|
Name |
Accession |
Description |
Interval |
E-value |
| ThuA |
pfam06283 |
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA ... |
29-241 |
2.12e-99 |
|
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA appears to be involved in utilization of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium. ThuA is involved in the conversion of of disaccharides to their respective 3-keto derivatives.
:
Pssm-ID: 461867 [Multi-domain] Cd Length: 213 Bit Score: 313.41 E-value: 2.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 29 KVLVFSKTMGFKHASIPAGIAALQKMGQENGFAVDTTKNADMFTDDNLKQYSAVVFLSTTGNVLDQFQEAAFERYIQAGG 108
Cdd:pfam06283 1 RVLVFSGTAGWRHESIPAGIEAIRKLGAENGFEVDATEDAAVFTDENLAQYDVVVFLNTTGDVLDEEQEAAFQRYVQAGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 109 GYVGIHAAADTEYDWGWYNDLAGAQFLSHPSGTPNADFIIKDKNFIATEFFTDSvWNRDDELYNYKNINPDVNVLMTLDE 188
Cdd:pfam06283 81 GFVGLHSAADTEYDWPWYGKLVGARFVAHDPAPQQATVDVEDRSHPITAGLPAE-WERTDEWYNFKPNPPGNHVLATTDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1532357307 189 STYEGGQ-NGDFHPIAWYHDFDGGRAFYTGGGHTDESFSEELFLKHVLGGIKYA 241
Cdd:pfam06283 160 SSYDGGGnMGVDHPVAWTREDGAGRVFYTALGHTTESYEDPEFRKHLLGGIRWA 213
|
|
| YliI |
COG2133 |
Glucose/arabinose dehydrogenase, beta-propeller fold [Carbohydrate transport and metabolism]; |
258-691 |
8.03e-92 |
|
Glucose/arabinose dehydrogenase, beta-propeller fold [Carbohydrate transport and metabolism];
:
Pssm-ID: 441736 [Multi-domain] Cd Length: 365 Bit Score: 298.77 E-value: 8.03e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 258 PPDTDRFSKVILSEGqFFEPTEMAVLPNNDVLIAQRRGEIMLYDDETKELKEVAKLDVYwktletpgVNAEEGVMGLQKD 337
Cdd:COG2133 21 PTLPPGFTVEVVADG-LDHPWGLAFLPDGRLLVTERAGRIRLLDDDGKLSTPVADLPVF--------AGGEGGLLGVALD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 338 PDYANNNWIYVYYAPTGDKwVNRLSRFKYADGNFdLDSEQIILDVDSQREiCCHTGGSIAFGPDNLLYLSTGDNSTPFne 417
Cdd:COG2133 92 PDFATNGYLYVAYTDPGGA-GTRVARFTLSDGDT-LTSEEVILDGLPAGG-GNHNGGRLAFGPDGKLYVSVGDRGNAC-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 418 kgekyvnngfaplndtpgheqyDARRSSGNTNDLRGKILRIKVneDGSydIPEGNLFPmGTEKTRPEIYTMGHRNPYRIS 497
Cdd:COG2133 167 ----------------------EARGNAQDLNSLRGKILRIDP--DGS--IPADNPFV-GTPGARPEIYAYGHRNPQGLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 498 VDVKRGYVYWGDVGPDarvdslktrgprGYDEMNQARQPGNFGWPLFIGDNyaykEYNyetgetgeafdpqkPMNTSRNN 577
Cdd:COG2133 220 FDPETGELWATEHGPD------------GGDELNRIEPGGNYGWPYCEGGQ----NYD--------------PIGDSTPD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 578 TGLTElppamPAYVFypydessqfpqttTGGRNAMAGPtyysdLYTGeDKLPDYYDGKVIIYDWMRGWMFAVHLKEDGSF 657
Cdd:COG2133 270 AGLTD-----PVATW-------------PPGHAPSGLA-----FYTG-DAFPAEYRGGLFVADLGSRRVVRVPLDGDGKV 325
|
410 420 430
....*....|....*....|....*....|....
