ID A0A1B7P1K7_9EURO Unreviewed; 561 AA.
AC A0A1B7P1K7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=FCP1 homology domain-containing protein {ECO:0000259|PROSITE:PS50969};
GN ORFNames=ACJ72_02754 {ECO:0000313|EMBL:OAX82898.1};
OS Emergomyces africanus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1955775 {ECO:0000313|EMBL:OAX82898.1, ECO:0000313|Proteomes:UP000091918};
RN [1] {ECO:0000313|EMBL:OAX82898.1, ECO:0000313|Proteomes:UP000091918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 136260 {ECO:0000313|EMBL:OAX82898.1,
RC ECO:0000313|Proteomes:UP000091918};
RA Cuomo C.A., Schwartz I.S., Kenyon C., de Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., de Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) 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:OAX82898.1}.
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DR EMBL; LGUA01000241; OAX82898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7P1K7; -.
DR STRING; 1658172.A0A1B7P1K7; -.
DR OrthoDB; 5473812at2759; -.
DR Proteomes; UP000091918; 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:UP000091918}.
FT DOMAIN 387..545
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 1..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 60907 MW; AB072CC842F4BC25 CRC64;
MTTSSNGPGS NSVLPLPNDA TSKNLSSTDT DQSINETPLE QHTPHTNSIQ DSSGNADLPK
KKRSFLRVPS RSSSDAKRRG QPAAPDRQHD GTESNAGSMK RGGSMASSKG SRRTDALNTA
GANPKESMPD ADDQPKEKLP KAPSKLFSFL SCCGGASNDD REEPIPPKIS VKPQSSQGRQ
PTPVEKAEPC AADSSIADSR EPTSFDEKVA LKANTDRKDL HTEDGVAPAR ALGEAGSDSS
TKIHLDKHSN PPAPSNSGSG SSSGSGSGSK AYTGRNSELP PIPASEKSAS SKSTSASIEK
KPGPNDVVSK QPNGDHDVAM KDTQSADSYI EEDFDTPLHE DPTQRAMEIP PPPPLDRNAE
SINRYIPPVP AIQPEKQQWL LPPIEPHLQN RKCLVLDLDE TLVHSSFKVL EKADFTIPVE
IEGQYHNIYV IKRPGVDQFM KRVGELYEVV VFTASVSKYG DPLLDQLDIH KVIHHRLFRD
SCYNHQGNYV KDLSQVGRDL RDTIIIDNSP TSYIFHPQHA IPISSWFSDA HDNELLDLIP
VLEDLADSQV RDVSLVLNVA L
//