ID A0A0D9NQY8_METAN Unreviewed; 638 AA.
AC A0A0D9NQY8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=FCP1 homology domain-containing protein {ECO:0000259|PROSITE:PS50969};
GN ORFNames=H634G_08280 {ECO:0000313|EMBL:KJK76389.1};
OS Metarhizium anisopliae BRIP 53293.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK76389.1, ECO:0000313|Proteomes:UP000054544};
RN [1] {ECO:0000313|Proteomes:UP000054544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA Ash G.J.;
RT "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT comparative genomics of Metarhizium species.";
RL BMC Genomics 15:660-660(2014).
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DR EMBL; KE384744; KJK76389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D9NQY8; -.
DR STRING; 1291518.A0A0D9NQY8; -.
DR Proteomes; UP000054544; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR013879; DUF1761.
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; PTHR40638; UPF0591 MEMBRANE PROTEIN C15E1.02C; 1.
DR PANTHER; PTHR40638:SF1; UPF0591 MEMBRANE PROTEIN C15E1.02C; 1.
DR Pfam; PF08570; DUF1761; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054544};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 578..596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 608..630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 305..478
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 638 AA; 69475 MW; 63DCACF69515514D CRC64;
MNSLNIITAR VSPSASPSPS RSNSLGNISA GLLPDEKSTD GNDGKDAASS DSFLGCDYDG
SQQTNEKSSY VATEDTPLLD GGKDGNKRAS WWHSIPRRLV SSIISSIRWV LATLASPGVY
LIACFYDEHG VFAPLSQVKR LFGVQKGGGM DSYGSHENHA ANHAEPPAVS GSSQPWGYRR
IAPRPAPSSG SSTSGQSSES EGETPKGSSS RHGRSKSLNP AEELSSARRS IRIKLHNDDA
LRQRKQHRRA QSAVARTKMD DEDLSAQLKS PTSPIAALTK YPKTPAPPRP LIPRRQPSYL
KLDASVKHQK TLILDLDETL IHSMSKGGRS SGHMVEVRLN TASLGMGTAP GGAAQHPILY
WVNKRPYCDE FLRRICKWFN LVIFTASVQE YADPVIDWLE AERKFFSARY YRQHCTYRQG
AYIKDLSSVE PDLSKVMILD NSPLSYLFHE DNAIPIQGWI NDPTDNDLMH LIPMLEGLQY
VHDVRALLAL RGDLPPVKPS AIALGTFFNH GIELAVLGPV FGQTYQRAKQ ANTKEEFIKS
KEASGAAIAW GTSFVGSALQ SYGVAALINA TGTLSYKGAA YLGGLIFAAT AAPGFLTQIF
SEKRPIDTVG VSIAAKLVET IGLSLFLTWW GTRTNPFD
//
