ID A0A178AVB3_9PLEO Unreviewed; 1045 AA.
AC A0A178AVB3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=GPI ethanolamine phosphate transferase 3 {ECO:0000256|ARBA:ARBA00020841};
GN ORFNames=IQ06DRAFT_272735 {ECO:0000313|EMBL:OAL01826.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL01826.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL01826.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL01826.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441710; OAL01826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AVB3; -.
DR STRING; 765868.A0A178AVB3; -.
DR InParanoid; A0A178AVB3; -.
DR OrthoDB; 5479199at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000077206; 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 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000077206};
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 54..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 614..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 642..659
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 671..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 746..765
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 787..806
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 848..873
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 885..903
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 933..956
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 968..987
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1030
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 1045 AA; 114833 MW; 0DFF803824B56D48 CRC64;
MQGEEVFTPL SEITAARQKA VPKAVPKRPA PARNVVAKDE DKAKRAGQVH FKAAHGLVVA
FFTFILILHI AGIYLFTSGF LLTRLVLDHK SECAIAPIDA ARGYASGDVQ KGCWHPKTFD
KAIVIIVDAL RYDFTVPFTA QFEPTDLNAI ASSNPPPIAP RHFHDAFPVL YETAQKQPNN
AFLLPFIADP PTTTLQRLKG LTTGTLPTFI DAGSNFAGTA IDEDNLVAQL RNASKRIVHL
GDDTWHSLFP GYFEPNLTHA YDSFNVWDLH TVDNGVNEHI FPLLQAENTK KWDIIFGHYL
GVDHAGHRYG PDHPAMTAKL NQMDDVFRRM IAELDDDTLL VVMGDHGMDT KGDHGGESDD
EIEAALWMYS KKGVFGRTSP AHALPPKSAK IRPVAQIDLV PTLSLLLGMP IPFNNLGKPI
EEAFIGSKGA DFENLAIVNR LAAAQIHRYQ DEYAKARGLD ESTRATSLAL WSAANEAWSS
LGARSKSEQF NSVYGAFSAY QRDTLSICRA LWARFDVPRM LSGVTILAST LIVLAMYARG
LQGDRTDLTP VFFTRGAIGA AIGAVVGLGA TFAISDLPQD HTLIFTTALT GIVGAASSFF
TIPHRILSPF PASIWGWTSV IFTLALSAGF AANSFTIWED EILLHFLTTF GVIAVVSSFR
QKDRVDRTLG IYHSILFTVL LRVASFSRLC REEQMPYCKS TYYASALSTT SAPWQLAIPA
TAALLVPTFI IGYFDGTKSY QHTAKLWLGL GLRFGLLLAA AYWALDAADD GNWYPGWDNV
ISITKRYVAQ IVLFISLAFG YSIYNWSKPL LSIIMNESQD KEGAPNQAIT VLGYANVHGS
RYAMLITIWY LAIALLQKPM GAGAIGILVW QLFSLFEIID TNSLHTSSIG PVVLGLLGSF
HYFKTGHQAT LSSIQWESAF IPLTTIRYPW TPLIVILNHF GAQILCAIAV PALVLWKIKP
QQKGLLGALA KVIATHILFY ATINLATTMW AGHLRRHLML YRIFSPRFML GASSLLIVDI
FAIFVGLWGA RMSILSVAEV FGFGG
//
