ID A0A0L6WLF0_9AGAR Unreviewed; 982 AA.
AC A0A0L6WLF0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=DNA repair protein RAD5 {ECO:0000313|EMBL:KNZ76370.1};
GN ORFNames=J132_10649 {ECO:0000313|EMBL:KNZ76370.1};
OS Termitomyces sp. J132.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC Termitomyces.
OX NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ76370.1, ECO:0000313|Proteomes:UP000053712};
RN [1] {ECO:0000313|Proteomes:UP000053712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA Hu H., Poulsen M.;
RT "The genome of Termitomyces.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; KQ412582; KNZ76370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6WLF0; -.
DR STRING; 1306850.A0A0L6WLF0; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000053712; 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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
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 InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45626:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053712};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 337..545
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 719..764
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 810..961
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 24..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 110600 MW; 6893A7205AE66F91 CRC64;
MGEILVPNAW SNVSGKGYIK INDPVKIHRD GQEEPKAGPS KSNSAQGKKS DGKKQMSLKA
MLKPQSSKTK KKVKGDTIVR LLNGKGTEFG RLPADVSWWV SKLLDLGIIE FRGTMTDCPE
TLTTGVSLFV TLQVYILESA FKPSTILNAD DEPTVIFSEG QETLDEKTLR ERKEAVLKLF
DVIGLKPEAG ANVRLPYDAA KIHEEALHRL AKHKSKKVTE IVGDDEEIEV DDAEDLSKND
LDAIYKRAQN NDRTLGTMEP SETFTLTLRG YQKQALLWMH SLESGKIDAR ESSSMHPLWS
RYVFPEKPAI DGNVIDLTAD EKPFYMNPYS GEMSLEFPKS ERKFRGGILA DVGMGKTIML
AALIHTSLSS EEDMKVPPGA KPRQLKLNAA FYPAAQRKPQ KSSSATLIVA PTSLLAQWSE
ELERSSKPES MKVLVWHGQN RLDLEAVIED SNDDNACIKV VITSYGVLAS EHARSEKSNS
GRSPVFEIDW LRVILDEAHS CKSRTSKTAK AVYALRARRR WAVTGTPIVN KLEDLYSLLK
FLNFKPWSDF AFFRSFITLP FLARDPKAIE IVQIILESVL LRREKNMRDI EGNKIVELPP
KKVVVETLEF SPLERKIYDR IYISAKRDFE RLDAKGLVKK NYTHILAMLM RLRRAVLHPN
LVLTPDDEHV LLSAGDGSID VDDLIRRFTD TERAEEGGDK SIFAEEVLAK LADAEAEECP
ICLDVMETPM IIPGCMHQCC RDCILAHLAT CEDRREESRC PTCSQGPLKA SELIEVIRRK
KNLDIFSSQT SEPEVTLRRN DFQTSTKIQA LLKSLKCLQN QDPRFRAVVF SQFTSFIDLI
QVALDREKYD HYRFDGSMDI KKKNAAVAEF RVPSEKPKIL VISLKAGGVG LNLTIANHVF
MMDCWWNAAT ENQAIDRVHR IGQEKTVYVT HFIVANTIEC RILQIQKRKT AIVKEAFRCS
GARGEGVDPE SIENLKIIFG DN
//
