP LAQSPSSALV RSASNARFL