ID A0A0K6FKY5_9AGAM Unreviewed; 1836 AA.
AC A0A0K6FKY5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Chromodomain-helicase-DNA-binding protein 1 {ECO:0000313|EMBL:CUA66828.1};
GN Name=hrp3 {ECO:0000313|EMBL:CUA66828.1};
GN ORFNames=RSOLAG22IIIB_00276 {ECO:0000313|EMBL:CUA66828.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA66828.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA66828.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA66828.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CYGV01000001; CUA66828.1; -; Genomic_DNA.
DR Proteomes; UP000044841; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000313|EMBL:CUA66828.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CUA66828.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000044841};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 192..264
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 295..360
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 401..569
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 699..855
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 947..976
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..90
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1836 AA; 206216 MW; A32982FDB3839935 CRC64;
MNIGALVSTR PPNHSSDRAD SPLSSELDVS HAVHQSDVDM NSLDDADADA DADGEAEADV
DVDVDADGEA DDYEDQRPEE RESSDEDAVD NDPGYDPKPR RKQAAPKVKR KKAKSKTTSP
STSYPQSPLS DSDYATGSKK KPKKGRATPN SRRAAANRPN YRDEDRPEWM GESDADEQED
TPTQLEQYDT EDEIEMVLGH SRDEEFKDDP EDKPTSNMRF HIKWKGFSHL HNTEEAYEFL
KRYKGLKRVD NYIKNVWARD NAFQARRAAG ELSPEEIEAY QLEKERIKDN LEQCRNVERI
VTCRQRMTED GETTDYFVKW KGGLTYEHCT WELQADVMRI AQSEIKAFEE REASGLFPYR
SQPYPKDRRP KPVVFREDPE YISKLGVELK DFQLTGLNWL AYIWSNGING ILADEMGLGK
TVQSVSFLSY LVHTQQQYGP FLVVVPLSTL PAWQMQFKTW APDLNVICYV GSGVARRVIR
EYEFGAPKKL KMNVLLTTYE YILKDKSELG TIKWQALMVD EAHRLKNSDS QLYEALMSFS
SAFKVLITGT PLQNNVKELL ALMHFLMPEK FPLAGNEFEL TDANNEGKIK DLHDKLEHMM
LRRLKKDVIK SLPTKSERIL RVEMSAMQTH YYKNILTKNF AALNKTATGE NARVSLLNIA
MECKKAANHP FLFDGAEVAK DSPEETLKGL VMNSGKMVLL DKLLGRLKQD GHRVLIFSQM
VRLLDILSDY MTLRGYLHQR LDGTVASDVR KRSIEHFNAP NSPDFAFLLS TRAGGLGINL
ETADTVIIFD SDWNPQNDLQ AMARAHRIGQ KSHVSVYRFV SKGTVEEDVL ERAKRKMVLE
YAIINQLDTT QSHLGPKPSA AKADFSKEEL SAILKFGAQN MFKADESQLN KQLDEMDLDD
ILNHAEAHET VSGGGEAAVS SLGGEAFLAN MAAITDVSTD MLSWDDIIPL EEREKFEQEE
AEQAEAEAIA QAAQGKKRAA AQVQPGAYEG MDVVETPTTT GGQKKAKANT GLPRKTAAQR
SMELKERDLR VLVRSLQRWG DIRXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
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EHRSRNHRCM GVWLMAVAGR ASTKPFLCAC YMCMRS
//