ID A0A1X6ZKC9_9RHOB Unreviewed; 751 AA.
AC A0A1X6ZKC9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ECO:0000313|EMBL:SLN53291.1};
GN ORFNames=ROA7450_02724 {ECO:0000313|EMBL:SLN53291.1};
OS Roseovarius albus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1247867 {ECO:0000313|EMBL:SLN53291.1, ECO:0000313|Proteomes:UP000193061};
RN [1] {ECO:0000313|EMBL:SLN53291.1, ECO:0000313|Proteomes:UP000193061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7450 {ECO:0000313|EMBL:SLN53291.1,
RC ECO:0000313|Proteomes:UP000193061};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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|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; FWFX01000008; SLN53291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6ZKC9; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000193061; 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; 1.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; 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; 2.
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:UP000193061};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 628..709
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 717..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..751
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 82273 MW; 640E1EBB23C55B9C CRC64;
MNKMPSKTEI LEWISDNPTK TAKRDIARAF GIKGAARIDL KRMLKELEAE GHLTKAKKTY
RDPEKLPPVS VLRVSGQTVD GDLTASALEW HGEGDEPLVL MIPRAGDPAL GQGDRILARL
QEVQGEDYQY EGRLIRRIGT NPRKVLGIFR KGAEGGRIVP IDKGDSKEWL VAVDGVRGAK
DGELVEAEQA GPKGRMGLPR ARVTDRLGDP TAPKAVSLIA IHQHGIPDAF PDEVISEADG
MKPAGLSGRE DLRDLPLVTI DPPDARDHDD AVWAHADDDP KNEGGHIIWV AIADVAHYVR
PNSALDAEAR KRGNSSYFPD RVVPMLPDRL SGDLCSLHEG VPRACLAVRM QIDAQGNKID
QRFVRGLMKS LASLNYAEVQ QAIDGAPNDK CAPLMEEVIE PLYAAYAALK AARQQRQPLD
LDLPERKVVL SDEGKVTSVS FAERYDAHKL IEECMVLANV AAAETLLAKK SPQLFRVHEE
PAPEKLESLR EVAQSAGLVL AKGQVLKTEH LNKLLHAAAG TDHAEVVNMS TLRAMTQAYY
APVHIGHFGL ALRSYSHFTS PIRRYADLIV HRSLVSAHGW GDDGLQPRDI ERLESTAQHI
SDTERRSMIA ERDTNDRYLA AFLSERLGEE FTGRISGIAK FGAFVRLDET GADGLIPMRA
LGREYYHLDR DAGTLTGSDT GIVIGLGQRV TVKLSEAAPV TGGVALELIS LDGKVIKREG
GSGRGRGSKH KFSKSKRKTD KGKRQVKRSR K
//
