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Database: UniProt
Entry: R7CSZ5_9FIRM
LinkDB: R7CSZ5_9FIRM
Original site: R7CSZ5_9FIRM 
ID   R7CSZ5_9FIRM            Unreviewed;       678 AA.
AC   R7CSZ5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   05-JUN-2019, entry version 31.
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=BN625_00538 {ECO:0000313|EMBL:CDD81125.1};
OS   Dialister sp. CAG:357.
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Dialister; environmental samples.
OX   NCBI_TaxID=1262869 {ECO:0000313|EMBL:CDD81125.1, ECO:0000313|Proteomes:UP000018365};
RN   [1] {ECO:0000313|EMBL:CDD81125.1, ECO:0000313|Proteomes:UP000018365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:357 {ECO:0000313|Proteomes:UP000018365};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) 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:CDD81125.1}.
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DR   EMBL; CBHT010000196; CDD81125.1; -; Genomic_DNA.
DR   Proteomes; UP000018365; 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; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018365};
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:SAAS00089892};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018365};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462035}.
FT   DOMAIN      565    645       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      653    678       Disordered. {ECO:0000256|MobiDB-lite:
FT                                R7CSZ5}.
FT   COILED      537    557       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    660    678       Basic. {ECO:0000256|MobiDB-lite:R7CSZ5}.
SQ   SEQUENCE   678 AA;  76889 MW;  638CA79095960D15 CRC64;
     MEKTEKLVYK PGVTLEGIYK AYSPRFGFLI TDDDHEDVYI GEDNHLNAVN NDKVEVKTIK
     GETGRHNTEG RITRVIERAN DTFVCTYEML KDGGEAVPID EKVDMVIEIP EGQEMEATTG
     ARVIVEVTEW PGKWTDAKGH VTEVIGYEGD KGLDIDIIIA QHRLPHVFSD ELMKEADALP
     REVVPENGVA DFRDLPIVTI DGPDSKDLDD AVYCIRKENG HFELGVHIAD VSRYVKKGML
     LDEEAYRRGN SVYLADRVIP MLPFQLSNDL CSLNHDEDRY AMSCVMDVDQ NGNVHTEKIT
     PSMVRVARRC NYPEINKAFE EGIEPDDLKP FLPMLKDLKA CADCLRKNRS ERGALNFDFP
     EYKVVLDLDG TPLRIEKRIR GAAEMMIEDA MIAANEAVAR FLEKTGNTSV YRVHDHPDEE
     KLNALKRLVS IMGLPIHIPE DPTPKDIQKL LESVEGEDIE PVVQVMTLRS LPQACYKTEN
     AGHFGIASKC YTHFTSPIRR YPDLMVHRLI RQALSEQLKK NQLKAQTDFL VRACDHCSET
     EQNATQTERD VDDLKMTEYM IPFVGEPFDA HITGITRFGI FVGLDNGVEG LIHIDTMEDD
     EYVYQEDSMT LKGRFSGKTY SMGMPVRVTL VKADKERKEV DFFMGEIHSP LNLEKKVRSS
     SKSHSKKGKK NKKSKGRR
//
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