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Database: UniProt
Entry: W0DXV2_MARPU
LinkDB: W0DXV2_MARPU
Original site: W0DXV2_MARPU 
ID   W0DXV2_MARPU            Unreviewed;       353 AA.
AC   W0DXV2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Appr-1-p processing protein {ECO:0000313|EMBL:AHF03445.1};
GN   ORFNames=MARPU_05835 {ECO:0000313|EMBL:AHF03445.1};
OS   Marichromatium purpuratum 984.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Marichromatium.
OX   NCBI_TaxID=765910 {ECO:0000313|EMBL:AHF03445.1, ECO:0000313|Proteomes:UP000005275};
RN   [1] {ECO:0000313|EMBL:AHF03445.1, ECO:0000313|Proteomes:UP000005275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=984 {ECO:0000313|EMBL:AHF03445.1,
RC   ECO:0000313|Proteomes:UP000005275};
RG   DOE Joint Genome Institute;
RA   Bryant D.A., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-(ADP-alpha-D-ribosyl)-thymidine in DNA + H2O = a
CC         thymidine in DNA + ADP-D-ribose; Xref=Rhea:RHEA:71655, Rhea:RHEA-
CC         COMP:13556, Rhea:RHEA-COMP:18051, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57967, ChEBI:CHEBI:137386, ChEBI:CHEBI:191199;
CC         Evidence={ECO:0000256|ARBA:ARBA00035885};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71656;
CC         Evidence={ECO:0000256|ARBA:ARBA00035885};
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DR   EMBL; CP007031; AHF03445.1; -; Genomic_DNA.
DR   RefSeq; WP_005220741.1; NZ_CP007031.1.
DR   AlphaFoldDB; W0DXV2; -.
DR   STRING; 765910.MARPU_05835; -.
DR   KEGG; mpur:MARPU_05835; -.
DR   eggNOG; COG2110; Bacteria.
DR   HOGENOM; CLU_049707_0_0_6; -.
DR   OrthoDB; 9780211at2; -.
DR   Proteomes; UP000005275; Chromosome.
DR   CDD; cd02901; Macro_Poa1p-like; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   PANTHER; PTHR12521:SF0; ADP-RIBOSE GLYCOHYDROLASE OARD1; 1.
DR   PANTHER; PTHR12521; PROTEIN C6ORF130; 1.
DR   Pfam; PF01661; Macro; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005275}.
FT   DOMAIN          1..155
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
SQ   SEQUENCE   353 AA;  39874 MW;  8D2EF424D707ADA6 CRC64;
     MIEFTQGNLL DADVDAIVNT VNTVGVMGKG IALMFKEKYP ENNRAYMAYC KAGAFEPGSL
     FVTRQSDLLG PLWIVNFATK QHWRHPSKME WIESGLRELR EFIEDNQVRS IAVPPLGAGN
     GKLDWSAVRP CIERALGDLE SVRVVVFEPT AKYQNVAKRT GVQALTPARA MIAELVRRYW
     ILGFECSLLE IQKLAWLLER AIERHELDNP LDLRFEANRY GPYAHRLHHL LDGLDGSYLH
     CDKRLADAGP LDVIWFEEAR KEYLSTYLAG PEMAPYREAF DETVALIDGF QSPLGMELLA
     TVDWLLSREG CEPSVQGVIA ALATWPGGKD AGERKRRLFD DRLIRLALDR LAS
//
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