ID A0A0V0TBT1_9BILA Unreviewed; 1746 AA.
AC A0A0V0TBT1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=GPI ethanolamine phosphate transferase 1 {ECO:0000256|ARBA:ARBA00020831};
GN Name=Pign {ECO:0000313|EMBL:KRX36019.1};
GN ORFNames=T05_2397 {ECO:0000313|EMBL:KRX36019.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX36019.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX36019.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX36019.1};
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:KRX36019.1}.
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DR EMBL; JYDJ01000391; KRX36019.1; -; Genomic_DNA.
DR STRING; 144512.A0A0V0TBT1; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000055048; 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; 1.
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:UP000055048};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRX36019.1};
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 428..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 570..587
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 593..611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 675..693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 699..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 752..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 790..813
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 825..845
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 857..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1023..1046
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1091..1409
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1434..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1656..1746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1457
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1660..1705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1746 AA; 196115 MW; CEA8A3D4A03CB6F7 CRC64;
MWKPILLGVF VHCVLLYAAL DIFYSSPVIH GMSPQGASSS PPAKRLVFIV ADGLRADALF
SQKRCLQKNS LFLRGSWGYS QCRVPTESRP GHVALLSGIY EDVNAVTRGW RENPVEFDSV
LNQSRYTWAW GSPDIVSLFV KGKYASHIFV DAYASQMQQF YQDSSQLDEW VFDKVEHFLN
DSYYNSTLRS MVMEEKVVFF LHLLGIDVAG HSYKPHSEEY EKSILLVDKG IEKLYELFEK
FFNDEQTAYV FTSDHGMTDW GSHGSGSLDE ISTPLIAWGA GIRTTTVPKN VPPCWNDIDE
QHCRINQVDV APLLASLIGI NFPMNSVGIL PLDLLNVSQK AESLLMWNNF KQILDQFLLL
RKRKVEAYFE MFFREFSDFS FAKMEMFVKT VEQLLVQKRY SYVVRLCQKW IPTLLRGVDY
YHRYEQRFLC FCIVCCFVTW IACAVSFLFA RDGIVKNDFT FMHSSTVYIY LIFCFFASIF
WLNSFAFSYY LYALLPFYLY NVATTGKTNI KLLLKLSKVN ISFMVEIILT VIFVEMLLAS
FFFRTSLVVC NAILMFWSVT ISLHDWTIKL FWIVLCMITS IFLNLPVVGQ SPFYSMVIGF
SCFITLFFSL FKLCNWNNNC TSIHPLCIVF HLALTINLSQ ATTELEEPLP WACRLCSWIL
LISSPFIPLT TNTRVIVRLL TVWSSILLPL SLMSVSYEPI FFSFYAIQLC LWIWIEMNLD
RHGRMLCLQD LNFKAECQFS QSIACMSDIR KSAIFIFFLL LGFFGTGNIA SINSFDPKFV
MLFVSEFSPF LMGALLMLKI LLPLLFACCT LRVLELFTCS KLSTIYWYAV VICDLLALQF
FFLLKDTGSW LEIGESISHY VIAMTLVAVN MEYLICLTIV SVFISGNVGA GEIRCKFYIS
PLLPAHLDVR EGLLGAGNVS SSNSDEQICF PQFSQCMTIW QYYPGNENIT TISLQGCWKS
NDYDCERHRC IAHADINTEF LTHSRYCCCS SSLCNENYTY EFIAKRPSET RSITDENNGA
KEFTISISIF VLFIVVALVA LVYLIVRLCF SSGSLFTVCT KHCLGKRQLL LFNGKTGAGL
DEHQDVNPAD ICLFHVLCTG RYSTTWLASF GGRHVAVKMY VDEAASSYAN ELAVFKLPLM
NHDNLVNFYC CSNSSSSSGG NTGANKDVNN HHPSLGKYWL VTGYEAGGTL TEFLNVNKLS
WIEMCRMAAS VTRGLAHLHS ELKSGGLVKP AIAHRDVKSG NVLVKSNGEC CLCDFGFAIV
LDKTALCKNG ICASLTEVGT FRYMAPELLE GAANLRDPET TLKQVDVYAL GLVLWEIVSR
CQHVYMMSHQ SVPEYILPFG DEVPACPSLE TMQLVVCKKK HRPLFAPAMY QTTHGPLKSL
RELIEDCWDQ DCEARISSLC AEERFNELIY AYDNTTETAE FIDNYQPLKI KQQNNTVAGE
DDDDDDEDED LVVDGDDGET EFLISNGQIS MPDSAVGSGS SDSNGQFYYR GNSSSDTNRT
DTSGFISVGL TNSSSSSSSD RGRSYNSSSG YQTNTSDSLM RSDDADPKGQ LSQKKKNPGY
DELHSNLKKI CTANGDDFDD DISLPNLSLS IKSLHYNNKN NNNHPMRRND LYPLLLVKSA
TSGTSSGTTT TNPCNLTTID QVLKSQIYDQ LKMKVEDDSS TDTGCMSTTT TQLSTEGTTS
SSSSSGSASS SSASASASNS ASSSSDDRSR LEEAEDSVFV QALYKKPSPK DDDTLPNFCS
SSYNIV
//
