ID H2AWT7_KAZAF Unreviewed; 167 AA.
AC H2AWT7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=ADP-ribose 1''-phosphate phosphatase {ECO:0000256|ARBA:ARBA00019744};
DE EC=3.1.3.84 {ECO:0000256|ARBA:ARBA00012983};
GN Name=KAFR0F02400 {ECO:0000313|EMBL:CCF58837.1};
GN ORFNames=KAFR_0F02400 {ECO:0000313|EMBL:CCF58837.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF58837.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF58837.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-alpha-D-ribose 1''-phosphate + H2O = ADP-D-ribose +
CC phosphate; Xref=Rhea:RHEA:25029, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57967, ChEBI:CHEBI:58753; EC=3.1.3.84;
CC Evidence={ECO:0000256|ARBA:ARBA00034427};
CC -!- SIMILARITY: Belongs to the POA1 family.
CC {ECO:0000256|ARBA:ARBA00006575}.
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DR EMBL; HE650826; CCF58837.1; -; Genomic_DNA.
DR RefSeq; XP_003957972.1; XM_003957923.1.
DR AlphaFoldDB; H2AWT7; -.
DR STRING; 1071382.H2AWT7; -.
DR GeneID; 13884305; -.
DR KEGG; kaf:KAFR_0F02400; -.
DR eggNOG; ENOG502S60W; Eukaryota.
DR HOGENOM; CLU_054419_1_2_1; -.
DR InParanoid; H2AWT7; -.
DR OrthoDB; 1601683at2759; -.
DR Proteomes; UP000005220; Chromosome 6.
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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005220}.
FT DOMAIN 1..167
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
SQ SEQUENCE 167 AA; 18660 MW; D8DEE4B3D6B0A23B CRC64;
MTNLKYVKGD ILKKTSYPRL LIHSCNCNGS WGGGIAYQLA VNYPLAEREY VGLCEENGSD
LLGKCKLIPS YTDDNLIIAC LFTSSYGGSS HDSAESILKY TKQALDDLSS IRLSSKVVLT
SKTGKQIRDY NLEMPKINSG IFGVPWKHTE ELLRAYKNEM NFTVYVL
//