MYO2_SACU7
ID MYO2_SACU7 Reviewed; 1568 AA.
AC Q876G9; Q876G8;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Myosin-2;
DE AltName: Full=Class V unconventional myosin MYO2;
DE AltName: Full=Type V myosin heavy chain MYO2;
DE Short=Myosin V MYO2;
GN Name=MYO2;
OS Saccharomyces uvarum (strain ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550
OS / MCYC 623 / NCYC 2669 / NRRL Y-11845) (Yeast) (Saccharomyces bayanus var.
OS uvarum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=659244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550 / MCYC 623 / NCYC 2669
RC / NRRL Y-11845;
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-271 AND 348-1046.
RC STRAIN=623-6C / CBS 9787 / CLIB 533;
RX PubMed=12594514; DOI=10.1038/nature01419;
RA Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT "Yeast genome duplication was followed by asynchronous differentiation of
RT duplicated genes.";
RL Nature 421:848-852(2003).
CC -!- FUNCTION: Myosin heavy chain that is required for the cell cycle-
CC regulated transport of various organelles and proteins for their
CC segregation. Functions by binding with its tail domain to receptor
CC proteins on organelles and exerting force with its N-terminal motor
CC domain against actin filaments, thereby transporting its cargo along
CC polarized actin cables (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with calmodulin (CMD1) and the myosin
CC light chain MLC1 through its IQ repeats (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AACA01000061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY144842; AAO32406.1; -; Genomic_DNA.
DR EMBL; AY144843; AAO32407.1; -; Genomic_DNA.
DR AlphaFoldDB; Q876G9; -.
DR SMR; Q876G9; -.
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-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 3.40.850.10; -; 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 Pfam; PF01843; DIL; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 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; ATP-binding; Cell cycle; Coiled coil; Motor protein; Myosin;
KW Nucleotide-binding; Protein transport; Repeat; Transport.
FT CHAIN 1..1568
FT /note="Myosin-2"
FT /id="PRO_0000123485"
FT DOMAIN 4..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 70..783
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 786..808
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 809..833
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 834..856
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 857..881
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 882..904
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 905..934
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1223..1498
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 443..523
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 619..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1568
FT /note="Non alpha-helical, tail domain"
FT COILED 944..1088
FT /evidence="ECO:0000255"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 350..353
FT /note="KKTR -> LTTT (in Ref. 2; AAO32407)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="S -> R (in Ref. 2; AAO32407)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="G -> C (in Ref. 2; AAO32407)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="S -> P (in Ref. 2; AAO32407)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="K -> N (in Ref. 2; AAO32407)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1568 AA; 179917 MW; E68F503416DA2D8C CRC64;
MSFEVGTRCW YPHKELGWIG AEVIKNEVKD GKYHLELSLE DDEVVSVDTE DLNDDKNQSL
PLLRNPPILE ATEDLTSLSY LNEPAVLHAI KQRYSQLNIY TYSGIVLIAT NPFDRVDQLY
TQDMIQAYAG KRRGELEPHL FAIAEEAYRL MKNDKQNQTI VVSGESGAGK TVSAKYIMRY
FASVEEENST TIQHQVEMSE TEQRILATNP IMEAFGNAKT TRNDNSSRFG KYLEILFDKE
TSIIGARIRT YLLERSRLVY QPPIERNYHI FYQLMAGLPA QTKEELHLTD ASDYFYMNQG
GDTKIAGIDD AEEYQTTVDA LTLVGITTAT QHQIFKILAA LLHIGNIEIK KTRNDASLSA
DEPSLKLACE LLGIDSYNFA KWITKKQIVT RSEKIVSNLN FNQAMVAKDS VAKFIYSALF
DWLVENINTV LCNPDVDDQI NSFIGVLDIY GFEHFEKNSF EQFCINYANE KLQQEFNQHV
FKLEQEEYVA EEIEWSFIEF NDNQPCIDLI ENKLGILSLL DEESRLPAGS DESWTQKLYQ
TLDKSPTNEV FSKPRFGQTK FIVSHYALDV AYDVEGFIEK NRDTVSDGHL EVLKASTNET
LINILEGLEN AAKKLEETKK AELEQNNPGN KKPGPARTVN RKPTLGSMFK QSLIELMSTI
NSTNVHYIRC IKPNADKEAW QFDNLMVLSQ LRACGVLETI RISCAGFPSR WTFEEFVLRY
YILIPHEEWD LIFQKKETTE DDIISVVKMI LDATVKDKTK YQIGNTKIFF KAGMLAYLEK
LRSNKMHNSI VTIQKKIRAK YYRNQYLKIS QAIKIWQSNT RGFIIRHRVY HEMKVHSATL
IQATYRGYAI RKNVFNVLIT IINLQTRIRE ELKRKQLKRE HEYNAAVTIQ SKVRTFEPRS
TFLNTKRDTV VVQSLIRRRA AQGRLRQLKS DAKSVHHLKE VSYKLENKVI ELTQNLASKV
KENKEMTERI KELQVQVEES AKLQETLENM KKEHLVNIDN QKNKDMELQK TIEDNLQSTE
QNLKNAQLEL EEMVKQHNEL KEESRKQLDE LDETKKALVE HQTLNGDLQN EVKSLKEEIS
RLQTAMSLGT VTTSVLPQTP LKDVMGGSTA NYNSLMLDNA ELSPGKSRTT PMSGNHIDSL
NIDQDNGANA TQINEELYRL LEDTEILNQE ITEGLLKGFE VPDAGVAIQL SKRDVVYPAR
ILIIVLSEMW RFGLTKQSES FLAQVLTTIQ KVVTQLKGND LIPSGVFWLA NVRELYSFVV
FALNSILTEE TFKNGMTDEE YKEYVSLVTE LKDDFEALSY NIYNIWLKKL QKQLQKKAIN
AVVISESLPG FSAGETSGFL NKIFANTEEY TMDDILTFFN SIYWCMKSFH IETEVFHAVV
TTLLNYVDAI CFNELIMKRN FLSWKRGLQL NYNVTRLEEW CKTHGLTGGT ECLQHLIQTA
KLLQVRKYTI EDIDILRGIC YSLTPAQLQK LISQYQVADY ESPIPQEILR YVADIVKKEA
ALSNDSKGHE HSSGIFITPE TGPFTDPFSL IKTRKFDQVE AYIPAWLSLP ATKRIVDLVA
QQVVQDGH
