ID C4LD74_TOLAT Unreviewed; 686 AA.
AC C4LD74;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Exoribonuclease 2 {ECO:0000256|HAMAP-Rule:MF_01036};
DE EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01036};
DE AltName: Full=Exoribonuclease II {ECO:0000256|HAMAP-Rule:MF_01036};
DE Short=RNase II {ECO:0000256|HAMAP-Rule:MF_01036};
DE Short=Ribonuclease II {ECO:0000256|HAMAP-Rule:MF_01036};
GN Name=rnb {ECO:0000256|HAMAP-Rule:MF_01036};
GN OrderedLocusNames=Tola_3016 {ECO:0000313|EMBL:ACQ94605.1};
OS Tolumonas auensis (strain DSM 9187 / TA4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Tolumonas.
OX NCBI_TaxID=595494 {ECO:0000313|EMBL:ACQ94605.1, ECO:0000313|Proteomes:UP000009073};
RN [1] {ECO:0000313|Proteomes:UP000009073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA Beller H.;
RT "Complete sequence of Tolumonas auensis DSM 9187.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACQ94605.1, ECO:0000313|Proteomes:UP000009073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073};
RX PubMed=22180815; DOI=10.4056/sigs.2184986;
RA Chertkov O., Copeland A., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P.,
RA Bruce D., Goodwin L., Han C., Tapia R., Saunders E., Schmutz J.,
RA Brettin T., Larimer F., Land M., Hauser L., Spring S., Rohde M.,
RA Kyrpides N.C., Ivanova N., Goker M., Beller H.R., Klenk H.P., Woyke T.;
RT "Complete genome sequence of Tolumonas auensis type strain (TA 4).";
RL Stand. Genomic Sci. 5:112-120(2011).
CC -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC polyribonucleotides processively in the 3' to 5' direction.
CC {ECO:0000256|HAMAP-Rule:MF_01036}.
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_01036};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01036}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily.
CC {ECO:0000256|ARBA:ARBA00009925, ECO:0000256|HAMAP-Rule:MF_01036}.
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DR EMBL; CP001616; ACQ94605.1; -; Genomic_DNA.
DR RefSeq; WP_015880054.1; NC_012691.1.
DR AlphaFoldDB; C4LD74; -.
DR STRING; 595494.Tola_3016; -.
DR KEGG; tau:Tola_3016; -.
DR eggNOG; COG4776; Bacteria.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000009073; 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-KW.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.640; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR HAMAP; MF_01036; RNase_II; 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; IPR011804; RNase_II.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR NCBIfam; TIGR02062; RNase_B; 1.
DR PANTHER; PTHR23355:SF37; EXORIBONUCLEASE 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 SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01036};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01036};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01036};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01036};
KW Reference proteome {ECO:0000313|Proteomes:UP000009073};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01036}.
FT DOMAIN 23..80
FT /note="Cold shock"
FT /evidence="ECO:0000259|SMART:SM00357"
FT DOMAIN 192..520
FT /note="Ribonuclease II/R"
FT /evidence="ECO:0000259|SMART:SM00955"
SQ SEQUENCE 686 AA; 77426 MW; C4B48AAFF593A51E CRC64;
MFQDNPLLAQ LKQQLRDNLP KKEGVVRASD RGFGFLETDH RGESYFIAPQ QMKRVMHGDR
IIAVIRAENG KEQAEPESLV TPFLTRFVAR IKVIKDRLFV VPDHPVMKDA IKARPMKGLD
EKQFKEGDWV IANLKRHGMS DASGHFAEIT EYVTHNNDPE APWWVVLRRH DLPRCAPDIE
QEWQLREEGL TREDLTALPF VTIDGESTRD MDDALYVEKT ADGWKMLVAI ADPTAYIEPG
SALDLEAAKR AFTVYLPGRN IPMIPRHLSD ELCSLHEGEE RPALCCEMLI TAAGELLPEP
RFFAANIRSQ GRLIYDQLSD WLENGSAEGF DPAPVIVEQI ELLHAATTAR QTWRKEHAIL
FKDRPDYDFE LNEAGEVVAI HASFRRSANK IVEESMIAAN QCAGDFLAAQ PGYGIFNVHA
GLDVEKFKGV QELLQLHEAP LTDETLLTLP GFCQLRHWLD AQPTSYLDNR IRRFQTYSLM
SAEPGPHFGL GLSHYATWTS PIRKYGDMIN HRILKAIISQ QEVPVRADAA LTDALSLSRR
SNRMAERDIG DWLYARFLLP AVASQQVFDA EIMDVMRSGL KVRLLENGAV CFIPGSLILK
DRKRFVCNHD EGRAYLDGEI HYELGQTIQV KLQDAIEATR TLVAIPTELP SAAAPVTKEV
LAESEHELMD ELLTEPEETA PEEDEA
//
