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Database: UniProt
Entry: C9LY73_SELS3
LinkDB: C9LY73_SELS3
Original site: C9LY73_SELS3 
ID   C9LY73_SELS3            Unreviewed;       867 AA.
AC   C9LY73;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   05-JUN-2019, entry version 72.
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   ECO:0000313|EMBL:EEX76267.1};
GN   ORFNames=Selsp_0281 {ECO:0000313|EMBL:AEB99257.1}, SELSPUOL_02432
GN   {ECO:0000313|EMBL:EEX76267.1};
OS   Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28).
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales;
OC   Selenomonadaceae; Selenomonas.
OX   NCBI_TaxID=546271 {ECO:0000313|EMBL:EEX76267.1, ECO:0000313|Proteomes:UP000003505};
RN   [1] {ECO:0000313|EMBL:EEX76267.1, ECO:0000313|Proteomes:UP000003505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35185 {ECO:0000313|EMBL:EEX76267.1}, and ATCC 35185 / DSM
RC   20758 / VPI D19B-28 {ECO:0000313|Proteomes:UP000003505};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B.,
RA   Courtney L., Fronick C., Harrison M., Strong C., Farmer C.,
RA   Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C.,
RA   Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEB99257.1, ECO:0000313|Proteomes:UP000011124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35185 {ECO:0000313|EMBL:AEB99257.1}, and ATCC 35185 / DSM
RC   20758 / VPI D19B-28 {ECO:0000313|Proteomes:UP000011124};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA   Wellnitz S., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Selenomonas sputigena DSM 20758.";
RL   Submitted (APR-2011) 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}.
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DR   EMBL; CP002637; AEB99257.1; -; Genomic_DNA.
DR   EMBL; ACKP02000050; EEX76267.1; -; Genomic_DNA.
DR   RefSeq; WP_006193796.1; NZ_GG698598.1.
DR   SMR; C9LY73; -.
DR   STRING; 546271.Selsp_0281; -.
DR   EnsemblBacteria; AEB99257; AEB99257; Selsp_0281.
DR   EnsemblBacteria; EEX76267; EEX76267; SELSPUOL_02432.
DR   KEGG; ssg:Selsp_0281; -.
DR   eggNOG; ENOG4105C40; Bacteria.
DR   eggNOG; COG0557; LUCA.
DR   KO; K12573; -.
DR   OMA; DWYEYRS; -.
DR   OrthoDB; 1602988at2; -.
DR   BioCyc; GCF_000160495-HMP:SELSPUOL_RS10565-MONOMER; -.
DR   Proteomes; UP000003505; Unassembled WGS sequence.
DR   Proteomes; UP000011124; Chromosome.
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; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF17876; CSD2; 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; 1.
DR   SUPFAM; SSF50249; SSF50249; 3.
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:UP000003505,
KW   ECO:0000313|Proteomes:UP000011124};
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, ECO:0000313|EMBL:EEX76267.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011124};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462035}.
FT   DOMAIN      632    712       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      728    867       Disordered. {ECO:0000256|MobiDB-lite:
FT                                C9LY73}.
FT   COMPBIAS    728    744       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                C9LY73}.
FT   COMPBIAS    755    788       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                C9LY73}.
FT   COMPBIAS    801    815       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                C9LY73}.
FT   COMPBIAS    837    859       Basic. {ECO:0000256|MobiDB-lite:C9LY73}.
SQ   SEQUENCE   867 AA;  96527 MW;  3B6223DC862DAB29 CRC64;
     MEQNELQERI VNYMRTAAYK PLTADDLAAA MNLAQEELAL FWTALEELEK TAAVIKTRHE
     RFGVPERMNL VVGRLSMSAK GFGFIIPEVR EKETDSDIFV PGVSLGGAMN GDRVVARISP
     SEIAGRSREG EIIRIVERAN EQIVGTFEES RHFGFVTPDD KKIGQDIFIP KGAVHGAKAG
     MKVVVRITKW PAGRRNAEGE VEEILGRAGE PGVDVLSVMS QYGLSEEFPA DVAAEAAAIE
     DAVSPEEFSG RRDRRGFRIV TIDGEDAKDL DDGVYAERRA DGSFFLGVYI ADVSWYVREN
     SPLDREARAR GTSVYLVDRV IPMLPKKLSN GICSLNAGED RLAMACEMEI GADGLVKSYE
     ILPVVIHVYR RLTYTLVNEI FAEGADAVRT ENADLLPLLT PLREVHDAME KARHERGSIG
     FDVPEIKVKL DESGKPVALI KRTGSLAESM IEQCMLAANE TVAEHMEKKE QPFLYRVHEQ
     PSDEKIERLN NLLATFSLHL VPNEAGEVAP KDVQQVLEKV KGRPEERIVS AVSLRSMQQA
     RYADAPLGHY GLAARHYTHF TSPIRRYPDL IVHRLLRETF ATGTIASERQ ERLRSLLPEI
     AEHTSARERI AIEAERETQD MKKIEYMAQF VGDAFDAVIS GVTAFGIFCE LENGVEGLVH
     VSSMVNDYYE YREDLYALVG GATHVSYRLG EPVRVVLVRA NIAERNLDFI LEDNGVFVAA
     KKKPEEGGVK RGESLKEKGA KKDARSKKGR GRKAAKEKRT DEIIADVKGD KRPEKTSAPA
     ETGEHKPHGK GHKGAKPHDK GRSARRPERF QAERQGALAD ESSSSRPKAF WMKPPKDLRK
     KGKKSAPKPE KKRRPHNKTQ RATANSD
//
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