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Database: UniProt
Entry: X0B5L6_FUSOX
LinkDB: X0B5L6_FUSOX
Original site: X0B5L6_FUSOX 
ID   X0B5L6_FUSOX            Unreviewed;       653 AA.
AC   X0B5L6;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|RuleBase:RU367106};
GN   ORFNames=FOMG_07313 {ECO:0000313|EMBL:EXK40466.1};
OS   Fusarium oxysporum f. sp. melonis 26406.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089452 {ECO:0000313|EMBL:EXK40466.1};
RN   [1] {ECO:0000313|EMBL:EXK40466.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=26406 {ECO:0000313|EMBL:EXK40466.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum melonis.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXK40466.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=26406 {ECO:0000313|EMBL:EXK40466.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of the Genome Sequence of Fusarium oxysporum f. sp. melonis
RT   26406.";
RL   Submitted (MAY-2012) 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; JH659332; EXK40466.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0B5L6; -.
DR   VEuPathDB; FungiDB:FOMG_07313; -.
DR   UniPathway; UPA00196; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:InterPro.
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   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        240..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        295..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        350..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        432..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        472..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        504..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        545..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        585..612
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   TRANSMEM        624..649
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367106"
FT   DOMAIN          232..651
FT                   /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19316"
SQ   SEQUENCE   653 AA;  72632 MW;  933AB5E7068ACE0B CRC64;
     MVLHYLGLDH IGHKAGPKSS NMFPKQREMD GIVKTLFEAM ESKPHLDSTL LVLCGDHGMN
     DAGNHGASSP GETSPALVFM SPRLKKVSHR LPAPAQPKDE FDYYSMVEQS DLAPTIAALL
     GFPVSKNNLG AFIPDFLPFW HKTSDQIQIL VRNARQILNI ITAAFGSELF DAQSSVDPCA
     LEQTEINELA CQWRRINKEA HVLAAGNKLD QKWLDDMSQW LRRAQDLMSS MASNYDMPKL
     YIGQAIAAVA ATASTVVLVS LGTHRDGQIL PFSLMTLSYG AMMYASSYVE EEQHFWYWSS
     SIWLVIQGVL HIRRRNSLAD IAWVFVALVA LRLTRGWNQT GQKFAGSPDI VKGFIVTHPQ
     LLWAIITFGY ILMSFRLLAR LKSLPSLAST STTSILLMSA YSFKLDFTSE DAPELVVGFA
     RSLNDMFVGQ SLLWRARTAF ILLGVLFGYG IYRSFTGGRN GQLQSAYLFH HLYTIFGITQ
     SRATNIPLFL LSDILFHALQ ATDLSVTGIT ITAILLQYTT FFAFGGSNAI SSVDLSSAYN
     GISGFNFFAV GFLTLVSNWA GPIFWTSAAN LLLLRKYHDG QRNAFWQYIT LQTVFVSATV
     ALVMAACTSL RTHLFIWTVF SPKYLYCMAW SLGQHLLINI GFGGLLFWLG SRN
//
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