ID E7GB48_9FIRM Unreviewed; 734 AA.
AC E7GB48;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=HMPREF9488_01988 {ECO:0000313|EMBL:EFW04864.1};
OS Coprobacillus cateniformis.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Coprobacillus.
OX NCBI_TaxID=100884 {ECO:0000313|EMBL:EFW04864.1, ECO:0000313|Proteomes:UP000003157};
RN [1] {ECO:0000313|EMBL:EFW04864.1, ECO:0000313|Proteomes:UP000003157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=29_1 {ECO:0000313|EMBL:EFW04864.1,
RC ECO:0000313|Proteomes:UP000003157};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Sibley C.D.,
RA White A., Strauss J., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Coprobacillus sp. strain 29_1.";
RL Submitted (DEC-2010) 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|ARBA:ARBA00004496,
CC 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:EFW04864.1}.
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DR EMBL; ADKX01000033; EFW04864.1; -; Genomic_DNA.
DR RefSeq; WP_008789089.1; NZ_GL636579.1.
DR AlphaFoldDB; E7GB48; -.
DR STRING; 100884.GCA_000269565_02083; -.
DR GeneID; 78229930; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_4_1_9; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000003157; 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; 2.
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; IPR003029; S1_domain.
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; 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; Nucleic acid-binding proteins; 4.
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:UP000003157};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 614..694
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 705..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..734
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 85107 MW; C3352DB06AD9B249 CRC64;
MKEEILQLLE DQTYTRRKMD ELAEHFGMTS TEDYIIFIKL INSMEDEGLI MRSRLNDYYL
INQLHFYSGT VQMNKKGFAF VKVDEEREFY IHENNMKDAF DKDTVLIEKI PSHGSREEGR
VVRVIKRGQM RYVGEVKRGK RDCYVDVDDA KFYQPIFVDS AHLHGAVPGH KVVVEIKTYK
PQIKGNIVKV IGHRNDPGVD ILSIVHAHDV DIEFPKEVYE QIEAINDEID PTDIQNRVDL
RSEMIVTIDG DDAKDLDDAI SLKKLANGHY QLGVHIADVS YYVTEGSPLD KEAVKRGTSI
YLVDRVIPML PHKLSNGICS LNPNTDRYTI SCIMEIDNNG EVVNHDIQPT VIHSSYRMTY
NNVNKILDGD VHVQQQYQEV VPLFFLMQEL ALLLRSKRDD RGAIDFDVNE AKVLVDDKGK
PIDIVPRTRG ASDKIIEEFM LRANETVAQH FKWMDLPFIY RVHEHPKLKK LQQFVSIVKP
LGYTIKGSLE HVYPNELSAI VDASKGTEEH TIISTLLLRC MQKARYDRQC LGHFGLADEY
YTHFTSPIRR YPDLLVHRCI RNFLFDQNYE ATAHFEEVIP LLAEQSSFRE REAIDIEREV
TDMKMAEYMS YHIGEEFEGM ISSITQFGFF VELPNTIDGL VHMTELTDDY YHYDEKNLML
VGEMTGKTYK LSDKVKVKVI SCSKKDRTID FELVGQKARI KKKKTIQIND KKVKTNPRKK
GKINKSKRFP RKRR
//
