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Database: UniProt
Entry: M1N627_9CLOT
LinkDB: M1N627_9CLOT
Original site: M1N627_9CLOT 
ID   M1N627_9CLOT            Unreviewed;       763 AA.
AC   M1N627;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   08-MAY-2019, entry version 47.
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:AGF58852.1};
GN   ORFNames=Cspa_c51010 {ECO:0000313|EMBL:AGF58852.1};
OS   Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF58852.1, ECO:0000313|Proteomes:UP000011728};
RN   [1] {ECO:0000313|EMBL:AGF58852.1, ECO:0000313|Proteomes:UP000011728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium saccharoperbutylacetonicum N1-
RT   4(HMT).";
RL   Submitted (FEB-2013) 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; CP004121; AGF58852.1; -; Genomic_DNA.
DR   STRING; 931276.Cspa_c51010; -.
DR   EnsemblBacteria; AGF58852; AGF58852; Cspa_c51010.
DR   KEGG; csr:Cspa_c51010; -.
DR   PATRIC; fig|931276.5.peg.5151; -.
DR   KO; K12573; -.
DR   Proteomes; UP000011728; 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; 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; 4.
DR   TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR   TIGRFAMs; TIGR02063; RNase_R; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011728};
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:AGF58852.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011728};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462035}.
FT   DOMAIN      664    744       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   COILED      636    656       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   763 AA;  88162 MW;  D746E4B5E8EF0975 CRC64;
     MSILILNKIK SILSEVIVVV YRYIGILYND NTMEENIMGI KQTLASFMSE PAYRPMDIEE
     LIAIFDIKKN EYNAFKKTLR MMEEEGIITR TKKDRYMIAD ENNKEEGLIS GTLQLHSKGF
     GFLLPDEEGQ KDVFIPSNCM KGAMNGDKIA VKVTREDTNT KKREGEVVEI IERNTTKIVG
     IYEDSQNFGF VVSEDPRISK DIFISKKDRN SAKNGDVVTV KITKWPEGNR KAEGVVTEIL
     GRKGDRGIDI LIIIKKLGLP EEFTEKVLKY AEGISEEINE EEIKGRRDLR DLRMVTIDGE
     DAKDLDDAVS IEKLSNGNYK LGVHIADVSH YVRENNPLDK EALKRATSVY LIDRVIPMLP
     RKLSNGICSL NPRVDRLALT CFMEINNSGK VVNHEIVESI IKTNERMTYT DVTKILKDHD
     EELIKRYDYL YEDFKLMEEL CNILREKRTR RGAIDFEIAE AKITLNDLGK PIEIKPYDRE
     IANRVIEEFM LVANETVAEH MFWTHLPFVY RIHENPDEEK LAKFKEFVYN LGYNVHWTEE
     IIPKSFQEIL EKVKGKNEET VVSTLLLRSM MQARYAPECT GHFGLAAQYY CHFTSPIRRY
     PDLQIHRIIK EYLHGELDEK RINKLKNTVG YAAKQSSEME RKAQDAEREV DDLKKAEYMQ
     ERIGEEFDGI ISSVTSFGVF VELPNTVEGL VHITDLDDDY YIFNESHLSL MGERTKKIYK
     LGDKVKVECV HVDITNREVF FKITQEPKRE EAEEAANETL QPV
//
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