ID C6XUJ2_PEDHD Unreviewed; 709 AA.
AC C6XUJ2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
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 OrderedLocusNames=Phep_1629 {ECO:0000313|EMBL:ACU03842.1};
OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457
OS / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU03842.1, ECO:0000313|Proteomes:UP000000852};
RN [1] {ECO:0000313|EMBL:ACU03842.1, ECO:0000313|Proteomes:UP000000852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 /
RC NCIMB 9290 / NRRL B-14731 / HIM 762-3
RC {ECO:0000313|Proteomes:UP000000852};
RX PubMed=21304637; DOI=10.4056/sigs.22138;
RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.C., Saunders E., Chertkov O.,
RA Brettin T., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Pedobacter heparinus type strain (HIM 762-
RT 3).";
RL Stand. Genomic Sci. 1:54-62(2009).
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 ---------------------------------------------------------------------------
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; CP001681; ACU03842.1; -; Genomic_DNA.
DR RefSeq; WP_015807456.1; NZ_AQGK01000001.1.
DR AlphaFoldDB; C6XUJ2; -.
DR STRING; 485917.Phep_1629; -.
DR KEGG; phe:Phep_1629; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_4_1_10; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000000852; 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; 3.
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:UP000000852};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 627..708
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 709 AA; 80562 MW; 26FD87822AD8A1BC CRC64;
MAKKKSAHLE LVLIQLISDV LEKSNKEALN YKQVSAKLNL TDADSRETIS EILKEQARKG
VFSEPEKGKF RLKDLKTFIT GKVDMTADGA AFIIPDDEFE KDVFVSARKL HNALHGDKVK
VYIYAKKSGR KNEGEVVEII ERSKTDFIGV IRISERYAFV NVDDRKMLHD IFVPLNDLNG
AKNGQKVQVS ITEWPEGVKN PIGKIINILG EQGENNTEMN AILAQYGFPL SFPAEVELEA
NAIPEQVSAA EIKGRKDFRN TTTFTIDPAD AKDFDDAISF KTLENGNYEI GVHIADVSHY
VKPNSSLDKE AYARATSVYL VDRVIPMLPE RLSNGVCSLR PNEDKLCFAA VFELDEKANL
VNEWFGRTVI HSDRRFSYEE AQEVIENKAG DYAAEILKLN ELAYILRDKK FKNGAISFES
TEVKFKLDET GKPIGVYVKE RKDAHKLIED FMLLANKKVA EFIAKKGKGK QKYTFVYRSH
DSPNLENLGN FALFAARFGY KINMKSDKEI AKSLNYLMED VEGKKEQNVL TQLAIRSMAK
AIYTTKKTSH YGLAFDHYTH FTSPIRRYPD VMVHRLLAAY LNNEKSANEE EYEIAASHSS
AMEKRAADAE RASIKYKQAE YLEENVGNIF AGIISGVTEW GMYVELTENK CEGMIRLRDI
TDDFYVLDEK NYCIVGQRKQ KKYQLGDEVQ VKVKKVDLAK RQIDFTLIQ
//
