ID B6QV66_TALMQ Unreviewed; 852 AA.
AC B6QV66;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|ARBA:ARBA00020830, ECO:0000256|RuleBase:RU367106};
GN ORFNames=PMAA_011380 {ECO:0000313|EMBL:EEA18858.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA18858.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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|ARBA:ARBA00004687,
CC ECO:0000256|RuleBase:RU367106}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367106}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU367106}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
CC {ECO:0000256|ARBA:ARBA00005315, ECO:0000256|RuleBase:RU367106}.
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DR EMBL; DS995906; EEA18858.1; -; Genomic_DNA.
DR RefSeq; XP_002153243.1; XM_002153207.1.
DR AlphaFoldDB; B6QV66; -.
DR VEuPathDB; FungiDB:PMAA_011380; -.
DR HOGENOM; CLU_004770_0_0_1; -.
DR OrthoDB; 5479199at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000001294; 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; cd16024; GPI_EPT_2; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037674; PIG-G_N.
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:UP000001294};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 468..492
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 498..519
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 567..584
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 596..619
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 640..664
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 753..773
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 793..816
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 828..850
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT DOMAIN 434..847
FT /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19316"
SQ SEQUENCE 852 AA; 93917 MW; B87B6EDA642ED389 CRC64;
MAGALSKWTL FLANALIPVA VLLFCSGYFP YKPILSGAAE PPVWGKAPPV FDKVILMVVD
ALRSDFVYSN NSGFVFTQDL IRTGAAWPFT AHASSPTVTM PRIKAITTGS VPSFSDVVLN
IAESESMSTL IHQDTIITQL KYGLPGKMLM YGDDTWLNLF PDTFDRFDGT SSFFVSDFTE
VDNNVTRHVS PELAQDDWSV MVLHYLGLDH IGHKAGPKSS HMIPKQREMD GIVEEIYNAM
LSETHLDSTL LVLLGDHGMN EAGNHGGSSA GETSPALTFI SPKLQKHSEN SELKGRDSPI
EAENFEFYHT VEQSDITPTL AGLLGVPIPL NSLGVFIPEF LGLWGNEVDR VTMLLENTVQ
IQNVIKMAYP KFSTNGDKIN EVSSANGTGL GSSALERLEY EFIAAGLSMS PDEKSTRTHY
KFLHSAQSLM SGAASSYKLS MLYSGTLTVA FACLVSAFIA YYTLPTPLVA STVFLFITSV
LHGAMMFASS FVEEEQQFWY WITTAWTVYI HLRATSFGLN RLSTKSIIYS ISFAAAGRIM
RRWNQTGQKF AGEPDIVQYL SSSQPKLLWA LVLLTYMVNC QSMIGSAPFR NVFGKSLWTI
LSIAVSFAAV VFKVSFTAAD APELLDPLIL RITRWGFQTS LVFQARLVFI GIASLLVICV
ISSFTSRGVQ NGRKRLFHEA ITLFLITQSR ATNIPLFVLF KVQASIIERV DLNSIETTLN
LILMQHVAFF AFGGSNALSS VDLSTAYNGV SDYNVVVVGL LTFVSNWAGP IWWMSETAIN
QRHLTQTEAT NRVALLSFNT TMELLAVMAA CTILRTHLFV WTVFSPKFLY SIAWALANHL
GMNLLATYGL SL
//
