ID A0A067R5W0_ZOONE Unreviewed; 354 AA.
AC A0A067R5W0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative GPI-anchor transamidase {ECO:0000313|EMBL:KDR17719.1};
GN ORFNames=L798_07259 {ECO:0000313|EMBL:KDR17719.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR17719.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR17719.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR17719.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
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}.
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DR EMBL; KK852722; KDR17719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067R5W0; -.
DR STRING; 136037.A0A067R5W0; -.
DR EnsemblMetazoa; KDR17719; KDR17719; L798_07259.
DR eggNOG; KOG1349; Eukaryota.
DR InParanoid; A0A067R5W0; -.
DR OMA; PGHTNNW; -.
DR OrthoDB; 1122658at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000027135; 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.
DR PIRSF; PIRSF500138; GPI8; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
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:UP000027135};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..354
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027611991"
FT REGION 321..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 203
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 354 AA; 40075 MW; 293224B026C22DB1 CRC64;
MKNMTYGVAN ILVILILMLV SSISSIHRSL PEDFLQAGHT NNWAVLVDTS RFWFNYRHVA
NVLSIYRSVK RLGIPDSQII LIIADDMACN PRNPRPATVF NNANQHINVY GDDVEVDYRG
YEVTVENFVR LLTGRLPPGT PRSKQLLTDE GSNVLVYLTG HGGDGFLKFQ DSEEVTSQEL
ADAVEQMWQK RRYHEMFFMI DTCQGASLYE KFYSPNILAV ASSLVGEDSL SHHVDPAIGV
YIIDRYTYYA LDFLERVEPD STKTMGEFLS VCPKRACIST VGVRKDLFPR DPHKVPITDF
FGSLRPVELT LSGLNVTAMS RTQNQSRREE LKRKVSDRSL QYAKQFPTSK LGSS
//
