ID A0A0V0V6Y5_9BILA Unreviewed; 1783 AA.
AC A0A0V0V6Y5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=GPI ethanolamine phosphate transferase 1 {ECO:0000256|ARBA:ARBA00020831};
DE Flags: Fragment;
GN ORFNames=T09_12094 {ECO:0000313|EMBL:KRX59280.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX59280.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX59280.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX59280.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.
CC {ECO:0000256|ARBA:ARBA00008400}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX59280.1}.
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DR EMBL; JYDN01000074; KRX59280.1; -; Genomic_DNA.
DR STRING; 181606.A0A0V0V6Y5; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16020; GPI_EPT_1; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR Gene3D; 2.10.60.10; CD59; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR007070; GPI_EtnP_transferase_1.
DR InterPro; IPR017852; GPI_EtnP_transferase_1_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037671; PIGN_N.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR PANTHER; PTHR12250:SF0; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 1; 1.
DR PANTHER; PTHR12250; PHOSPHATIDYLINOSITOL GLYCAN, CLASS N; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF04987; PigN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57302; Snake toxin-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 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 Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRX59280.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 532..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..598
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 604..622
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 686..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 710..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 763..781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..824
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 836..856
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 868..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1054..1077
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1122..1440
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1463..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1690..1745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1488
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1692..1736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1783
FT /evidence="ECO:0000313|EMBL:KRX59280.1"
SQ SEQUENCE 1783 AA; 200576 MW; 99BD3672D1044EE8 CRC64;
MWKPILLGVF VHCVLLYAAL DIFYSSPVIH GMSPQGASSS PPAKRLVFIV ADGLRADALF
SQKRCLQKNS LFLRRMSLRG SWGYSQCRVP TESRPGHVAL LSGIYEDVNA VTRGWRENPV
EFDSVLNQSR YTWAWGSPDI VSLFVKGKYA SHIFVDAYAS QMQQFYQDSS QLDEWVFDKV
EHFLNDSYYN STLRSMVMEE KVVFFLHLLG IDVAGHSYKP HSEEYEKSIL LVDKGIEKLY
ELFEKFFNDE QTAYVFTSDH GMTDWGSHGS GSLDEISTPL IAWGAGIRTT TVPKNVPPCW
NDIDEQHCRI NQVVFSWPVD VAPLLASLIG INFPMNSVGI LPLDLLNVSQ KAESLLMWNN
FKQILDQFLL LRKRKVEAYF EMFFREFSDF SFAKMEMFVK TVEQLLVQKR YSYVVRLCQK
WIPTLLRGVD YYHRYEQRFL CFCIVCCFVT WIACAVSFLF ARDGIVKNDF TFMHSSTVYI
YLIFCFFASI FWLNSFAFSY YLYALLPFYL YNVATTGKTN IKLLLKLSKV NISFMVEIIL
TVIFVEMLLA SFFFRTSLVV CNAILMFWSV TISLHDWTIK LFWIVLCMIT SIFLNLPVVG
QSPFYSMVIG FSCFITLFFS LFKHCNWNNN CTSIHPLCIV FHLALTINLS QATTELEEPL
PWACRLCSWI LLISSPFIPL TTNTRVIVRL LTVWSSILLP LSLMSVSYEP IFFSFYAIQL
CLWIWIEMNL DRHGRMLCLQ DLNFKAECQF SQSIACMSDI RKSAIFIFFL LLGFFGTGNI
ASINSFDPKF VMLFVSEFSP FLMGALLMLK ILLPLLFACC TLRVLELFTC SKLSTIYWYA
VVICDLLALQ FFFLLKDTGS WLEIGESISH YVIAMTLVAV VMTVYPLARF LTNCELFPQK
NMEYLICLTI VSVFISGNVG AGEIRCKFYI SPLLPAHLDV REGLLGAGNV SSSNSDEQIC
FPQFSQCMTI WQYYPGNENI TTISLQGCWK SNDYDCERHR CIAHADINTE FLTHSRYCCC
SSSLCNENYT YEFIAKRPSE TRSITDENNG AKEFTISISI FVLFIVVALV ALVYLIVRLC
FSSGSLFTVC TKHCLGKRQL LLFNGKTGAG LDENQDVNPA DICLFHVLCT GRYSTTWLAS
FGGRHVAVKM YVDEAASSYA NELAVFKLPL MNHDNLVNFY CCSNSSSSSG GNTGANKDVN
NHHPSLGKYW LVTGYEAGGT LTEFLNVNKL SWIEMCRMAA SVTRGLAHLH SELKSGGLVK
PAIAHRDVKS GNVLVKSNGE CCLCDFGFAI VLDKTALCKN GICASLTEVG TFRYMAPELL
EGAANLRDPE TTLKQVDVYA LGLVLWEIVS RCQHVYMMSH QSVPEYILPF GDEVPACPSL
ETMQLVVCKK KHRPLFAPAM YQTTHGPLKS LRELIEDCWD QDCEARISSL CAEERFNELI
YAYDNTTDTA EFIDNYQPLK IKQQNNTVAG EDDDDDDEDE DLVVDGDDGE TEFLISNGQI
SMPDSAVGSG SSDSNGQFYY RGNSSSDTNR TDTSGFISVG LTNSSSSSSS SDRGRSYNSS
SGYQTNTSDS LMRSDDADPK GQLSQKKKNP GYDELHSNLK KICTANGDDF DDDISLPNLS
LSIKSLHYNN KNNNNHPMRR NDLYPLLLVK SATSGTSSGT TTTNPCNLTT IDQVLKSQIY
DQLKMKVEDD SSTDTGCMST TTTQLSTEGT TSSSSSASAS SASASASASN SASSSSDDRS
RLEEAEDSVF VQALYKKPSP KDDDTLPNFC SSSYNIVCVY FSY
//
