GLEYA domain; The GLEYA domain is related to lectin-like binding domains found in the S. cerevisiae Flo proteins and the C. glabrata Epa proteins. It is a carbohydrate-binding domain that is found in fungal adhesins (also referred to as agglutinins or flocculins). Adhesins with a GLEYA domain possess a typical N-terminal signal peptide and a domain of conserved sequence repeats, but lack glycosylphosphatidylinositol (GPI) anchor attachment signals. They contain a conserved motif G(M/L)(E/A/N/Q)YA, hence the name GLEYA. Based on sequence homology, it is suggested that the GLEYA domain would predominantly contain beta sheets. The GLEYA domain is also found in S. pombe protein Swiss:Q92344, thought to be a kinetochore portein (Sim4 complex subunit), however no direct evidence for kinetochore association has been found. Furthermore, a global protein localization study in S. pombe identified it as a secreted protein localized to the Golgi complex.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418607224   93 FTLQIDGYFLAPETGEYTFSI-GTNSGIDFKFGSNGK-CCDDPkasvNNDMRVTILNDPDQKTLTqrivkVNLQKGLYYP 170
Cdd:pfam10528    1 FALNHRGYFYAPVTGTYTFTLpNADDIAYLWLGDKAYsGWTRA----NADLVATYGGGGGSGTYT-----VTLTAGTYYP 71

                           90
                   ....*....|
gi 1418607224  171 FLLVWfTNRG 180
Cdd:pfam10528   72 IRIVY-ANGG 80

GLEYA domain; The GLEYA domain is related to lectin-like binding domains found in the S. cerevisiae Flo proteins and the C. glabrata Epa proteins. It is a carbohydrate-binding domain that is found in fungal adhesins (also referred to as agglutinins or flocculins). Adhesins with a GLEYA domain possess a typical N-terminal signal peptide and a domain of conserved sequence repeats, but lack glycosylphosphatidylinositol (GPI) anchor attachment signals. They contain a conserved motif G(M/L)(E/A/N/Q)YA, hence the name GLEYA. Based on sequence homology, it is suggested that the GLEYA domain would predominantly contain beta sheets. The GLEYA domain is also found in S. pombe protein Swiss:Q92344, thought to be a kinetochore portein (Sim4 complex subunit), however no direct evidence for kinetochore association has been found. Furthermore, a global protein localization study in S. pombe identified it as a secreted protein localized to the Golgi complex.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418607224   93 FTLQIDGYFLAPETGEYTFSI-GTNSGIDFKFGSNGK-CCDDPkasvNNDMRVTILNDPDQKTLTqrivkVNLQKGLYYP 170
Cdd:pfam10528    1 FALNHRGYFYAPVTGTYTFTLpNADDIAYLWLGDKAYsGWTRA----NADLVATYGGGGGSGTYT-----VTLTAGTYYP 71

                           90
                   ....*....|
gi 1418607224  171 FLLVWfTNRG 180
Cdd:pfam10528   72 IRIVY-ANGG 80

GLEYA domain; The GLEYA domain is related to lectin-like binding domains found in the S. cerevisiae Flo proteins and the C. glabrata Epa proteins. It is a carbohydrate-binding domain that is found in fungal adhesins (also referred to as agglutinins or flocculins). Adhesins with a GLEYA domain possess a typical N-terminal signal peptide and a domain of conserved sequence repeats, but lack glycosylphosphatidylinositol (GPI) anchor attachment signals. They contain a conserved motif G(M/L)(E/A/N/Q)YA, hence the name GLEYA. Based on sequence homology, it is suggested that the GLEYA domain would predominantly contain beta sheets. The GLEYA domain is also found in S. pombe protein Swiss:Q92344, thought to be a kinetochore portein (Sim4 complex subunit), however no direct evidence for kinetochore association has been found. Furthermore, a global protein localization study in S. pombe identified it as a secreted protein localized to the Golgi complex.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418607224   93 FTLQIDGYFLAPETGEYTFSI-GTNSGIDFKFGSNGK-CCDDPkasvNNDMRVTILNDPDQKTLTqrivkVNLQKGLYYP 170
Cdd:pfam10528    1 FALNHRGYFYAPVTGTYTFTLpNADDIAYLWLGDKAYsGWTRA----NADLVATYGGGGGSGTYT-----VTLTAGTYYP 71

                           90
                   ....*....|
gi 1418607224  171 FLLVWfTNRG 180
Cdd:pfam10528   72 IRIVY-ANGG 80

PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418607224   82 DTFGVVMHRSNFTLQIDGYFLAPETGEYTFSIGTnsgidfkfgsngkcCDDPKASVNNdmRVTI-LNDPDQKTLTQRIV- 159
Cdd:pfam07691   35 DVPGFGEAPGDFSARWTGYLLPPESGTYTFGVAS--------------DDGARLWIDG--ELVIdNWGQHPPDASPEESn 98

                           90
                   ....*....|....*..
gi 1418607224  160 KVNLQKGLYYPFLLVWF 176
Cdd:pfam07691   99 TLYLVAGKLYPIRIEYF 115