SLX1_TALSN
ID SLX1_TALSN Reviewed; 389 AA.
AC B8MDD1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Structure-specific endonuclease subunit slx1 {ECO:0000255|HAMAP-Rule:MF_03100};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03100};
GN Name=slx1; ORFNames=TSTA_116830;
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- FUNCTION: Catalytic subunit of the slx1-slx4 structure-specific
CC endonuclease that resolves DNA secondary structures generated during
CC DNA repair and recombination. Has endonuclease activity towards
CC branched DNA substrates, introducing single-strand cuts in duplex DNA
CC close to junctions with ss-DNA. {ECO:0000255|HAMAP-Rule:MF_03100}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03100};
CC -!- SUBUNIT: Forms a heterodimer with slx4. {ECO:0000255|HAMAP-
CC Rule:MF_03100}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03100}.
CC -!- SIMILARITY: Belongs to the SLX1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03100}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ962655; EED17894.1; -; Genomic_DNA.
DR RefSeq; XP_002481886.1; XM_002481841.1.
DR AlphaFoldDB; B8MDD1; -.
DR SMR; B8MDD1; -.
DR STRING; 441959.B8MDD1; -.
DR EnsemblFungi; EED17894; EED17894; TSTA_116830.
DR GeneID; 8102075; -.
DR VEuPathDB; FungiDB:TSTA_116830; -.
DR eggNOG; KOG3005; Eukaryota.
DR HOGENOM; CLU_030739_1_0_1; -.
DR InParanoid; B8MDD1; -.
DR OMA; LQFEHAW; -.
DR OrthoDB; 844266at2759; -.
DR PhylomeDB; B8MDD1; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0033557; C:Slx1-Slx4 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.1440.10; -; 1.
DR HAMAP; MF_03100; Endonuc_su_Slx1; 1.
DR InterPro; IPR026850; FANCL_C.
DR InterPro; IPR000305; GIY-YIG_endonuc.
DR InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR InterPro; IPR027520; Slx1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF11793; FANCL_C; 1.
DR Pfam; PF01541; GIY-YIG; 1.
DR SUPFAM; SSF82771; SSF82771; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..389
FT /note="Structure-specific endonuclease subunit slx1"
FT /id="PRO_0000383800"
FT DOMAIN 17..99
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT ZN_FING 227..281
FT /note="SLX1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT REGION 303..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 43280 MW; 95C0138C4E51E0E8 CRC64;
MTTTVSEEAV LTKPIPAFYC CYLLRSAKRP SALYIGSTPD PARRLEQHNG FAKGGAKRTE
RNTLRPWEMV AIVEGFPSRT GALQFEWSWQ HVHTTRHIGA VETDQLNRKR KNPPTDKGSG
IWTSTPKVLG NLHQLLRSTY FGTWPLTVRF LSSEAHNHWQ RWIERADGLL PDTIRVKLDF
RAEGASVLDS NLPANDMTHI DATYGGIQEH LAKSTSLLGD NTNSLSCEVC QQQLSTQTEI
IVVCSHRRCH AVFHVNCISQ LFLEDEGSSG LVPILGECPA CRQEVTWVEL MKELSMRLHG
GKNATKLLKG ERKDKANTQG TKSSKGGKKP AKTGDYTLDG DYEDLDEDWM NAVNVEPSSE
DGDRNAANVK GSTGRVEIVI DDSEEDGFD