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Database: UniProt
Entry: A0A1G5PJW1_9GAMM
LinkDB: A0A1G5PJW1_9GAMM
Original site: A0A1G5PJW1_9GAMM 
ID   A0A1G5PJW1_9GAMM        Unreviewed;       725 AA.
AC   A0A1G5PJW1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Ribonuclease R {ECO:0000256|HAMAP-Rule:MF_01895};
DE            Short=RNase R {ECO:0000256|HAMAP-Rule:MF_01895};
DE            EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01895};
GN   Name=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN   ORFNames=SAMN03097708_00265 {ECO:0000313|EMBL:SCZ49794.1};
OS   Thiohalomonas denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thiohalomonas.
OX   NCBI_TaxID=415747 {ECO:0000313|EMBL:SCZ49794.1, ECO:0000313|Proteomes:UP000199648};
RN   [1] {ECO:0000313|EMBL:SCZ49794.1, ECO:0000313|Proteomes:UP000199648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLD2 {ECO:0000313|EMBL:SCZ49794.1,
RC   ECO:0000313|Proteomes:UP000199648};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC       monophosphates and is involved in maturation of structured RNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_01895}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.13.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001849, ECO:0000256|HAMAP-
CC         Rule:MF_01895};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01895}.
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DR   EMBL; FMWD01000001; SCZ49794.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5PJW1; -.
DR   STRING; 415747.SAMN03097708_00265; -.
DR   OrthoDB; 9764149at2; -.
DR   Proteomes; UP000199648; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04471; S1_RNase_R; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR   HAMAP; MF_01895; RNase_R; 1.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR040476; CSD2.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR013223; RNase_B_OB_dom.
DR   InterPro; IPR001900; RNase_II/R.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   InterPro; IPR004476; RNase_II/RNase_R.
DR   InterPro; IPR011805; RNase_R.
DR   InterPro; IPR013668; RNase_R_HTH_12.
DR   InterPro; IPR003029; S1_domain.
DR   NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR   NCBIfam; TIGR02063; RNase_R; 1.
DR   PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR   PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR   Pfam; PF17876; CSD2; 1.
DR   Pfam; PF08461; HTH_12; 1.
DR   Pfam; PF08206; OB_RNB; 1.
DR   Pfam; PF00773; RNB; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00357; CSP; 2.
DR   SMART; SM00955; RNB; 1.
DR   SMART; SM00316; S1; 2.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_01895};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01895};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199648};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          642..723
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   725 AA;  82397 MW;  5BD5B2619CDB2108 CRC64;
     MAKRFSNKKD PHQTREARKY ENPIPSREFI MDLLAEQGRP MARQQIAKAL KLEGDEPLEA
     LRRRLRAMER DGQLMQNRRG GYGLISKMDL VRGRVVGHAD GFGFLIPDEG GEDLFLSPKE
     MHGALHGDRV VARVSGIDRR GRKEGTIVEV LEHGNTHVVG RYYVEGGVGF LIPDNKRINQ
     DILVPLDQVY GAEFGQLVTV ELIEYPTRYR QAIGRVIEIL GDHMAPGMEV DLAIRAHGLP
     HEWSVLMDTE IAELPREVAE IDKEGRTDLR DMHLVTIDGE DAKDFDDAVF CEPRGDGWRL
     VVAIADVSHY VRPGGALDAE ARVRGNSVYF PGRVIPMLPE ALSNGLCSVN PDVDRLVMVC
     DMEVSARGKL EGYRFYPAVM RSHARLTYNK VAAMLVDNDR ELREQYRHVV PDLENLYNVF
     HALHAERKRR GAIDFETTET RIVFGENKKI DCIVPVERND AHRLIEECML IANVATADFL
     SSSKLPSLYR VHPGPSLEKL ERVREFLGEL GLSLEGGDEP QPKDYGTLLD QVRGRSDAYL
     IQTVLLRSLA QAVYTPDNKG HFGLSYKAYA HFTSPIRRYP DLLVHRAIRH RLSNESAEEF
     HYSMEDMVLL GEHCSMTERR ADDATRDATD WLKCEFMMDR VGDEYDGIIT GVTGFGLFVT
     LDDIHAEGLV HVTALSNDYY HFDPAKHRLT GERTRRMYRL ADKVRIRVLA VNLDERKIDF
     EMVEE
//
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