ID T0LCQ5_COLGC Unreviewed; 417 AA.
AC T0LCQ5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Peptidase C13 family protein {ECO:0000313|EMBL:EQB46120.1};
GN ORFNames=CGLO_14868 {ECO:0000313|EMBL:EQB46120.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB46120.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB46120.1}.
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DR EMBL; AMYD01003526; EQB46120.1; -; Genomic_DNA.
DR AlphaFoldDB; T0LCQ5; -.
DR STRING; 1237896.T0LCQ5; -.
DR MEROPS; C13.005; -.
DR eggNOG; KOG1349; Eukaryota.
DR HOGENOM; CLU_044656_2_2_1; -.
DR OMA; PGHTNNW; -.
DR OrthoDB; 1122658at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000015530; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000015530};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..417
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027663737"
FT REGION 398..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 306..356
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 148
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 190
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 417 AA; 46697 MW; 6D97904379A777F3 CRC64;
MKLSRLLQLP VLLAASTLAP AVLAEHTSNW AVLVCTSRFW FNYRHLANVL SIYRTVKRLG
IPDSQIILML PDDMACNPRN AFPGTVYSNS DRAVDLYGDN IEVDYRGYEV TVENFIRLLT
DRVGDEMPRS KRLLTDDRSN ILVYMTGHGG NEFLKFQDAE EIGAFDLADA FEQMWEKKRY
HEILFMIDTC QANTMYSKLY SPNIIATGSS ELDQSSYSHH ADNDVGVAVI DRYTYYNLEF
LESQVQDLSS KKTVGELFDS YTYEKIHSNA GVRYDLFPGG ADAARSRRIT DFFGNVQNVE
VDGAKNMVLD EELLELSQKI AALKKRAEEA DAAARNATLA EKAARGEEQK AKAQAKRVQM
AKPLTNDNWW EKKLVGATAL LGCALLWALG SFLEAPKKSD DEAKKTSGQN GHAAVKA
//
