UniProt: B9SID8

Database: UniProt
Entry: B9SID8_RICCO

LinkDB:  B9SID8_RICCO 
Original site:  B9SID8_RICCO

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Ontology (10)   
   GO (10)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (3)   
   RefSeq(pep) (3)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (3)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (30)   

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ID   B9SID8_RICCO            Unreviewed;      1223 AA.
AC   B9SID8;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Myosin vIII, putative {ECO:0000313|EMBL:EEF36593.1};
GN   ORFNames=RCOM_1254430 {ECO:0000313|EMBL:EEF36593.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
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; EQ973972; EEF36593.1; -; Genomic_DNA.
DR   RefSeq; XP_002525757.1; XM_002525711.2.
DR   RefSeq; XP_015578849.1; XM_015723363.1.
DR   RefSeq; XP_015578850.1; XM_015723364.1.
DR   AlphaFoldDB; B9SID8; -.
DR   STRING; 3988.B9SID8; -.
DR   GeneID; 8282424; -.
DR   KEGG; rcu:8282424; -.
DR   eggNOG; KOG0160; Eukaryota.
DR   InParanoid; B9SID8; -.
DR   OrthoDB; 5489458at2759; -.
DR   Proteomes; UP000008311; 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:0016459; C:myosin complex; IEA:UniProtKB-KW.
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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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; cd01383; MYSc_Myo8; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.20.240.20; -; 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; 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; IPR036022; MYSc_Myo8.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 3.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 3.
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}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, 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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000008311}.
FT   DOMAIN          150..199
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          203..873
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..775
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1069..1112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1000..1048
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1086..1111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         294..301
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1223 AA;  138694 MW;  CB9AE7399846E16A CRC64;
     MMLSESPAST VTRSSLEEML DSIRRRDEAM EKSKDLPPAL PARPTSRARL PSARKSLPTD
     FKVGANGQLE SKVETVVEVD KRKDDTKRKE KELGHKTGSF GSKKMRKDQN CVDSNPYAEE
     KNEAVRGPVI ASMSKAEEPD WDDNIGYFIK KKLRIWCQLA NGQWGSGKIQ STSGDEAVVS
     LSAGNFVKVS TADLLPANPD ILEGVDDLIK LSYLNEPSVL YNLKHRYSQD MIYSKAGPVL
     IAFNPFKVVP LYGNEIIGAY KQKLVDSPHV YAIADTAYNE MMRDGKNQSL IISGESGAGK
     TETAKYAMQY LAALGGGSGG IETEILQTNC VLEAFGNAKT YRNGNSSRFG KLIEIHFSSL
     GKICGAKIQT FLLEKSRVVQ LANGERSYHI FYQLCAGAPS ILRERLNLKM ASEYNYLNQS
     EGLVIDGVDD ALKFEKLMEA LEIVQISKAD QEQAFSMLAA ILWLGNISFQ VIDNENHVEV
     LADEALTNAA RLMGCSFHEL MLALSTHRIR FGKDDIVKKL TFRQAIDRRD ALAKFIYASL
     FDWLVEQINK SLEVGKLRTG RSINILDIYG FESFKNNSFE QFCINYANER LQQHFNRHLF
     KLEQEEYDED GIDWTKVDFD DNQDCLNLFE KKPLGLLSLL DEESNFPNAT DLTFANKLKQ
     HLGGNPCFKA ERGRAFVVRH YAGEVVYDTN GFLEKNRDPL HSDLFQLLSS CSCRLAQLFV
     SKMSNQFVSS SFNQSYGLES SKQSVGTKFK GQLFKLMHQL ENTTPHFIRC LKPNSKQLPG
     EHEDDLVLQQ LRCCGVLEVV RISRSGYPTR ITHQDFAQRY GFLLSNTSVS QDPLSISVAV
     LQQFNILPEM YQVGYTKVYL RTGSIAKLEE SRKQVLQGIL GVQKYFRGSQ VRRDLNELKR
     GVTIIQSFVR GENARRNYNS IANRCAFRNE GPPTMVDKKL MAVIFLQSAI RGWLARKQFS
     DKRKLKELHE NINSRRKHVK KISEVKVLPQ EQVDIQAMIL TELHRRVAKA EVALLQKEDE
     NASLREQLQQ FERRWSEYET KMKTMEQTWQ MQMESLQASL AAARKSLAAD STAGQHGKLE
     SFSSPHYYDS EDNMSTGVQT PGSNTPNKSS IAIPDVKLGR ETNGSINAVS ILAKEFEQQR
     QNFDDHAKAL AEVKLGQQSA SDKNPDEELR KLKIRFEDWK KDYKVRLRET KVRLHKVGRG
     EGDRRTRRWW GKIGPRGFQR SHF
//

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