ID A0A1H3SDB1_9BACI Unreviewed; 787 AA.
AC A0A1H3SDB1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 05-FEB-2025, entry version 30.
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=SAMN05421736_110111 {ECO:0000313|EMBL:SDZ35089.1};
OS Evansella caseinilytica.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Evansella.
OX NCBI_TaxID=1503961 {ECO:0000313|EMBL:SDZ35089.1, ECO:0000313|Proteomes:UP000198935};
RN [1] {ECO:0000313|Proteomes:UP000198935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP {ECO:0000313|Proteomes:UP000198935};
RA Varghese N., Submissions S.;
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; FNPI01000010; SDZ35089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3SDB1; -.
DR STRING; 1503961.SAMN05421736_110111; -.
DR Proteomes; UP000198935; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:TreeGrafter.
DR CDD; cd04471; S1_RNase_R; 1.
DR FunFam; 2.40.50.140:FF:000273; Ribonuclease 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; IPR050180; RNR_Ribonuclease.
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:UP000198935};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 627..707
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 718..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..787
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 89588 MW; 1E6D230A64D300AE CRC64;
MSEKMTKERL LTYMKEEATK PLSIKDLEEA MELKDSSQFK EFVKLLNQLE EEGELVRTRS
NRYGIPDKMN LLKGKVIMHP KGFAFVKTEE GHDDIYVAGA EMNGAMNEDK VLVRLHPHTG
GARPEGAIIR ILERGIKTTV GTYVDDKHYG IVIPDDKRIP NDIFIPKKKE GAAVDGHKVL
VEITKYPEGR MSAEGRVLEV LGHKNDPGVD ILSIIYKHGL PGEFAQETLD HANSVPDEID
PAVLENRRDL REETIVTIDG ADAKDLDDAV QVKKLDNGNY ILGVHIADVS YYVEENSPID
TEAAERGTSA YLVDRVIPMI PHRLSNGICS LNPQVDRLTL SCEMEFTPSG ELVNHDIFQS
VINTTERMTY TDVRKILQEE DEEVLKRYDP LIPFFQGMAE LAEILRSKRM ARGAIDFDFK
EAKVLVDEDG KPVDVVMRER SVAERLIEEF MLAANETIAE HFHWMKVPFM YRVHEDPDEE
KLNRFLEFIT NFGYVVKGSA NTIHPRALQE LLEQVKGEPE EAVISTVMLR SMKQAKYDPE
NTGHFGLSAD FYTHFTSPIR RYPDLIVHRL IRTYLLEGKT DDETVEKWAG MLYDIARHSS
DMERRAEDAS RETDEMKKVQ FMEDKVGEEF EGIISGVTNF GLFVELPNTI EGLVHVSYLT
DDYYHYDENQ YAMIGERTGN VFRIGDEMEV RVVNVNLDER IIDFEVVGMK ARKERKLDAP
RVIEGGKRTK RKKGDNGGGK GNGNGRLNIG ANPPEKKKEK SNGKKKKKAF YENAPSNKRN
KGKKKKK
//
