ID S9VY50_SCHCR Unreviewed; 1524 AA.
AC S9VY50;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Myosin type V {ECO:0000313|EMBL:EPY51154.1};
GN ORFNames=SPOG_02331 {ECO:0000313|EMBL:EPY51154.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY51154.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY51154.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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; KE546991; EPY51154.1; -; Genomic_DNA.
DR RefSeq; XP_013023727.1; XM_013168273.1.
DR STRING; 653667.S9VY50; -.
DR EnsemblFungi; EPY51154; EPY51154; SPOG_02331.
DR GeneID; 25036655; -.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_9_0_1; -.
DR OMA; TSEFKKW; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:EnsemblFungi.
DR GO; GO:1902716; C:cell cortex of growing cell tip; IEA:EnsemblFungi.
DR GO; GO:0090726; C:cortical dynamic polarity patch; IEA:EnsemblFungi.
DR GO; GO:0097575; C:lateral cell cortex; IEA:EnsemblFungi.
DR GO; GO:1990819; C:mating projection actin fusion focus; IEA:EnsemblFungi.
DR GO; GO:0031097; C:medial cortex; IEA:EnsemblFungi.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProt.
DR GO; GO:0000146; F:microfilament motor activity; IEA:EnsemblFungi.
DR GO; GO:0061573; P:actin filament bundle retrograde transport; IEA:EnsemblFungi.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:EnsemblFungi.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; IEA:EnsemblFungi.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:EnsemblFungi.
DR GO; GO:1990896; P:protein localization to cell cortex of cell tip; IEA:EnsemblFungi.
DR GO; GO:1904601; P:protein transport to mating projection actin fusion focus; IEA:EnsemblFungi.
DR GO; GO:0030050; P:vesicle transport along actin filament; IEA:EnsemblFungi.
DR CDD; cd15474; Myo5p-like_CBD_fungal; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 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 InterPro; IPR002710; Dilute_dom.
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; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF841; MYOSIN-52; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51126; DILUTE; 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}; Coiled coil {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:UP000015464}.
FT DOMAIN 7..62
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 73..772
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1183..1435
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 626..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..675
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1069..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 938..965
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1000..1027
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 167..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1524 AA; 175249 MW; 8DFB6704097CAD80 CRC64;
MSSGIYYKGL QCWIPDNERQ WLSGTVKSCK SESNKATLIV EDEDGNEVTF HAKPEDLEEE
GKNGLPFLRS NLSDPDDLTN LAYLNEPSVL DALLTRYNQL QIYTYSGIVL IALNPFQSLP
KLYTPEVVRV YSEKSRDQLD PHLYAIAEDS FKCMNREKKN QTIIISGESG AGKTVSARYI
MRYFASVQTL SDPSSNGALN SDSVQLTAVE NEILATNPIM EAFGNSKTSR NDNSSRFGKY
IQIMFDKNSI IIGAKIQTYL LERSRLVFQP KSERNYHIFY QLLAGASPQQ LEEWRLSANV
DDYHYLRQGE SHTIDGVDDA KEFQETVNAL KTVAIGDDTC KSIFNLLAAL LHVGNIEIKG
SRNDSYIDSK SEHLLNASKL LGVDPSLLIK WLTKRKIKMA SEGIIKPLTD YQGFVVRDSV
SKFLYASLFD WLVATINTAL MDSAEKQNQT SESFIGVLDI YGFEHFEKNS FEQFCINYAN
EKLQQEFYKH VFKLEQDEYA NEGLNWSYID YQDNQQCISM IENRMGILSL LDEECRMPTN
SDENWVTKLN DAFDKPEFKN SYKKARFGND SFTVKHYALD VTYNAEGFIE KNKDTISDEL
IDLFSESSVP FIKDLVHFRL KQTASQDSSA SNNKRSKAKP KSNTLGSMFK NSLISLMGTI
NETNAHYIRC IKPNEQKEAW KFDNVMVTSQ LRACGVLETI KISCAGFPSR WTFGDFVSQY
YMLVPSSDRS SDPLAFSTAI LDKSIDSTKY QVGKSKIFFR SGVTPQLEAA KERALKHAAQ
LLYDAFATNY YRTRFLNLRK RVSYFQAMAH GFLRRRTTQA ELISKSISVI SLFWKTHIER
KKFLEAKASI LLLQRTVRGF LFRRNQLVDK MEQAVATIKS IWKTYRERQF FTKLKHFTIR
IQSLIRMKYA KRQLVELRIE SKKASHFKQV SYKLESKLFD VTKKLDNSEQ ENAKLKDRIF
KLESHLSNYA EATLSKEREL EQTHVLLSDH SQDQEFKSAI SEKEKELSDL KNSFNQFKDD
NQELIRMNTT LKSQLGKDAE VISAQATEIK EKNKIIAKLT KASQVLNSSF GSEQTRTSEE
KSKRDSSLME MRTQKELLIL LMNDGLKHDL DKLTEFAGKT YVWEKTVELL NSSEENESKP
HLFLAKALFI IISQMWKTNL SQESIALIER YCVHILEYIS QRTQIRREVR ADMGFWIANT
HTLLYLVRTK LYGLKRSSSL TLSFSESYDA IQTIFDMLDS HLSRIVSTWI DQINTALRPL
IVDGIIVSGN QIDKGEKRLI PRVFDKDVKS IEHILHILNE VHDSCQTYRV SLAIFASVVS
SLYRFIDVEA FNALMTKEKG SWKRGVNMSY NFSRLREWCT QRGVVEATLQ LEEISQASKF
LQTCMNKQKI LDNVSLLWIL NMQQLRKLLD KYVAETYESK VPKKVMDELS NMARAEGLDR
PETISYDKVI YELNDTFEEE PSLEQVTIPV ECNVTYIQRI IDLASAEESF DQALLTLHDN
SVETNRFENQ ENELRDIGNG IKAL
//