gi 1532357307 658 NKMEPFAPEVkLNNLIDMEMSPDGRVYLLEYGSG 691
Cdd:COG2133 326 VGEEDFLTGA-GGRPRDVAQGPDGALYVLDDNDG 358
|
|
| CytC552 |
COG4654 |
Cytochrome c551/c552 [Energy production and conversion]; |
864-950 |
2.01e-33 |
|
Cytochrome c551/c552 [Energy production and conversion];
:
Pssm-ID: 443692 [Multi-domain] Cd Length: 88 Bit Score: 123.86 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 864 SAAVTGKALAQSMDCKTCHKEAEASIGPNYMDVAQKYKNRRDALSYLQTRIKTGGNGVWGEVTMPAHPKITSDETRQIAL 943
Cdd:COG4654 2 ADAAAGKALAKKSGCLACHAVDKKLVGPSYKDVAKKYKGKADAVAKLAKKIKKGGSGVWGDVPMPPHPQLSDAEAKALVK 81
|
....*..
gi 1532357307 944 YILSLAG 950
Cdd:COG4654 82 WILSLKK 88
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
723-788 |
3.29e-15 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
:
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 71.26 E-value: 3.29e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1532357307 723 TAGKTPLAINASVV--ASDREGDNITYTWDFGNGETKETTEPNVSYTYTDAGAYNLSVTVGDDKGESA 788
Cdd:pfam00801 2 SASGTVVAAGQPVTftATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSAN 69
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
720-855 |
7.35e-09 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
:
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 58.91 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 720 VETTAGKTPLAINASVVASdreGDNITYTWDFGNGETkeTTEPNVSYTYTDAGAYNLSVTVGDDKGESAVSESTGIVAGN 799
Cdd:COG3291 3 ATPTSGCAPLTVQFTDTSS---GNATSYEWDFGDGTT--STEANPSHTYTTPGTYTVTLTVTDAAGCSDTTTKTITVGAP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1532357307 800 SRPEVTINLNGGTPAFYLPGQKIAYEVSVTDPDGGTVDESNVFVSVDYLEGLDKVT 855
Cdd:COG3291 78 NPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTT 133
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThuA |
pfam06283 |
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA ... |
29-241 |
2.12e-99 |
|
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA appears to be involved in utilization of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium. ThuA is involved in the conversion of of disaccharides to their respective 3-keto derivatives.
Pssm-ID: 461867 [Multi-domain] Cd Length: 213 Bit Score: 313.41 E-value: 2.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 29 KVLVFSKTMGFKHASIPAGIAALQKMGQENGFAVDTTKNADMFTDDNLKQYSAVVFLSTTGNVLDQFQEAAFERYIQAGG 108
Cdd:pfam06283 1 RVLVFSGTAGWRHESIPAGIEAIRKLGAENGFEVDATEDAAVFTDENLAQYDVVVFLNTTGDVLDEEQEAAFQRYVQAGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 109 GYVGIHAAADTEYDWGWYNDLAGAQFLSHPSGTPNADFIIKDKNFIATEFFTDSvWNRDDELYNYKNINPDVNVLMTLDE 188
Cdd:pfam06283 81 GFVGLHSAADTEYDWPWYGKLVGARFVAHDPAPQQATVDVEDRSHPITAGLPAE-WERTDEWYNFKPNPPGNHVLATTDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1532357307 189 STYEGGQ-NGDFHPIAWYHDFDGGRAFYTGGGHTDESFSEELFLKHVLGGIKYA 241
Cdd:pfam06283 160 SSYDGGGnMGVDHPVAWTREDGAGRVFYTALGHTTESYEDPEFRKHLLGGIRWA 213
|
|
| YliI |
COG2133 |
