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Database: UniProt
Entry: Q5KV84_GEOKA
LinkDB: Q5KV84_GEOKA
Original site: Q5KV84_GEOKA 
ID   Q5KV84_GEOKA            Unreviewed;       344 AA.
AC   Q5KV84;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Hypothetical conserved protein {ECO:0000313|EMBL:BAD77402.1};
GN   OrderedLocusNames=GK3117 {ECO:0000313|EMBL:BAD77402.1};
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD77402.1, ECO:0000313|Proteomes:UP000001172};
RN   [1] {ECO:0000313|EMBL:BAD77402.1, ECO:0000313|Proteomes:UP000001172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426 {ECO:0000313|EMBL:BAD77402.1,
RC   ECO:0000313|Proteomes:UP000001172};
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD77402.1; -; Genomic_DNA.
DR   RefSeq; WP_011232587.1; NC_006510.1.
DR   AlphaFoldDB; Q5KV84; -.
DR   STRING; 235909.GK3117; -.
DR   GeneID; 69833923; -.
DR   KEGG; gka:GK3117; -.
DR   eggNOG; COG2110; Bacteria.
DR   HOGENOM; CLU_049707_0_0_9; -.
DR   Proteomes; UP000001172; 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:UP000001172}.
FT   DOMAIN          1..194
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
SQ   SEQUENCE   344 AA;  39630 MW;  AEDB0FECF44DF3F2 CRC64;
     MIILKQGNLL EDEAEALVNT VNCVGVMGKG IALQFKQAYP EMFSEYEKAC RRKEVQPGKM
     HVVSTKSLLN PKYIINFPTK RHWKNKSRME DIELGLADLI KVVKELNIKS IALPPLGCGN
     GGLRWDEVRP KIEAAFKHLK EVEVHLYEPA GSPNPDQIKI RTKPPKMTRS RALLLMLMND
     YSIPGYKLSL LEVQKLAYFL QVVGEPMRLR FEKGKYGPYA DNLNHVLLRL DGHFIRGFGD
     RNRDAEIYLL PNAVQEAEQY LQGDSEADEH LEKVRNVIQG FETPYGLELL STVHWVVKEN
     PDIKDDVRSI IEEIHNWNER KRKIFKEKHI TKAWQHLKGI GMLN
//
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