ID D4GNZ2_PANAM Unreviewed; 811 AA.
AC D4GNZ2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
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:ADD78697.1};
GN OrderedLocusNames=PANA_3530 {ECO:0000313|EMBL:ADD78697.1};
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD78697.1, ECO:0000313|Proteomes:UP000001702};
RN [1] {ECO:0000313|EMBL:ADD78697.1, ECO:0000313|Proteomes:UP000001702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD78697.1,
RC ECO:0000313|Proteomes:UP000001702};
RX PubMed=20348253; DOI=10.1128/JB.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(2010).
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 -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-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; CP001875; ADD78697.1; -; Genomic_DNA.
DR RefSeq; WP_013027397.1; NC_013956.2.
DR AlphaFoldDB; D4GNZ2; -.
DR STRING; 706191.PANA_3530; -.
DR GeneID; 57266580; -.
DR KEGG; pam:PANA_3530; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_0_6; -.
DR Proteomes; UP000001702; Chromosome.
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; IPR013668; RNase_R_HTH_12.
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; PF08461; HTH_12; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000001702};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 645..726
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 732..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 37..65
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 732..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 91955 MW; 47DF7CBEF637ED16 CRC64;
MSKDPFLDRE AEKYENPIPS REFILALLEK REKPASREEL AQEMNLQEEE HLEALRRRLR
AMERDGQLVF TRRQCYALPE RLDLLRGKVI GHRDGYGFLR AEGQKDDLYL SAEQMKFCMH
GDVILAQPLG ADRKGRREAR VVRVQEPRNN QIVGRYFTDA GVGFVVPDDS RLSFDILIGP
DETMNARMGS VVVVELLQRP TRRSKAIGKI AEILGDDMGT SLAVDMALRT HEIPHSWPPE
VEAQVGKLNE EVPESAKKGR VDLRDLPLVT IDGEDARDFD DAVYCEKKRG GGWRLWVAIA
DVSYYVRPGT PLDNEAQQRG TSVYFPSQVV PMLPEVLSNG LCSLNPQVDR LCMVCEMTVS
SKGKLTGFKH YEAVMNSHAR LTYNKVWNIL QGNPELREQY APLVKDLQEL HNMYQVLETA
REERGGISFE TEEAKFIFNA ERRIERVERT SRNDAHKLIE ECMILANIAS ARFVEKHQEP
ALFRDHDRPS DDSIKSFRTV LNELGLSLPG GNKPQPIDYA ALLDQVADRP DAEMLQTMLL
RSMKQAVYDP ENRGHFGLAL ASYAHFTSPI RRYPDLLLHR AIKYLLAKEQ GEVKGLTTAT
GGYHYDMQQM LQLGQHCSMT ERRADEATRD VADWLKCDFM QDQVGNVFNG VISSVTGFGF
FVRLSDLFID GLVHVSTLDN DYYRFDPVGQ RLIGESGGRT YRLGDTVEVR VEAVHMDERK
IDFALVSSKR QVRGEGKTER DKAKRNAKAP TKHRRQAGRK TNFEPDSAFR NSSSQPAAAK
TEKKSKKVSE KTRKIAAATK AKRAAKKAKP A
//
