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 16-SEP-2015, entry version 55. 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 / CCRC 21498 / NBRC OS 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces OS kluyveri). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea. OX NCBI_TaxID=226302; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 58438 / CBS 3082 / CCRC 21498 / NBRC 1685 / JCM 7257 / RC NCYC 543 / 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 RT of 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 CC motor domain against actin filaments, thereby transporting its CC cargo along polarized actin cables (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer. Interacts with calmodulin (CMD1) and the CC myosin light chain MLC1 through its IQ repeats (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Myosin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 dilute domain. {ECO:0000255|PROSITE- CC ProRule:PRU00503}. CC -!- SIMILARITY: Contains 6 IQ domains. {ECO:0000255|PROSITE- CC ProRule:PRU00116}. CC -!- SIMILARITY: Contains 1 myosin motor domain. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY145011; AAO32574.1; -; Genomic_DNA. DR ProteinModelPortal; Q875Q8; -. DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003774; F:motor activity; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002710; Dilute_dom. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR001609; Myosin_head_motor_dom. DR InterPro; IPR008989; Myosin_S1_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01843; DIL; 1. DR Pfam; PF00063; Myosin_head; 1. DR PRINTS; PR00193; MYOSINHEAVY. DR SMART; SM00015; IQ; 5. DR SMART; SM00242; MYSc; 1. DR SUPFAM; SSF50084; SSF50084; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS51126; DILUTE; 1. DR PROSITE; PS50096; IQ; 3. DR PROSITE; PS51456; MYOSIN_MOTOR; 1. PE 3: Inferred from homology; KW Actin-binding; ATP-binding; Cell cycle; Coiled coil; Motor protein; KW Myosin; Nucleotide-binding; Protein transport; Repeat; Transport. FT CHAIN 1 1554 Myosin-2. FT /FTId=PRO_0000123488. FT DOMAIN 70 774 Myosin motor. FT DOMAIN 778 798 IQ 1. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 800 824 IQ 2. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 825 847 IQ 3. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 848 872 IQ 4. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 873 895 IQ 5. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 896 925 IQ 6. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT DOMAIN 1205 1480 Dilute. {ECO:0000255|PROSITE- FT ProRule:PRU00503}. FT NP_BIND 164 171 ATP. {ECO:0000255}. FT REGION 443 523 Actin-binding. {ECO:0000250}. FT REGION 1080 1554 Non alpha-helical, tail domain. FT COILED 926 1079 {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 //