GenomeNet

Database: UniProt
Entry: B6W7V2_9FIRM
LinkDB: B6W7V2_9FIRM
Original site: B6W7V2_9FIRM 
ID   B6W7V2_9FIRM            Unreviewed;       700 AA.
AC   B6W7V2;
DT   20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2009, sequence version 1.
DT   27-MAR-2024, entry version 84.
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:EEB36351.1};
GN   ORFNames=ANHYDRO_00651 {ECO:0000313|EMBL:EEB36351.1};
OS   Anaerococcus hydrogenalis DSM 7454.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Anaerococcus.
OX   NCBI_TaxID=561177 {ECO:0000313|EMBL:EEB36351.1, ECO:0000313|Proteomes:UP000005451};
RN   [1] {ECO:0000313|EMBL:EEB36351.1, ECO:0000313|Proteomes:UP000005451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7454 {ECO:0000313|EMBL:EEB36351.1,
RC   ECO:0000313|Proteomes:UP000005451};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB36351.1, ECO:0000313|Proteomes:UP000005451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7454 {ECO:0000313|EMBL:EEB36351.1,
RC   ECO:0000313|Proteomes:UP000005451};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Anaerococcus hydrogenalis (DSM 7454).";
RL   Submitted (OCT-2008) 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:EEB36351.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABXA01000019; EEB36351.1; -; Genomic_DNA.
DR   RefSeq; WP_004813236.1; NZ_ABXA01000019.1.
DR   AlphaFoldDB; B6W7V2; -.
DR   STRING; 561177.ANHYDRO_00651; -.
DR   eggNOG; COG0557; Bacteria.
DR   Proteomes; UP000005451; 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; 3.
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; 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; SM00357; CSP; 2.
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   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          619..698
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   700 AA;  81528 MW;  2B3202D22A3CD81D CRC64;
     MNFKDLILNI VNDENYKPMT IKEMLKYLDC DKYIKKDVKK IIKKLAKDNE IKISSKKKIH
     PLSTEDKSLI GQINLAQGGY GFFISDNKDF KDVFISANNL NTANNLDRVR IKIIKNKEFG
     KNAEGKVVEI IERNSNKIVG LYQKNKGFGF VISDSNNITS DIYVDEKNSK KAKSNDKVLV
     EIINYPKKGS PEGKVIEVLG NKDEANVDLI SIVKSHGLKE NFSKKVKKEA VFIEKDVDLS
     KVKNREDLRD LFTVTIDGRD SKDFDDAISI EKDNEDYILY VHIADVSHYV KEKSEIDKEA
     YQRGNSTYLY NLVLPMLPEE LSNGICSLNP NENRLSLSLK MKINDKGKVI DYKIYKALIR
     SNYRLVYDDV NDYLDYNKKV YDDEVLLEKL DLFNDLYKIL KKKREKRGSI DFNFTESQID
     VSNQGDVLNI SLFERGSANK MIEEFMLVSN ETIASLFAFM DFPSIYRIHE KPKEEKVESF
     KNILNTLGYN IKGKELHPKD FQDILKQIKG KDDESLINML MLRTMRKAKY TNYRDMHFGL
     ATKYYTHFTA PIRRYPDLIV HRLVKDFIDN KLESINQTSL EKKLSKFAEH LSITERNSED
     CERDVEDLYK CKYMKKFIGE RFEGIISSIT DFGIFVELEN TVEGCFMYKF SDSHFEYIED
     KLSCINIDKN KRYKIGQKVM IEVKNVDLDK RNIDFDLMEG
//
DBGET integrated database retrieval system