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Database: UniProt
Entry: H9GM13_ANOCA
LinkDB: H9GM13_ANOCA
Original site: H9GM13_ANOCA 
ID   H9GM13_ANOCA            Unreviewed;       268 AA.
AC   H9GM13;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 2.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSACAP00000014957.3};
GN   Name=slx1a {ECO:0000313|Ensembl:ENSACAP00000014957.3};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000014957.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000014957.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000014957.3};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000014957.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|HAMAP-Rule:MF_03100}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03100};
CC   -!- SUBUNIT: Forms a heterodimer with SLX4. {ECO:0000256|HAMAP-
CC       Rule:MF_03100}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03100}.
CC   -!- SIMILARITY: Belongs to the SLX1 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03100}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03100}.
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DR   RefSeq; XP_008115360.1; XM_008117153.2.
DR   AlphaFoldDB; H9GM13; -.
DR   STRING; 28377.ENSACAP00000014957; -.
DR   Ensembl; ENSACAT00000015260.4; ENSACAP00000014957.3; ENSACAG00000015221.4.
DR   GeneID; 100567090; -.
DR   KEGG; acs:100567090; -.
DR   CTD; 548593; -.
DR   eggNOG; KOG3005; Eukaryota.
DR   GeneTree; ENSGT00390000013368; -.
DR   HOGENOM; CLU_030739_0_0_1; -.
DR   OrthoDB; 276644at2759; -.
DR   TreeFam; TF352344; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000015221; Expressed in kidney and 12 other cell types or tissues.
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 DNA endonuclease 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   CDD; cd10455; GIY-YIG_SLX1; 1.
DR   Gene3D; 3.40.1440.10; GIY-YIG endonuclease; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR048749; SLX1_C.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR20208; STRUCTURE-SPECIFIC ENDONUCLEASE SUBUNIT SLX1; 1.
DR   PANTHER; PTHR20208:SF10; STRUCTURE-SPECIFIC ENDONUCLEASE SUBUNIT SLX1; 1.
DR   Pfam; PF01541; GIY-YIG; 1.
DR   Pfam; PF21202; SLX1_C; 1.
DR   SUPFAM; SSF82771; GIY-YIG endonuclease; 1.
DR   PROSITE; PS50164; GIY_YIG; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_03100};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_03100};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_03100};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_03100};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03100};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_03100};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03100};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          7..91
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000259|PROSITE:PS50164"
FT   DOMAIN          177..232
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   268 AA;  30807 MW;  7B5FE0E69C76A719 CRC64;
     MVVEVCSFFG VYLLYCTNPR YHGRIYIGFT VNPERRIIQH NAGKRRGGAW KTSGRGPWDM
     VLIVHGFPSD VAALRFEWAW QHPHSSRRLN HVTRRTSRER QFDFHLRVLA HMLRTAPWCR
     LPLTIRWLKQ EYARDFPPDL EPPLHMPVAF GPVRAVKETK GAKAAPSEGQ GVTLKRCSVC
     LKRFQEGDDD ILLHCFHPGC TMVAHIMCLA NFFLEKEPDH ILPIEGPCPG CKNLVLWGDL
     IRHHKGCYGD LEADPTSSQE HWANELQL
//
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