Glucose/arabinose dehydrogenase, beta-propeller fold [Carbohydrate transport and metabolism]; |
258-691 |
8.03e-92 |
|
Glucose/arabinose dehydrogenase, beta-propeller fold [Carbohydrate transport and metabolism];
Pssm-ID: 441736 [Multi-domain] Cd Length: 365 Bit Score: 298.77 E-value: 8.03e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 258 PPDTDRFSKVILSEGqFFEPTEMAVLPNNDVLIAQRRGEIMLYDDETKELKEVAKLDVYwktletpgVNAEEGVMGLQKD 337
Cdd:COG2133 21 PTLPPGFTVEVVADG-LDHPWGLAFLPDGRLLVTERAGRIRLLDDDGKLSTPVADLPVF--------AGGEGGLLGVALD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 338 PDYANNNWIYVYYAPTGDKwVNRLSRFKYADGNFdLDSEQIILDVDSQREiCCHTGGSIAFGPDNLLYLSTGDNSTPFne 417
Cdd:COG2133 92 PDFATNGYLYVAYTDPGGA-GTRVARFTLSDGDT-LTSEEVILDGLPAGG-GNHNGGRLAFGPDGKLYVSVGDRGNAC-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 418 kgekyvnngfaplndtpgheqyDARRSSGNTNDLRGKILRIKVneDGSydIPEGNLFPmGTEKTRPEIYTMGHRNPYRIS 497
Cdd:COG2133 167 ----------------------EARGNAQDLNSLRGKILRIDP--DGS--IPADNPFV-GTPGARPEIYAYGHRNPQGLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 498 VDVKRGYVYWGDVGPDarvdslktrgprGYDEMNQARQPGNFGWPLFIGDNyaykEYNyetgetgeafdpqkPMNTSRNN 577
Cdd:COG2133 220 FDPETGELWATEHGPD------------GGDELNRIEPGGNYGWPYCEGGQ----NYD--------------PIGDSTPD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 578 TGLTElppamPAYVFypydessqfpqttTGGRNAMAGPtyysdLYTGeDKLPDYYDGKVIIYDWMRGWMFAVHLKEDGSF 657
Cdd:COG2133 270 AGLTD-----PVATW-------------PPGHAPSGLA-----FYTG-DAFPAEYRGGLFVADLGSRRVVRVPLDGDGKV 325
|
410 420 430
....*....|....*....|....*....|....
gi 1532357307 658 NKMEPFAPEVkLNNLIDMEMSPDGRVYLLEYGSG 691
Cdd:COG2133 326 VGEEDFLTGA-GGRPRDVAQGPDGALYVLDDNDG 358
|
|
| COG3828 |
COG3828 |
Type 1 glutamine amidotransferase (GATase1)-like domain [General function prediction only]; |
23-246 |
1.36e-90 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain [General function prediction only];
Pssm-ID: 443040 [Multi-domain] Cd Length: 222 Bit Score: 289.87 E-value: 1.36e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 23 KREGEPKVLVFSKtmGFKHAsIPAGIAALQKMGQENGFAVDTTKNADMFTDDNLKQYSAVVFLSTTGNVLDQFQEAAFER 102
Cdd:COG3828 2 KAAKKKKVLVFSG--GFRHD-IEAGVPALKELLEENGFEVDVTEDAADFTPENLAKYDLVVFNNTTGDVLTDEQQAALED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 103 YIQAGGGYVGIHAAADTEYDWGWYNDLAGAQFLSHPSGTPnADFIIKDKNFIATEFFTDSvWNRDDELYNYK-NINPDVN 181
Cdd:COG3828 79 YVEAGGGFVGIHAATDTFRDWPWYGELVGGQFVSHPPIQE-ATVTVEDPDHPITKGLPDE-FTVTDEWYNFLrDPRPDVT 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1532357307 182 VLMTLDESTYEGGQNGDFHPIAWYHDFDGGRAFYTGGGHTDESFSEELFLKHVLGGIKYAIGENE 246
Cdd:COG3828 157 VLATTDESTYPGGGMGGDHPVAWTREYGKGRVFYTALGHDEESFEDPGFRTLLLRGILWAAGGKV 221
|
|
| GSDH |
pfam07995 |
Glucose / Sorbosone dehydrogenase; Members of this family are glucose/sorbosone dehydrogenases ... |
276-549 |
5.65e-38 |
|
Glucose / Sorbosone dehydrogenase; Members of this family are glucose/sorbosone dehydrogenases that possess a beta-propeller fold.
