ID R9AEX3_WALI9 Unreviewed; 462 AA.
AC R9AEX3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE RecName: Full=FCP1 homology domain-containing protein {ECO:0000259|PROSITE:PS50969};
GN ORFNames=J056_000527 {ECO:0000313|EMBL:EOR00717.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR00717.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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DR EMBL; KE007233; EOR00717.1; -; Genomic_DNA.
DR RefSeq; XP_009268430.1; XM_009270155.1.
DR AlphaFoldDB; R9AEX3; -.
DR STRING; 1299270.R9AEX3; -.
DR GeneID; 20373479; -.
DR KEGG; wic:J056_000527; -.
DR eggNOG; KOG1605; Eukaryota.
DR HOGENOM; CLU_020262_9_0_1; -.
DR OMA; STHQHHE; -.
DR OrthoDB; 5473812at2759; -.
DR Proteomes; UP000014064; 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:UP000014064}.
FT DOMAIN 287..445
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 1..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..255
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 50642 MW; 3806F5C0DCFD37B1 CRC64;
MTAAGTSSGE TPAALAELVT QVSPNSQPQR NTRQPVRKTK KKKQPAPSET EKNIGSHENT
NKQPQQSLST SENDAQSPHT EQPPQRPEQI PTTATNNVKE ETQPTKEPSK PVPKQRKKKS
KLSSFFSSIV PCVGESSRNP AHDISSSEAP HKTQNQPSAS TSRRKSNNNI NNSSTVDLSQ
NNEDDIPPAT PVIPSQGVDM PLSDTAGLTS GAVMPPGKEL NPPTPSRQPS THQHHESESS
EEEEEEEVDE FESELADEER IIAKGGMGIP VGEDGQPNPL LPPLITSDNG KKCLVLDLDE
TLVHSSFKLI QHADYVVPVE IESQTHNVYV IKRPGVDAFL KRMGDLFEIV VFTASLSKYA
DPVLDMLDIN RVVRHRLFRE SCYNHKGNYV KDLSQLGRLI NDSIIIDNSP ASYVFHPNNA
VPVSSWFNDP HDTELTDLCP FLTDLTAVDD VRGILNGTLL AS
//