RAD5_KLULA
ID RAD5_KLULA Reviewed; 1114 AA.
AC Q6CJM4;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=DNA repair protein RAD5;
DE EC=3.6.4.-;
GN Name=RAD5; OrderedLocusNames=KLLA0F17479g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98573.1; -; Genomic_DNA.
DR RefSeq; XP_455865.1; XM_455865.1.
DR PDB; 6L8N; X-ray; 3.60 A; A=163-1114.
DR PDB; 6L8O; X-ray; 3.30 A; A=163-1114.
DR PDBsum; 6L8N; -.
DR PDBsum; 6L8O; -.
DR AlphaFoldDB; Q6CJM4; -.
DR SMR; Q6CJM4; -.
DR STRING; 28985.XP_455865.1; -.
DR PRIDE; Q6CJM4; -.
DR EnsemblFungi; CAG98573; CAG98573; KLLA0_F17479g.
DR GeneID; 2895607; -.
DR KEGG; kla:KLLA0_F17479g; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_5_1; -.
DR InParanoid; Q6CJM4; -.
DR OMA; WSNFSFW; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0000400; F:four-way junction DNA binding; IEA:EnsemblFungi.
DR GO; GO:0009378; F:four-way junction helicase activity; IEA:EnsemblFungi.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0000403; F:Y-form DNA binding; IEA:EnsemblFungi.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IEA:EnsemblFungi.
DR GO; GO:0042275; P:error-free postreplication DNA repair; IEA:EnsemblFungi.
DR GO; GO:0070987; P:error-free translesion synthesis; IEA:EnsemblFungi.
DR GO; GO:0042276; P:error-prone translesion synthesis; IEA:EnsemblFungi.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; IEA:EnsemblFungi.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:EnsemblFungi.
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; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
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; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1114
FT /note="DNA repair protein RAD5"
FT /id="PRO_0000056125"
FT DOMAIN 471..676
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 943..1114
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 858..906
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 25..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 627..630
FT /note="DEGH box"
FT COMPBIAS 31..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 484..491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT STRAND 176..188
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:6L8O"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 278..288
FT /evidence="ECO:0007829|PDB:6L8O"
FT TURN 289..293
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 312..329
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 363..373
FT /evidence="ECO:0007829|PDB:6L8O"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 398..410
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:6L8O"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 477..484
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 490..500
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 505..513
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 546..550
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 555..565
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 584..589
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 595..600
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 601..609
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 615..627
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 629..633
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 638..645
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 648..654
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 665..673
FT /evidence="ECO:0007829|PDB:6L8O"
FT TURN 676..679
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 681..687
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 689..693
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 697..708
FT /evidence="ECO:0007829|PDB:6L8O"
FT TURN 709..711
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 722..724
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 726..728
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 732..740
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 744..766
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 770..773
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 774..789
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 791..793
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 833..846
FT /evidence="ECO:0007829|PDB:6L8O"
FT TURN 859..861
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 869..871
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 872..874
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 880..882
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 883..894
FT /evidence="ECO:0007829|PDB:6L8O"
FT TURN 895..897
FT /evidence="ECO:0007829|PDB:6L8O"
FT TURN 903..905
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 911..913
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 915..917
FT /evidence="ECO:0007829|PDB:6L8O"
FT TURN 923..925
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 929..933
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 939..954
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 959..965
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 967..980
FT /evidence="ECO:0007829|PDB:6L8O"
FT TURN 983..985
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 986..990
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 993..995
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 997..1007
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 1014..1021
FT /evidence="ECO:0007829|PDB:6L8O"
FT TURN 1022..1028
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 1034..1039
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 1046..1054
FT /evidence="ECO:0007829|PDB:6L8O"
FT STRAND 1065..1072
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 1076..1090
FT /evidence="ECO:0007829|PDB:6L8O"
FT HELIX 1098..1113
FT /evidence="ECO:0007829|PDB:6L8O"
SQ SEQUENCE 1114 AA; 127147 MW; C60053E25C6AD308 CRC64;
MTQPQKADEK PRFFRDEDES VINLNESRSL FVQDEADDSD DGQGHVESSS EVSSNTSNHK
ERFFESLKEI LGENMISSSQ LHTLWSSYGL LKDGISIAAD KFFEDKELLS KSKTESKMPA
GDNIEVIDLS DEENDDELSI LPSSSQLSQL FTNKRTSTQA GLESPMSSDK GRNRWSRYIG
SIHTMGFATR PTVKPVPIGS RLGFKKSVPK DLPLGKSLQH QHCSHLVRLI DTSQDRELGR
MPEDVARILY PLLDYSEQVS LEPYLLINNG KRFSVGDNIY IRIDCYLTSQ AFVRIEGGSI
LNKSFINDHG MDTRQLHRAG AIMALFDAIN IQPVYGDTKN EMIPNYQENT VSSSQFQDEA
LNINQLKSFY RITQSAASLQ NLPETTPDES LFKLQLRRYQ KQSLSWMLKR EYEYSHLSEK
AAEVSIDGNS MNPLWKKFRW PSNSKQGTPN HEDDCFFYAN LYTGEFSIEK PVIKTIINGG
ILADEMGLGK TISALALICT ASYDEAHEKK IESTKKPSMK EMSSQVDSSP LRHSQHKHDT
YAYRTTLIVV PMSLLNQWQS EFEKANKDLK KRCEIYYGNN IKDLRAYVLG PNAPSVIITT
YGIIQSEYGR TSTSGLFNVV FFRIILDEGH TIRNRSTRTS KAVIALRSSR KWILTGTPII
NRLDDLFSLV QFLNLEPWSH INYWKRYVSV PFEKGNYAQA FDVINAVLEP VLLRRTKNMK
DVDGKPLVSL PPKEVIVEKL QLSSSEKRVY QSMLEDAENS VKEGLAKGDL LKNYTNILVH
ILRLRQVCCH LDLLKKTPDL GDPDLEDLEN STQNISSILM PKNIKSPKSS ISQDKLDALS
ANFRDIHSAS EQLPSFECAI CTTECIEPLS AVSITECLHT FCEPCLAEYI EFQQNKKLSI
NCPYCRMPIS EANVLKLKEP IDAERGYELI SFHSHFQSTK IKALLRHLKQ IQETSPGEQI
IVFSQFSSFL DILEIELRSH LPRDQVIIYK FDGRLDMKER TRILEQFHDK DLSCIKLLLL
SLKTGGVGLN LTCASRAFMM DPWWSPGMED QAIDRIHRIG QQQTVKVVRF IIDNSVEEKM
LRIQERKRML GDIVEGDEAE RRQKRIEEIQ MLFQ
