ID L1LGC3_THEEQ Unreviewed; 555 AA.
AC L1LGC3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Gpi-anchor transamidase, putative {ECO:0000313|EMBL:EKX74411.1};
GN ORFNames=BEWA_044910 {ECO:0000313|EMBL:EKX74411.1};
OS Theileria equi strain WA.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=1537102 {ECO:0000313|EMBL:EKX74411.1, ECO:0000313|Proteomes:UP000031512};
RN [1] {ECO:0000313|EMBL:EKX74411.1, ECO:0000313|Proteomes:UP000031512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA {ECO:0000313|EMBL:EKX74411.1,
RC ECO:0000313|Proteomes:UP000031512};
RX PubMed=23137308; DOI=10.1186/1471-2164-13-603;
RA Kappmeyer L.S., Thiagarajan M., Herndon D.R., Ramsay J.D., Caler E.,
RA Djikeng A., Gillespie J.J., Lau A.O., Roalson E.H., Silva J.C., Silva M.G.,
RA Suarez C.E., Ueti M.W., Nene V.M., Mealey R.H., Knowles D.P., Brayton K.A.;
RT "Comparative genomic analysis and phylogenetic position of Theileria
RT equi.";
RL BMC Genomics 13:603-603(2012).
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SIMILARITY: Belongs to the peptidase C13 family.
CC {ECO:0000256|ARBA:ARBA00009941}.
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:EKX74411.1}.
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DR EMBL; ACOU01000001; EKX74411.1; -; Genomic_DNA.
DR AlphaFoldDB; L1LGC3; -.
DR STRING; 1537102.L1LGC3; -.
DR MEROPS; C13.005; -.
DR EnsemblProtists; EKX74411; EKX74411; BEWA_044910.
DR VEuPathDB; PiroplasmaDB:BEWA_044910; -.
DR eggNOG; KOG1349; Eukaryota.
DR OrthoDB; 1122658at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000031512; Unassembled WGS sequence.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; IEA:InterPro.
DR GO; GO:0003923; F:GPI-anchor transamidase activity; IEA:InterPro.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1460; -; 1.
DR InterPro; IPR028361; GPI_transamidase.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR48067; GPI-ANCHOR TRANSAMIDASE; 1.
DR PANTHER; PTHR48067:SF1; GPI-ANCHOR TRANSAMIDASE; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
PE 3: Inferred from homology;
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000031512};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..555
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003952718"
FT REGION 386..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 63132 MW; 806E6B3CA321608E CRC64;
MNMYLYCIFI ICTLISVKCR NIVQSDFIAG VSTVVGPDTY GVLQDYKDVY ARWDEYDVSG
LTLTTSKGIS GTKRSTHRDG DSTEGQEALN GFSVDISKYR SFIKSLNDLE NEIHTKYRRV
NSTFMSTSRF YYNYRHSGNV FAVMSSLLKF GNLSNNDTQV VVPETCLCHP TNTAMGRLYV
NSSVNKSEYK GKLANDSTNV FLENTKVTFK GHLVSKDSFR YLVTNRFPKK YPNSYKTYTS
DDFARFIYVT GHGGDSYLQF QAKTFISSAE YGLYHLELGI KEPKLPVLSI LDTCQASTMY
EKVDKGTKLA WIASSIRGES SYSHNPNHFI SVSTVDKFTF ILQNHLRNVM QGIMTGSKAS
VSRFSLHQLL RTYQRENPKD KLEYEVHNSM GKGGNSDQTT ENPEDTDAEK NLFIKYSRWI
KGTLSQLSTA YTFSMSTNRR SKDGISVNYG KDKKKTEKLY LGQFAFNYRK LYYNSIPFPY
GGGINTESQK LHERVAMDTH EKYRGSMNAS TDKLHAKRMA KHGLIVDIED NILQNYRLAA
SVMAALYILC TLTRN
//
