ID G2WNJ0_YEASK Unreviewed; 1574 AA.
AC G2WNJ0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=K7_Myo2p {ECO:0000313|EMBL:GAA26633.1};
GN Name=K7_MYO2 {ECO:0000313|EMBL:GAA26633.1};
GN ORFNames=SYK7_067261 {ECO:0000313|EMBL:GAA26633.1};
OS Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=721032 {ECO:0000313|EMBL:GAA26633.1, ECO:0000313|Proteomes:UP000001608};
RN [1] {ECO:0000313|EMBL:GAA26633.1, ECO:0000313|Proteomes:UP000001608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyokai no. 7 / NBRC 101557 {ECO:0000313|Proteomes:UP000001608};
RX PubMed=21900213; DOI=10.1093/dnares/dsr029;
RA Akao T., Yashiro I., Hosoyama A., Kitagaki H., Horikawa H., Watanabe D.,
RA Akada R., Ando Y., Harashima S., Inoue T., Inoue Y., Kajiwara S.,
RA Kitamoto K., Kitamoto N., Kobayashi O., Kuhara S., Masubuchi T.,
RA Mizoguchi H., Nakao Y., Nakazato A., Namise M., Oba T., Ogata T., Ohta A.,
RA Sato M., Shibasaki S., Takatsume Y., Tanimoto S., Tsuboi H., Nishimura A.,
RA Yoda K., Ishikawa T., Iwashita K., Fujita N., Shimoi H.;
RT "Whole-genome sequencing of sake yeast Saccharomyces cerevisiae Kyokai no.
RT 7.";
RL DNA Res. 18:423-434(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; DG000051; GAA26633.1; -; Genomic_DNA.
DR HOGENOM; CLU_000192_3_1_1; -.
DR Proteomes; UP000001608; Chromosome XV.
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:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051641; P:cellular localization; IEA:UniProt.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd15480; fMyo2p_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 2.
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; IPR002710; Dilute_dom.
DR InterPro; IPR046943; Fungal_Myo2/2A_CBD.
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 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; PS50096; IQ; 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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 4..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 70..781
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1226..1501
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 651..673
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 598..625
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 916..1083
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1574 AA; 180707 MW; D76D41D1DF55A3A0 CRC64;
MSFEVGTRCW YPHKELGWIG AEVIKNEFND GKYHLELQLE DDEIVSVDTK DLNNDKDQSL
PLLRNPPILE ATEDLTSLSY LNEPAVLHAI KQRYSQLNIY TYSGIVLIAT NPFDRVDQLY
TQDMIQAYAG KRRGELEPHL FAIAEEAYRL MKNDKQNQTI VVSGESGAGK TVSAKYIMRY
FASVEEENSA TVQHQVEMSE TEQKILATNP IMEAFGNAKT TRNDNSSRFG KYLEILFDKD
TSIIGARIRT YLLERSRLVY QPPIERNYHI FYQLMAGLPA QTKEELHLTD ASDYFYMNQG
GDTKINGIDD AKEYKITVDA LTLVGITKET QHQIFKILAA LLHIGNIEIK KTRNDASLSA
DEPNLKLACE LLGIDAYNFA KWVTKKQIIT RSEKIVSNLN YNQALVAKDS VAKFIYSALF
DWLVENINTV LCNPAVNDQI SSFIGVLDIY GFEHFEKNSF EQFCINYANE KLQQEFNQHV
FKLEQEEYVK EEIEWSFIEF NDNQPCIDLI ENKLGILSLL DEESRLPAGS DESWTQKLYQ
TLDKSPTNKV FSKPRFGQTK FIVSHYALDV AYDVEGFIEK NRDTVSDGHL EVLKASTNET
LINILEGLEK AAKKLEEAKK LELEQAGSKK PGPIRTVNRK PTLGSMFKQS LIELMNTINS
TNVHYIRCIK PNADKEAWQF DNLMVLSQLR ACGVLETIRI SCAGFPSRWT FEEFVLRYYI
LIPHEQWDLI FKKKETTEED IISVVKMILD ATVKDKSKYQ IGNTKIFFKA GMLAYLEKLR
SNKMHNSIVM IQKKIRAKYY RKQYLQISQA IKYLQNNIKG FIIRQRVNDE MKVNCATLLQ
AAYRGHSIRA NVFSVLRTIT NLQKKIRKEL KQRQLKQEHE YNAAVTIQSK VRTFEPRSRF
LRTKKDTVVV QSLIRRRAAQ RKLKQLKADA KSVNHLKEVS YKLENKVIEL TQNLASKVKE
NKEMTERIKE LQVQVEESAK LQETLENMKK EHLIDIDNQK SKDMELQKTI ESNLQSTEQT
LKDAQLELED MVKQHDELKE ESKKQLEELE QTKKTLVEYQ TLNGDLQNEV KSLKEEIARL
QTAMSLGTVT TSVLPQTPLK DVMGGGASNF NNMMLENSDL SPNDLNLKSR STPLSGNNHI
DSLSVDRENG VNATQINEEL YRLLEDTEIL NQEITEGLLK GFEVPDAGVA IQLSKRDVVY
PARILIIVLS EMWRFGLTKQ SESFLAQVLT TIQKVVTQLK GNDLIPSGVF WLANVRELYS
FVVFALNSIL TEETFKNGMT DEEYKEYVSL VTELKDDFEA LSYNIYNIWL KKLQKQLQKK
AINAVVISES LPGFSAGETS GFLNKIFANT EEYTMDDILT FFNSIYWCMK SFHIENEVFH
AVVTTLLNYV DAICFNELIM KRNFLSWKRG LQLNYNVTRL EEWCKTHGLT DGTECLQHLI
QTAKLLQVRK YTIEDIDILR GICYSLTPAQ LQKLISQYQV ADYESPIPQE ILRYVADIVK
KEAALSSSGN DSKGHEHSSS IFITPETGPF TDPFSLIKTR KFDQVEAYIP AWLSLPSTKR
IVDLVAQQVV QDGH
//
