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
//