ID A0A1I6VRC0_9SPHI Unreviewed; 709 AA.
AC A0A1I6VRC0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN05660206_11660 {ECO:0000313|EMBL:SFT16273.1};
OS Sphingobacterium wenxiniae.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=683125 {ECO:0000313|EMBL:SFT16273.1, ECO:0000313|Proteomes:UP000198785};
RN [1] {ECO:0000313|EMBL:SFT16273.1, ECO:0000313|Proteomes:UP000198785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22789 {ECO:0000313|EMBL:SFT16273.1,
RC ECO:0000313|Proteomes:UP000198785};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOZZ01000016; SFT16273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6VRC0; -.
DR STRING; 683125.SAMN05660206_11660; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000198785; 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; 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:UP000198785};
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; 81169 MW; 0963C1D9C7FDF5DF CRC64;
MKQKKENPYK EVLTQLIVDV FEKSGNQALN YKQVSAKLNL ADTDSKVAIA DILSDASKSG
KFLQVSRGKF KLRQLQVYVV GKVDMTADGS AYIIPEDELE DDIHIAPRKL RQALHNDIVK
VHVYERSRGR KREGEVVEII QRAKTDFTGT IDISKSYAFF LPDDRKMIHD IFIPLDNLNG
AKDGEKVLVS IVEWPKNAKN PIGQVKNVLG KKGENNTEMN AILADFGFPL EFPKAVEKEA
NAIPLEIQQK DIEGRRDFRS ITTFTIDPID AKDFDDALSF QKLENGNYEI GVHIADVSHY
VKPETELDKE AFQRATSVYL VDRVIPMLPE RLSNGVCSLR PNEDKLCFSA VFEIDEKANV
LDQWFGRTII NSDRRFTYEE AQEVIENQAG DFAEEILKLN ELAYILRERK FKNGAIAFES
EEVKFHLDEN GKPLGVYTKV RKDAHKLIED FMLLANRKVA EFIGKQGRGK NKLTFVYRFH
DTPNPETLTT FSQFASRFGH KLSIKSDKET AKSLNALMTK IEGSKEQNLL TSLAIRSMAK
AIYTTKGSSH YGLAFDYYTH FTSPIRRYPD VMVHRLLQFY LDGGKKINAE HYEKMSEHSS
QMEKKAAEAE RASIKYKQAE FLQDQIGVEY KGIVSGVTEW GMYVEIEENK CEGMVRLRDI
TDDFYTLDEK NYAIIGQRKK KKYQLGDEVQ IRVKKVDLEK RQIDFTLLG
//
