GenomeNet

Database: UniProt
Entry: D5E4Y9_MYCCM
LinkDB: D5E4Y9_MYCCM
Original site: D5E4Y9_MYCCM 
ID   D5E4Y9_MYCCM            Unreviewed;       741 AA.
AC   D5E4Y9;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=vacB {ECO:0000313|EMBL:ADE19794.1};
GN   Synonyms=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN   OrderedLocusNames=MCRO_0161 {ECO:0000313|EMBL:ADE19794.1};
OS   Mycoplasma crocodyli (strain ATCC 51981 / MP145).
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=512564 {ECO:0000313|EMBL:ADE19794.1, ECO:0000313|Proteomes:UP000001845};
RN   [1] {ECO:0000313|Proteomes:UP000001845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51981 / MP145 {ECO:0000313|Proteomes:UP000001845};
RA   Glass J.I., Durkin A.S., Hostetler J., Jackson J., Johnson J., May M.A.,
RA   Paralanov V., Radune D., Szczypinski B., Brown D.R.;
RT   "The complete genome of Mycoplasma crocodyli MP145.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MP145;
RA   Ma Z., Wang X., Liu H.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ADE19794.1, ECO:0000313|Proteomes:UP000001845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51981 / MP145 {ECO:0000313|Proteomes:UP000001845};
RX   PubMed=21460083; DOI=10.1128/JB.00309-11;
RA   Brown D.R., Farmerie W.G., May M., Benders G.A., Durkin A.S., Hlavinka K.,
RA   Hostetler J., Jackson J., Johnson J., Miller R.H., Paralanov V., Radune D.,
RA   Szczypinski B., Glass J.I.;
RT   "Genome sequences of Mycoplasma alligatoris A21JP2T and Mycoplasma
RT   crocodyli MP145T.";
RL   J. Bacteriol. 193:2892-2893(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001991; ADE19794.1; -; Genomic_DNA.
DR   RefSeq; WP_013054570.1; NC_014014.1.
DR   AlphaFoldDB; D5E4Y9; -.
DR   STRING; 512564.MCRO_0161; -.
DR   KEGG; mcd:MCRO_0161; -.
DR   eggNOG; COG0557; Bacteria.
DR   HOGENOM; CLU_002333_7_0_14; -.
DR   OrthoDB; 9764149at2; -.
DR   Proteomes; UP000001845; Chromosome.
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   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_01895; RNase_R; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR001900; RNase_II/R.
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; 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; 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:UP000001845};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          639..717
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   741 AA;  85145 MW;  192034BF302E6530 CRC64;
     MNIKEELLKY LQSSNEVRSF LSIAKGLNIK PNKNKELTKV LQECQQNFLI FKNEKDEYFA
     PVFKEEIEGN ISISNNGKFA FVDYNINEEL NTKNSVFIIK NNFNGAIHND LVVVKIFEDI
     TRNKEQRLFG VVSKIKQRMT NQLIGFVKQK GIYVDFEPID KKFKFNKYKI VGMKQQANLN
     DLVTVKIEEI TKSFILVSIE KVITNDADTK LFIKAYLEGV NVPKIFPDSL ESEVSLIPQN
     IDNENKENRE DFTNDLIVTI DGDDTKDFDD AINVVKLDNG NYLLSVHIAD VSYYVREGSK
     INEEALKRGT SIYLADKVIP MLPEALSNGI CSLNPNEKRF VLSCIMEIDN SGKTVKTVIK
     QGIIDSKYRL TYKQVNDFYD TQVIKNEWFS SNPNLNSKEF GVDNLSKMLN EAKELSLILH
     KFKVNEGYID FEIQEPKILF NEDGSVKDIT FYPRGFSEEL IEDFMVRANE EVAKYLSGHH
     FPAMYRVHEK PDEERLLSFR NVLSTLGVKV VLPIGQITPL IYSGIIEKIK EQRNDEFIKM
     LFLRTMQKAV YSGDNLGHFG LASQCYCHFT SPIRRYPDLV IHRILRELVL NKDISKKEEL
     TNLVFSVSKA NSASEQGAVE IERKVNDLLF SEYYKNKIGT VLKGQIVSVV KFGFFVEFEN
     KTNALVHKSV LQDDTLEPND TMTQLKGKND TYTIGSYIDV VVAAVDLVDG KVDCVPQKFY
     QDFLNQKINR RAVEDKHFRK N
//
DBGET integrated database retrieval system