ID A0A1T0AV29_9PAST Unreviewed; 659 AA.
AC A0A1T0AV29;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ORFNames=B0187_01235 {ECO:0000313|EMBL:OOS00635.1};
OS Haemophilus paracuniculus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=734 {ECO:0000313|EMBL:OOS00635.1, ECO:0000313|Proteomes:UP000190867};
RN [1] {ECO:0000313|EMBL:OOS00635.1, ECO:0000313|Proteomes:UP000190867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 43573 {ECO:0000313|EMBL:OOS00635.1,
RC ECO:0000313|Proteomes:UP000190867};
RA Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome sequence of Haemophilus paracuniculus CCUG 43573 type
RT strain.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:OOS00635.1}.
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DR EMBL; MUYA01000002; OOS00635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T0AV29; -.
DR STRING; 734.B0187_01235; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000190867; Unassembled WGS sequence.
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 SMART; SM00316; S1; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
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:UP000190867};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01036}.
FT DOMAIN 17..77
FT /note="S1 motif"
FT /evidence="ECO:0000259|SMART:SM00316"
FT DOMAIN 23..78
FT /note="Cold shock"
FT /evidence="ECO:0000259|SMART:SM00357"
FT DOMAIN 189..532
FT /note="Ribonuclease II/R"
FT /evidence="ECO:0000259|SMART:SM00955"
FT DOMAIN 574..658
FT /note="S1 motif"
FT /evidence="ECO:0000259|SMART:SM00316"
SQ SEQUENCE 659 AA; 75674 MW; 831D4F020EEBFA15 CRC64;
MFQNNPLLAQ LKQQIEASKE YVEGVVRASD KSYGFLECEK KSYFIPPAEM KKVMHGDTVK
AVVKRDGDKE QVEVDSLIEP MLDRFIAQVR FNRDGKLQLA VDHPSIKNLI SANVQKNVSE
KLENGDWVVA KLKTHPLRDD RFLFAQVIQL ICKESDNFAP WWVTLARHEQ PREPVPNEAS
YELHDELGRE DLTSLYFTTI DSPSTQDMDD ALYIEPVMTN GEQTGWQLVV AIADPTAYIP
EHSNIEKAAR QRCFTNYLPG FNIPMLPREL SDDLCSLVPN EKRPALVGYI ETDLLGNIVK
PARFVSAWVE SKAKLAYDNV SDYLEQVENA WQPDNGETKQ QIDWLHQFTQ ARIQWRGENA
LLFKEQGDYA FELNEDGSVK GIHVEYRRIA NQIIEESMII ANICAAQFLA ENAKTGVFNT
HSGFDPKNLE PAKNFLLDTL ATEENREQLA ERYSAERLTT LNGYCEMRRD IDAFPEKFLE
LRLRRYLTFA EFKGEVAPHF GLGISHYATW TSPIRKYGDM VNHRLIKQCL LNQQAKAVDE
SILARLQEAR RQNRLVERDI ADWLYARYLA PRVEQNVEFE CEIADVSRGG VRARVIENGA
SIFVPFSTLH DNKEEMDYRP EEIALYIKGE KAYQIGQTVR VKLTEVRLET RSIVGNIIV
//