Pssm-ID: 429776 [Multi-domain] Cd Length: 327 Bit Score: 145.39 E-value: 5.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 276 EPTEMAVLPNNDVLIAQRRGEIMLYDDETKELKEVAkldvywktlETPGVNAEE--GVMGLQKDPDYANNNWIYVYYA-P 352
Cdd:pfam07995 3 HPWGLAFLPDGRMLVTERPGRLRIVDADGKLSTPIA---------GVPEVAARGqgGLLDVALHPDFAENRWVYLSYAeA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 353 TGDKWVNRLSRFKYADGNFDLDSEQIILDVDSQREICCHTGGSIAFGPDNLLYLSTGDNSTpfnekgekyvnngfaplnd 432
Cdd:pfam07995 74 GGGGAGTAVARARLSDDGTALEDVEVIFRQIPKVSGGGHFGSRLVFGPDGTLFVTTGDRGD------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 433 tpgheqydaRRSSGNTNDLRGKILRIkvNEDGSydIPEGNLFpMGTEKTRPEIYTMGHRNPYRISVDVKRGYVYWGDvgp 512
Cdd:pfam07995 135 ---------RDLAQDLDSHLGKILRL--NPDGS--IPADNPF-VGRPGALPEIWSYGHRNPQGLAFDPDTGRLWEHE--- 197
|
250 260 270
....*....|....*....|....*....|....*...
gi 1532357307 513 darvdslktRGPRGYDEMNQARQPGNFGWPLFI-GDNY 549
Cdd:pfam07995 198 ---------HGPRGGDEINLIEAGKNYGWPVVSyGDNY 226
|
|
| CytC552 |
COG4654 |
Cytochrome c551/c552 [Energy production and conversion]; |
864-950 |
2.01e-33 |
|
Cytochrome c551/c552 [Energy production and conversion];
Pssm-ID: 443692 [Multi-domain] Cd Length: 88 Bit Score: 123.86 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 864 SAAVTGKALAQSMDCKTCHKEAEASIGPNYMDVAQKYKNRRDALSYLQTRIKTGGNGVWGEVTMPAHPKITSDETRQIAL 943
Cdd:COG4654 2 ADAAAGKALAKKSGCLACHAVDKKLVGPSYKDVAKKYKGKADAVAKLAKKIKKGGSGVWGDVPMPPHPQLSDAEAKALVK 81
|
....*..
gi 1532357307 944 YILSLAG 950
Cdd:COG4654 82 WILSLKK 88
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
723-788 |
3.29e-15 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 71.26 E-value: 3.29e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1532357307 723 TAGKTPLAINASVV--ASDREGDNITYTWDFGNGETKETTEPNVSYTYTDAGAYNLSVTVGDDKGESA 788
Cdd:pfam00801 2 SASGTVVAAGQPVTftATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSAN 69
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
729-796 |
3.40e-13 |
|
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.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 65.98 E-value: 3.40e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1532357307 729 LAINASVVASDR-EGDNITYTWDFGNGETKETTEPNVSYTYTDAGAYNLSVTVGDDKGESAVSESTGIV 796
Cdd:cd00146 13 LGASVTFSASDSsGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
737-787 |
2.71e-11 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 60.54 E-value: 2.71e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1532357307 737 ASDREGDNITYTWDFGNGETkeTTEPNVSYTYTDAGAYNLSVTVGDDKGES 787
Cdd:smart00089 22 TSSDDGSIVSYTWDFGDGTS--STGPTVTHTYTKPGTYTVTLTVTNAVGSA 70
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
720-855 |
7.35e-09 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 58.91 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 720 VETTAGKTPLAINASVVASdreGDNITYTWDFGNGETkeTTEPNVSYTYTDAGAYNLSVTVGDDKGESAVSESTGIVAGN 799
Cdd:COG3291 3 ATPTSGCAPLTVQFTDTSS---GNATSYEWDFGDGTT--STEANPSHTYTTPGTYTVTLTVTDAAGCSDTTTKTITVGAP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1532357307 800 SRPEVTINLNGGTPAFYLPGQKIAYEVSVTDPDGGTVDESNVFVSVDYLEGLDKVT 855
Cdd:COG3291 78 NPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTT 133
|
|
| PCC |
TIGR00864 |
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
720-791 |
6.02e-06 |
|
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.
Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 50.85 E-value: 6.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1532357307 720 VETTAGKTPLAINASV--VASDREGDNITYTWDFGNGETKETTEPNVSYTYTDAGAYNLSVTVGDDKGESAVSE 791
Cdd:TIGR00864 1700 LMLAASDNPAAVNALInlSAELAEGSGLQYRWFLEEGDDLETSEPFMSHSFPSAGLHLVTMKAFNELGSANASE 1773
|
|
| Cytochrom_C |
pfam00034 |
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ... |
869-948 |
4.99e-05 |
|
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.
