ID E8U9L6_DEIML Unreviewed; 1281 AA.
AC E8U9L6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=Deima_2112 {ECO:0000313|EMBL:ADV67755.1};
OS Deinococcus maricopensis (strain DSM 21211 / LMG 22137 / NRRL B-23946 /
OS LB-34).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=709986 {ECO:0000313|EMBL:ADV67755.1, ECO:0000313|Proteomes:UP000008635};
RN [1] {ECO:0000313|EMBL:ADV67755.1, ECO:0000313|Proteomes:UP000008635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC {ECO:0000313|Proteomes:UP000008635};
RX PubMed=21677853; DOI=10.4056/sigs.1633949;
RA Pukall R., Zeytun A., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brambilla E.M., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Deinococcus maricopensis type strain (LB-
RT 34).";
RL Stand. Genomic Sci. 4:163-172(2011).
RN [2] {ECO:0000313|Proteomes:UP000008635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC {ECO:0000313|Proteomes:UP000008635};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Kyrpides N.,
RA Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Pukall R., Gehrich-Schroeter G.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Deinococcus maricopensis DSM 21211.";
RL Submitted (JAN-2011) 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; CP002454; ADV67755.1; -; Genomic_DNA.
DR RefSeq; WP_013557260.1; NC_014958.1.
DR STRING; 709986.Deima_2112; -.
DR KEGG; dmr:Deima_2112; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_2_0_0; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000008635; 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 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:UP000008635};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 977..1057
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..342
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1281 AA; 139165 MW; FD36EE28469E8EDE CRC64;
MPKAKKERVA DSQAAPASEK RRRKADPDAD NTPQRTAQES VSASPRRTRA VSAEPTETPS
RKPRANRAKT PTAPLEADAT EPTAAEAPTP ARRGRKPKAA LADAEATTLK RTRGRKAALQ
EPQAVPAPVA ELDAAPEVAA ERPDITPAPE AEPVVADTPA VQAEPAAAPA PTEAKPRRGR
RKNAEPDAPT PEPTPAVSTV AEAPAESAPA KRTRRKNARV PDAPTPAPVA EALSVEAAVE
GDEQEPPVPE APAMDAPVTA KPTPEAPARQ TRRRSVRANR AAPTPDAPST PRADAPAQPD
SPVPVAPAAD LTPEPASLDE PDANERLDNE ASDDDAGEIV TDDLPDTADA QNVDAARELL
LAQLKKLGRP VHVRDLERTF TRRDRDVLGS RRAFTDLLSD LATQGLVVRT RKHTYGLPEA
MNLVRGRFQA SAAGFGFVVP DDGGDDYYVA PEGTLEAWNG DIVLVRPEGR GGRRGDSPAA
VVVRIVQRAY TQLVGTLEYA RGYAILKADD ARARHRIMLV PDGTEDVPGG ARVVAALFWP
EQTGEDEVYG QITRVLGEQD DPETETQAVI VKYGLHDDFP EEALAEAEAI PRQLPPSALV
GRLDLRDRNI FTVDGRDAKD FDDAIHIQPT EAGNFLIGVH IADVSHYVTQ GSALDDEAYA
RATSVYLPGR VLPMLPEHLS NGVCSLVPYE DRLTMSALIE LTADGDILNV ELANSVINSK
ARLTYDEVQA YSEGTATMPH HARHLEGDLH LLLKLTTRMR QRRLRAGSLD FKLREVKVDV
GPDGRMELIP IREETARGMI EDLMLLANKV VARYLLEHHV PTLYRVHEEP TAGRFGEVSA
ALGRMGLAFQ GSDPTPQAYQ GVLKQVRGTP QESAVNTLLL RSLKQARYAE ENLGHFGLAF
DEYLHFTSPI RRYPDLLVHR VLKAQLSGEA TERYKADMSA KLPEMGQHTS DRERTAAEAE
RDLTKYYQAK WAEEHLGETF EGHVSGVVAS GLYIALDNGV EGKLHISNLD DDYYLFLEDA
MMLRGRSTGR MFRLGDAVTV TIAQVNPLAR QIDFTQENPM NAGDSKARAR RRDEKEKEVR
PGRGAPRQGG TDGDRERGGE RRSGPGARTN GTLSAAGQGS GRGRSGSYES ARPQSGGGQR
RRIVTLERAR NEHLRPVNIT VQRMYFGDWS IENLPPDDGQ GNGGGRDRGG LRERGGFRDR
SAPREGRGER PERSGGDRER GPARQASARP AQPRERAERA PAAPAPEAQA APVAESGLDA
DGQRRRRRRR GRRGGGNGTA E
//
