ID A0A087SP99_AUXPR Unreviewed; 881 AA.
AC A0A087SP99;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Apurinic endonuclease-redox protein {ECO:0000313|EMBL:KFM27553.1};
GN ORFNames=F751_4132 {ECO:0000313|EMBL:KFM27553.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM27553.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM27553.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM27553.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2};
CC Note=Probably binds two magnesium or manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR604808-2};
CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC {ECO:0000256|ARBA:ARBA00007092}.
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DR EMBL; KL662149; KFM27553.1; -; Genomic_DNA.
DR RefSeq; XP_011400536.1; XM_011402234.1.
DR AlphaFoldDB; A0A087SP99; -.
DR STRING; 3075.A0A087SP99; -.
DR GeneID; 23615523; -.
DR KEGG; apro:F751_4132; -.
DR eggNOG; KOG1294; Eukaryota.
DR eggNOG; KOG2276; Eukaryota.
DR OrthoDB; 161558at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd09087; Ape1-like_AP-endo; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR004808; AP_endonuc_1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR00195; exoDNase_III; 1.
DR NCBIfam; TIGR00633; xth; 1.
DR PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR PANTHER; PTHR43270:SF12; SUCCINYL-DIAMINOPIMELATE DESUCCINYLASE; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:KFM27553.1};
KW Hydrolase {ECO:0000313|EMBL:KFM27553.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR604808-2};
KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604808-2};
KW Nuclease {ECO:0000313|EMBL:KFM27553.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028924}.
FT DOMAIN 18..246
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT DOMAIN 588..745
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT SITE 170
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 240
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ SEQUENCE 881 AA; 96004 MW; 79FCA3F90BE76CC7 CRC64;
MRAPALPSTA AAATILCWNV AGLRGLLKKD PTAIASLIAR EQPHVLCLQE IKLQTSHCDE
ELHNLLALDP EWQITWNCST AKKGYSGTAI LTRIPPVSTV CGMGSPGHDE EGRVLAAEFD
TFYLVTVYVP NSGEGLKRLE YRVGSWDEAF SSFIKKLEAR KPVVVCGDLN CARQSIDIHS
PKTNLRSAGF TQEERDSFQQ RYMDAGWVDA FRTRYPEHTG YTYWSYRFNL RARNKGWRLD
YFLAPSIPVY HRQEAALMQT SRKSGSGDVL ADSKDPVESG KVFFFYRPRV GLDHVGKLED
VQRFYLLLEP SQPGSKSRLI VIGKKRLPAI FNHEGMGVQR YQTTTMGERV VGACRAAGEG
AYSILEHGSG TNFVYRLELP TEPSEAQRMC GIELEGSFGL SVKNPNKTSN PAVGLREKAD
LPEALEDEFQ GYAWIAARDP KNVEILPTKG PRPVVFGQYI SRPEARTVLI YGHYDVQPPE
PLDKWTSGPF DPEERDGFLY GRGASDDKGG FLAAVQASGR AVEAVLRGGG GLRALNVKVL
IEGEEEVLSP HLEDFLAAHA SLLAADFALS ADGGQVGEGR PSLTLGYRGA AGIEVQVGAL
ARDVHSGMYG GAVQNPVRAL AQLLGSMFNA DGSVAVRGFY DRVRPITQAD RDDILAYNYD
EDEELKGGVG AVEAYGEEGF SSLERLWLRP TLEIVGFKGG HTGEGMKTIV PATAVAKLAA
RLVADQRPGE VVALLEAHIA AHHPPACNVT VRELGFAANP YSLDRASPVL ATAAEVLREV
LGAAPVHDRC GATIPALAAF QTLLGIDTVP FAFALPGDGP HAPDERVKLS MFHKGREAYV
RLLHRLDGLL PCLRALRPDV CGLELGVRHV LSDLQSTKER G
//
