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   27-MAR-2024, entry version 90.
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 /
RC   NRRL 181 / 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; 331117.A1DBH2; -.
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; MAFHWQS; -.
DR   OrthoDB; 1094820at2759; -.
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:0000281; P:mitotic cytokinesis; IEA:EnsemblFungi.
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; 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; 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; 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
//