ID A0A2A7UU33_COMTR Unreviewed; 799 AA.
AC A0A2A7UU33;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ECO:0000313|EMBL:PEH88800.1};
GN ORFNames=CRM82_09535 {ECO:0000313|EMBL:PEH88800.1};
OS Comamonas terrigena.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=32013 {ECO:0000313|EMBL:PEH88800.1, ECO:0000313|Proteomes:UP000220246};
RN [1] {ECO:0000313|Proteomes:UP000220246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_394 {ECO:0000313|Proteomes:UP000220246};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-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 -!- 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:PEH88800.1}.
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DR EMBL; PDEA01000001; PEH88800.1; -; Genomic_DNA.
DR RefSeq; WP_066536286.1; NZ_UIGV01000001.1.
DR AlphaFoldDB; A0A2A7UU33; -.
DR STRING; 1219032.GCA_001515545_01797; -.
DR GeneID; 80800845; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000220246; 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; 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; 2.
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:UP000220246};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 601..682
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 692..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 799 AA; 88811 MW; DB8429B0201FE43E CRC64;
MNLRTKTANL SKEIEGTVQG HRDGHGFVLR DDGEGDIFLP PNEMRAVLHK DQVRVRIVGQ
DRRGRPEGHV LEIVERPTKT LIGRLLQESG VWLVAPEDKR YGQDVLVPGT GIGTAKAGQV
VVVELTEAPA LFGQPVGRVI EVLGEVDDPG MEIEIAVRKY GVPHIFSDAC LAEAKALPDK
VRAVDRKNRV DLRDVPLVTI DGEDARDFDD AVYCEPAKVG RSKGWRLLVA IADVSHYVQN
GNAIDIDAYE RATSVYFPRR VIPMLPEKLS NGLCSLNPAV DRLCMVCDML VNNKGEVQAY
QFYPAVMHSH ARFTYTEVAA ILSNTRGPEA AQRKERVQDL LNLHDVYRAL LQARQARGAV
DFDTVETQIV CDDNGRIEKI IPRTRNDAHR LIEEAMLAAN VCSADFIEEN GQNGLFRVHD
RPSAEKIDIL RGYLKALGVG MSVSDTPHPR EFQAIADATK DRPDSQQIHT MLLRSMMQAF
YTPENNGHFG LAFEAYTHFT SPIRRYPDLL VHRVIKSILA GSHYRLPTLP TPGEAQAKLA
KRLASRVTEP QQKPRSRAAQ AELQGWEAAG LHCSANERRA DEASRDVEAW LKCKYMRDHL
GEEFAGTVSS VTTFGIFVTL DAMYVEGLVH ITELGGDYFR FDEHRQELRG ERTGIRYTIG
TRMRVQVSRV DLDGRKIDFR IVHDEEEMAL RNATRSRAGK RARREAASDD GSEEAAAPAR
APVEAVDSWN QGKPGRSGSG KPARRDNRNA HQAPREAAAP DMQDLRASVQ QAAVAKQGKA
AAKTAKNSRA GKRKPRTGR
//
