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Database: UniProt
Entry: A0A024TEG7_9STRA
LinkDB: A0A024TEG7_9STRA
Original site: A0A024TEG7_9STRA 
ID   A0A024TEG7_9STRA        Unreviewed;       852 AA.
AC   A0A024TEG7;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=GPI ethanolamine phosphate transferase 3 {ECO:0000256|ARBA:ARBA00020841};
GN   ORFNames=H310_13816 {ECO:0000313|EMBL:ETV91757.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV91757.1};
RN   [1] {ECO:0000313|EMBL:ETV91757.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETV91757.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.
CC       {ECO:0000256|ARBA:ARBA00008695}.
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DR   EMBL; KI914007; ETV91757.1; -; Genomic_DNA.
DR   RefSeq; XP_008879683.1; XM_008881461.1.
DR   AlphaFoldDB; A0A024TEG7; -.
DR   STRING; 157072.A0A024TEG7; -.
DR   EnsemblFungi; H310_13816-t26_1; H310_13816-t26_1-p1; H310_13816.
DR   EnsemblProtists; ETV91757; ETV91757; H310_13816.
DR   GeneID; 20090866; -.
DR   VEuPathDB; FungiDB:H310_13816; -.
DR   eggNOG; KOG2126; Eukaryota.
DR   OrthoDB; 5479199at2759; -.
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   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16023; GPI_EPT_3; 1.
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; IPR037675; PIG-O_N.
DR   InterPro; IPR045687; PIGG/GPI7_C.
DR   InterPro; IPR039524; PIGO/GPI13.
DR   PANTHER; PTHR23071:SF1; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 3; 1.
DR   PANTHER; PTHR23071; PHOSPHATIDYLINOSITOL GLYCAN; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        450..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        477..495
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        539..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        565..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        612..634
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        646..665
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        677..702
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        753..773
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        785..804
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        816..836
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          692..830
FT                   /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19316"
SQ   SEQUENCE   852 AA;  94228 MW;  A78FF53A72E8E09A CRC64;
     MVAGAVVVSF VLHAAAVLLF TNGFFLTRYE AKEVSTCTEE AAVASSMHHH LRRQNGSTSG
     CWSNVKFPRV VYIVIDALRY DFMHEASQIE QRQKAKDGGQ YFLNHLPHVH AVLRDRPAHS
     LLLRFVADAP TMTMQRLKGL TTGTLPTFLD IKDNMHSEEI VEDSWIKQLT ALNKSIVFMG
     DDTWGKLYPT SFLRNYSYDS FNVKDLDTVD NGVLEHFFPE LVNQTDWDVL IAHFLGVDHV
     GHTFGPNHPK MQSKLHQMNE FLVELTNTLP SDVLAVVLGD HGMSSDGNHG GATDDETGAA
     LFLFSKARPL HALDQDRSMY DVLFDSPNEV AQVDLVPTLS LLMGLPIPFG NLGAVIPNLF
     FESTGPGAFN VTDALTHLND ALWVNAHQLR HQFLTTQTIR MDLPAMIQLE KVFAAAQASA
     MDAHATHRLL QTYLRDALSL SRALYTQFDL VSMIHGIALQ LAAFVALHFG SFCLRRLPMA
     LGVGCFVGFT WPFIASHVSA LLPGAPLPRY LATAGLSTAL LAFRYRPFVS ASTHLSRRSV
     GLAMLVVLHC ASLFSNSYLV VQDRVLLFLS ATTVALLGMD ILVQRKWSHL PPFMLLCVVH
     RLFAAWPHPN IVFTTVTVQM TWIPMAALGV WICFVHPLSL ISYVCVWLYW FDVFPLFLPW
     VVYGWTILHL RQPSSPLLVL VLLHGPSSPG TFALFIAMAT LFHSLDKSPS VPTTVGYCFL
     VHTLYFQSGH GNSFASLQNA AAFVGMAKFQ WHIAGVLLAV NTFGAFWLGL ALVPTPATQT
     TTVVTGYFTL SAICTTIFVA ICRRHLMVWA IFAPKFVFDA AISVAVHGLV LAQALLGHVE
     KSDGDCKMAH LS
//
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