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Database: UniProt
Entry: A0A099FGF1_9RHOB
LinkDB: A0A099FGF1_9RHOB
Original site: A0A099FGF1_9RHOB 
ID   A0A099FGF1_9RHOB        Unreviewed;       756 AA.
AC   A0A099FGF1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=IC63_02395 {ECO:0000313|EMBL:KGJ09321.1};
OS   Paracoccus sphaerophysae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=690417 {ECO:0000313|EMBL:KGJ09321.1, ECO:0000313|Proteomes:UP000029917};
RN   [1] {ECO:0000313|EMBL:KGJ09321.1, ECO:0000313|Proteomes:UP000029917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ09321.1,
RC   ECO:0000313|Proteomes:UP000029917};
RA   McGinnis J.M., Wolfgang W.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGJ09321.1, ECO:0000313|Proteomes:UP000029917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ09321.1,
RC   ECO:0000313|Proteomes:UP000029917};
RA   Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT   "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT   York State patients.";
RL   Submitted (OCT-2014) 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}.
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:KGJ09321.1}.
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DR   EMBL; JRKS01000003; KGJ09321.1; -; Genomic_DNA.
DR   RefSeq; WP_036716540.1; NZ_JRKS01000003.1.
DR   AlphaFoldDB; A0A099FGF1; -.
DR   STRING; 690417.IC63_02395; -.
DR   OrthoDB; 9764149at2; -.
DR   Proteomes; UP000029917; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_01895; RNase_R; 1.
DR   InterPro; IPR040476; CSD2.
DR   InterPro; IPR012340; NA-bd_OB-fold.
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; IPR003029; S1_domain.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
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; PF00773; RNB; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00955; RNB; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
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:UP000029917};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          633..714
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          722..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..747
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   756 AA;  83642 MW;  BC7682ADF8324523 CRC64;
     MNQFPTRQQI LDWIADNPDA TAKRDIAKAF NIKGSARIEL KRLLRELEAE GVVDRRRRSY
     RDHERLPPVS VLEILPPDAD GDLFARPMEW QGTAPMPRIL FSPRKADPAV APGERILARL
     TEVEGEDYAY QARLMRRIGA VAHKVVGIFR KETEGGRIVP IDKGQDRQWR VRGDATLDAQ
     DGELVEAEQV GSRNRLGLAQ ARIIERLGDP SAPRAVSLIA IYQHGIPDDF PDAVMAEADA
     TVPATMSGRE DLRALPLVTI DPADARDHDD AVAAMPDDDP RNPDGMVIWV AIADVAAYVR
     PGTALDREAR HRGNSTYFPD RVVPMLPDIL SGDLLSLHEG VDRPVIAVRM RLDARGNKIS
     HDFHRGMMHS AASLSYEQAQ AAADGTPDEA TAPLMDSVIR PLFAAYELLK SARARRQPLD
     LDLPERRIEL TPDGRVKSVA FRDRYDAHRL IEEFMVLANV AAAEELTRLR RPLLFRVHEE
     PSPEKLNALR DVAEASGFAL AKGQVLQTSH LNRLLAQAEG TDFDELINVS TLRSMTQAYY
     HPENFGHFGL ALKSYAHFTS PIRRYSDLIV HRALISGHGW GGGAKGGDGL SPQDIETLSE
     TAQHISDTER RSMAAERDTT DRYLAAYLAD RVGSEFAGRI SGVQRFGAFV KLDETGADGL
     LPIREIGREY FHFDRDRQVL EGADTGLTIG IGQRVTVRLA EAIPTTGGLT LELVEIEGRG
     IPAGPRGARG KGPRRRDVTS AKAGEARARK LRRIRK
//
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