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Database: UniProt
Entry: A0A1V6PHR0_PENDC
LinkDB: A0A1V6PHR0_PENDC
Original site: A0A1V6PHR0_PENDC 
ID   A0A1V6PHR0_PENDC        Unreviewed;       711 AA.
AC   A0A1V6PHR0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQD76585.1};
GN   ORFNames=PENDEC_c004G04055 {ECO:0000313|EMBL:OQD76585.1};
OS   Penicillium decumbens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD76585.1, ECO:0000313|Proteomes:UP000191522};
RN   [1] {ECO:0000313|Proteomes:UP000191522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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:OQD76585.1}.
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DR   EMBL; MDYL01000004; OQD76585.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6PHR0; -.
DR   STRING; 69771.A0A1V6PHR0; -.
DR   OMA; WHDALFD; -.
DR   OrthoDB; 180318at2759; -.
DR   Proteomes; UP000191522; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:UniProt.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR11782:SF121; NUCLEOSIDE-DIPHOSPHATASE MIG-23; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU003833};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191522};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        519..537
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          595..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..620
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        145
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         182..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   711 AA;  78410 MW;  15B2C9F0090184EF CRC64;
     MGKWRYGVVL DAGSSGTRVH VYRWLRNAAA RKDADVDELT SLPEIKTKEE WVKKIHPGVS
     SFADRPEAVG SEHLAGLLEH AKSIIPKEDA KDTPIFLLAT AGMRLVGNLE RQLLLDQICA
     YARANTDFLL PDCGVHIQVI PGVTEGLYGW IATNYLMGTF DSPNAHNHGK GHSTYGFLDM
     GGASAQIAFA PNATETEKHA NDLTLVRLRN IDGSVQEHRV FVTSWLEFGV HEARRRYVEA
     LQGMTRPDVL ELPDPCLPSG LRTTLNGKEV SSTSDAGATL LGTGRFDECL RQTFPLLDKD
     APCMDNPCLL HGIHVPSIDF DVNHFIGISE YWHTTHEIFE MGYKDKAYDF NTYQERVKTF
     CSQDWSSIED GIQAQKWGKK IDSQKAYEVC FKASWIINML HNGIGIPRVG LEDTSGSSHN
     GTKEVLSHGQ EKGYLDAFQA VNKIDSTEVS WTLGKIVLYA SSQVPTQVEE DLPVGFGSNV
     AGVPADFQYP SVELLPDSEG FHSEHWHDAL FDGDSPRRIP GFLLFLFIIV LACFFLCGRS
     RRLRMYHHIS KLLRRGPSHP NHPKKRKGVA SMLPFLNRGG QSYERVLEDG AQDFELGVTD
     SDGSDVDGSR LSETDAKPRP PKRASSWGSP SNPPNLKYTL DNSSSGTIGL GISGDSGIAM
     DRAGLVVRTE SRDHLAPIAL GPTINGRRSR AGSPTRSHHQ KSPTMTPLAD D
//
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