ID G1WZZ4_ARTOA Unreviewed; 1621 AA.
AC G1WZZ4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Transcriptional regulator {ECO:0008006|Google:ProtNLM};
GN ORFNames=AOL_s00006g195 {ECO:0000313|EMBL:EGX53329.1};
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:EGX53329.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX53329.1, 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: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EGX53329.1}.
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DR EMBL; ADOT01000012; EGX53329.1; -; Genomic_DNA.
DR RefSeq; XP_011117806.1; XM_011119504.1.
DR STRING; 756982.G1WZZ4; -.
DR GeneID; 22888703; -.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_000315_29_2_1; -.
DR InParanoid; G1WZZ4; -.
DR OMA; WVQIRDD; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR041150; Cdh1_DBD.
DR InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF18196; Cdh1_DBD_1; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 289..361
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 388..450
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 486..657
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 787..952
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..111
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1466
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1621 AA; 184694 MW; F935A41413838D1B CRC64;
MTSATVSDVS RLPPIHSTYT PDVSVEGNSP EKVESPSASD LTDLGVAAAA SSSPASASEE
DDSPMDHEEP VMTDSESSSE QERSENGDDD FDAGNASEDA EGEEEEDVLE IISSPEPAGR
RLAKLKKPKD SAAEDYSQNP ELWGLRRSSR PVARNKRIIL SSEDDEGEED QEEEDDDVPS
DDSDVRPRKR SKPKSSRPTK AATSKVTTPR VSAESSDDGG DSDFYSNKKS ARRKKRRLNP
VVEHEVRVPT RAATKVLNYN EDADDSDDFR ITDDEQAQYA EWVEEDTTPN IDVILDHRVK
EGFDPEEYAG SKEHLEFLIK WTEQAHIHAT WEQTSELTHK KYIRKLTNYM AKLKKEIAKR
SDPETTREDL ERLTLERERQ VEAALEARGV ERVVASRGGQ DDEPLEYLVK WRSLTYEHCT
WETESFLGPV APTEISQFRK RTRSARNYAV TPVKDRKKYK LWSKQPDYIQ YGELRDFQMK
GVNWLRYNWS VHRNSILADE MGLGKTVQTV AFLSWLKNEM EIDGPFLVVV PLSTVPAWCE
TFVKWAPDLN FIVYNGPNKA RGIIQDYEMF QDEKRKKTKF HVMITTYEYV NHDAQLLQSI
RWNYLAVDEA HRLKNVESRL YESLKQFKVE DRLLITGTPL QNNLSELVAL LEFLDPGNIN
IDRNIDLQSE GAEQEIKKLQ ETLQPYILRR VKKDVEASLP QKTEKIIRVE LSDIQTEWYK
NIYTRNYSAL NAKSKQKVSL LNIVMELKKI SNHPFLFPSA EEEIMKGLET KADRLNAMIM
CSGKMVLMDR FLTKMKADGH RVLIFSQMVN MLDLLQEYLT LRGFSYQRID GTVSASNRKT
AIDRYNAPGS EDFCFLLSTR AGGLGINLTS ADTVIIFDSD WNPQADLQAM ARAHRIGQKN
HVMIYRFVSK DTIEEEVLER ARVKLLMEYA VYMGITDSTI TDKVKKNTKS LSQAELANVL
AARAHKIFEG DKEKQNQKKL ETLDIEDYLQ HAEDHDTDAQ GASLIRNEGG EAFQELLKQF
EVTDIDVDWD SVLPPEQLES LRAADKLKQD EEFLQEQIQA NAKRIRRPMN GIDESDSSGS
EKAPARGRRG PPKKRRGEAR RRDDTSDEEG EIPDPSRPLL EREIRNLYNA FIRYGLMDDR
YTEIVKDAKL QDRDREVVVS TIKEIVRLSE EAIKTHETAQ KEGGATRKDK KAILFEYQGV
KDINAEKVTQ IPDFLRVLRT AVSGCPDPLE FRIATAKVKT EKWSCEWGAK EDGMLCLGID
RHGYKNWVPI RDDPELGLQG KMFLEEHRVD KKAERVKGGA AKLSPGAEHL SRRANYLLGL
LKDQQEKTAQ QQAAATARYQ RGNRNSNSAS PIPGKGRKGI NKPVGAISKK RPITDRDGGD
ESPSKRPKNG KTDKKEVQKN GILNYYGKKE NTGSSLKKHR RESDVSRDDA TPNKKRRDDE
KRTSSHPDKH SKDHHHHHKA NGSTKNGVKR KSHERDEPNG SASKGSHGAS GSPVPKVGAI
TQRAEDCMWG IRETLQKLQK LDRDEQEHRT YAISIRKGLM DAGEYIRDVL EMRARTPGPA
RNQLELELWE VVAHHWPHRE KRMPGDTYRR MYKKYQERII QMKAKDGQGA DGATPTASVS
K
//
