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Database: UniProt
Entry: A0A1G5FNB1_9PROT
LinkDB: A0A1G5FNB1_9PROT
Original site: A0A1G5FNB1_9PROT 
ID   A0A1G5FNB1_9PROT        Unreviewed;       728 AA.
AC   A0A1G5FNB1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-JUN-2019, entry version 11.
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=SAMN05216308_11018 {ECO:0000313|EMBL:SCY40726.1};
OS   Nitrosospira sp. Nsp13.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=1855332 {ECO:0000313|EMBL:SCY40726.1, ECO:0000313|Proteomes:UP000198731};
RN   [1] {ECO:0000313|EMBL:SCY40726.1, ECO:0000313|Proteomes:UP000198731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nsp13 {ECO:0000313|EMBL:SCY40726.1,
RC   ECO:0000313|Proteomes:UP000198731};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FMVD01000010; SCY40726.1; -; Genomic_DNA.
DR   Proteomes; UP000198731; 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; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000198731};
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};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462054};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462035}.
FT   DOMAIN      639    720       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION        1     21       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1G5FNB1}.
SQ   SEQUENCE   728 AA;  82751 MW;  0442172F730DF929 CRC64;
     MSIKKKRKLR SLDPHLEREK QRYGHALPSR EFMLQILEEQ GVPVNEEALQ GLLEITEEEN
     EIFSRRVSAM VREGQIMRNR KGDICVVEKL NLIKGRIQGH PDGFGFLVPD DGSPDLFLSA
     KEMHKALHGD RVMVREIGVD RRGRREGTIV EVLERAVTQL VGRLHADHGI LFVEAENRRI
     SQDILIPSEE SMNAGAGQVV MVEIIQQPSK HAQPIGRIVE ILGEYTAPGM EIEIALRKHD
     LPNLFPPDVE KLSTRFPEKV LTEELAERED IRHLPLVTID GETARDFDDA VYCERDGKGF
     KLYVAIADVS HYVRPHDALD REALNRGNSV YFPRRVIPML PEVLSNGLCS LNPQVERLCM
     VCEMQLDAAG DFRDYRFYPA VMYSHARLTY TKVAGMLENP KGEDAKQYQA LLPHIQLLYK
     LFKVLLKART KRGAIDFETI ETQMIFNAQG KIERILPIKR NDAHRLIEEC MLAANVCASD
     FLQKHKQPTV YRVHEGPTPE KLAALRDFLK EFGVQLSGGD APSAKDYAKT LTRIKDRPDA
     QLLQTVMLRS LRQAVYSPDN VGHFGLAYES YTHFTSPIRR YPDLLVHRAI KAVLSGTVYS
     PGSWHELGMH CSQTERRADE ATRDVETWLK CYYMQDRIGE SFEGVVSGVT GFGLFVALDG
     IYVEGLVHIS ALPSDYFHFD ATKHMLLGER SGKRYRLGDR LRIRLVRVDL ESSKIDFVLA
     ENSDKDST
//
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