ID   RAD5_YARLI              Reviewed;        1025 AA.
AC   Q6C2R8;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=DNA repair protein RAD5;
DE            EC=3.6.4.-;
GN   Name=RAD5; OrderedLocusNames=YALI0F05698g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Probable helicase, member of the UBC2/RAD6 epistasis group.
CC       Functions with DNA repair protein RAD18 in error-free postreplication
CC       DNA repair. Involved in the maintenance of wild-type rates of
CC       instability of simple repetitive sequences such as poly(GT) repeats.
CC       Seems to be involved in maintaining a balance which acts in favor of
CC       error-prone non-homologous joining during DNA double-strand breaks
CC       repairs (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; CR382132; CAG77851.1; -; Genomic_DNA.
DR   RefSeq; XP_505044.1; XM_505044.1.
DR   AlphaFoldDB; Q6C2R8; -.
DR   SMR; Q6C2R8; -.
DR   STRING; 4952.CAG77851; -.
DR   EnsemblFungi; CAG77851; CAG77851; YALI0_F05698g.
DR   GeneID; 2907973; -.
DR   KEGG; yli:YALI0F05698g; -.
DR   VEuPathDB; FungiDB:YALI0_F05698g; -.
DR   HOGENOM; CLU_000315_2_5_1; -.
DR   InParanoid; Q6C2R8; -.
DR   OMA; WSNFSFW; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
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; IPR000330; SNF2_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
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   SUPFAM; SSF52540; SSF52540; 2.
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; Cytoplasm; DNA damage; DNA repair; DNA-binding; Helicase;
KW   Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..1025
FT                   /note="DNA repair protein RAD5"
FT                   /id="PRO_0000056129"
FT   DOMAIN          427..607
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          860..1012
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         782..826
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          93..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           558..561
FT                   /note="DEAH box"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         440..447
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1025 AA;  115535 MW;  917A4E5FC7EB4A76 CRC64;
     MEPRQKKARF FDSEEDFGPD TKSLIRPGSS HKPGKPASNS LARPTPAPST FRSDLEAFLG
     PLSDQRFGLL LAKSKGNVEQ AVNIHFDLPE EVQQATSEET AEEAEVSQTT TSGFETTQKP
     SQNTQVPSRV HTRGGCSTSR FIGSLVVTAW ASKSSKGKVK YQDRLVVERQ SHDHSKSIRK
     NPTDNSHVHI RTVSGELLGR ISGEHDYSIA SLIDSRVCDF EASCVYADHN LSLGSNFVVE
     LKCYLTEEAF QDVAMPLLDS KTAKKREYVF DNSRESHVEK MLRNRQIAIV DLFGKLNLIK
     ENEANADMVK DMLRAKSQPP SSQPPSQNSE DESEPIPTDE LDALYKRIEK EDVEQPETEV
     EGFPLELRRY QKQGLTWMIS RETEVSEYFD NDDSGPINPL WTKVDFPGSD EKFYVNFSSG
     ALTLKFPKQE RSFSGGILAD EMGLGKTIST LAMVYRDRHV GCTLVVAPMS LLWQWEQECE
     RVGLSTYVYH EKGADIDLDE LFKTYSPNIL ITSYHTLVSH YGQIKALGGG LDRNVISETS
     SHERPKIFTK HFHRIVLDEA HVIKNRNTVS AKACCLLRAT NKWALTGTPI HNRLEDLFSI
     LKFLGAAPWN DFIYWRNFIT LPFQEGKIVS ALMTVQCILE PIVLRRTKNM KQADGSPLVV
     LPKKTINIEK VALTDQERVI YSYVLARAQT SLQKSEASEA VGRNYLNILT QILRLRQSCC
     DPALILRPEA EVPTDEQLQI EENESQLKSM IQQYNDDTQT SACEYSSEII AQLQDQSAPP
     ECPICAEDVT KLAISKCLHM GCVDCLADNV RFQESKKQTP VCCICRQPAA LKDIFEVERT
     GEDCKDIRLK KLSDRPRSSK LVALVSKLKQ LPKDAKSVVF SQFTSYLDII QTELRREKIQ
     AFRFDGTLSR QQRTDVLKAF GLSKGSVLLI SLKTGGVGLN LVTANHAFIM DPWWTFAQEA
     QAIDRIHRMG QTKDVHVTRF IVENSVEEKM LKIQQQKMVL AGTLGMSEQE QKAQRIENIK
     TLLGE