ID A0A0D1WFZ6_9EURO Unreviewed; 1167 AA.
AC A0A0D1WFZ6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DNA repair protein rad5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV11_03220 {ECO:0000313|EMBL:KIV87690.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV87690.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV87690.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV87690.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) 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; KN846951; KIV87690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1WFZ6; -.
DR STRING; 1016849.A0A0D1WFZ6; -.
DR HOGENOM; CLU_000315_2_5_1; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000053599; 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; 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 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; PS00690; DEAH_ATP_HELICASE; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599};
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 489..697
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 888..933
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 993..1167
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 28..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1167 AA; 129717 MW; B4FC4408AE48E954 CRC64;
MDVDVRPRKK RRFFVDDPED VVDQQLPSAA AITSSRPTSA TSSISHDVKS SQTDAVDLQP
NSDEVKPPTF DADTFRAFIG EDVSQDVVDK VQAAADGDTE RAINMYLDGS WKTSARMTTT
TPLPSRGVDG WLNAPSKAQN NTSRGSFDTQ EQPKEDVGLK PALLHSMPKE RYVGSFGVAA
WMTKSGTNLL AHGEAVRIER SRLAPKTKVG KGGKLVPLIG RIQKVDVVTR FTNARGNELG
RLPEETASWV SALLDQKICR LEGTCVYAPD RVRVNDTVYL QLRAYLLKSA FESSAFVVPK
DDNRATGFFL EKESSEEKDL RLRQVALVRL FDEVNLSPTT TNETAAKHRK QGLLRAAEMA
EQYDKDKTSK GKSGTSTPNS EEEEEGEELE EDQLDALYQK AQSFDFNTPE AEPASTFTLD
LRKYQRQALH WMLGKERDEK SSKQQSMHPL WEEYTWPTRD ADDKPVPQVE GQDKFYVNLY
SGEIGLDFPV QEQNCLGGIL ADEMGLGKTI EIYALIHSNR SPAELEGADK SVTSVNHLPR
LPQSSTEIVP APYTTLVVAP MSLLAQWESE AVKCSKFGTL KTMVYYGSEK TVNLQTLCSA
ANAASAPNVI ITSYGIVLSE FGQVSAAGGD RGSHGGLFSV DFHRVILDEA HNIKNRQAKT
SKACYELKAK HRWVLTGTPI VNRLEDLFSL VRFLKVEPWS NFSFWKTFIT VPFESKDIAR
ALNVVQTVLE PLVLRRTKDM KTPDGEALVP LPSKTISVEE VELSKTEREV YDLIFTRAKR
AFNESVQAGT VLKSYTTIFA QILRLRQSCC HPVLTRNKDV VADEEDAAVA AAADANGFAD
DMDLQDLIKR FTTDTDQAEK ENPATKDPIT TFTTNALRQI QDESSGECPL CYEEPMINPA
VTTCWHSACK ECLEKYITHQ IEKGEMPRCF SCRETINPRD VFEVVKYHNQ SESFDSEGDM
YAADESAPKP PKISLRRIHP YSPTASTSAK IGALLNHLAA LPKGTKSVVF SQFTSFLDLI
SPQLSKHGFS HLRFDGTMSQ KVRAQVIRNF NAENASDPKA PTVLLLSLRA GGVGLNLTAA
SRCYMMDPWW SFAVEAQAID RVHRMGQTAK VEVVRFITKE SIEGRMLRVQ ERKMAVAGSL
GVGQSGAGES EEERKKKRIE ELEMLLG
//
