ID A0A1W1VNR5_9DEIO Unreviewed; 1293 AA.
AC A0A1W1VNR5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN00790413_02657 {ECO:0000313|EMBL:SMB95025.1};
OS Deinococcus hopiensis KR-140.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=695939 {ECO:0000313|EMBL:SMB95025.1, ECO:0000313|Proteomes:UP000192582};
RN [1] {ECO:0000313|EMBL:SMB95025.1, ECO:0000313|Proteomes:UP000192582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KR-140 {ECO:0000313|EMBL:SMB95025.1,
RC ECO:0000313|Proteomes:UP000192582};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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 ---------------------------------------------------------------------------
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; FWWU01000009; SMB95025.1; -; Genomic_DNA.
DR STRING; 695939.SAMN00790413_02657; -.
DR Proteomes; UP000192582; 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; 2.
DR HAMAP; MF_01895; RNase_R; 1.
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; 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:UP000192582};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 983..1063
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1093
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1293 AA; 140982 MW; 3BAE5C289CD5D942 CRC64;
MPRAKKERVA AEEQQQQPVN TPSAEAKKTA VRRGRKAETA APTPVAEPID TPASPAPTRG
RPRKTQKTQI PAPQVAEATP EPQPAAPEAK PRRGRKPKAE QVPSAAEVQE AAVPVAPTDV
PAEAAPAEPP RARRGRKPRA EVPVAMTEAV REEAPQEAEG PAPAPLQTAV EPDAAAAPEK
PRRGRKPRAA ASTEAVPEPG VLPTETRAAE SVLLEVPKRR GRKPKSAVQA VQETAPESNG
DPEAQVPLGA MLGGVEAVEA SVPSDASPEP AAQVGAAPTV TATMRGDTPD PAVDLPLGET
ETAAVTPDAG GRRNRKPRRE PQATATGDED SSTGPASGEA EGEEAARQLV TAQLRKLGRP
IHVRDLERTF TRQMLDRLGN WRDLESLLDE LTRTGEVIRT RRRTYGLPEA MSLVRGRFQA
SAAGFGFVVP DSGGEDFYVA PEHTMEAWNG DTVLVRMEGR GDGGRDGRNN GPRRGQRGDG
SPRASVARIV QRAYKQLVGS LELSKGHPIL RADDPRARHR ILLLPDGLEG LPSGARVVAE
LFWPEQTGED EVFGQVRRVL GEQDDPETET EAVIVKYGLR GEFPVDVLDQ ANAIPAQIPD
EALVGRLDLR DFNIFTVDGR DAKDFDDAIH IQPTPEGTFV VGVHIADVSH YVREGTPLDD
EAYARATSVY LPGRVLPMLP EHLSNGVCSL VPNEDRLTMT AMVELSAEGE ILNVQLAPSV
IRSKARLTYD EVQAYSEATA TLPDHARHLE GDLHLLLKIT TKLRQKRLRE GSLDFKLREV
KVDVGPDGRM ELIPIREETA RGMIEDLMLL ANKVVAHELL QRDIPALFRI HEEPTLQRFQ
EVTGAIGRLG LSFPGNEPTP QAYQAVLKQV RGTPREGVVN TLLLRSMQQA KYAGENLGHF
GLAFDEYLHF TSPIRRYPDL LVHRVLRGML SGELRSGGRA VNELRGKLPG MGDHTSDRER
AAAEAERDLT KYYQAKWAQE HLGETFTGNV SGVVSSGLFV MLDNGVEGKL HISNLDDDYY
IYLEDAQMLR GRSGGRTFRL GDTLTVTISQ VNPLARLIDF TQEDTDMDDA PTRPRARRRE
DREAEKRERL STITPTAPRK FTLDEPQPAV QSTTPRGQSG QGQGRGVRTQ QGRDGGGRDG
GSRDSGFQGG RGPVRPQNGG QRPRRVITLE RPRNEHLRPV NITVQRMYFG DWTVENMPPD
DGQGEGGRPP RSFDRGFDRS GGGRSPGQRY SRGGSDRGAV RDLNGRPDGG RSERSEPPRQ
DPVPQDGGAA GNDADAKRRR RRRGRRSGNG PQG
//
