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Database: UniProt
Entry: A0A136IV67_9PEZI
LinkDB: A0A136IV67_9PEZI
Original site: A0A136IV67_9PEZI 
ID   A0A136IV67_9PEZI        Unreviewed;       726 AA.
AC   A0A136IV67;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|RuleBase:RU367106};
GN   ORFNames=Micbo1qcDRAFT_166219 {ECO:0000313|EMBL:KXJ88778.1};
OS   Microdochium bolleyi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX   NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ88778.1, ECO:0000313|Proteomes:UP000070501};
RN   [1] {ECO:0000313|Proteomes:UP000070501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG   DOE Joint Genome Institute;
RA   David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA   Barry K., Grigoriev I.V.;
RT   "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT   beachgrass.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC       glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC       ethanolamine phosphate to the GPI second mannose.
CC       {ECO:0000256|RuleBase:RU367106}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000256|RuleBase:RU367106}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU367106}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU367106}.
CC   -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
CC       {ECO:0000256|RuleBase:RU367106}.
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DR   EMBL; KQ964257; KXJ88778.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136IV67; -.
DR   STRING; 196109.A0A136IV67; -.
DR   InParanoid; A0A136IV67; -.
DR   OrthoDB; 5479199at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000070501; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   InterPro; IPR039527; PIGG/GPI7.
DR   InterPro; IPR045687; PIGG/GPI7_C.
DR   PANTHER; PTHR23072:SF0; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 2; 1.
DR   PANTHER; PTHR23072; PHOSPHATIDYLINOSITOL GLYCAN-RELATED; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   Pfam; PF19316; PIGO_PIGG; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU367106};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502,
KW   ECO:0000256|RuleBase:RU367106};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367106};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367106};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU367106};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU367106}.
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        355..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        424..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        447..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        498..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        535..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        568..589
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        609..635
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        663..687
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        699..724
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   DOMAIN          292..725
FT                   /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19316"
SQ   SEQUENCE   726 AA;  80182 MW;  2FFABD72D9ECD63C CRC64;
     MKHKKPGKLV MHGDDTWLKL FPGIFDRADG TTSFFVSDFT EVDTNVTRHV PEELENDDWN
     TMVLHYLGLD HIGHKTGPRG PNMVPKQHEM DGIVRQIYEG IQNKPHLEST LLVLIGDHGM
     NDAGNHGASS AGETSPALVF VSPKLKTIAK QTKTPADFVE DFRYYSFVEQ SDLAPTLAAL
     LGFPIPKNSL GSFITEFLPM WQGNDRMEIL LRNGRQIYDI LVATFGVPQA SEPLSEQFCS
     TPASTAESLA CAWRTIQGTA DAAYEGSSFD PDWLNDITKW LNEAQSLMTS MASNYDVPRL
     TLGSGISAAA VALSTISVVL SSTVSFTGLV PYTLITLLYG IMMFASSYVE EEQHFWYWAT
     SIWFFFLTVK SLARKNGKPT RQTLITMGSA LLYLRVLRNW NQTGQKFAGE PDIVTIMLVP
     HPSLLWLLVL SAYALVAWQL YHELRDVAPV ISGSLITGLV TSAVSFKLAF TREDAPELMT
     GFASTLSNAF SGPTLVELAR AVFMGLGLAA IYPVYILLRR PAGSSPQSAM RTLHMLYTIF
     AMTQSRATNI PLFIVYSGIS TLLVRLDLSV MEVATTSLLL QFASFFAMAG NNAISGIDLS
     SAYNGVSGFD IGAVGVLTFL SNWAAPVWWS FWGVLRLLDC RHRGRDTALG AQQQHQQRPL
     QQYIALQTAF VAASLAFVMA ACMALRTHLF IWTVFSPKYL YSMAWSLGQH LGINVLFGSL
     LYWLGH
//
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