ID A0A135LX50_PENPA Unreviewed; 535 AA.
AC A0A135LX50;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE SubName: Full=Dullard phosphatase domain, eukaryotic {ECO:0000313|EMBL:KXG53552.1};
GN ORFNames=PGRI_006020 {ECO:0000313|EMBL:KXG53552.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG53552.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG53552.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG53552.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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:KXG53552.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LHQR01000014; KXG53552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LX50; -.
DR STRING; 5078.A0A135LX50; -.
DR OMA; SMVLDCT; -.
DR OrthoDB; 5473812at2759; -.
DR Proteomes; UP000070168; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR12210:SF171; PHOSPHATASE HERZOG; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000070168}.
FT DOMAIN 361..519
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 1..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 57806 MW; D3863FC6A3789EE3 CRC64;
MNTSGVPGSA IESEQGRGTD ATEIQDATSV APSDPALSST APVDKTSAAE GVNAPKKRHL
LIPIPSRRSL RNKQQGSEKS EEAAQDEPSR RSSKVSILRS KRDHSRASSR RSRRTQDGVN
VEESKEVSTM PEDSSKSQQK KSPSKLLAFL GCCSSDVDAD DTALPAKKTT MRPPASNKLP
TPDKAEAPTG DSSTVESREP YLDEKANSTV SADQAGDEDR NVPVQTATAS VQGEGPSADA
TQPEVSAQKD QTNDVTPPAK TGIAMGSVPE VNADTAKADV NTQDWEGQST TTTEDLTSAS
TSTMPKNFGT DGQEEVTSHQ EMKLPVVIPP PPPPLPPAPP APPRGHYEDA GHPLLPAPLP
HLSGRKCLVL DLDETLVHSS FKVLERADFT IPVEIEGQYH NIYVIKRPGV DAFMKRVGEL
YEVVVFTASV SKYGDPLLDQ LDIHNVIHHR LFRESCYNHQ GNYVKDLSQV GRDLKETIII
DNSPTSYIFH PEHAIPISSW FSDAHDNELL DLIPVLEDLA GAQVQDVSMV LDCTL
//
