ID G1XJ29_ARTOA Unreviewed; 831 AA.
AC G1XJ29;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Actin-like ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AOL_s00097g356 {ECO:0000313|EMBL:EGX46930.1};
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:EGX46930.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX46930.1, 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 -!- 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:EGX46930.1}.
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DR EMBL; ADOT01000174; EGX46930.1; -; Genomic_DNA.
DR RefSeq; XP_011124491.1; XM_011126189.1.
DR AlphaFoldDB; G1XJ29; -.
DR STRING; 756982.G1XJ29; -.
DR GeneID; 22895406; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_009958_6_2_1; -.
DR InParanoid; G1XJ29; -.
DR OMA; MGRCTSR; -.
DR OrthoDB; 1377857at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10229; HSPA12_like_NBD; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR14187; ALPHA KINASE/ELONGATION FACTOR 2 KINASE; 1.
DR PANTHER; PTHR14187:SF79; HSP70 FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G15200); 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784}.
FT REGION 1..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 90447 MW; 8FAA2C94E433C78C CRC64;
MDQVNSRFKK FGFNRKGSTN NGSTPPLHPS ASQSSLNQQQ PARQTPPPQP NSLGRPPSYT
GAPQGQAQGQ QPSGPTPPAQ NPFPPQGPPQ PQHQQQPPPP HGGQQSPPVG PPSHPPQQQP
NVRPPHPQQQ GPPQQGPPQQ GPPQQGPPQQ GPPLNGPQGR NGSPMPQGHP GQQYGGHGQF
PPPINTAQYG RPPQGPGVPY PGPGGQAPPY GQGHPGGPGG PGYPQGGPGG PPPFQQQQQQ
PQHPPQHGPA HAAHEVPGAG RSQSQLIVGI DFGTTFSGVA YAFVAPGQEP QESIIAEWPG
AGNTTRQKVP TVLYYDQYQK VVGWGPDIGD ALAPTGYPKQ GVQKVEWFKL QLMVSGNTYI
DPINLPPLPP GKSEIDVAAD YLFKLRQAMR AALQKSLGEV FNREERNIKY FLTVPAIWND
AGKAATRQAA IQAGFLRDAN DNRLTLITEP EAAAMFCSKM GLLNLKIHDA VLIVDCGGGT
VDLIAYEVEE EVPFSVAECT AGSGDSCGST ALNRNFSNIL RAKIRKMKLP DGSKTAGKVY
AKCIMDFENR IKADFRNNGQ KWAVDVGIET DFPDAGIEEG YMTFTNEEIL QCFEPVVNRI
LELVRNQIIA IQAQNRQLQN VLVVGGFGAS EYLFQQIKLH VPPQFQNKVV RPMDSVAAIV
KGAVTAGITE RVVTSRVARR HYLMATLQPF KEGHHPEAYR VPSLDGKDRC KYTRQIFVTK
GQRVKIGEPV KVSFFRQVAP GATLMYEDIL YACDDDVCPE YTKDSRIKEV VTLTSDLSRK
NLEKDFERMD TPQGTFYRVY FDIYLTLDGS EFNAELVCQG EVMGRCSAKF R
//