ID G1XAX1_ARTOA Unreviewed; 1262 AA.
AC G1XAX1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Myosin-1 {ECO:0000256|ARBA:ARBA00016187};
DE AltName: Full=Class I unconventional myosin {ECO:0000256|ARBA:ARBA00032645};
DE AltName: Full=Type I myosin {ECO:0000256|ARBA:ARBA00029665};
GN ORFNames=AOL_s00078g68 {ECO:0000313|EMBL:EGX49579.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX49579.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX49579.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000256|ARBA:ARBA00004134}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGX49579.1}.
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DR EMBL; ADOT01000133; EGX49579.1; -; Genomic_DNA.
DR RefSeq; XP_011121633.1; XM_011123331.1.
DR AlphaFoldDB; G1XAX1; -.
DR STRING; 756982.G1XAX1; -.
DR GeneID; 22893128; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; G1XAX1; -.
DR OMA; GCHEHFN; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000008784; 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-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0051179; P:localization; IEA:UniProt.
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 {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 52..734
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 792..982
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1103..1163
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 607..629
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 966..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1103
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 145..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1262 AA; 139533 MW; 01B73C8C40E7B64B CRC64;
MAVTKRAGRN KTKDAAGVTS KVPFMKGAVG SSAGGQGPPK KAFYEGSKKK EVGVSDLTLI
SKISNEAINE NLMKRFEAAE IYTYIGHVLI SVNPFRDLGI YVDSVMEAYK GKNRLEMPPH
VFAIAEASYY NMNAYRDNQC IIISGESGAG KTEAAKRIMQ YIANVSGGQQ NSHITEIKNM
VLATNPLLEA FGCAKTLRNN NSSRHGKYLE IQFNAQGEPC GANITNYLLE KGRVVGQIMN
ERNFHIFYQF AKAASPAYRE LFGIQTPEAY AYTSNSRCLD VPGIDDTKEF SETLQAMKVI
GLTQQEQDDI FRLLAAILWI GNVQFREEES GSAAIVDPGV TDFAAYLLQV DGVALNKALS
IRIVETSRGG RRGSIYESPL NAAQATSVRD TLAKAIYNNL FEWIVDRINV SMKAREQTSY
TIGILDIYGF EIFDKNSFEQ LCINYVNEKL QQIFIELTLK TEQEEYVREQ IEWQPIKYFN
NKIVCDLIEE KRPPGVFAAL NDACATAHAD PSAADGTFIQ RLNALSTNPH FAQRQTQFII
KHYAGDVTYQ IEHMTDKNKD QLLRDILELM EASDNQFLHT IFPQQVGATD TKGRRPPTAS
DKIKASANDL VNTLSKATPS YIRTIKPNQN KSPKEYDSAA VLHQIKYLGL QENVRIRRAG
FAYRQTFERF VDRFYLLSSK TSYAGDYIWT GDPRSGSEQI LKDTRIPKEE WQMGTTKAFI
KTPETLFALE TMRDRYWHNM AIRIQRAWRN YLRYRTECAV RIQRWWRNLT GSTDFVKLRD
YGHTVLAGRK ERRRFSIIGS RRFMGDYLGV DNRGGYGEHV RNSVQIPASD QTLFSCRGEM
LVSKLGRSSK PNPRLIVLTN RNFYIVTQSI VNNQLQILSD RTIPLGTIKF IGTSNLRDDW
FSLGVGAPGQ PDPLISCIFK TELFTHMKGL MTGIFDLRIG PTIEYNKKPG KIAVVKTLKD
PAVPRDDLYK SGTIHVGPGE PPNSVSRPTP KPRAKPAKAI TSGGLLKKSV NGKLSSQARG
RTTPQPQARP VPRQLPGGGS STVSSNPSTV MPAAIKPVTP VLQQQPMSNG YGGNQQRNSM
GSSVASTRAP PPPPPPPPAA TPSQDPMARA LYDFAGQSAN ELTLTKGEIL IILQKEGNGW
WLAKKADDTQ GWAPSAYLKE EEAAKPPPPP PPPPAVAGKA KPPPPPRPKP SAAAAAAVRK
PSSMHQPAET VTSSTGTRAS NLSVQSQPDG GAPNSSLAGG LAAALKKRSQ ANRGSDEDND
DW
//
