ID I4Z5N8_9BURK Unreviewed; 734 AA.
AC I4Z5N8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=LepocDRAFT_00002610 {ECO:0000313|EMBL:EIM31530.1};
OS Leptothrix ochracea L12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=735332 {ECO:0000313|EMBL:EIM31530.1, ECO:0000313|Proteomes:UP000053899};
RN [1] {ECO:0000313|EMBL:EIM31530.1, ECO:0000313|Proteomes:UP000053899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L12 {ECO:0000313|EMBL:EIM31530.1,
RC ECO:0000313|Proteomes:UP000053899};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stepanauskas R., Masland D.,
RA Poulton N., Emerson D., Fleming E., Woyke T.;
RT "Improved High-Quality Draft sequence of Leptothrix ochracea L12.";
RL Submitted (APR-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 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}.
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DR EMBL; JH660678; EIM31530.1; -; Genomic_DNA.
DR AlphaFoldDB; I4Z5N8; -.
DR HOGENOM; CLU_002333_7_0_4; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000053899; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; 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; 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:UP000053899};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 580..661
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 702..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 82018 MW; A77EA52E01A4F386 CRC64;
MQYPSQKFSL MSEIEGTVQG HRDGHGFLIT GMDEPDIYLS PQEMRAVLHR DRVRVRVIRQ
DRKGRPEGRI LEIIERRKTP IIGRLLHEGG QWIVAPEDRR FGQDILIPRH NVADAQVGQV
VAVELTEVAS LHTQPVGRIA EVLGDIDDPG MEIEIAVRKF EVPHRFSPET LAQAGKLPSR
LRAVDRQQRI DLTDVPLVTI DGEDARDFDD AVYCEPCRVD RGKGWRLLVA IADVSHYVKP
GQPLDNDAFE RSTSVYFPRR VIPMLPEKLS NGLCSLNPDE DRLSMVCDML VTAQGDVQAY
QFYPAVICSH ARLTYTTVAA LLANTRGPEA QMHADLVPQL IHLHEVYRAL LKARGVRGAV
DFETTETQIV CDDNGRIEKI VPRVRTEAHR LIEEAMLAAN VCAADFIERA KHPALFRVHE
GPTPEKRQTL INYLRSVGVT AELSEDPKPA ELQAIALQTR DRPDAVQIHT MLLRSMQQAI
YTPHNSGHFG LAYAAYTHFT SPIRRYPDLL VHRVIKALLQ AKRYKLEIPL PQVGATATAT
PAEAWDVAGA HCSANERRAD EASRDVEAWL KCKFMRDRLG EVYAGTVSAV TSFGLFVQLD
ALFVEGLIHI TELGGEYFRL DDARQELRGE RTGVRYGIGA RVRVQVSRVD LDGRRIDFRL
MTESQSVGAA SSAPSGGFGR ERLAGSEATL ASIKEADRAL RQVARDKKKK PTVRHARDEG
AGREKARPGR KGAR
//
