ID Q49W08_STAS1 Unreviewed; 796 AA.
AC Q49W08;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 130.
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=SSP1907 {ECO:0000313|EMBL:BAE19052.1};
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451 {ECO:0000313|EMBL:BAE19052.1, ECO:0000313|Proteomes:UP000006371};
RN [1] {ECO:0000313|EMBL:BAE19052.1, ECO:0000313|Proteomes:UP000006371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41
RC {ECO:0000313|Proteomes:UP000006371};
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE19052.1; -; Genomic_DNA.
DR RefSeq; WP_011303580.1; NZ_MTGA01000039.1.
DR AlphaFoldDB; Q49W08; -.
DR KEGG; ssp:SSP1907; -.
DR PATRIC; fig|342451.11.peg.1902; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_4_1_9; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000006371; 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:UP000006371};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 632..712
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 715..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 91174 MW; 927205E11DAD945F CRC64;
MNLKQSIEEI IKQPDYEPMS VSDFQDALGL NSADSFRDLI KVLVELEQTG LIQRTKTDRY
QRKASNNAKQ SKLIKGKLSQ NKKGFAFLRP EEEDMDDIFI PPTKINRAMD GDTVLVEVHQ
SKGEHKGKLE GEVKTIETHS VTQVVGTYSE ARHFGFVLPD DKRIMQDIFI PKGQNLGAVD
GHKVLVQITK YADGTDNPEG IVSAILGHKN DPGVDILSII YQHGIEIEFP DNVLAEAEAV
PDHIEPSQIE GRRDLRDELT ITIDGADAKD LDDAISVKKL SNGHTQLTVS IADVSYYVTE
DSALDKEAYS RATSVYLVDR VIPMIPHRLS NGICSLNPQV DRLTLSCQME IDERGDVVDH
EIFDSVIHSN YRMTYDEVNE IITDQDTETR NQYSEVTPML DLAQDLSQRL IHMRRRRGEI
DFDINEAKVL VNEEGIPTDV EMRQRGEGER LIESFMLAAN ETIAEHFDRL EVPFIYRVHE
QPKSERLRQF FDFVTNFGLM IKGTGEDIHP STLQKIQQEV EGQPEQMVIS TMMLRSMQQA
RYDDVNLGHF GLSAEYYTHF TSPIRRYPDL IVHRLIRKYI IEQSMDRKEK NKWEALLPEI
AEHTSQRERR AIEAERDTDE LKKAEYMVQH IGEEFEGIIS SVANFGMFIE LPNTIEGMVH
VSNMTDDYYH FDERQMAMIG ERQAKVFRIG DPVQIKVINV DVDERMIDFQ IVGMPIPNRD
RGQRPSRGKT IQAKPRGNSS DKSKDDKNGK GGRGRTKQKQ RKGKNKRQSD QSKGNTKHKP
FYKDKNVKNK ARKKKK
//
