EXRBN_MYCTO
ID EXRBN_MYCTO Reviewed; 168 AA.
AC P9WJ72; F2GJZ2; I6Y8M5; L7N5T0; O53513; Q7D7E6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=3'-5' exoribonuclease MT2234.1 {ECO:0000255|HAMAP-Rule:MF_00977};
DE EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_00977};
GN OrderedLocusNames=MT2234.1;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Exonuclease that cleaves single-stranded 3' overhangs of
CC double-stranded RNA. {ECO:0000255|HAMAP-Rule:MF_00977}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00977};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00977};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00977}.
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DR EMBL; AE000516; AAK46520.1; -; Genomic_DNA.
DR PIR; E70936; E70936.
DR RefSeq; WP_003411331.1; NZ_KK341227.1.
DR PDB; 4OKE; X-ray; 1.70 A; A/B=2-168.
DR PDB; 4OKJ; X-ray; 2.10 A; A/B=2-168.
DR PDB; 4OKK; X-ray; 2.21 A; A/B=2-168.
DR PDBsum; 4OKE; -.
DR PDBsum; 4OKJ; -.
DR PDBsum; 4OKK; -.
DR AlphaFoldDB; P9WJ72; -.
DR SMR; P9WJ72; -.
DR EnsemblBacteria; AAK46520; AAK46520; MT2234.1.
DR GeneID; 45426155; -.
DR KEGG; mtc:MT2234.1; -.
DR PATRIC; fig|83331.31.peg.2410; -.
DR HOGENOM; CLU_114979_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0004532; F:exoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00977; 3_5_Exoribonuc_actinobact; 1.
DR InterPro; IPR030853; 3_5_Exoribonuc_actinobac.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR033390; Rv2179c-like.
DR Pfam; PF16473; DUF5051; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease.
FT CHAIN 1..168
FT /note="3'-5' exoribonuclease MT2234.1"
FT /id="PRO_0000427880"
FT REGION 6..9
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00977"
FT BINDING 6
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00977"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:4OKE"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:4OKE"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:4OKE"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4OKE"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:4OKE"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:4OKE"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:4OKE"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:4OKE"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:4OKE"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:4OKE"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:4OKE"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4OKE"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:4OKE"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:4OKE"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:4OKE"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:4OKE"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:4OKE"
SQ SEQUENCE 168 AA; 19520 MW; D6CE7EF4D2FB7FA1 CRC64;
MRYFYDTEFI EDGHTIELIS IGVVAEDGRE YYAVSTEFDP ERAGSWVRTH VLPKLPPPAS
QLWRSRQQIR LDLEEFLRID GTDSIELWAW VGAYDHVALC QLWGPMTALP PTVPRFTREL
RQLWEDRGCP RMPPRPRDVH DALVDARDQL RRFRLITSTD DAGRGAAR