ID   SLX1_CAEBR              Reviewed;         439 AA.
AC   A8WJ66;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Structure-specific endonuclease subunit SLX1 homolog {ECO:0000255|HAMAP-Rule:MF_03100};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03100};
DE   AltName: Full=GIY-YIG domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03100};
GN   Name=slx-1 {ECO:0000312|WormBase:CBG23741};
GN   Synonyms=giyd-1 {ECO:0000255|HAMAP-Rule:MF_03100};
GN   ORFNames=CBG23741 {ECO:0000312|WormBase:CBG23741};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Catalytic subunit of a heterodimeric 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 (Potential). Has a preference for
CC       replication forks over 5' flap structures or Holliday junctions and
CC       shows much lower activity toward 3' flap structures (By similarity).
CC       Required for proper crossover distribution through inhibition of
CC       crossover formation at the central region of chromosomes (By
CC       similarity). {ECO:0000250|UniProtKB:P91351, ECO:0000255|HAMAP-
CC       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 him-18/slx-4. {ECO:0000255|HAMAP-
CC       Rule:MF_03100}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03100}.
CC   -!- DOMAIN: Both the N- and C-terminal regions are required for interaction
CC       with him-18. {ECO:0000250|UniProtKB:P91351}.
CC   -!- SIMILARITY: Belongs to the SLX1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03100}.
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DR   EMBL; HE601040; CAP20508.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8WJ66; -.
DR   SMR; A8WJ66; -.
DR   STRING; 6238.CBG23741; -.
DR   WormBase; CBG23741; CBP39087; WBGene00042011; Cbr-slx-1.
DR   eggNOG; KOG3005; Eukaryota.
DR   HOGENOM; CLU_052232_0_0_1; -.
DR   InParanoid; A8WJ66; -.
DR   OMA; SHFHSKC; -.
DR   OrthoDB; 1171480at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   GO; GO:0033557; C:Slx1-Slx4 complex; IBA:GO_Central.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR   GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.1440.10; -; 1.
DR   HAMAP; MF_03100; Endonuc_su_Slx1; 1.
DR   InterPro; IPR000305; GIY-YIG_endonuc.
DR   InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR   InterPro; IPR027520; Slx1.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF01541; GIY-YIG; 1.
DR   SMART; SM00465; GIYc; 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..439
FT                   /note="Structure-specific endonuclease subunit SLX1
FT                   homolog"
FT                   /id="PRO_0000383750"
FT   DOMAIN          166..253
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         335..390
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  50886 MW;  BA33D4EBAAC4C139 CRC64;
     METFILSSDS DDDCPPPPKR RSIEGVPKSF DGDKKMRFSF DVTRDIILED SEAPCSSNNI
     FTPSFRRDSN KTLLKTPVSL RRRSRSMNCM TPIVDTINEP PINQVCSAFV QKEIQLDDDD
     DDEKESSTEH ADDDLNLRAL LSPEKKKRKE KVDKRRPFGV EEVQNEFYGV YCLISRSERQ
     CYKNRCYIGY TVDPNRRIMQ HNGGRFKGGA KKTDSRGPWD MVCVVHGFPN HVAALRFEWA
     WQNPAVSKSL KEKQLKKERK ETPFAYQLRI ACELMNSEAF SRFALTFRWL NTKEELPFPI
     SCTPPNHVKL RYGKVKKEMS LVPAKSADYV AMGECRLCGK DIEKLWGLVR CISQSCHSHF
     HSKCLAEHGL KNKNEYADQI YPLKSNCPIC GHFYLWGDVV REQRRIIKVS TKCAEEFRNK
     VVRKDLPHRE ISSRLRLKK