ID A0A317XAI7_9EURO Unreviewed; 580 AA.
AC A0A317XAI7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 13-SEP-2023, entry version 12.
DE SubName: Full=General stress response phospho protein phosphatase Psr1/2 {ECO:0000313|EMBL:PWY95603.1};
GN ORFNames=BO94DRAFT_131313 {ECO:0000313|EMBL:PWY95603.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY95603.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY95603.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY95603.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PWY95603.1}.
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DR EMBL; MSFK01000002; PWY95603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317XAI7; -.
DR STRING; 1450535.A0A317XAI7; -.
DR OrthoDB; 5473812at2759; -.
DR Proteomes; UP000246702; 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:UP000246702}.
FT DOMAIN 406..564
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 1..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 63205 MW; 3A3D9E1B7FAC55B4 CRC64;
MLGGSLERDS SPSNSKTATG EAPMPIATSH PDFNPESSPQ DQLASTDASP LSTHLEPSNA
VQESVAPAQG SVGDSAATST DAPKKQHTLL PIPSRASLKA DRQSTLDKSQ DTAHDDSENT
LRGSKRSIFK GRRDRSRGSS MRSRRQNQEG ASLEEDKAAS PDLREPVRPE RRNKVSYRLF
AFLSCCSSSS DDPEDPAIPA KRTSRRPSVP NTQPAPEKTD ANAGDSSTAE SKDPSYYRDE
KPNMTVTSNQ SMTQVDEERT VTTPDQGSQL DGAGVPSNSL ETDHGPSLPQ DNAASQGPGV
GQSTLPAATT AEVNLISSET EDLAQETEDP GTTPTEKTQD AVATDELPKP PSSETSYEDE
KYTSHDEEAT VLPAELPPLM APSGNQADTL LQDVQQQFLL PPALPHLRDR KCLVLDLDET
LVHSSFKVLE RADFTIPVEI EGQYHNIYVI KRPGVDQFMK RVGELYEVVV FTASVSKYGD
PLLDQLDIHN VVHHRLFRDS CYNHQGNYVK DLSQVGRDLR DTIIIDNSPT SYIFHPQHAI
PISSWFSDAH DNELLDLIPV LEDLAGAQVK DVSLVLDIAL
//
