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Database: UniProt
Entry: S9W371_SCHCR
LinkDB: S9W371_SCHCR
Original site: S9W371_SCHCR 
ID   S9W371_SCHCR            Unreviewed;      2039 AA.
AC   S9W371;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Myosin type-2 heavy chain 2 {ECO:0000313|EMBL:EPY52395.1};
GN   ORFNames=SPOG_01721 {ECO:0000313|EMBL:EPY52395.1};
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:EPY52395.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY52395.1, 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; KE546989; EPY52395.1; -; Genomic_DNA.
DR   RefSeq; XP_013022279.1; XM_013166825.1.
DR   STRING; 653667.S9W371; -.
DR   EnsemblFungi; EPY52395; EPY52395; SPOG_01721.
DR   GeneID; 25036047; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   HOGENOM; CLU_000192_5_3_1; -.
DR   OMA; TTQTDEY; -.
DR   OrthoDB; 2728955at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0000931; C:gamma-tubulin ring complex; IEA:EnsemblFungi.
DR   GO; GO:0031097; C:medial cortex; IEA:EnsemblFungi.
DR   GO; GO:0120104; C:mitotic actomyosin contractile ring, proximal layer; IEA:EnsemblFungi.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR   GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; IEA:EnsemblFungi.
DR   GO; GO:1990274; P:mitotic actomyosin contractile ring disassembly; IEA:EnsemblFungi.
DR   GO; GO:0090561; P:nuclear migration during mitotic telophase; IEA:EnsemblFungi.
DR   CDD; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 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; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF706; MYOSIN-2; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   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|PROSITE-ProRule:PRU00782};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015464}.
FT   DOMAIN          35..87
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          91..770
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          649..671
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   COILED          893..927
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          956..1085
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1166..1252
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1559..1607
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1665..1837
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1866..2021
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         184..191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2039 AA;  236259 MW;  C49D8545B42AE9E5 CRC64;
     MSYFSRDDSS YAQRSIQNIV SGKTVENAAK KASFDERTWV WIPDPEEIYL KAWIEEKMNS
     NSRYRVRLEK DGSERIVDSK STGEVNPPKF DMVNDMAELT CLNEPSVIHN LIQRYERGLI
     YTYSGLFLVA VNPYRSLPIY GEDIIKKYHA KQLPEVKPHI FRVADIAYRN LLERDQDQSI
     LVTGESGAGK TETTKKVIQY LTAITGTSSN DSQLLENKIL DTNPVLEAFG NAQTVRNNNS
     SRFGKFIRIE FSKDGSIVGA NLDWYLLEKS RVTNPSPKER NYHIFYQLLR GSNSDLLREL
     FLERSIDKYA YLKNCAKVIS GVDDASEFRQ LCAGLTTLGF NSDDTKQLFT TIAAVLHLGN
     IEVASDRSGQ ARFPSLTHID QLCHLLGIPA EAFMNAVLHP KTKAGREWIV NARTKEQVLH
     TLQSLAKSLY ERNFAFLVDK LNRTMYQTQS ENNSFIGVLD IAGFEIFAHN SFEQLCINYT
     NEKLQQFFNH YMFVLEQEEY FQEKIEWNFV DYGNDLQPTI EIIEKSEPIG ILSCLDEDCV
     MPMATDNTFT EKLHLLLKGK PDIYRPTRFS SEGFILRHYA GNVVYSTEGW LEKNKDPLNS
     NLANLISQSS SMHISSLFSD YSSENNFNSD HYEKKGIFRT VSQRHRRQLN NLMKQLEATQ
     PHFVRCIIPN STKKPKLIEK GLVLHQLRCN GVLEGIRIAQ TGFPNKLLYT EFRSRYGILS
     RTLEKGYVEA RKATMSIIKE LNLSESVYRL GETKVFFKAN VLGFLEDQRN AMLRDIFKAF
     SSTIRGFLVR RRLYRLNHRQ DAAILLQHNL RELLVLGKHP WWHLFLKLKP LLGTTQTDEY
     LRRKDVLINN LRTQLEKAEL VSVELEANRQ QISKISKDLS EEQAISKEKE ILVERANSRV
     EVINERLSDL EEQLRLSHNK YDLLYNEKKE TDDQLAICTS QINHLQELLL ALQEKLEFAV
     TAEKEMKNKY KELETTYINL QADYDHSAQL LNSQQNSLIE EQAKYDKLKE TMSKLEEDII
     SKDSLHEEEL DEYKSENSNL RNQCNTYESQ IANLVSDYSR TESELNKKEA EILMFQRELA
     DYRDQLANSL KKRASSDFLG EEEALSLDSQ ESALSSSSTT LSILKDVQDL KSLHSKEAVQ
     LSDRIKDVSQ LLEQSIAAED KLRLKNNELS DVVEALKYQL QEQDSEILEL NAVNTNLRKT
     NDILEKNATD FIDLQSVKTR YECKVSELFN QLHKERKRVE QLKTELESFG NNEKENHHFG
     FSKDNDLRKG PGKESLRMIT DLLSSAMSSS TFEKHHLVKL LNTLKQQISD FNLSPQQENL
     ISSNLEPLKS RSSLEGNMEP VLSPSKINNS DPSNFTKMLQ GSPSKRSGKM EALIRNFDQN
     SDSFLSQPNK EEGNPKSLNF RSEIMKLNFN LEEAKRNGVL DPSAVDNGVA AVMQSLLEEN
     QALKSLATAN VSIENSTDEQ EELLNKVPAQ LQGELRKQFD QLRTSKDTLS KLHNITEDKL
     HSADLALKET TKERDHLLRN FSLSSKPTFT INDETEELGY ESSDDFDEQK LEEVNLLRMR
     KLESALSKYR SRLTEYQLRN ENSESSIHKL ERAKEGLSSK LEEREAHINE LLDIRKKMET
     VLLESIAKQK EFESLFNERN NDLLELKQHK EKLMKQIDEF HIVRVQDLEE RERKDELLFQ
     RYQKELNGFK VQLEEEREKN LRIRQDNRHI HIEVGKLRTK VDELLLEKTG LVKENSRLQS
     EIQSVYKVRN NSSIAHRTAQ SQLLDLTSQL QEIRETNESL RSEQSNLQNE KRILEQKVQE
     LMTQLNTSKV SEYPPELADT EKEMIDLRAS MEQKDELLTS LVDRMKQMEF FASETQKDSN
     QHREENLNLH RQIGVLENEK KELELRLFDL DAKSYPMSSS KDVRMLQKQI AELETSIADS
     DNERLKGLDE CRLRDRAIRH LETRLQKFDE EKQNLTSSIS RLEERNNLLY SQLEDTKASE
     TQSKLALRRA EHEVQEEREN LRNLERDLEK YRLILEGQRA RRLDSRMSVR SSTKSPTLH
//
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