SLX1_CRYNJ
ID SLX1_CRYNJ Reviewed; 487 AA.
AC P0CN80; Q55ZX6; Q5KP85;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 53.
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 {ECO:0000255|HAMAP-Rule:MF_03100}; OrderedLocusNames=CNA03830;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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}.
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DR EMBL; AE017341; AAW41340.1; -; Genomic_DNA.
DR RefSeq; XP_567159.1; XM_567159.1.
DR AlphaFoldDB; P0CN80; -.
DR SMR; P0CN80; -.
DR STRING; 5207.AAW41340; -.
DR PaxDb; P0CN80; -.
DR EnsemblFungi; AAW41340; AAW41340; CNA03830.
DR GeneID; 3253877; -.
DR KEGG; cne:CNA03830; -.
DR VEuPathDB; FungiDB:CNA03830; -.
DR eggNOG; KOG3005; Eukaryota.
DR HOGENOM; CLU_030739_0_0_1; -.
DR InParanoid; P0CN80; -.
DR OMA; HETHGIW; -.
DR OrthoDB; 844266at2759; -.
DR Proteomes; UP000002149; Chromosome 1.
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 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..487
FT /note="Structure-specific endonuclease subunit SLX1"
FT /id="PRO_0000383782"
FT DOMAIN 27..109
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT ZN_FING 262..328
FT /note="SLX1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT REGION 44..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 55142 MW; F05C940A5F2FDDFB CRC64;
MSDDAEVTNN KKTTKSTLLD GNHIFPPFYA CYLLRSKATA NSNRTYVGST PDPPRRIRQH
NGELKQGAWS TSRHRPWEMQ MIVYGFPSKL AALQFEWAWQ KPELSRHLRI RGEDQEYYHI
FTKDARRNWV ERKVCVAYAL ISLTPFNRLP LHVRFFNHET HGIWQSIHEQ AGVNTIQRGK
SRAKPVNPLH LLSQSVAPAV TIILDLGGVS GTSGKRRECT KGVMSHEGPI DVKDVEFRQG
FGVRGKWLEI RKRILSGQDL CCHLCQERIA FNDHLTFSIC PLAESQDCFC ITHLICLAKH
FQDEAPVEDR RAPSQPKILP YQGLCPNCKR TVQWGQHIRA CYARKEQVEK AEKAEKAEKA
EKAEKAEKAE KAEKAEKAEK AGRKVRQREM KTKKGDQSNG TVAQPESIYS ATPVHTTFGL
SNASATLIDP SMPARSMKSK DVGGEGIRHS THTDDSDGII SVYSETEDES ESEPEWEIFE
AEMMALS
