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Database: UniProt
Entry: A0A0U1LLL2_TALIS
LinkDB: A0A0U1LLL2_TALIS
Original site: A0A0U1LLL2_TALIS 
ID   A0A0U1LLL2_TALIS        Unreviewed;       630 AA.
AC   A0A0U1LLL2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   22-FEB-2023, entry version 24.
DE   RecName: Full=DJ-1/PfpI domain-containing protein {ECO:0000259|Pfam:PF01965};
GN   ORFNames=PISL3812_01249 {ECO:0000313|EMBL:CRG83893.1};
OS   Talaromyces islandicus (Penicillium islandicum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Islandici.
OX   NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG83893.1, ECO:0000313|Proteomes:UP000054383};
RN   [1] {ECO:0000313|EMBL:CRG83893.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG83893.1};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
CC       {ECO:0000256|ARBA:ARBA00005290}.
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DR   EMBL; CVMT01000001; CRG83893.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U1LLL2; -.
DR   STRING; 28573.A0A0U1LLL2; -.
DR   OrthoDB; 168004at2759; -.
DR   Proteomes; UP000054383; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd17871; GPN2; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   InterPro; IPR004130; Gpn.
DR   InterPro; IPR030231; Gpn2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR21231:SF3; GPN-LOOP GTPASE 2; 1.
DR   PANTHER; PTHR21231; XPA-BINDING PROTEIN 1-RELATED; 1.
DR   Pfam; PF03029; ATP_bind_1; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054383}.
FT   DOMAIN          52..186
FT                   /note="DJ-1/PfpI"
FT                   /evidence="ECO:0000259|Pfam:PF01965"
FT   REGION          588..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..612
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  70175 MW;  B575A80B0AA9B7F7 CRC64;
     MAPTQFGTLA IAYQVVDSAG PTDLLASASK SALLAIREYV PIGDDIISRA PEFEFHHIGV
     TRDPVDLGTS QMTILPTTTV DECPELDILL VGGPYLGTFD LHPKHADLIR RHVAAGKLLF
     TTCTGASLVA STGVLDGRMA TVNNIEYEWV RKRWPKVNWT REKKWIVDGN IWTGSGAIAA
     TDMVAHWLQE NYGLDVLIQA AATLDYEPRD ADGLFNVFPQ STDVAGQFSA SDYRPRQKTI
     PPNIKHIDEL AHQPRFQIDF LYAPASKGTS HHLTALSLGA HPISHKDMPF AQLVIGPPGA
     GKSTYCNGMH QFMGAIGRKC SIVNIDPAND KTSYPCALDV RDLVTLEEIM EEDALGPNGG
     VLYALEELEN NFEWLKDGLK ELEDDYVLFD CPGQVELFTH HSSLRNIFFQ ISKLGYRLIV
     IHLVDSYCLT LPSMYISALI LSLRSMLQMD LPHINVLTKI DNLSNYSALP FNLDYYTEVQ
     DLNYLLPHLE AETSRLSHDK FGALNSAIVQ LVQEFALVAF ETLAVEDKKS MMHLLQVIDR
     ASGYAFGPAE GANDTIWQVA VREGWGNLDI QDVQERWIDA KDEYDEHERN ELEAEAKAKE
     EAARRAQENE DELDFQNMLP TGGTTVIRKS
//
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