ID A0A1V8UYI3_9PEZI Unreviewed; 261 AA.
AC A0A1V8UYI3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=ADP-ribose 1''-phosphate phosphatase {ECO:0000256|ARBA:ARBA00012983};
DE EC=3.1.3.84 {ECO:0000256|ARBA:ARBA00012983};
GN ORFNames=B0A51_02949 {ECO:0000313|EMBL:OQO28706.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO28706.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Highly specific phosphatase involved in the metabolism of
CC ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of
CC tRNA splicing. {ECO:0000256|ARBA:ARBA00002432}.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQO28706.1}.
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DR EMBL; NAEU01000110; OQO28706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8UYI3; -.
DR STRING; 1974281.A0A1V8UYI3; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR InterPro; IPR012664; CHP02452.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR019261; PARG_cat_microbial.
DR NCBIfam; TIGR02452; TIGR02452 family protein; 1.
DR PANTHER; PTHR35596; DUF2263 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR35596:SF1; DUF2263 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF10021; PARG_cat_microb; 1.
DR PIRSF; PIRSF014899; UCP014899; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386}.
FT DOMAIN 53..119
FT /note="Microbial-type PARG catalytic"
FT /evidence="ECO:0000259|Pfam:PF10021"
FT DOMAIN 153..218
FT /note="Macro"
FT /evidence="ECO:0000259|Pfam:PF01661"
SQ SEQUENCE 261 AA; 27884 MW; DF915CCABF197E04 CRC64;
MLNLAARQRA CENTIARTPS IAASSPNPTA VLSSTFVPSF LPPLTSSHPL YPSLTRSQIE
IHNSDAFALA RTLPPSPGKT SVLNLASETS RAGGWRHTLS TTQEEALCYS STLYETLKGS
CAAIFSSEVV VFKDTLANDL LDLPLESRHS VAVITIAAPR WPAVTQDGKD FAKQSDLQEL
QQKILLVLRL AATNGVTKLV LGAMGCGAFG CPPRAVASEM KAALESAEFQ GWFENVVFAV
YAAGPAGEKN LRVFKEVFGD T
//
