ID U3A3S3_VIBPR Unreviewed; 289 AA.
AC U3A3S3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Probable endonuclease 4 {ECO:0000256|HAMAP-Rule:MF_00152};
DE EC=3.1.21.2 {ECO:0000256|HAMAP-Rule:MF_00152};
DE AltName: Full=Endodeoxyribonuclease IV {ECO:0000256|HAMAP-Rule:MF_00152};
DE AltName: Full=Endonuclease IV {ECO:0000256|HAMAP-Rule:MF_00152};
GN Name=nfo {ECO:0000256|HAMAP-Rule:MF_00152,
GN ECO:0000313|EMBL:GAD67997.1};
GN ORFNames=VPR01S_10_01930 {ECO:0000313|EMBL:GAD67997.1};
OS Vibrio proteolyticus NBRC 13287.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219065 {ECO:0000313|EMBL:GAD67997.1, ECO:0000313|Proteomes:UP000016570};
RN [1] {ECO:0000313|EMBL:GAD67997.1, ECO:0000313|Proteomes:UP000016570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13287 {ECO:0000313|EMBL:GAD67997.1,
RC ECO:0000313|Proteomes:UP000016570};
RA Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Vibrio proteolyticus NBRC 13287.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves
CC phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating
CC a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
CC {ECO:0000256|HAMAP-Rule:MF_00152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end-
CC products.; EC=3.1.21.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00152};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00152};
CC Note=Binds 3 Zn(2+) ions. {ECO:0000256|HAMAP-Rule:MF_00152};
CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
CC {ECO:0000256|ARBA:ARBA00005340, ECO:0000256|HAMAP-Rule:MF_00152}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD67997.1}.
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DR EMBL; BATJ01000010; GAD67997.1; -; Genomic_DNA.
DR RefSeq; WP_021705968.1; NZ_BATJ01000010.1.
DR AlphaFoldDB; U3A3S3; -.
DR STRING; 1219065.VPR01S_10_01930; -.
DR eggNOG; COG0648; Bacteria.
DR Proteomes; UP000016570; Unassembled WGS sequence.
DR GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd00019; AP2Ec; 1.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR HAMAP; MF_00152; Nfo; 1.
DR InterPro; IPR001719; AP_endonuc_2.
DR InterPro; IPR018246; AP_endonuc_F2_Zn_BS.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR NCBIfam; TIGR00587; nfo; 1.
DR PANTHER; PTHR21445:SF0; APURINIC-APYRIMIDINIC ENDONUCLEASE; 1.
DR PANTHER; PTHR21445; ENDONUCLEASE IV ENDODEOXYRIBONUCLEASE IV; 1.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR SMART; SM00518; AP2Ec; 1.
DR SUPFAM; SSF51658; Xylose isomerase-like; 1.
DR PROSITE; PS00729; AP_NUCLEASE_F2_1; 1.
DR PROSITE; PS00730; AP_NUCLEASE_F2_2; 1.
DR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00152};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00152};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_00152,
KW ECO:0000313|EMBL:GAD67997.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00152};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00152}; Nuclease {ECO:0000256|HAMAP-Rule:MF_00152};
KW Reference proteome {ECO:0000313|Proteomes:UP000016570};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00152}.
FT DOMAIN 29..286
FT /note="Xylose isomerase-like TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01261"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
SQ SEQUENCE 289 AA; 32469 MW; 7CFF5B1408AFA147 CRC64;
MTQWKKRVGE KFIGAHVSAA GGVDKAPIRA HEIGANAFAL FTKNQRQWKA KPLDIATIEA
FKTNCARFGF SAEQILPHDS YLINLGAPEE EKLNKSRAAF VDEFERCHQL GLTLLNFHPG
SHLNQISEQE CLAKIAESIN IAHRSVPEVV AVIENTAGQG TNLGWQFEHL AEIIDQVEDK
SRVGVCIDTC HTFAAGYDLS SKAACESTFA NFERVVGMHY LRAMHLNDSK IPLSGRVDRH
HSLGIGEIGW DCFEYIAKDQ RFDGIPLILE TIDPSIWHQE IRQLREFYQ
//