Pssm-ID: 459641 [Multi-domain] Cd Length: 89 Bit Score: 42.91 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 869 GKALAQsMDCKTCHKEAEASIGPNYMDVAQKYKnrRDALSYLQTRIKTGGNGVWGEVT---------MPAHPKITSDETR 939
Cdd:pfam00034 3 GKKLFA-ANCAACHGVNGEGAGAGGPDLAGLAA--RYPGDALGAIRENKHAIGGGGVDraggppgtgMPAFDGLTDEEIA 79
|
....*....
gi 1532357307 940 QIALYILSL 948
Cdd:pfam00034 80 DLVAYLLSL 88
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
710-835 |
1.04e-03 |
|
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 43.49 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 710 NRPPVIDNMIVETTAGKTPLAINASvvASDREGDNITYTWDFGNGETKETTEPNV---SYTYTDAGA---YNLSVTVGDD 783
Cdd:NF038112 1373 NRAPVANAGADQTVDERSTVTLSGS--ATDPDGDALTYAWTQTAGPTVTLTGADTataSFTAPEVAAdteLTFQLTVSAD 1450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1532357307 784 KGESAVSESTGIVAG-NSRPEVtinlNGGTPAFYLPGQKIAYEVSVTDPDGGT 835
Cdd:NF038112 1451 GQASADVTVTVTVRNvNRAPVA----HAGESITVDEGSTVTLDASATDPDGDT 1499
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThuA |
pfam06283 |
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA ... |
29-241 |
2.12e-99 |
|
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA appears to be involved in utilization of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium. ThuA is involved in the conversion of of disaccharides to their respective 3-keto derivatives.
Pssm-ID: 461867 [Multi-domain] Cd Length: 213 Bit Score: 313.41 E-value: 2.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 29 KVLVFSKTMGFKHASIPAGIAALQKMGQENGFAVDTTKNADMFTDDNLKQYSAVVFLSTTGNVLDQFQEAAFERYIQAGG 108
Cdd:pfam06283 1 RVLVFSGTAGWRHESIPAGIEAIRKLGAENGFEVDATEDAAVFTDENLAQYDVVVFLNTTGDVLDEEQEAAFQRYVQAGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 109 GYVGIHAAADTEYDWGWYNDLAGAQFLSHPSGTPNADFIIKDKNFIATEFFTDSvWNRDDELYNYKNINPDVNVLMTLDE 188
Cdd:pfam06283 81 GFVGLHSAADTEYDWPWYGKLVGARFVAHDPAPQQATVDVEDRSHPITAGLPAE-WERTDEWYNFKPNPPGNHVLATTDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1532357307 189 STYEGGQ-NGDFHPIAWYHDFDGGRAFYTGGGHTDESFSEELFLKHVLGGIKYA 241
Cdd:pfam06283 160 SSYDGGGnMGVDHPVAWTREDGAGRVFYTALGHTTESYEDPEFRKHLLGGIRWA 213
|
|
| YliI |
COG2133 |
Glucose/arabinose dehydrogenase, beta-propeller fold [Carbohydrate transport and metabolism]; |
258-691 |
8.03e-92 |
|
Glucose/arabinose dehydrogenase, beta-propeller fold [Carbohydrate transport and metabolism];
Pssm-ID: 441736 [Multi-domain] Cd Length: 365 Bit Score: 298.77 E-value: 8.03e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 258 PPDTDRFSKVILSEGqFFEPTEMAVLPNNDVLIAQRRGEIMLYDDETKELKEVAKLDVYwktletpgVNAEEGVMGLQKD 337
Cdd:COG2133 21 PTLPPGFTVEVVADG-LDHPWGLAFLPDGRLLVTERAGRIRLLDDDGKLSTPVADLPVF--------AGGEGGLLGVALD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 338 PDYANNNWIYVYYAPTGDKwVNRLSRFKYADGNFdLDSEQIILDVDSQREiCCHTGGSIAFGPDNLLYLSTGDNSTPFne 417
Cdd:COG2133 92 PDFATNGYLYVAYTDPGGA-GTRVARFTLSDGDT-LTSEEVILDGLPAGG-GNHNGGRLAFGPDGKLYVSVGDRGNAC-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 418 kgekyvnngfaplndtpgheqyDARRSSGNTNDLRGKILRIKVneDGSydIPEGNLFPmGTEKTRPEIYTMGHRNPYRIS 497
Cdd:COG2133 167 ----------------------EARGNAQDLNSLRGKILRIDP--DGS--IPADNPFV-GTPGARPEIYAYGHRNPQGLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 498 VDVKRGYVYWGDVGPDarvdslktrgprGYDEMNQARQPGNFGWPLFIGDNyaykEYNyetgetgeafdpqkPMNTSRNN 577
Cdd:COG2133 220 FDPETGELWATEHGPD------------GGDELNRIEPGGNYGWPYCEGGQ----NYD--------------PIGDSTPD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 578 TGLTElppamPAYVFypydessqfpqttTGGRNAMAGPtyysdLYTGeDKLPDYYDGKVIIYDWMRGWMFAVHLKEDGSF 657
Cdd:COG2133 270 AGLTD-----PVATW-------------PPGHAPSGLA-----FYTG-DAFPAEYRGGLFVADLGSRRVVRVPLDGDGKV 325
|
410 420 430
....*....|....*....|....*....|....
