ID C1G766_PARBD Unreviewed; 1632 AA.
AC C1G766;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Myosin-1 {ECO:0000256|ARBA:ARBA00016187};
DE AltName: Full=Class I unconventional myosin {ECO:0000256|ARBA:ARBA00032645};
DE AltName: Full=Type I myosin {ECO:0000256|ARBA:ARBA00029665};
GN ORFNames=PADG_03021 {ECO:0000313|EMBL:EEH46923.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH46923.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH46923.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH46923.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000256|ARBA:ARBA00004134}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; KN275959; EEH46923.2; -; Genomic_DNA.
DR RefSeq; XP_010758239.1; XM_010759937.1.
DR STRING; 502780.C1G766; -.
DR GeneID; 22582395; -.
DR KEGG; pbn:PADG_03021; -.
DR VEuPathDB; FungiDB:PADG_03021; -.
DR eggNOG; KOG0162; Eukaryota.
DR eggNOG; KOG3335; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; C1G766; -.
DR OMA; KPMPTPG; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
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-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11858; SH3_Myosin-I_fungi; 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; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035535; Fungal_myosin-I_SH3.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR010754; OPA3-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF837; MYOSIN-3-RELATED; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF07047; OPA3; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 419..1098
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1156..1346
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1449..1510
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 211..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..993
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1336..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1514..1632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 266..307
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 363..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1448
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1528
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1584..1609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 512..519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1632 AA; 181051 MW; 5DF6F90B0951582C CRC64;
MLLYSDTTTR SFSEHRSSNS PLGLIDGMEL KGIDDGLVFS KWNIRLYSEP SPRANQRTAL
AWAAGTSNLT RNIFRVSYPQ LQPKVQPSTV QRRIGKAPSP RRIELQHPVR QEMSITLKLS
SLVIRTLSKP IANQIKAQAR EHERFRRVCV SFAQAIHRVD MRMRLGLLQS SAALDKQAAR
ETAQSQAKKH KPQVATVKTE AQIKLEESLA AKEKEKAQEP PKPPPPLRIR PLSEAKAIDS
GATFISETFL FIVAGSLIVF EALRSRRKET SRREDVADRL AELEESEQAA RRGLVALERE
VLQLKAKLEK QSPKNMQRIL PKDVWNVEEA EAETEELGWK SRLVHYFRIS KLEEINDIHA
RGSKKPVASD DFSAGHSRRP RDTEKKGRGF GRSRHAEGGA VGKPQVKKAV FESTKKKEVG
VSDLTLLSKV SNEAINENLK KRFEHGEIYT YIGHVLVSVN PFRDLGIYTD QVLDSYRGKN
RLEVPPHVFA VAESAYYNMN AYKENQCVII SGESGAGKTE AAKRLMQYIA NVSGGSDSSI
QHTKDMVLAT NPLLESFGNA KTLRNNNSSR FGKYLELQFN SVGEPVGATI TNYLLEKSRV
VGQITNERNF HIFYQFTKAA PQAYRDNFGI QQPQSYVYTS RSKCFDVSGI DDAMDFKDTL
EAMRIIGLSQ AEQDNIFRIL SAILWLGNMQ FVEDDSSNAS ITDQSVVDFV AYLLEVDSAQ
VSKALTLRIL ETARGGRRGS VYEVPLNTVQ ATAVRDALAK ALYFNLFDWI VERVNASLAA
RGSVANSIGI LDIYGFEIFD KNSFEQLCIN YVNEKLQQIF IQLTLKTEQE EYAREQIKWT
PITYFDNKVV CSLIEDKRPP GIFAALNDAC ATAHADSGAA DQTFVGRLNF LSQNPNFESR
QGQFIVKHYA GDVGYTVKGM TDKNKDQLLK DLLNLVGSSS NSFVHTLFPD QVNQDDKRRP
PTAGDKIKAS ANDLVATLMK AQPSYIRTIK PNDNKSPSEY NVGNVMHQIK YLGLQENVRI
RRAGFAYRQT FDKFVERFYL LSPKTSYAGD YTWTGDAESG ARQILKDTSI PAEEYQMGTT
KAFIKTPETI FALEHMRDRY WHNMAIRIQR AWRNYLRYRI ECAIRIQRFW RRVTGGLEYI
KLRDQGHKIL GGMKERRRYS LVGSRRFLGD YLGVGNTGGP GEMIRDSVRI GKSETVLFSC
RCELLVTKFG RSSKPAPRIL ILTSHNVYIV VQSVVNHQLN ISAERTISVG AIKFVSASKL
KDDWFALGVG AAQEPDPLIN CVFKTEFFTY LSNALHGQLN LKLADVIEYN KKPGKLAIVK
TMKDPAIARD DIYKSGTIHT SQGEPPNSVS RPTPRPKQVA GKPITKGKLL RPGGPGGGPS
KLASRPAASR PTPAAQPLPH AIAQPATTTS RPVPQPVATV SASHNRTNSA QARAPPPPPP
PPPAAPPAAK KDTAKVLYDF NSERTNELSI RVGEIVQIMA KEGNGWWLCM NTTTSAQGWA
PEAYLEEIVA PTPAAAPPLP PPPPSAPRAA TISNSNNNNN NPVNPITTNG ASRAAAKAKP
TPPAPPAKRP VAGRKPAAPA TPRDSAVSMN SQDSPGGSGR ATPNSMNNFA GGLAEALRQR
QSAMKPQDDD DW
//
