ID K8GLJ4_9CYAN Unreviewed; 781 AA.
AC K8GLJ4;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=OsccyDRAFT_3132 {ECO:0000313|EMBL:EKQ68594.1};
OS Leptolyngbyaceae cyanobacterium JSC-12.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ68594.1, ECO:0000313|Proteomes:UP000001332};
RN [1] {ECO:0000313|EMBL:EKQ68594.1, ECO:0000313|Proteomes:UP000001332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ68594.1,
RC ECO:0000313|Proteomes:UP000001332};
RG DOE Joint Genome Institute;
RA Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL Submitted (OCT-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}.
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:EKQ68594.1}.
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DR EMBL; AJUB01000011; EKQ68594.1; -; Genomic_DNA.
DR AlphaFoldDB; K8GLJ4; -.
DR STRING; 864702.OsccyDRAFT_3132; -.
DR PATRIC; fig|864702.5.peg.3355; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_3_3; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000001332; Chromosome.
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; 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 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; 3.
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:UP000001332};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 675..756
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 758..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..781
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 88021 MW; 886049B39928802E CRC64;
MEFSIAALLA NFTDDKLVAP KALEKKLDCN DDNSIRSLQI ALDALEKIGV LAKERGRYRR
IYEEGVIEGK LRCSSKGFCF AIQDVEGADD IYIRESQLNN AWNGDRVLVK VTKEGSRRRS
PEGEVKLILE RSNPSVLARV KQVDSDYRAV PLDDRLLFEL ALQENGIDLE QAIDQLVHVQ
VTRYPLGQHP PQGRIARILG GDSEAADVDI VCCKHDLPHE FPSAIQPAAK ALPTKISKTE
IKRRVDLRDL TTLTIKANPE DSNDSLDDAI TLERTEDDQW RLGIHIADVS YYVEPDSVID
REAQKRGVSV YLGDLVIPML PSQISGNLCA FLVGKDRLAL SVLVTLNDEG EVLEYAIHPT
VIQVDYQLSY DQAEAILERS EAEDDGDLEE FAPIFELLDD LAAVSHALKE QRRKRGAFEL
NLPEKPLSSD DADAQNKSLL TPKFHYDDEG ALGAMVVTPS AQTHAIIAEF MLLANQLVAA
HLQALGVPGI YRVHPTPDPE DVQELMKLAG SMGIDLHLEQ ENEVHPQDYQ HFTQKFAESD
AERVLTYLLL ETLKPAFYST TPKSHFGLAL EQGYTHFTSP VRRYPDLLVH RVLHAVFELG
RDRKTTRAKE VVDLRHSSCH GEISWNVLPP EVHQELENQF HAIVVHLTER ERVAQEAEQD
LEGLKKAELM RERTGEIFHG LITGVQSYGL FVEIEELLVE GLVHVSSLKD DWYEYRSRQQ
TLVGRKNRKQ YRLGDRIEVQ VKSVDYYRQQ IDLLAVGGGS DIEDEASEAL DDEPDMEDEE
D
//
