ID   MYO2_LACK1              Reviewed;        1554 AA.
AC   Q875Q8;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 76.
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   Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 /
OS   JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=226302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543
RC   / NRRL Y-12651;
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; AY145011; AAO32574.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q875Q8; -.
DR   SMR; Q875Q8; -.
DR   PRIDE; Q875Q8; -.
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; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51126; DILUTE; 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; ATP-binding; Cell cycle; Coiled coil; Motor protein; Myosin;
KW   Nucleotide-binding; Protein transport; Repeat; Transport.
FT   CHAIN           1..1554
FT                   /note="Myosin-2"
FT                   /id="PRO_0000123488"
FT   DOMAIN          4..57
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT   DOMAIN          70..774
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          778..798
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          800..824
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          825..847
FT                   /note="IQ 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          848..872
FT                   /note="IQ 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          873..895
FT                   /note="IQ 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          896..925
FT                   /note="IQ 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1205..1480
FT                   /note="Dilute"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT   REGION          443..523
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1080..1554
FT                   /note="Non alpha-helical, tail domain"
FT   REGION          1082..1109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          926..1079
FT                   /evidence="ECO:0000255"
FT   BINDING         164..171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1554 AA;  178198 MW;  412A25F7A4C3A8FD CRC64;
     MSYEVGTRCW YPDKQQGWIG GEITKHTNLS NKHQLELTLE DNQIVEIESE TLDETKDDRL
     PLLRNPPILE ATEDLTSLSY LNEPAVLHAI KARYAQLNIY TYSGIVLIAT NPFDRVEQLY
     SQDMIQAYAG KRRGELEPHL FAIAEEAYRL MKNDKQNQTI VVSGESGAGK TVSAKYIMRY
     FASVEQNNEE NAHHNLEMSE TEKKILATNP IMEAFGNAKT TRNDNSSRFG KYLEILFDKE
     ISIIGARIRT YLLERSRLVF QPKSERNYHI FYQLLAGLTN EEKSQLKLTG VEDYHYMNQG
     GEAQIKGIDD AEEYQTTVEA LSLVGISKDT QYQLFKILAA LLHIGNVEIK KTRNDASLSS
     DEPNLAIACE LLGIDSFNFA KWITKKQINT RSEKIVSNLN YNQALVARDS VAKFIYSALF
     EWLVDNINTV LCNPEVASEI NSFIGVLDIY GFEHFEKNSF EQFCINYANE KLQQEFNQHV
     FKLEQEEYVK EEIEWSFIEF NDNQPCIDLI ENKLGILSLL DEESRLPAGS DETWTQKLYQ
     TLDKPPTNTV FSKPRFGQTK FVVSHYALDV SYDVEGFIEK NRDTVSDGHL EVLKASTNET
     LLSILETLDK HAAKLAEKEQ VNKKPGPARM VNRKPTLGSI FKQSLIELMG TINSTNVHYI
     RCIKPNEVKE AWVFDNLMVL SQLRACGVLE TIRISCAGFP SRWTYNEFVL RYHILIPSEH
     WSKMFSSDTT EEDIRDLCRT ILGAIVEDKQ KYQLGNTKIF FKAGMLAYLE KLRSDRLHNS
     SVLIQKKVKA VYYRKKYLAI ISSIRNFHSR SEGFLTRQRV DLEFKTQAAI LIQSMVRSTS
     TRNKTISLLS AITRLQSLVR KQLAQKELLQ RRQRDAAVSI QKKIRAFEPR QSFNTTRRST
     VVVQSLVRKK FAQKKLKDLK TEAKSVNHLK EVSYKLENKV IQLTESLAEK VKENKGMTAR
     IQELQQSLNE SANIKELLNS QKDEHSKVLQ QQKDAHDVQF NEVQEKLVNA KKEVEEAKEE
     IEQLIAKQDE LKAEVRTKIE ELNKAKKTFT EFQTQNSDLK NEVKSLKDEI ARLQAAVRSG
     VTSSTITSTP TASRRFSAHS SVADGTSPRQ LNVISMNNGG IEDDARSTAS ALSQINDELY
     KLLEDTKSLN TEIVEGLLKG FKIPETGVAV ELTRKEVLYP ARILIIVLSD MWRLGLTKQS
     ESFLAEVLST IQKLVTNLKG DDMILHGAFW LTNVRELYSF VVFAQESILN DDSYNNGLNE
     DEYKEYVTLV TELKDDFESL SYNIYNIWLK KLQKDLERKA ISAVVMSQSL PGFIAPESSP
     FLPKLFSQSS HYKMDDILTF FNNIYWSMKT YHVETEVFRE VIMTLLKYVD AICFNDLIMR
     RNFLSWKRGL QLNYNVTRLE EWCKSHQLPE GTECLQHMLQ ASKLLQLKKA NLEDINIIWE
     ICSSLKPAQI QKLISQYAVA DYEVPIPQEI LNFVADRVKK ESSLSSDGKS QTHSSDIFLS
     VDSGPFEDPF GQIETREFGK IEAYIPAWLN LPITRRVVEL VTQHVTVQES QRTE