ASCHD_ZYMMA
ID ASCHD_ZYMMA Reviewed; 148 AA.
AC A0A0H3G0N3;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=ASCH domain-containing ribonuclease {ECO:0000303|PubMed:28951575};
DE Short=ZmASCH {ECO:0000303|PubMed:28951575};
DE EC=3.1.-.- {ECO:0000269|PubMed:28951575};
GN OrderedLocusNames=Zmob_0380 {ECO:0000312|EMBL:AEH62228.1};
OS Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 /
OS NCIMB 8938 / NRRL B-806 / ZM1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=555217 {ECO:0000312|Proteomes:UP000001494};
RN [1] {ECO:0000312|Proteomes:UP000001494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10988 / DSM 424 / CCUG 17860 / LMG 404 / NCIMB 8938 / NRRL
RC B-806 / ZM1 {ECO:0000312|Proteomes:UP000001494};
RX PubMed=21725006; DOI=10.1128/jb.05395-11;
RA Pappas K.M., Kouvelis V.N., Saunders E., Brettin T.S., Bruce D., Detter C.,
RA Balakireva M., Han C.S., Savvakis G., Kyrpides N.C., Typas M.A.;
RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. mobilis
RT lectotype strain ATCC 10988.";
RL J. Bacteriol. 193:5051-5052(2011).
RN [2] {ECO:0007744|PDB:5GUQ, ECO:0007744|PDB:5GUS, ECO:0007744|PDB:5Y6B}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), FUNCTION, COFACTOR, AND MUTAGENESIS
RP OF TYR-47; LYS-53 AND SER-128.
RX PubMed=28951575; DOI=10.1038/s41598-017-12186-w;
RA Kim B.N., Shin M., Ha S.C., Park S.Y., Seo P.W., Hofmann A., Kim J.S.;
RT "Crystal structure of an ASCH protein from Zymomonas mobilis and its
RT ribonuclease activity specific for single-stranded RNA.";
RL Sci. Rep. 7:12303-12303(2017).
CC -!- FUNCTION: Shows sequence-specific endoribonuclease activity towards
CC single-stranded RNA (ssRNA), with a preference for the bond between
CC pyrimidine and adenine nucleotides. May also have 5'-exonuclease
CC activity. {ECO:0000269|PubMed:28951575}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:28951575};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:28951575};
CC Note=Active in the presence of Mn(2+) or Ni(2+) ions. No activity
CC detected with Zn(2+) or Co(2+). {ECO:0000269|PubMed:28951575};
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DR EMBL; CP002850; AEH62228.1; -; Genomic_DNA.
DR RefSeq; WP_012817070.1; NC_017262.1.
DR PDB; 5GUQ; X-ray; 1.70 A; A/B/C/D=1-148.
DR PDB; 5GUS; X-ray; 1.95 A; A/B=1-148.
DR PDB; 5Y6B; X-ray; 2.00 A; A/B/C/D=1-148.
DR PDB; 5Y6C; X-ray; 2.40 A; A/B=1-148.
DR PDBsum; 5GUQ; -.
DR PDBsum; 5GUS; -.
DR PDBsum; 5Y6B; -.
DR PDBsum; 5Y6C; -.
DR AlphaFoldDB; A0A0H3G0N3; -.
DR SMR; A0A0H3G0N3; -.
DR STRING; 555217.Zmob_0380; -.
DR EnsemblBacteria; AEH62228; AEH62228; Zmob_0380.
DR KEGG; zmm:Zmob_0380; -.
DR eggNOG; COG4933; Bacteria.
DR HOGENOM; CLU_135561_0_0_5; -.
DR OMA; PQSFRYI; -.
DR Proteomes; UP000001494; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR007374; ASCH_domain.
DR InterPro; IPR015947; PUA-like_sf.
DR Pfam; PF04266; ASCH; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Endonuclease; Exonuclease; Hydrolase; Nuclease;
KW RNA-binding.
FT CHAIN 1..148
FT /note="ASCH domain-containing ribonuclease"
FT /id="PRO_0000452341"
FT DOMAIN 13..70
FT /note="ASCH"
FT /evidence="ECO:0000255"
FT MUTAGEN 47
FT /note="Y->F: Significantly reduced binding to ssRNA and
FT ssDNA, and impaired ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:28951575"
FT MUTAGEN 53
FT /note="K->E: Reduced binding to ssRNA and ssDNA. No effect
FT on ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:28951575"
FT MUTAGEN 128
FT /note="S->A: Slightly reduced binding to ssRNA and ssDNA.
FT No effect on ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:28951575"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:5Y6B"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:5GUQ"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:5GUQ"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:5GUQ"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:5GUQ"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:5GUQ"
FT STRAND 54..68
FT /evidence="ECO:0007829|PDB:5GUQ"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:5GUQ"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:5GUQ"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:5GUQ"
FT STRAND 95..112
FT /evidence="ECO:0007829|PDB:5GUQ"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:5GUQ"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:5GUS"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:5GUQ"
SQ SEQUENCE 148 AA; 17224 MW; 7CFB32B63BBB8D2F CRC64;
MTDIPDRKEA VISLWPEFAK AIVSGKKTVE FRRRIPLPAL SARIWIYATR PVKSVIGFAY
LEAIVQGDVN TLWSRYGREA FLSEQQYRDY FEGTEKATAF LLRDHQPIRP INLDQLKEIR
ANFQPPQSLT WLRKEETQKL VSLTSQVE
