ID A8Y189_CAEBR Unreviewed; 2121 AA.
AC A8Y189;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Protein CBR-LET-75 {ECO:0000313|EMBL:CAP38650.2};
GN Name=myo-1 {ECO:0000313|WormBase:CBG21911};
GN Synonyms=Cbr-let-75 {ECO:0000313|EMBL:CAP38650.2}, let-75
GN {ECO:0000313|WormBase:CBG21911};
GN ORFNames=CBG21911 {ECO:0000313|WormBase:CBG21911}, CBG_21911
GN {ECO:0000313|EMBL:CAP38650.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP38650.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP38650.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP38650.2,
RC ECO:0000313|Proteomes:UP000008549};
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., 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., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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}.
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DR EMBL; HE600952; CAP38650.2; -; Genomic_DNA.
DR STRING; 6238.A8Y189; -.
DR WormBase; CBG21911; CBP05201; WBGene00040581; Cbr-myo-1.
DR eggNOG; KOG0161; Eukaryota.
DR HOGENOM; CLU_000192_8_0_1; -.
DR InParanoid; A8Y189; -.
DR OMA; TWDWFLL; -.
DR OrthoDB; 2878043at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0030017; C:sarcomere; IEA:UniProt.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.20.5.340; -; 3.
DR Gene3D; 1.20.5.370; -; 3.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
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; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 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; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF51; MYOSIN-1; 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; 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:UP000008549};
KW Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 30..80
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 84..847
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 16..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..744
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 981..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1170..1373
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1416..1493
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1522..1992
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 986..1015
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2121 AA; 244539 MW; B112BA392F37EAA2 CRC64;
MSLEYEKDPG WQYLKRSREQ QLADQSRPYD SKKNVWIPDP EEGYIEGEIK GPGPKADTVI
VTAGGKDVTL KKDIVQEMNP PKFEKTEDMS NLTFLNDASV LWNLRSRYAA MLIYVSLFFL
LSVFRRFGIK RELLDRQTVC APTQKTYSGL FCVVINPYKR LPIYTDSVAR MFMGKRRTEM
PPHLFAVSDE AYRNMLQDHE NQSMLITGES GAGKTENTKK VIAYFATVGA SQKAQPKEGE
KTVTLEDQIV QTNPVLEAFG NAKTVRNNNS SRFGKFIRIH FNKYGTLASC DIEHCEFTLM
RPKKLKLFFQ TFSRNLVSSV KLQESVATTF STKSSRTSSH SFATSFFLTS QLRTTGSSPR
LSCSSMVGPS LRTYSQSIDF TGIDDTEEFQ LTDEAFDVLK FSETEKMDCY RLMSGHMHMG
NMKFKQRPRE EQAEPDGQDE AEKACAMFGV DADQFLKALV SPRVKVGTEW VSKGQNVDQV
HWAIGAMAKG LYARVFNWLV KKCNLTLDQK GIDRDYFIGV LDIAGFEIFD FNSFEQLWIN
FVNEKLQQFF NHHMFVLEQE EYAREGIQWT FIDFGLDLQA CIELIEKPLG IISMLDEECI
VPKATDMTLA QKLTDQHLGK HPNFEKPKPP KGKQGEAHFA MRHYAGTVRY NVLNWLEKNK
DPLNDTVVSV MKASKKNDLL VEIWQDYTTQ EEAAAAAKSG GGRKGGKSGS FMTVSMMYRE
SLNKLMTMLH KTHPHFIRCI IPNEKKQSGM IDAGLVLNQL TCNGVLEGIR ICRKGFPNRT
LHPDFVHRYA ILAAKEAKSS DDPKTAAGAI LQSLINAKKL NDEQFRIGHT KVFFKAGVVA
HIEDLRDEKL NQIITGFQSA IRWYTATADA GARRKQLNSY IILQRNIRSW CVLRTWDWFL
LFGKIRPQLK CGKMAEEMAK MAEEQKVLEV EAKKAEAARK AQEEAYAKLS AERSKLLEAL
ELTQGGSAAI EEKLTRLNSA RQEVEKSLND ANDRLSEHEE KNADLEKQRR KAQQEVENLK
KSIEAVDGNL SRSLEEKAAK ENQIRSLQDE MNSQDETIGK INKEKKHLEE NNRQLIDDLQ
AEEAKQAQAN RLRGKLEQTL DEMEEAVERE KRIRAETEKS KRKVEGELKG AQESIDELTA
IKLEADASLK KKEADIHALG VRIEDEQALA NRLTRQSKEN AQRIIEIEDE LEHERQSRSK
ADRARAELQR ELDELNERLD EQNKQLEIQQ ENNKKKDSEI IKFRRDLDEK NMANEDQMAM
IRRKNNDQIQ DLTNTLDALQ KGKAKIEKEK GVLQKELDDI NAQVDQETKS RVEQERLAKQ
YEIQVAELQQ KVDEQTRQIT EFTSTKGRLS NDNSDLARQV EELEIHLATI NRAKTAFSSQ
LVEAKKAAED ELHERQEFHA ACKNLEHELD QCHELLEEQI NGKDDIQRQL SRINSEISQW
KARYEGEGLV GSEELEELKR KQMNRVMDLQ EALSAAQNKV ISLEKAKGKL LAETEDARSD
VDRHLTVIAS LEKKQRAFDK IVDDWKRKVD DIQKEIDATT RDSRNTSTEV FKLRSSMDNL
SEQIETLRRE NKIYSQEIRD INEQITQGGR TYQEVHKSVR RLEQEKDELQ HALDEAEAAL
EAEESKVLRL QIEVQQIRSE IEKRIQEKEE EFENTRKNHQ RALESIQASL ETEAKSKAEL
ARAKKKLETD INQLEIALDH ANKANVDAQK NLKKLFDQVK ELQGQVDDEQ RRREEIRENY
LAAEKRLAVA LSESEDLAHR IDASEKHKKQ LEIEQAELKS SNTELIGNNA ALSAMKRKVE
NEVQIARNEL DEYLNELKAS EERARKAAAD ADRLAEEVRQ EQEHAVHVDR QRKSLELNAK
ELQAKIDDAE RAMIQFGAKA LSKVEERVRS VEAELHSEQR RHQEAVKGFT KQERRARELQ
FQVEEDKKAF DRLQENVEKL QQKIRVQKRQ IEEAEEVATQ NLSKFRQIQL ALENAEERAE
VAENSLVRMR GQVVRSATAK NQFDLFVQSQ KIKIHKKNLS HQKNGVFSKR NKVNFWEKWT
WALGFKRGGQ KERPSKFRKN SKFADEFRWL SFTVLNEERK SKRKFERCQN GGRINRTMRE
FGFLPSEVRK HCHMSEYNKK I
//
