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Database: UniProt
Entry: R7HE77_9MOLU
LinkDB: R7HE77_9MOLU
Original site: R7HE77_9MOLU 
ID   R7HE77_9MOLU            Unreviewed;       699 AA.
AC   R7HE77;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=BN672_00351 {ECO:0000313|EMBL:CDE37710.1};
OS   Mycoplasma sp. CAG:472.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=1262904 {ECO:0000313|EMBL:CDE37710.1, ECO:0000313|Proteomes:UP000018408};
RN   [1] {ECO:0000313|EMBL:CDE37710.1, ECO:0000313|Proteomes:UP000018408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:472 {ECO:0000313|Proteomes:UP000018408};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDE37710.1}.
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DR   EMBL; CBIV010000011; CDE37710.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7HE77; -.
DR   STRING; 1262904.BN672_00351; -.
DR   Proteomes; UP000018408; 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; 2.
DR   HAMAP; MF_01895; RNase_R; 1.
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; 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:UP000018408};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          612..690
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   699 AA;  79117 MW;  4B1A822A2A36E96E CRC64;
     MKDKIIEKLS NESKGLSLIE INDLLNLTSV EDYKELQKNM DALVTEGIVH KSKKDKFILM
     EKCSSLLTGI IHINKHGNGF VDTKFDEDTF VKRENLNGAV DGDFVEIDVQ NDEGIVVNIL
     KRDINLLVGE MVKTKNGNLE FALDDKKKKI KVKLTKETSS HLVEGHKVLV KIQKELASNL
     YLADVIKVLG HKNDPGVDIL SIACKHEISL DVSDEVKKQV ANMVTSVSEK ELVGRTDLRN
     EVIFTIDGDD TKDIDDAVSI KKEDGYYILG VHIADVTNYV KEGSPLFESA YEKGTSSYLA
     DTVLPMLPHE LSNGICSLNE GVDRLTISCV MKIDTRGKIV DHDIFPSVIN SKKKMTYKNV
     NKIIMEDIIP EGYENFADDL KLMHELAQIL RKEKINRGYI DFDLDEAKII QDENGKAIDV
     VKRQQLDGEK LIEDFMIAAN ETVATHIYNM DLPFVYRIHG KPNPEKIEDF VNFVKLLGYK
     LDVSTEDITP KKMQDILDSL HEKKEFEILS DMLLRSMKKA VYSSNNIGHF GLASKIYTHF
     TSPIRRFPDL MVHTLLHKYL FENMVNMPTI RYYENYLPDA CEHASKKEVD AQSAEREVLD
     MKMAEYMESH IGQEYTGIIS GVTNFGLFVK LPNLIEGLVH ISTLKGFCTY VPNLLSLVSD
     GKIRYSLGQQ VKVRVTGASK ENSTIDFEII GDTNDRDKK
//
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