ID Q1H0U3_METFK Unreviewed; 840 AA.
AC Q1H0U3;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
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=Mfla_1626 {ECO:0000313|EMBL:ABE49894.1};
OS Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylobacillus.
OX NCBI_TaxID=265072 {ECO:0000313|EMBL:ABE49894.1, ECO:0000313|Proteomes:UP000002440};
RN [1] {ECO:0000313|EMBL:ABE49894.1, ECO:0000313|Proteomes:UP000002440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT / ATCC 51484 / DSM 6875 {ECO:0000313|Proteomes:UP000002440};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT "Complete sequence of Methylobacillus flagellatus KT.";
RL Submitted (MAR-2006) 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; CP000284; ABE49894.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1H0U3; -.
DR STRING; 265072.Mfla_1626; -.
DR KEGG; mfa:Mfla_1626; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_0_4; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000002440; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; 2.
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; 1.
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:UP000002440};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 655..736
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 94008 MW; C6EB7B753D9F0B31 CRC64;
MSTKKKQIAK TGVKEAAPQR KLKGGRAGDP YAEREQEKYA NPLPSREFIL SVMEEQGVPV
TVEELYRLVG VKKSEQEIFS RRLRAMERDG QIIQNRKGAL CIAEKVNLLA GRVQGHPDGF
GFFIPDGGGD DLFLSPREMA QVMHGDRVMV RPAGTDRRGR PEGRIVEVLE RATKTLVGRV
ISSHGVTIVA AEDKRVNQDI LIPYHLDMGA KDGQVVTVEL TEQPSIHAKP VGKVIEILGN
YADPGMEIEI ALRKHHLPHE FSEAAIKQAQ KYPKKVRAAD WKGRIDLREL PLVTIDGETA
RDFDDAVYCE PQGTGWRLVV AIADVSFYVR PGDSLDKDAY ERGNSVYFPR RVIPMLPEAL
SNGLCSLNPD VDRLCMICDM QISNTGRIKQ YKFYPSVMRS KARMTYTKVF DMISNPAGEV
AREYDWLMPH VQHLYRLYKV MLAAREKRGA IEFESNETLM VFNDNGKIER IEATSRNEAH
RLIEECMLAA NVCAANFLDK CKHPALYRVH DGPTEEKLEA LRTFMGEFGF TLGGGDTPHA
KDYGKLLAQI KGRPDEQLLQ TVLLRSMQQA VYSPDNIGHF GLAYEAYTHF TSPIRRYPDL
LIHRAIKAAL NGEVYKAGDW NELGKHCSMT ERRADDATRD VEAWLKCYYM QDKIGEEFDG
TVAGVTSFGL FVALDGVYVE GLLHVTELGN DYFNYDKARH EMLGERTGVR FRLGDRLRVK
VNRVDLETSR IDFGLVARQD QMQASSTPPA PANRRRGKPA PAAATVKAAA APDAEKPKRR
QSATVTSTEL PTKSPVQEAV KKPRARRADA TPAQKTTRTR PPRASGGKSR ATVTTKKKAS
//
