MYO1_ASPFC
ID MYO1_ASPFC Reviewed; 1249 AA.
AC B0Y9Q4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=myoA; ORFNames=AFUB_081890;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP48747.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS499600; EDP48747.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; B0Y9Q4; -.
DR SMR; B0Y9Q4; -.
DR PRIDE; B0Y9Q4; -.
DR PhylomeDB; B0Y9Q4; -.
DR Proteomes; UP000001699; 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; Repeat;
KW SH3 domain.
FT CHAIN 1..1249
FT /note="Myosin-1"
FT /id="PRO_0000338538"
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..42
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..1249
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..1154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1224
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 1249 AA; 137289 MW; DF7F820A1423C050 CRC64;
MGHSRRPAGG EKKSRGFGRS KAVADVGDGR QTGGKPQVKK ATFESTKKKE IGVSDLTLLS
KISNEAINDN LKLRFEHDEI YTYIGHVLVS VNPFRDLGIY TDNVLQSYRG KNRLEVPPHV
FAVAESAYYN MKSYKDNQCV IISGESGAGK TEAAKRIMQY IASVSGGTDS SIQHTKDMVL
ATNPLLESFG NAKTLRNNNS SRFGKYLELE FNTNGEPVGA NITNYLLEKS RVVGQITNER
NFHIFYQFTK AAPQKYRDLF GIQQPQSYLY TSRSKCFDVP GVDDSAEFRD TLNAMNVIGM
TEGEQDEVFR MLAAILWIGN VQFAEDDSGN AVITDQSVVD YVAYLLEVDA AQVNKAFTIR
VMETARGGRR GSVYEVPLNT VQALAVRDAL AKAIYFNLFD WIVQRVNASL TARGEVANSI
GILDIYGFEI FEKNSFEQLC INYVNEKLQQ IFIQLTLKAE QDEYAREQIQ WTPIKYFDNK
VVCSLIEDKR PPGVFAALND ACATAHADSS AADNTFVGRL NFLSQNPNFE NRQGQFIIKH
YAGDVSYAVA GMTDKNKDQL LKDLLNLVGT SGNQFVHTLF PEQVNQDDKR RPPTASDKIK
ASANDLVATL MKAQPSYIRT IKPNDNKAPR EYNVGNVLHQ IKYLGLQENV RIRRAGFAYR
QTFDKFVERF YLLSPKTSYA GDYTWTGDAE SGARQILKDT SIPAEEYQMG ITKVFVKTPE
TLFALEAMRD RYWHNMAIRI QRAWRNYLRY RTECAIRIQR FWRRTTGGLE FIKLRDQGHQ
LLNGRKERRR MSLLGSRRFL GDYIGVGNKG GPGEMVRNGA GISGSEEILF SCRGEVLVSK
FGRSSKPAPR ILALTNRHVY IIAQNLVNNQ LVISSERTIP IGAIKAVGAS NLKDDWFSIV
VGSPQEPDPL VNCVFKTEFF THLNNALRGQ LNLKIADHIE YNKKPGKLAT VKVVKDPAVA
RDDSYKSGTI HTGPGEPANS VSKPTPRPKQ VSARPVTKGK LLRPGGPGGG PSKLAARPTP
AAQPLPRATP QPAEPQPAAR AVPQPVAAVA ASHTRTGSTA SVRAPPPPPP AAAPAPKKPT
AKVLYDFNSQ QSNELSIKAG EIVQIVSKEG NGWWLCMNMT TSAQGWTPEA YLEEQVAPTP
KPAPPPPPAA PRSTPAPATN GAAAAAKAKP APPAPPAKRP NMAARKAVPT PPPAPRDSAV
SMNSHDSSGG SGRGTPNSMS NASLAGGLAE ALRARQHAMQ GKQDDDDDW
