ID M1ZED2_NITG3 Unreviewed; 193 AA.
AC M1ZED2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Oligoribonuclease {ECO:0000256|HAMAP-Rule:MF_00045};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00045};
GN Name=orn {ECO:0000256|HAMAP-Rule:MF_00045,
GN ECO:0000313|EMBL:CCQ91919.1};
GN ORFNames=NITGR_90058 {ECO:0000313|EMBL:CCQ91919.1};
OS Nitrospina gracilis (strain 3/211).
OC Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC Nitrospinales; Nitrospinaceae; Nitrospina.
OX NCBI_TaxID=1266370 {ECO:0000313|EMBL:CCQ91919.1, ECO:0000313|Proteomes:UP000011704};
RN [1] {ECO:0000313|EMBL:CCQ91919.1, ECO:0000313|Proteomes:UP000011704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3/211 {ECO:0000313|EMBL:CCQ91919.1,
RC ECO:0000313|Proteomes:UP000011704};
RX PubMed=23439773; DOI=10.3389/fmicb.2013.00027;
RA Luecker S., Nowka B., Rattei T., Spieck E., and Daims H.;
RT "The genome of Nitrospina gracilis illuminates the metabolism and evolution
RT of the major marine nitrite oxidizer.";
RL Front. Microbiol. 4:27-27(2013).
CC -!- FUNCTION: 3'-to-5' exoribonuclease specific for small
CC oligoribonucleotides. {ECO:0000256|HAMAP-Rule:MF_00045}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00045}.
CC -!- SIMILARITY: Belongs to the oligoribonuclease family.
CC {ECO:0000256|ARBA:ARBA00009921, ECO:0000256|HAMAP-Rule:MF_00045}.
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:CCQ91919.1}.
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DR EMBL; CAQJ01000099; CCQ91919.1; -; Genomic_DNA.
DR RefSeq; WP_005011265.1; NZ_HG422173.1.
DR AlphaFoldDB; M1ZED2; -.
DR STRING; 1266370.NITGR_90058; -.
DR HOGENOM; CLU_064761_2_0_0; -.
DR InParanoid; M1ZED2; -.
DR OrthoDB; 9801329at2; -.
DR Proteomes; UP000011704; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR CDD; cd06135; Orn; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR HAMAP; MF_00045; Oligoribonuclease; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR022894; Oligoribonuclease.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR11046; OLIGORIBONUCLEASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11046:SF0; OLIGORIBONUCLEASE, MITOCHONDRIAL; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00045};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_00045};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00045, ECO:0000313|EMBL:CCQ91919.1};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_00045};
KW Reference proteome {ECO:0000313|Proteomes:UP000011704}.
FT DOMAIN 8..181
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT ACT_SITE 130
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00045"
SQ SEQUENCE 193 AA; 22485 MW; FBD7BD6508D1BF35 CRC64;
MSLVDSSNLV WMDLEMTGLD PDKEEIIEIA TIVTDSQLNI LAEGPCLVIH QDDAILERMD
DWNQKTHSAS GLIQKVKEST LTVEEAEQRT LDFIKQYVPY KTSPLCGNSI QQDRRFLDRY
MKNLTDYLHY RNIDVTSIKE VIRRWYPNGT RLPKKSDAHM ALTDVRESIE ELIFYRNNFF
VDVSNYMSEE GNL
//
