PKAT, KLD domain; This is the Kringle-like domain (KLD) found in Melanocyte protein PMEL, Transmembrane glycoprotein NMB (GPNMB) and TMEM130, which is downstream the PKD domain. It contains six highly conserved cysteine residues that form the disulphide bonds of mature PMEL dimers. (Chrystal et. al., Molecules 2021, 26(12), 3529; https://doi.org/10.3390/molecules26123529). This domain is perfectly conserved in PMEL and GPNMB which suggests that GPNMB also forms dimers. PMEL and GPNMB, together with TMEM130 (its most ancient paralogue), have a conserved domain architecture and have been recently described as the PKAT (PKD- and KLD-Associated Transmembrane) protein family (Chrystal et. al., Molecules 2021, 26(12), 3529; https://doi.org/10.3390/molecules26123529). PMEL and GPNMB share overlapping phenotypes and disease associations, such as melanin-based pigmentation, cancer, neurodegenerative disease and glaucoma.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 992319621  473 SCQGGLPKEACMEISSPGCQPPAQRLCQPVLPSPACQLVLHQILKgGSGTYC 524
Cdd:pfam20433   1 TCQGSLPTEVCTVVSDPTCQTPQNTVCNPVSPSPECQLVLRRAFN-GSGTYC 51

DNA polymerase III subunit gamma/tau;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319621 297 PLTSCGSSPVPGTTDGHRPTAEAP------NTTAGQVPTTEVVGTTPGQAPTAEPSGTTSVQVPTTEV------ISTAPV 364
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPaaapvaQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAApaaapaAAPAAV 445

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 992319621 365 QMPTAESTAAQVTTTEWVETTARELPIPEPEGPDASSIMSTESITGSLGPLLDGT 419
Cdd:PRK14951 446 ALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEGDVWHAT 500

PKAT, KLD domain; This is the Kringle-like domain (KLD) found in Melanocyte protein PMEL, Transmembrane glycoprotein NMB (GPNMB) and TMEM130, which is downstream the PKD domain. It contains six highly conserved cysteine residues that form the disulphide bonds of mature PMEL dimers. (Chrystal et. al., Molecules 2021, 26(12), 3529; https://doi.org/10.3390/molecules26123529). This domain is perfectly conserved in PMEL and GPNMB which suggests that GPNMB also forms dimers. PMEL and GPNMB, together with TMEM130 (its most ancient paralogue), have a conserved domain architecture and have been recently described as the PKAT (PKD- and KLD-Associated Transmembrane) protein family (Chrystal et. al., Molecules 2021, 26(12), 3529; https://doi.org/10.3390/molecules26123529). PMEL and GPNMB share overlapping phenotypes and disease associations, such as melanin-based pigmentation, cancer, neurodegenerative disease and glaucoma.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 992319621  473 SCQGGLPKEACMEISSPGCQPPAQRLCQPVLPSPACQLVLHQILKgGSGTYC 524
Cdd:pfam20433   1 TCQGSLPTEVCTVVSDPTCQTPQNTVCNPVSPSPECQLVLRRAFN-GSGTYC 51

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992319621 233 LRNQPLTFALQLHDPSGYlaeADLSYTWDFGDSSGTLiSRALVVTHTYLEPGPVTAQVVLQAA 295
Cdd:cd00146   10 VAELGASVTFSASDSSGG---SIVSYKWDFGDGEVSS-SGEPTVTHTYTKPGTYTVTLTVTNA 68

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319621   197 YVPLAHSSSAF-TITDQVPFSVSVSQLR-ALDGGNKHFLRNQPLTF-ALQLHDPSGYLaeadlsYTWDFGDSSGTLISRA 273
Cdd:TIGR00864 1062 YLATVLASNAFeNISQQINMSVRAILPRvAIGTEDGLLLAGKPADFeAHPLPSPGGIH------YEWDFGDGSALLQGRQ 1135

                           90
                   ....*....|..
gi 992319621   274 LVVTHTYLEPGP 285
Cdd:TIGR00864 1136 PAAAHTFAKRGP 1147

PKAT, KLD domain; This is the Kringle-like domain (KLD) found in Melanocyte protein PMEL, Transmembrane glycoprotein NMB (GPNMB) and TMEM130, which is downstream the PKD domain. It contains six highly conserved cysteine residues that form the disulphide bonds of mature PMEL dimers. (Chrystal et. al., Molecules 2021, 26(12), 3529; https://doi.org/10.3390/molecules26123529). This domain is perfectly conserved in PMEL and GPNMB which suggests that GPNMB also forms dimers. PMEL and GPNMB, together with TMEM130 (its most ancient paralogue), have a conserved domain architecture and have been recently described as the PKAT (PKD- and KLD-Associated Transmembrane) protein family (Chrystal et. al., Molecules 2021, 26(12), 3529; https://doi.org/10.3390/molecules26123529). PMEL and GPNMB share overlapping phenotypes and disease associations, such as melanin-based pigmentation, cancer, neurodegenerative disease and glaucoma.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 992319621  473 SCQGGLPKEACMEISSPGCQPPAQRLCQPVLPSPACQLVLHQILKgGSGTYC 524
Cdd:pfam20433   1 TCQGSLPTEVCTVVSDPTCQTPQNTVCNPVSPSPECQLVLRRAFN-GSGTYC 51

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992319621 233 LRNQPLTFALQLHDPSGYlaeADLSYTWDFGDSSGTLiSRALVVTHTYLEPGPVTAQVVLQAA 295
Cdd:cd00146   10 VAELGASVTFSASDSSGG---SIVSYKWDFGDGEVSS-SGEPTVTHTYTKPGTYTVTLTVTNA 68

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 992319621  236 QPLTF-ALQLHDPSGYLaeadLSYTWDFGDssGTlISRALVVTHTYLEPG--PVT 287
Cdd:pfam18911  18 ETVTFdASASDDPDGDI----LSYRWDFGD--GT-TATGANVSHTYAAPGtyTVT 65

DNA polymerase III subunits gamma and tau; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992319621 297 PLTSCGSSPVPGTTDGHRPTAEAP------NTTAGQVPTTEVVGTTPGQAPTAEPSGTTSVQVPTTEV------ISTAPV 364
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPaaapvaQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAApaaapaAAPAAV 445

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 992319621 365 QMPTAESTAAQVTTTEWVETTARELPIPEPEGPDASSIMSTESITGSLGPLLDGT 419
Cdd:PRK14951 446 ALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEGDVWHAT 500