ID K9ZW27_DEIPD Unreviewed; 1235 AA.
AC K9ZW27;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=Deipe_0162 {ECO:0000313|EMBL:AFZ65766.1};
OS Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS KR-200).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ65766.1, ECO:0000313|Proteomes:UP000010467};
RN [1] {ECO:0000313|Proteomes:UP000010467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC {ECO:0000313|Proteomes:UP000010467};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT 19664.";
RL Submitted (MAR-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; CP003382; AFZ65766.1; -; Genomic_DNA.
DR RefSeq; WP_015234077.1; NC_019793.1.
DR AlphaFoldDB; K9ZW27; -.
DR STRING; 937777.Deipe_0162; -.
DR KEGG; dpd:Deipe_0162; -.
DR PATRIC; fig|937777.3.peg.172; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_2_0_0; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000010467; 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:UP000010467};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 948..1028
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1067
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1235 AA; 134753 MW; AA1AB857997DD06E CRC64;
MPQNKKDVAA PKRKAQAKKP ASPGAAAQST AKRQRQVKVA DAVPQTLPET PETASGTSPR
PKRGRKIAPV ANSPIDTPTP TPTGEISALP TGTEAPVKPA RKTRRSAVPT ALPESPDPSV
DSVAEAQAGA ALQNETAPEV AVQIEEAPSK PARRGRKPRQ EAVRVVPEAA DPTPAAAPSE
DTSLPARVAE AAQVSVETGV TVRPKPRRGR GAKASDEELP AALSEPVTLA PSATDSAQDA
DAPAATPTSK AKRGKRTTKP QVEASPTRRG RKTKAAGRDE ASLSDTAGAA SPLPAAELSH
TEADLDTPFT PDESDLPLEV GPMLNEREAR ELLLQVMRKQ DRPLHVRDLE RLLSRRERES
IGSRAEIEGL LERFVASGDL VRTRKRTYGL PDAMNLVKGR FQSSASGFGF LIPEAGGDDY
YVAPESTLEA WNGDIVLVRP EGRVRRGESP RATVVRVLQR AHSRLVGSLE HSKGYALLKS
DDSRVKHRVL LMPEGTEGVP TGARVLAELF WPETTGEDEV FGRITKVLGE TDDPETETQA
VIIKFDLRDE FPPEVLQEAQ AIPARIPEEA LTGRLDLRSY NIFTVDGKDA KDFDDAIHIE
PSPGGNFVVG VHIADVSHYV KAGGPLDREA YLRATSVYLP GHVLPMLPEH LSNGVCSLVP
NEDRLTLSAM IEVSADGDVL NVQLTPSVIR SQARLTYDEV QAYSEGVATL PEHARKVEGD
LHLLLKLTSR MRQKRLREGS LDFKLREVKV DVDKEGNLQL IPIREETARG MIEDLMLLAN
KVVARFMLEQ NAPALYRVHE EPTLGRFGEV SAALARMGVV LGEEPTPQAY QAALKKVRGT
PQETVVNTLL LRSLKQARYT GENLGHFGLA FEEYLHFTSP IRRYPDLIVH RALRAALQGK
THGTTMNELR GQLPQMGDHT SERERSAAEA ERDLTKYYQA KWAQAHLGES FDGTVSGVTS
FGLFVALENG VEGLLHISNL DDDYYFFLED ALMLKGRSSG RTYRMGDQVR ITIAQVNPLG
RQIDFSQETD MTDDGVKPRA RKRGEREQER AADRAVRITE RPPRLAALDE QRQNNGPSTP
RVAAAEPRGR SDDRRGRVGR GQPSERLAPP ARTPERGERG GKRRVVTLDR PRNEHNRPVA
VTVQRMYFGD WSSENLREDE GQGGTNPNGY RRPSGPRPQQ GPQSRGPSQG PRNAAPQSGP
GPGDAQAAAA PAGDGDRNRR RRRRRGRGNG KGSGE
//
