MYO51_SCHPO
ID MYO51_SCHPO Reviewed; 1471 AA.
AC O74805;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Myosin-51;
DE AltName: Full=Myosin type V-1;
GN Name=myo51; ORFNames=SPBC2D10.14c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11112691; DOI=10.1242/jcs.114.1.69;
RA Win T.Z., Gachet Y., Mulvihill D.P., May K.M., Hyams J.S.;
RT "Two type V myosins with non-overlapping functions in the fission yeast
RT Schizosaccharomyces pombe: Myo52 is concerned with growth polarity and
RT cytokinesis, Myo51 is a component of the cytokinetic actin ring.";
RL J. Cell Sci. 114:69-79(2001).
CC -!- FUNCTION: Involved in cytokinesis. {ECO:0000269|PubMed:11112691}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11112691}.
CC Note=Component of the cytokinetic actin ring (CAR).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21172.1; -; Genomic_DNA.
DR PIR; T40117; T40117.
DR RefSeq; NP_596233.1; NM_001022153.2.
DR AlphaFoldDB; O74805; -.
DR SMR; O74805; -.
DR BioGRID; 277087; 40.
DR STRING; 4896.SPBC2D10.14c.1; -.
DR MaxQB; O74805; -.
DR PaxDb; O74805; -.
DR PRIDE; O74805; -.
DR EnsemblFungi; SPBC2D10.14c.1; SPBC2D10.14c.1:pep; SPBC2D10.14c.
DR GeneID; 2540560; -.
DR KEGG; spo:SPBC2D10.14c; -.
DR PomBase; SPBC2D10.14c; myo51.
DR VEuPathDB; FungiDB:SPBC2D10.14c; -.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_9_0_1; -.
DR InParanoid; O74805; -.
DR OMA; RDIRMHL; -.
DR PhylomeDB; O74805; -.
DR Reactome; R-SPO-9013419; RHOT2 GTPase cycle.
DR Reactome; R-SPO-9013425; RHOT1 GTPase cycle.
DR PRO; PR:O74805; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:1990819; C:actin fusion focus; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0070648; C:formin-nucleated actin cable; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0120104; C:mitotic actomyosin contractile ring, proximal layer; IDA:PomBase.
DR GO; GO:0016459; C:myosin complex; ISM:PomBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IDA:PomBase.
DR GO; GO:1903478; P:actin filament bundle convergence involved in mitotic contractile ring assembly; IMP:PomBase.
DR GO; GO:0061572; P:actin filament bundle organization; IMP:PomBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; IMP:PomBase.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:1904601; P:protein localization to actin fusion focus; EXP:PomBase.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
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; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 3: Inferred from homology;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Motor protein; Myosin; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1471
FT /note="Myosin-51"
FT /id="PRO_0000123482"
FT DOMAIN 7..61
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 65..749
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 753..773
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 776..796
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 801..821
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 824..844
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 849..869
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 872..892
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1171..1417
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 628..650
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT COILED 909..952
FT /evidence="ECO:0000255"
FT BINDING 159..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1471 AA; 167657 MW; C4079A033DE232ED CRC64;
MSHARLSVGS ECWVSNNNGH WDAARLIEIK DNGGGKVVAT VAKSSGVLET VNYQQLQNRN
IGQSESPSDL TNLPYLNEPS VLHALHNRYN NKQIYTYSGI VLVSINPYQN LPEFYNDNLI
KHFHKDPEAA KVPHLYSIAS SCYHALTTDS KNQTIIVSGE SGAGKTVAAK YIMRYLTSVQ
GVDHNGVVKR SVENQVLATN PIMEAFGNAK TIRNDNSSRF GKYVTISFDE NLLITGANVN
TYLLERSRVV SLLKGERNYH IFYQLITGCT EEQRDKWFLE SASSFNYLSQ GNCDEISGVD
DSNDFTITCR ALSTIGISES RQEDVFCLLA ALLHLGNIEV CATRNEAQIQ PGDGYLQKAA
LLLGVDSSTL AKWIVKRQLK TRSETIITSS TLEHAISIRD SVAKYLYSAL FLWIVHMINA
SLDHNKVKRA AYKYIGVVDI YGFEHFEKNS MEQFCINYAN EKLQQEFNKH VFKLEQEEYV
KEGLDWRLIE YSDNQGCISL IEDKLGILSL LDEECRLPSG NHQSFLQKLN NQLPTKHSQF
YKKSRFNDGS FMVKHYALDV SYQVHDFLAK NSDAIPDEFI SLLQNSKNEF ITYLLDFYMQ
LVSSQNKNPR KTAISRKPTL SSMFKSSLSQ LMTTVSSTNV HYIRCIKPNE EKLPWTFSPP
MVLSQLRACG VFETIRISSL GFPARFSYEE FAHRFRILLS SKEWEEDNKK LTLNIVNSVI
PHDNLNFQVG RSKIFFRSNV IGNFEEAHRA TCSKSTVLLQ SAIRGFFTRK EYQRTVKFII
KLQSVIMGWL TRQRFEREKI ERAAILIQAH WRSYIQRKRY LSLIKCAIVI QSIVRKNIAY
SRYINELRES SATLLAKFWR AYNARKTFRG LKKSVIALQC VSRSVLTRRY LRRLQDSAGR
TSILYEKQKN LQASITEVSK QLKSNSKKVT VLRNKLNILN NSLSKWKCLI KKPSDFSEPV
SMDFTSNDEQ LVQLLQAESK LRQASQQLYM AAKKSELGFV QSQTARENLS NYYQALQMTV
SEKFEYDTEQ LPSRVLFYAM DRYFSIHKKL KQLLELVGVE NASLLPNEVV NKQTKDLLYE
KRVVFLKQIK QALTVSSLFN AVGYKDGVMR LLETDQNSLL FAGVVNFLIF AGISLDLKTQ
ISEFLSQLCS YFTKIVDGTV IENDKTLDFY EKPLQAVLYW FATLHKIRSF LVHLLSINSH
GKQSVVEDLW NPLILKFSKH FSNLENSFHS LVQKLLSCCT EGSINALLNS KCLPEFIDAA
DENTTPTGMN IYELIDRMNL IHKLLISSAL QPNLLELTIS HMLQHIGQRA FQTLIHGRSP
YTWKSASQVS YNASLLINWC HQKGISYVNS SLLPLMQSPL VFCLRKNDAN DLDVILSVCN
LLSPFEVVCL LNRYQPCAGE NPLPKSFSKA VEALSCKYKQ SGFTNGKITN TNGHAIPIAA
SKNPLLSLEN NHIYEELRLS ELINLLAKAT L
