ID   ADPRH_STAAW             Reviewed;         266 AA.
AC   Q8NYB7;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Protein-ADP-ribose hydrolase {ECO:0000250|UniProtKB:P67343};
DE            Short=SpyMacroD {ECO:0000250|UniProtKB:P0DN70};
DE            EC=3.2.1.- {ECO:0000250|UniProtKB:P67343};
GN   OrderedLocusNames=MW0302;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-
CC       cysteine bonds (By similarity). Specifically reverses the SirTM-
CC       mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from
CC       the target protein. May be involved in the modulation of the response
CC       to host-derived oxidative stress. {ECO:0000250|UniProtKB:P0DN70,
CC       ECO:0000250|UniProtKB:P67343}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose
CC         + H(+) + L-aspartyl-[protein]; Xref=Rhea:RHEA:54428, Rhea:RHEA-
CC         COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29961, ChEBI:CHEBI:57967,
CC         ChEBI:CHEBI:138102; Evidence={ECO:0000250|UniProtKB:P67343};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000033; BAB94167.1; -; Genomic_DNA.
DR   RefSeq; WP_000449060.1; NC_003923.1.
DR   AlphaFoldDB; Q8NYB7; -.
DR   SMR; Q8NYB7; -.
DR   EnsemblBacteria; BAB94167; BAB94167; BAB94167.
DR   KEGG; sam:MW0302; -.
DR   HOGENOM; CLU_046550_2_1_9; -.
DR   OMA; AQRFSND; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02906; Macro_1; 1.
DR   Gene3D; 3.40.220.10; -; 1.
DR   InterPro; IPR035801; Macro_1.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   Pfam; PF01661; Macro; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; SSF52949; SSF52949; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..266
FT                   /note="Protein-ADP-ribose hydrolase"
FT                   /id="PRO_0000089213"
FT   DOMAIN          74..265
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
SQ   SEQUENCE   266 AA;  30129 MW;  11D8AD2AABA3C083 CRC64;
     METLKSNKAR LEYLINDMHR ERNDNDVLVM PSSFEDLWEL YRGLANVRPA LPVSDEYLAV
     QDAMLSDLNR QHVTDLKDLK PIKGDNIFVW QGDITTLKID AIVNAANSRF LGCMQANHDC
     IDNIIHTKAG VQVRLDCAEI IRQQGRNEGV GKAKITRGYN LPAKYIIHTV GPQIRRLPVS
     KMNQDLLAKC YLSCLKLADQ HSLNHVAFCC ISTGVFAFPQ DEAAEIAVRT VESYLKETNS
     TLKVVFNVFT DKDLQLYKEA FNRDAE