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Database: UniProt
Entry: A0A1C3ED63_9GAMM
LinkDB: A0A1C3ED63_9GAMM
Original site: A0A1C3ED63_9GAMM 
ID   A0A1C3ED63_9GAMM        Unreviewed;       902 AA.
AC   A0A1C3ED63;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   05-JUN-2019, entry version 17.
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=A8L45_18055 {ECO:0000313|EMBL:ODA31154.1};
OS   Enterovibrio pacificus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Enterovibrio.
OX   NCBI_TaxID=1080227 {ECO:0000313|EMBL:ODA31154.1, ECO:0000313|Proteomes:UP000094936};
RN   [1] {ECO:0000313|EMBL:ODA31154.1, ECO:0000313|Proteomes:UP000094936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAIM 1920 {ECO:0000313|EMBL:ODA31154.1,
RC   ECO:0000313|Proteomes:UP000094936};
RA   Gomez-Gil B., Enciso-Ibarra J.;
RT   "Genomic Taxonomy of the Vibrionaceae.";
RL   Submitted (MAY-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
CC         yield nucleoside 5'-phosphates.; EC=3.1.13.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01895,
CC         ECO:0000256|SAAS:SAAS01124678};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895,
CC       ECO:0000256|SAAS:SAAS00089931}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01895}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ODA31154.1}.
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DR   EMBL; LYBM01000040; ODA31154.1; -; Genomic_DNA.
DR   RefSeq; WP_068904757.1; NZ_LYBM01000040.1.
DR   EnsemblBacteria; ODA31154; ODA31154; A8L45_18055.
DR   BioCyc; GCF_001707825:A8L45_RS18055-MONOMER; -.
DR   Proteomes; UP000094936; 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   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; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
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; 1.
DR   SMART; SM00955; RNB; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 4.
DR   TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR   TIGRFAMs; TIGR02063; RNase_R; 1.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000094936};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462075};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00089915};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00446781};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094936};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462035}.
FT   DOMAIN      661    742       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION        1     32       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1C3ED63}.
FT   REGION      745    902       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1C3ED63}.
FT   COMPBIAS    758    793       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1C3ED63}.
FT   COMPBIAS    839    860       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1C3ED63}.
FT   COMPBIAS    879    902       Basic. {ECO:0000256|MobiDB-lite:
FT                                A0A1C3ED63}.
SQ   SEQUENCE   902 AA;  101362 MW;  AA4A9B2A3B02AE4D CRC64;
     MSPLEKETSM DKHLHSNDPH LDREAEKYEN PVPSREHLLE VIKGFSTPVS RDQLFEVLGL
     STEDQYEGLR RRLRAMERDG QLVFTRRQCY ALPERLDLVK GTVIGHRDGF GFLRPEGKGN
     REDWLLPHHQ MKSVMHGDFI LVQPAGTDKR GRKEARVVRV LEERKGQIVG RYFVENGQGF
     VVPDDSRLGQ DIVIPDDSRK GARMGNVVVV EIFQRPTRQH NPVGRIVDVL GENMAPGMEI
     EIAMRTHNIP NEWPKEVGQQ IKRLTEEVPE EAKQGRVDLR DLPLVTIDGE DARDFDDAVY
     CEKKRSGGWR LWVAIADVSY YVRPDSALDK EAINRGNSVY FPSQVVPMLP EVLSNGLCSL
     NPQVDRLCMV CEMTVSAAGK LSGFKHYEAV MNSHARLTYT KVSQILDGDK ELRDRYNNLV
     PHLEQLNAMY KALKGAREQR GAIEFETRET KFLFNAMRKI DRIVPVERND AHKIIEECMI
     LANIASARFV EKNKEAALYR VHEAPGEERL TGFKDFLKEL GLSLHGGLDP SPTDYAQLAH
     AIQNRPDQEL IQTMLLRSMK QAVYQADNAG HFGLALKQYA HFTSPIRRYP DLLLHRAIKY
     LLAKQEGHNT DKWTPTGGYH YSPDDMDVMG EQCSMTERRA DDATRDVSDW LKCEYMQDHV
     GDIMDGVIAN VTGFGFFVRL NELHIDGLVH ISNLDNDYYR FDMVGQKLVG ESSGRIFRLG
     DEVQVKVLSV NLDERMIDFE LAGSKRRARG QGKTARKNAR SHSRDDSRSS NTRRKKGRAE
     SGKDAEASRE RMSVRQQLKS GAIPQVEGDK APGGKKGGRK GKKKGKGGKP GAKNTGVAKG
     PSNAKQNGNA KPTGNANGAK QNGGADKPAA SGNPARKKTK AEKARKKKAQ KRKPAQSGNK
     KK
//
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