ID A0A067LMU5_JATCU Unreviewed; 837 AA.
AC A0A067LMU5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Structure-specific endonuclease subunit SLX1 homolog {ECO:0000256|HAMAP-Rule:MF_03100};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_03100};
GN ORFNames=JCGZ_17331 {ECO:0000313|EMBL:KDP45724.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP45724.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP45724.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP45724.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
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. {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 a member of the SLX4 family.
CC {ECO:0000256|HAMAP-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 EMBL; KK914227; KDP45724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067LMU5; -.
DR STRING; 180498.A0A067LMU5; -.
DR Proteomes; UP000027138; 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:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd10455; GIY-YIG_SLX1; 1.
DR Gene3D; 3.40.1440.10; GIY-YIG endonuclease; 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 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 PROSITE; PS50164; GIY_YIG; 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 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:UP000027138}.
FT DOMAIN 50..132
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 96264 MW; 9C8CDD42616FCE1B CRC64;
MRKRTTKQRP KKPETMWQRT AKRRPEKLNP PREEEGDGNE QEDKSKEGKG FYACYLLTSL
CPRFKGHTYI GFTVNPRRRI RQHNGEITSG AFRTKKRRPW EMVFCIYGFP TNVSALQFEW
AWQHPTESVA VRQAAATFKS FSGVANKIKL AYTMLNLPAW QGLNITVNYF STKYSSHSAS
SPSLLEHMRI RVCPIDELPC YTETNESLFE GEDAEDRFDD TEEYENTTNI SETLNMNVMD
LQAYSTEEFP CYNRDEETSF EGEGSKVSKE NEKDSSTKYA NHSASSPSFR EQVKIRVCPI
NELPCYTETN ESLFEGEDAV KRFDDKEEYE NTTNRSETMN MNVIDLQAYS ANDFPYYNRV
EEILFEGEGS KVRKEDEEDC DSGNTSRTAK ETHADTIIQI SSNNATSHEE TRQFEEYSNM
QQSLRSISSF FLPTLEEDHM QPSVSINSVV GTALTGFSME EMLVNNTVPE LDWLNGKEYT
GKSDKDLQPI HSYTVPDEIE KKRKEKKRDE SLFEGEDAED RFDDTEEYEN TTNISETLNM
NVMDLQAYST EEFPCYNRDE ETSFEGEGSK VSKENEKDSS TKYANHSASS PSFREQVKIR
VCPINELPCY TETNESLFEG EDAVKRFDDK EEYENTTNRS ETMNMNVIDL QAYSANDFPY
YNRVEEILFE GEGSKVRKED EEDCDSGNTS RTAKETHADT IIQISSNNAT SHEETRQFEE
YSNMQQSLRS ISSFFLPTLE EDHMQPSVSI NSVVGTALTG FSMEEMLVNN TVPELDWLNG
KEYTGKSDKD LQPIHSYTVP DEIEVIDLLS PSPECRIRAS RKKRRVSIVC PEIIDLT
//
