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Database: UniProt
Entry: A8XFA7_CAEBR
LinkDB: A8XFA7_CAEBR
Original site: A8XFA7_CAEBR 
ID   A8XFA7_CAEBR            Unreviewed;      1131 AA.
AC   A8XFA7;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 115.
DE   SubName: Full=Protein CBR-HUM-1 {ECO:0000313|EMBL:CAP31368.2};
GN   Name=hum-1 {ECO:0000313|WormBase:CBG12380};
GN   Synonyms=Cbr-hum-1 {ECO:0000313|EMBL:CAP31368.2};
GN   ORFNames=CBG12380 {ECO:0000313|WormBase:CBG12380}, CBG_12380
GN   {ECO:0000313|EMBL:CAP31368.2};
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:CAP31368.2, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP31368.2, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP31368.2,
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   -!- 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; HE600913; CAP31368.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8XFA7; -.
DR   STRING; 6238.A8XFA7; -.
DR   WormBase; CBG12380; CBP03005; WBGene00033338; Cbr-hum-1.
DR   eggNOG; KOG0162; Eukaryota.
DR   HOGENOM; CLU_000192_7_6_1; -.
DR   InParanoid; A8XFA7; -.
DR   OMA; MAFHWQS; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
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:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
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; PF14604; SH3_9; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00326; SH3; 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:UP000008549};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          14..719
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          757..951
FT                   /note="TH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51757"
FT   DOMAIN          1075..1131
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          596..618
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          949..1023
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1046..1075
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        949..964
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1059..1075
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1131 AA;  128488 MW;  AEA3CB91B387942F CRC64;
     MAFHWQSKVN VQHVGVDDMV LLPKLTEQSI VENLKKRLQA NSIFTYIGPV LISVNPFKQM
     PYFTEKEMLL YQGAAQYENA PHIYALADNM YRYRLIKSAF RNMLIDNESQ CVIISGESGA
     GKTVNAKFIM NYISRISGGG QKVQVLQHVK DVILQSNPLL EAFGNSATVR NWNSSRFGKY
     VEIVFSRGGE PIGGKLSNFL LEKSRVVHQN EGDRNFHIFY QLCAGADKNL RSTLGIGELQ
     YYNYLNMSGV FKADDTDDGK EFESTLHALK VVGVNDQEQL EVLRIVSAVL HIGNISFTEE
     NNFAAVSGKD CMRLDTNFNF FVTLKIPDLE FPAFLLGLTN ADIESKLTGR KMESKWGTQK
     EEIDMKLNVD QANYTRDAWV KAIYARLFDY LVKKVNDALN ITSQSSSDNF SIGILDIYGF
     EIFNNNGFEQ FCINFVNEKL QQIFIELTLK AEQEEYVREG IKWTEIDYFD NKIVCDLIEV
     KRPPGIMSLL DDTCAQNHGQ REGVDRQLLT TLSKSFAGHP HFGPGSDSFL IKHYAGDVTY
     NVDGFCDRNR DVLYPDLILL MQKSSNAFIR SLFPENVAAS AGKRPTTFST KIRTQANTLV
     ESLMKCSPHY VRCIKPNETK RPNDWEESRV KHQVEYLGLR ENIRVRRAGF AYRRAFDKFA
     QRYAIVSPQT WPSFQGDQQR ACEIICDSVH MEKSQYQMGR TKIFVKNPES LFLLEETRER
     KFDGFARVIQ KAWRQFAARK QHIKQKEQAA DLMYGKKERR RYSLNRNFVG DYIGLEHHPT
     LQSLVGKRQR ILFACTANKY DRKFRATKLD MLLTANHLFL IGKEKVKSGP EKGKIVEIIK
     RQLDLPQIKS IGLSPYQDDF VIIYMNGEEY TSLLETPFKT EFCTALLKAY KERKNSPLHL
     DFRDTHVVSY KKMKFDFSDG KRTVQFGCDG SSSAEKTLKP NGKVLNVSIG TGLPNTTRPS
     TERPQGGYTP RRDQLRTSTR RTNKNTHGAQ PMRAPVPAHA MNNNYNQPPP HAAAPTPVST
     NHQYNQEPAR IPVMGNVISQ LNNMNLAASG NSNPAAGRGP PPARGPKPAP PAKPKLNPVV
     IAVYPYEAQD TDELCFEAGD EIELMNKDAS GWWQGKLNNR VGLFPGNYVK E
//
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