MYO1_MALGO
ID MYO1_MALGO Reviewed; 1322 AA.
AC A8PWF6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; ORFNames=MGL_1086;
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966;
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L. Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC -!- FUNCTION: Type-I myosin implicated in the organization of the actin
CC cytoskeleton. Required for proper actin cytoskeleton polarization. At
CC the cell cortex, assembles in patch-like structures together with
CC proteins from the actin-polymerizing machinery and promotes actin
CC assembly. Functions as actin nucleation-promoting factor (NPF) for the
CC Arp2/3 complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250}.
CC -!- DOMAIN: The myosin motor domain displays actin-stimulated ATPase
CC activity and generates a mechanochemical force. {ECO:0000250}.
CC -!- DOMAIN: The tail domain participates in molecular interactions that
CC specify the role of the motor domain (By similarity). It is composed of
CC several tail homology (TH) domains, namely a putative phospholipid-
CC binding myosin tail domain (also named TH1), an Ala- and Pro-rich
CC domain (TH2), followed by an SH3 domain and a C-terminal acidic domain
CC (TH3). {ECO:0000250}.
CC -!- PTM: Phosphorylation of the TEDS site (Ser-369) is required for the
CC polarization of the actin cytoskeleton. Phosphorylation probably
CC activates the myosin-I ATPase activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP44604.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAYY01000003; EDP44604.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001731818.1; XM_001731766.1.
DR AlphaFoldDB; A8PWF6; -.
DR SMR; A8PWF6; -.
DR STRING; 425265.A8PWF6; -.
DR EnsemblFungi; EDP44604; EDP44604; MGL_1086.
DR GeneID; 5856123; -.
DR KEGG; mgl:MGL_1086; -.
DR InParanoid; A8PWF6; -.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000008837; 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-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11858; SH3_Myosin-I_fungi; 1.
DR Gene3D; 3.40.850.10; -; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 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; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1322
FT /note="Myosin-1"
FT /id="PRO_0000338556"
FT DOMAIN 42..728
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 732..752
FT /note="IQ 1"
FT DOMAIN 753..778
FT /note="IQ 2"
FT DOMAIN 786..980
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1184..1243
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 417..499
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 966..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1322 AA; 144430 MW; AB9D9C35DEE6DBC0 CRC64;
MVISKRAGGR RAAGGAAAQA APPVNRGIAK ADWREGFKKP QAGVSDMTLL TQITNEAVND
NLHKRFSNAE IYTYIGNVLI SVNPFRDLGI YTDEILRSYR GKNRLEMPPH VYAIAEGAYY
NMLAYKENQC VIISGESGAG KTEAAKRIMQ YIAAVSGDTT GTGSTSSGIH TIKDMVLATN
PLLESFGCAK TLRNNNSSRH GKYLEIMFDA NGSPVGATIT NYLLEKARVV GQIRNERNFH
IFYQLTKAAS PQQRELFGLQ GPEAYAYTAD SQCLDVPGID DHADFAAAFE AMRIIGLTDD
EQMSMVRMLA TILWLGNVHF VENAQGDAEL ANPDVTAFCA YLLEVDPSAV QRALTQRIME
TQRGGRRGSV YEVPLNPTQA AAVRDALSKA IYNNLFDWIV ARINRSLQAQ SQTAASVIGV
LDIYGFEIFE NNSFEQLCIN YVNEKLQQIF IELTLKKEQE EYAQEQIQWT PIQYFNNKIV
CDLIEAKRPP GIFSALNDAV ATAHADSSAA DNSFMQRTSM LSSNPHFEAR GSKFLVRHYA
GDVMYNVQGM TEKNKDALLK DILNLVDSSS NAFLIGLFPE RPDPNSKKRP PSAGDRIKAS
ANALVDNLMQ AQPSYIRTIK PNQNKSPTEY DTQAVLHQIK YLGLRENIRV RRAGFAYRNT
FEKIVQRFYL LSRATSYAGD YIWQGDARSG CERIFLDTGI ARDEWQLGVT KGFIKNPETL
FALETMRDRY WHNMAMRIQR AWRAFMRRRE ESARRIQRAW RRSREGHEFL ELREYGHQLL
AGRKERRRFS LISMRRFMGD YLDLNGSSAE GRMLRASANL PPNEPIVFSA RAQLLVSRLG
RTSIPSPRFL LMSPRAVYIL VTHLVNKRPQ TTCERVIPLS TIRQVGLSTL RDDWIVLQVG
TDEGDPLLHC DFKTEFVAYL LQQTGGRTHV VIAPQLEYVR KGRKKAHVSF RKDESIPVGD
VYKSSIVSVG SGEPPTSVSR PPAKKLPRSA QPSTKRRTTS RPVTSRRPVP TVLPTTTASR
GLPPAPGGTA SASALAVPTT STVAPASSAS GNASGARHVP APPPVSGGSG LPPYLQAPAT
SAPSSGMPSY LQRAVPAAPT APAAPAASAA PTAAQSTSGI PSYLGSSTTK LAPPVTVQQL
GSSSTAQTRS VPAPPSASAT PAVATPALAP VKAAPLPPPP PTGRRLPRYR ALYDFETQEA
GELPLRTGDI VELEEKEENG WWLVKKGSTE GWSPADYLEL IAEPAAAKPR PPPPAKPASA
KPAAAPARVS QSSVTSSWTP PDSHAAPVAV MPGMGDPGGF AAILARKKAE RAAAAEQAHV
PE
