ID A3HX56_9BACT Unreviewed; 733 AA.
AC A3HX56;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
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=ALPR1_19123 {ECO:0000313|EMBL:EAZ81179.1};
OS Algoriphagus machipongonensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=388413 {ECO:0000313|EMBL:EAZ81179.1, ECO:0000313|Proteomes:UP000003919};
RN [1] {ECO:0000313|EMBL:EAZ81179.1, ECO:0000313|Proteomes:UP000003919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR1 {ECO:0000313|EMBL:EAZ81179.1,
RC ECO:0000313|Proteomes:UP000003919};
RX PubMed=21183675; DOI=10.1128/JB.01421-10;
RA Alegado R.A., Ferriera S., Nusbaum C., Young S.K., Zeng Q., Imamovic A.,
RA Fairclough S.R., King N.;
RT "Complete genome sequence of Algoriphagus sp. PR1, bacterial prey of a
RT colony-forming choanoflagellate.";
RL J. Bacteriol. 193:1485-1486(2011).
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:EAZ81179.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAXU02000001; EAZ81179.1; -; Genomic_DNA.
DR RefSeq; WP_008202889.1; NZ_CM001023.1.
DR AlphaFoldDB; A3HX56; -.
DR STRING; 388413.ALPR1_19123; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_4_1_10; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000003919; 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; 3.
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; 2.
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:UP000003919};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 639..720
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 84115 MW; 7735F4DEC4BAFE94 CRC64;
MGRKSNKKNS RNNKKGHSND AANLTRRIVQ FLDTNYGVEF NSKQIIKKLD IRDSLSKGAV
EPILAKLLES GHVSKNPRNY YSSTKDPSFI EGTVDFVNPR FAFIIPDDPE KSEGDIMVKE
ADMKQALDGD KVRVMVNPLK SKFGKPEGRV LEVVERARDE FVGRVEISPR FAFVVPDFKK
MHKDIFVHRG DLEGAKHNEK VVVKLTEWRE GDKNPTGKVI RVLGEAGLHE VEIHSIMAEF
GLPFEYPEEP NKEANAISEK ITAKEIKSRK DFRGVPTFTI DPADAKDFDD AISYQVLPNG
NLEIGVHIAD VTHYVQPKTA LEKEAFNRAT SVYLVDRTIP MLPERLSNGL CSLRPNEDKL
TFSCVFEMDR EANILKHWIG RTVIHSDRRF AYEEAQENID NQSGDFFAEL TLLNDLAKKV
RKKRFNNGAV NFETVEVKFK LDDKGTPLGL IVKERKDIHK LIEEFMLLAN KFVAEFIYKK
NKGKDTFVYR THDFPDMERL DTFSGFAKRF GHEFDIENEQ KISGALNKLM DEIQGKPEQN
VLEQLAIRSM AKAKYTTEPK GHFGLAFAHY THFTSPIRRY PDMMVHRLLD HYLQGGKSPD
PDSWEQKCVH SSDREKRAAD AERASIKYKQ VEFMSLAEDK DYEGIVSGIT EWGVFVEISE
TKCEGMIRVQ DMEDDYYEFD QKNMRLVGSK TKKMITLGDK VKVRVVNTDI DRRTIDLEFA
DNDGKKPRNR AFR
//
