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Database: UniProt
Entry: Q1QY78_CHRSD
LinkDB: Q1QY78_CHRSD
Original site: Q1QY78_CHRSD 
ID   Q1QY78_CHRSD            Unreviewed;       646 AA.
AC   Q1QY78;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 127.
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=Csal_1225 {ECO:0000313|EMBL:ABE58580.1};
OS   Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS   NCIMB 13768 / 1H11).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE58580.1, ECO:0000313|Proteomes:UP000000239};
RN   [1] {ECO:0000313|EMBL:ABE58580.1, ECO:0000313|Proteomes:UP000000239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11
RC   {ECO:0000313|Proteomes:UP000000239};
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA   Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(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; CP000285; ABE58580.1; -; Genomic_DNA.
DR   RefSeq; WP_011506526.1; NC_007963.1.
DR   AlphaFoldDB; Q1QY78; -.
DR   STRING; 290398.Csal_1225; -.
DR   KEGG; csa:Csal_1225; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OrthoDB; 9764149at2; -.
DR   Proteomes; UP000000239; 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; 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; 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; 4.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR   PROSITE; PS50126; S1; 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:UP000000239};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01036}.
FT   DOMAIN          563..643
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   646 AA;  72473 MW;  DDCE4C29D81CB61C CRC64;
     MLQNNSALAQ LKQQIRETTP RVQGVIKATD RGFGFLEADD GSSYFVPPPA MKQVLHGDRV
     DALLKQEGDK TSVEPDTLIE AGLDRFVARL VKRDGRLSVV PDHPSINNQL RARLKNSLDE
     STLGDGDWVV ARLVRHPLKP DDRGFFAQVD ELVVKADNPA VPWRVTLARH ALEQASPQFG
     EQWPLHDEGL EREDLTATPF FTIDGEKTRD MDDALYIETL EDGWRLSVAI ADPTAYVREG
     DAVDREAQTR AFTVYLPGQN VTMLPELLAD DLCSLKEGEE RPTLVCTLDV HRDGSLGEYR
     FFAAQVRSQA RLVYDQVSDW LEGQGDWAPA DDTIATQLQA LAEMTKARNA WREQHTLVFK
     DRPDYVFDVD DAGNVLAVRI EERRVAQRMI EESMIAANAC CADLLAAHVG HGIFNVHQAF
     EPEKADQAIE FLANQDISVE REQLLELSRY RELRRALEAR EDAWLDARLR RFQGYTNMSA
     QPGPHFGLGL SAYATWTSPI RKYGDMVNHR LIKRVLKGEA APAEASQALT EQLTERRRLN
     RMAERDVKDW LYVRYLGPAA EAGEVFEADI IAINRGGMRV RLTANGATAF VPAPFMHSDR
     DKVAIDDKEG RIQIEGEPRY KLGDTIKVAL AEAVESTRSL VARPAA
//
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