MYO1_BOTFB
ID MYO1_BOTFB Reviewed; 1222 AA.
AC A6SED8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=myoA; ORFNames=BC1G_10821;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN32293.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476921; EDN32293.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001550348.1; XM_001550298.1.
DR AlphaFoldDB; A6SED8; -.
DR SMR; A6SED8; -.
DR PRIDE; A6SED8; -.
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 Gene3D; 3.40.850.10; -; 1.
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 PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 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; Repeat; SH3 domain.
FT CHAIN 1..1222
FT /note="Myosin-1"
FT /id="PRO_0000338542"
FT DOMAIN 39..713
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 717..737
FT /note="IQ 1"
FT DOMAIN 738..763
FT /note="IQ 2"
FT DOMAIN 771..961
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1076..1153
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..485
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 945..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1020
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1077
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1136
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1222 AA; 135374 MW; 0C5A3835A86FF132 CRC64;
MGISRRPKGN NNASAAESAP SGKPNIQKAQ FDTTKKKEVG VSDLTLISKV SNEAINENLK
KRFDNREIYT YIGHVLVSVN PFRDLGIYTD AVLDSYKGKN RLEMPPHVFA VAESAYYNMN
GYKDNQCVII SGESGAGKTE AAKRIMQYIA NVSGGSNSSI QEIKDMVLAT NPLLESFGNA
KTLRNNNSSR FGKYLQLQFN AQGEPVGADI TNYLLEKTRV VTQIKDERNF HIFYQFTKGA
SQAYRENFGI QQPSQYLYTS KAGCFDVDGI DDLAEYQDTL NAMKIIGLSQ AEQDEIFRML
AAILWTGNIQ FREDEDGYAA VVDQSVVDFL AYLLDCDAGH VIQAITIRIL TPRNGEVIES
PANVPQALAT RDALAKAIYN NLFDWIVERV NKSLTARSAT SNSIGILDIY GFEIFEKNSF
EQLCINYVNE KLQQIFIQLT LKTEQEEYAR EQIQWTPIKY FDNKIVCDLI ESMRPPGIFS
AMKDATKTAH ADPAACDRTF MQAISGMSNP HLTPRQGNFI VKHYAGDVSY TVEGITDKNK
DQLLKGLLNL FGQSKNQFIH ELFPHQVDQD NRKQPPSAGD KIKASANDLV ATLMKATPSY
IRTIKPNENK SPTEYNEKNV LHQVKYLGLQ ENVRIRRAGF AYRQTFDKFV ERFYLLSPKT
SYAGDYIWTG DSKTGAMQIL KDTNIPVEEY QMGVTKAFIK APETLFALEH MRDRYWHNMA
ARIQRVWRAF LQIRIEAATR IQRMFRKKRE GKEFLELREK GHQVLQGRKE RRRYSLLGSR
RFMGDYLGIA ATTGPGSKIR GSINLPANEA TIFSCRGEIL ETKFGRSSKL SPRIFIMTKA
KFYIVSQQLV NKQVQIAVEK AIPLGAIKFV SISTCRDDWF SLGVGSPQEA DPLLTCVFKT
ELFTHMQGAM PGGGFNLKIG DSIEYAKKPN KMQLIKVVKD SQQAQDHYKS ATIHTQAGEP
PTSRSKPLPK GKPVAPKPFT SGRLIKPGGP GGRPSKLTNG NRPTPKPVPS PAAARPVPTP
AAAAMPIPAP IPAANPIAAS IPVHTRNPSL QSAQSTRAVP PPPPPAPPAP PPAPASKEPQ
YRVLYEFAGQ SANEFSLKQG EIETVLQKRQ WKWHRHPPPP IASRLTPPPP PGPPKMNGAN
GAAVRSKHTP PAPPAKRPVA GRKPAPPPAP RDSGMSISSN GSGNNSGRST PTPSLAGGLA
EALRARQSAM QGNAKKEDED DW
