ID J2IGT6_9ALTE Unreviewed; 790 AA.
AC J2IGT6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=AEST_07280 {ECO:0000313|EMBL:EJI86412.1};
OS Alishewanella aestuarii B11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alishewanella.
OX NCBI_TaxID=1197174 {ECO:0000313|EMBL:EJI86412.1, ECO:0000313|Proteomes:UP000012043};
RN [1] {ECO:0000313|EMBL:EJI86412.1, ECO:0000313|Proteomes:UP000012043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11 {ECO:0000313|EMBL:EJI86412.1,
RC ECO:0000313|Proteomes:UP000012043};
RX PubMed=22965096; DOI=10.1128/JB.01255-12;
RA Jung J., Choi S., Chun J., Park W.;
RT "Genome Sequence of Pectin-Degrading Alishewanella aestuarii Strain B11T,
RT Isolated from Tidal Flat Sediment.";
RL J. Bacteriol. 194:5476-5476(2012).
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:EJI86412.1}.
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DR EMBL; ALAB01000005; EJI86412.1; -; Genomic_DNA.
DR RefSeq; WP_008607104.1; NZ_ALAB01000005.1.
DR AlphaFoldDB; J2IGT6; -.
DR PATRIC; fig|1197174.4.peg.714; -.
DR Proteomes; UP000012043; 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; IPR013668; RNase_R_HTH_12.
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; PF08461; HTH_12; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 640..721
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 746..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 88686 MW; 7100B46879A53944 CRC64;
MTVNDPHLAR EQEKYDNPIP SREFILEHIE KRQQPAYFEE LVSELGLNDD EAIFALKKRL
RAMERDGQLL FTKSKRYGLV DHMDLVKGTV IGHREGFGFL KLEQGGPDWY LPFHEMQRLL
PGDKVLATAA SVKSKDKIEA RVVRVLEPRS EAIVGRYYKD HALCVVVPDD ARICQDIIVP
EGEQGAARHG QVVLVEITQR PSKRVNAMGR VVEVLGEHMA PGMEIEVAIR NHQIPHVFSD
AVIQQVAKFG EEVPAAAKQG RVDLTQLPLV TIDGEDARDF DDAVYAEAKE NGGWKLWVAI
ADVSAYVQFG TPLDHSALER GNSVYFPDHV VPMLPEALSN GLCSLNPHVD RLCFVAEMHI
SAHGKLESYQ FYEAVMHSAA RFTYNKVHAI LQGDPKLRQE YAAQLTNLET LYSLYKKLAK
VRAQRGAIEF ETVETRFIFN SHRKIEQIVP VHRNEAHKII EECMIMANVA AARFIEKHEA
HALFRVHERP DGDRFANFKR FLAELGIEAN LSDEPTPLEL TEVLARLSER PDRELIETTM
LRSMKQAVYQ GDNQGHFGLA LEAYAHFTSP IRRYPDLVLH RAIKAILAKQ GQQVTGPKAY
IEKDMAPLGE QCSMTERRAD DATREVADWL KCEYMQDHLG SEFPGVVSTV TNFGLFVRLS
DLYIEGLVHV TSLQNDYYRF DTERQILTGE HSGVSYRMGD AVTVKVVAVN LEARKIDLVL
VGEIRTQVSG RQIKASKNAA FEEKLARQAG KTAPAKAGKV TKAGKTTKAA KAPAGKKPAA
PKAKKSKSRR
//
