ID N9AHR5_9GAMM Unreviewed; 803 AA.
AC N9AHR5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 ORFNames=F950_01295 {ECO:0000313|EMBL:ENV60912.1};
OS Acinetobacter soli NIPH 2899.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217677 {ECO:0000313|EMBL:ENV60912.1, ECO:0000313|Proteomes:UP000018433};
RN [1] {ECO:0000313|EMBL:ENV60912.1, ECO:0000313|Proteomes:UP000018433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 2899 {ECO:0000313|EMBL:ENV60912.1,
RC ECO:0000313|Proteomes:UP000018433};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter soli NIPH 2899.";
RL Submitted (FEB-2013) 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:ENV60912.1}.
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DR EMBL; APPV01000007; ENV60912.1; -; Genomic_DNA.
DR AlphaFoldDB; N9AHR5; -.
DR PATRIC; fig|1217677.3.peg.1246; -.
DR HOGENOM; CLU_002333_7_0_6; -.
DR Proteomes; UP000018433; Unassembled WGS sequence.
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; 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; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 632..713
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 723..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..803
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 90778 MW; 38CE0631F3E9F1AE CRC64;
MKNWIDPEAK AEAERYDNPI PSRTLILSTL EQLNTPQSHA ELVEHFDIFD QKSIDALSHR
LIAMVRDGQL AKDGFRFQLI GEQPTFDATV YINAKGLGSA HIDGQTDLLL PERELRLVFN
GDRVTVRQSS VDRKGKAWGF ITEVLQRRVK QVIGKLNVHD GEYFLQPSAP NAHQPIPLEK
ELVEHAKVNV GDHLRIAIDD YPTREEFATG HIVQSMSDKA DTEIIIPQTI LEFGLPYEFP
DEVIQEAESF KEPSKKDIEG RIDLRDLPLV TIDGEDARDF DDAVYAEKRA GGGYRVVVAI
ADVSHYVRVG KPLDDEAQER GTSVYFPHFV LPMLPEALSN GLCSLNPHVD RLCMVCDLKL
SRAGRVMSYE FYPSVMHSKA RLTYTQVARY FEGQTDAIPN DKSVQKSLNT LFQLYQTLKD
LRAKRHAMEF ETVETYMTFD ALGGINEILP RTRNDAHKLI EECMLLANVA AAEYALANDI
PMLYRVHEPP EFSRIQKVKD FVKLLGLPFP DQPTQADYQR VIEATKDRID APSIHSVLLR
SMMQAYYGAK NAGHFGLAYE AYTHFTSPIR RYPDLLLHRA LKAHLQHKPS PLSGAALDEA
GEHFSRTERR ADEASRSVTT WLKCHYMQQH LGEEFIGNIS AVTEFGLFVT LKDLYVDGMI
HVSQLGDDFF IYDQASQSLV GQNRGQIFGL GDEVKIKVAG VNLDERKIDF ELTQQITHAG
RIIRSRAPRT TKAQATEQVF HGASDTQPRE QQRSEKKDKS KPSSYTKKTG KKKTSSKTAV
KAEKDKKKSK VKKKKSNAKP KSD
//
