MYO1_NEOFI
ID MYO1_NEOFI Reviewed; 1250 AA.
AC A1DBH2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=myoA; ORFNames=NFIA_098420;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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. Plays an important role in polarized growth, spore
CC germination, hyphal morphogenesis, and septal wall formation (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250}. Note=Localizes to cortical patch-like structures.
CC Enriched at sites of polarized growth, like the growing hyphal tips and
CC sites of septum formation (By similarity). {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-372) 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}.
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DR EMBL; DS027694; EAW20212.1; -; Genomic_DNA.
DR RefSeq; XP_001262109.1; XM_001262108.1.
DR AlphaFoldDB; A1DBH2; -.
DR SMR; A1DBH2; -.
DR STRING; 36630.CADNFIAP00009077; -.
DR EnsemblFungi; EAW20212; EAW20212; NFIA_098420.
DR GeneID; 4588724; -.
DR KEGG; nfi:NFIA_098420; -.
DR VEuPathDB; FungiDB:NFIA_098420; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR OMA; MESKWGT; -.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0051285; C:cell cortex of cell tip; IEA:EnsemblFungi.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0031097; C:medial cortex; IEA:EnsemblFungi.
DR GO; GO:0045160; C:myosin I complex; IEA:EnsemblFungi.
DR GO; GO:0044853; C:plasma membrane raft; IEA:EnsemblFungi.
DR GO; GO:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR GO; GO:0051015; F:actin filament binding; IEA:EnsemblFungi.
DR GO; GO:0071933; F:Arp2/3 complex binding; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IEA:EnsemblFungi.
DR GO; GO:0000147; P:actin cortical patch assembly; IEA:EnsemblFungi.
DR GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IEA:EnsemblFungi.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:EnsemblFungi.
DR GO; GO:0044855; P:plasma membrane raft distribution; IEA:EnsemblFungi.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:EnsemblFungi.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IEA:EnsemblFungi.
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..1250
FT /note="Myosin-1"
FT /id="PRO_0000338557"
FT DOMAIN 51..730
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 734..754
FT /note="IQ 1"
FT DOMAIN 755..780
FT /note="IQ 2"
FT DOMAIN 788..978
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1076..1137
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..501
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 962..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1039
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1076
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1250 AA; 137301 MW; 1E806FE5DAEF438B CRC64;
MGHSRRPAGG EKKSRGFGRS KAAADVGDGR QTGGKPQVKK ATFESTKKKE IGVSDLTLLS
KISNEAINDN LKLRFEHDEI YTYIGHVLVS VNPFQDLGIY TDNVLQSYRG KNRLEVPPHV
FAVAESAYYN MKSYKDNQCV IISGESGAGK TEAAKRIMQY IASVSGGTDS SIQHTKEMVL
ATNPLLESFG NAKTLRNNNS SRFGKYLELE FNTNGEPVGA NITNYLLEKS RVVGQITNER
NFHIFYQFTK AAPQKYRDLF GIQQPQSYLY TSRSKCYDVP GVDDSAEFRD TLNAMNVIGM
TEGEQDDVFR MLAAILWIGN VQFAEDDSGN AVITDQSVVD YVAYLLEVDA AQVNKAFTIR
VMETARGGRR GSVYEVPLNT VQALAVRDAL AKAIYFNLFD WIVQRVNASL TARGEVANSI
GILDIYGFEI FEKNSFEQLC INYVNEKLQQ IFIQLTLKAE QDEYAREQIQ WTPIKYFDNK
VVCSLIEDKR PPGVFAALND ACATAHADSS AADNTFVGRL NFLSQNPNFE NRQGQFIVKH
YAGDVSYAVA GMTDKNKDQL LKDLLNLVGT SGNQFVHTLF PEQVNQDDKR RPPTASDKIK
ASANDLVATL MKAQPSYIRT IKPNDNKAPK EYNVGNVLHQ IKYLGLQENV RIRRAGFAYR
QTFDKFVERF YLLSPKTSYA GDYTWTGDAE SGARQILKDT SIPAEEYQMG ITKVFVKTPE
TLFALEAMRD RYWHNMAIRI QRAWRNYLRY RTECAIRIQR FWRRTTGGLE FIKLRDQGHQ
LLNGRKERRR MSLLGSRRFL GDYIGVGNKG GPGEMVRNGA GISGSEDILF SCRGEVLVSK
FGRSSKPAPR ILVLTNRHVY IIAQNLVNNQ LVISSERTIP IGAIKAVSAS NLKDDWFSIV
VGSPQEPDPL VNCVFKTEFF THLNNTLHGQ LNLKIADHIE YNKKPGKLAT VKVVKDPAVA
RDDSYKSGTI HTGPGEPANS VSKPTPRPKQ VSARPVTKGK LLRPGGPGGG PSKLAARPTP
AAQPLPRATP QPAAPQPAAR AVPQPVAAVA ASHTRTGSTA SVRAPPPPPP AAAPAPKKPT
AKVLYDFNSQ QSNELSIKAG EIVQIVSKEG NGWWLCMNMT TSAQGWTPEA YLEEQVAPTP
KPAPPPPPPA APRSTPAPAT NGAAAAAKAK PAPPAPPAKR PNMAARKAVP TPPPAPRDSA
VSMNSHDSSG GSGRGTPNSM SNASLAGGLA EALRARQHAM QGKQDDDDDW
