XPF_SACS2
ID XPF_SACS2 Reviewed; 233 AA.
AC Q7LXL5; Q9UXB7;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=3'-flap repair endonuclease Xpf;
DE Short=XPF;
GN Name=xpf; OrderedLocusNames=SSO0729; ORFNames=ORF-c10_001;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, INTERACTION WITH PCNA1 AND PCNA3,
RP SUBUNIT, AND MUTAGENESIS OF ASP-52 AND 228-SER--LEU-233.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=12675797; DOI=10.1046/j.1365-2958.2003.03444.x;
RA Roberts J.A., Bell S.D., White M.F.;
RT "An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA.";
RL Mol. Microbiol. 48:361-371(2003).
CC -!- FUNCTION: A structure-specific endonuclease, cleaves 5' of ds/ssDNA
CC interfaces in 3' flap structures, although it also cuts bubble, Y-DNA
CC structures and mobile and immobile Holliday junctions. Cuts
CC preferentially after pyrimidines, may continue to progressively cleave
CC substrate upstream of the initial cleavage, at least in vitro. May be
CC involved in nucleotide excision repair. {ECO:0000269|PubMed:12675797}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12675797};
CC -!- ACTIVITY REGULATION: Nuclease function requires interaction with the
CC PCNA heterotrimer. Inhibited by SSB, even in the presence of PCNA.
CC {ECO:0000269|PubMed:12675797}.
CC -!- SUBUNIT: Interacts with PCNA heterotrimer via PCNA1 and PCNA3.
CC {ECO:0000269|PubMed:12675797}.
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DR EMBL; Y18930; CAB57574.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41026.1; -; Genomic_DNA.
DR PIR; C90221; C90221.
DR RefSeq; WP_009991296.1; NC_002754.1.
DR AlphaFoldDB; Q7LXL5; -.
DR SMR; Q7LXL5; -.
DR STRING; 273057.SSO0729; -.
DR EnsemblBacteria; AAK41026; AAK41026; SSO0729.
DR GeneID; 44129725; -.
DR KEGG; sso:SSO0729; -.
DR PATRIC; fig|273057.12.peg.726; -.
DR eggNOG; arCOG04206; Archaea.
DR HOGENOM; CLU_101253_0_0_2; -.
DR InParanoid; Q7LXL5; -.
DR OMA; IIEGDLW; -.
DR PhylomeDB; Q7LXL5; -.
DR BRENDA; 3.1.99.B2; 6163.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR Pfam; PF02732; ERCC4; 1.
DR SMART; SM00891; ERCC4; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Endonuclease; Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT CHAIN 1..233
FT /note="3'-flap repair endonuclease Xpf"
FT /id="PRO_0000429324"
FT DOMAIN 8..127
FT /note="ERCC4"
FT MUTAGEN 52
FT /note="D->A: Loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:12675797"
FT MUTAGEN 228..233
FT /note="Missing: Loss of interaction with PCNA heterotrimer,
FT no nuclease activity."
FT /evidence="ECO:0000269|PubMed:12675797"
SQ SEQUENCE 233 AA; 26683 MW; 21AD036DC5ED134E CRC64;
MVIRIYADDR EKASGIPELL KELGITVIFS QLTVADYVIT DDVAVERKSV NDLVNSVFDK
RFFDQISRLS EVYRFPILLV EGDINDIRKI TEKWRAINNA LISATIDYDV KVFYSRDKKD
TAEVLKKIAE KFQFGENKSN RISLHNKAKL ESVSDIQLYI VESFPNVGSI LAERLLLKFG
TIQNICNASI SELEKALGSR KKAEDIYKIL RTHYSKTNLD NDSKKTTSLF DFL
