ID A0A246WWN1_9BURK Unreviewed; 830 AA.
AC A0A246WWN1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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 ECO:0000313|EMBL:OWY31101.1};
GN ORFNames=CEJ42_03310 {ECO:0000313|EMBL:OWY31101.1};
OS Herbaspirillum robiniae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=2014887 {ECO:0000313|EMBL:OWY31101.1, ECO:0000313|Proteomes:UP000197596};
RN [1] {ECO:0000313|EMBL:OWY31101.1, ECO:0000313|Proteomes:UP000197596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ10 {ECO:0000313|EMBL:OWY31101.1,
RC ECO:0000313|Proteomes:UP000197596};
RA Fan M., Lin Y.;
RT "Herbaspirillum phytohormonus sp. nov., isolated from the root nodule of
RT Robinia pseudoacacia in lead-zinc mine.";
RL Submitted (JUN-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:OWY31101.1}.
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DR EMBL; NJGU01000001; OWY31101.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246WWN1; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000197596; 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; IPR001387; Cro/C1-type_HTH.
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; 3.
DR PROSITE; PS50943; HTH_CROC1; 1.
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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 19..41
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
FT DOMAIN 665..746
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 601..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 90896 MW; D804C6A648C94496 CRC64;
MSQFPYSIPS REEILGILRT SPTAQSASSL AAALGVKPDE IDGMTRRLNA MERDGQIKPD
RAGNYKLTHS PDFIEGRVSS HRDGFGFLLP DDGSDDLFLP EKEMQKVMHG DRVQARIVGT
DRRGRPEGTI VEVVERANSH VIGRLLNENG VWVVAPEDKR IGHDVLLAGP PGKAKAGQVV
SVELTEHPSR YTQPVGKIVE ILGDIDDPGM EIEIAVRKYG VPHEFSDAAK KLSAKLPSEV
RAADLKDRVD LRDVPLVTID GEDARDFDDA VYCEPVKIGR AKGYRLIVAI ADVSHYVKPN
DALDADALER STSVYFPRRV IPMLPEKLSN GLCSLNPDVD RLTLVCDAVI TAKGEIKAYQ
FYPAVIHSAA RLTYTEVAAV LANTKGPEAA RRIGLVPHLT HLYEVFQALL QARQARGAID
FETTETYIVC NAAGKIEKIL PRTRNDAHRL IEECMLAANV CAADLLKRHD HPALYRVHAG
PTKEKLTQLR NFLKQTGLSL GGGDTPGAAD YAELMPKIKA RPDALLIQTM LLRSMQQAVY
SPDNIGHFGL SYESYAHFTS PIRRYPDLLT HRAIKAVLQG KRYDPKGIDS SALNTSISPA
ARKMQQQQRA ADKAAGKKTQ ARNEGSQGIW EALGLHCSAN ERRADEASRD VEAWLKCYFI
RDKLGEEFTG TISGVATFGI FVQLDALYIE GLVHVTELGA DYFQYDEARH ELRGERTGIR
YQLTDRVTVQ VSRVDLDARK IDLALVNEPG IRTLIKNEAK RAESAARGKP AGNGGARQQQ
PAAKAKKAAA PKPAKAAKAN GAAAARGRPG EADRKRAAAK GFGKGGKKKR
//