gi 1532357307 658 NKMEPFAPEVkLNNLIDMEMSPDGRVYLLEYGSG 691
Cdd:COG2133 326 VGEEDFLTGA-GGRPRDVAQGPDGALYVLDDNDG 358
|
|
| COG3828 |
COG3828 |
Type 1 glutamine amidotransferase (GATase1)-like domain [General function prediction only]; |
23-246 |
1.36e-90 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain [General function prediction only];
Pssm-ID: 443040 [Multi-domain] Cd Length: 222 Bit Score: 289.87 E-value: 1.36e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 23 KREGEPKVLVFSKtmGFKHAsIPAGIAALQKMGQENGFAVDTTKNADMFTDDNLKQYSAVVFLSTTGNVLDQFQEAAFER 102
Cdd:COG3828 2 KAAKKKKVLVFSG--GFRHD-IEAGVPALKELLEENGFEVDVTEDAADFTPENLAKYDLVVFNNTTGDVLTDEQQAALED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 103 YIQAGGGYVGIHAAADTEYDWGWYNDLAGAQFLSHPSGTPnADFIIKDKNFIATEFFTDSvWNRDDELYNYK-NINPDVN 181
Cdd:COG3828 79 YVEAGGGFVGIHAATDTFRDWPWYGELVGGQFVSHPPIQE-ATVTVEDPDHPITKGLPDE-FTVTDEWYNFLrDPRPDVT 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1532357307 182 VLMTLDESTYEGGQNGDFHPIAWYHDFDGGRAFYTGGGHTDESFSEELFLKHVLGGIKYAIGENE 246
Cdd:COG3828 157 VLATTDESTYPGGGMGGDHPVAWTREYGKGRVFYTALGHDEESFEDPGFRTLLLRGILWAAGGKV 221
|
|
| GSDH |
pfam07995 |
Glucose / Sorbosone dehydrogenase; Members of this family are glucose/sorbosone dehydrogenases ... |
276-549 |
5.65e-38 |
|
Glucose / Sorbosone dehydrogenase; Members of this family are glucose/sorbosone dehydrogenases that possess a beta-propeller fold.
Pssm-ID: 429776 [Multi-domain] Cd Length: 327 Bit Score: 145.39 E-value: 5.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 276 EPTEMAVLPNNDVLIAQRRGEIMLYDDETKELKEVAkldvywktlETPGVNAEE--GVMGLQKDPDYANNNWIYVYYA-P 352
Cdd:pfam07995 3 HPWGLAFLPDGRMLVTERPGRLRIVDADGKLSTPIA---------GVPEVAARGqgGLLDVALHPDFAENRWVYLSYAeA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 353 TGDKWVNRLSRFKYADGNFDLDSEQIILDVDSQREICCHTGGSIAFGPDNLLYLSTGDNSTpfnekgekyvnngfaplnd 432
Cdd:pfam07995 74 GGGGAGTAVARARLSDDGTALEDVEVIFRQIPKVSGGGHFGSRLVFGPDGTLFVTTGDRGD------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 433 tpgheqydaRRSSGNTNDLRGKILRIkvNEDGSydIPEGNLFpMGTEKTRPEIYTMGHRNPYRISVDVKRGYVYWGDvgp 512
Cdd:pfam07995 135 ---------RDLAQDLDSHLGKILRL--NPDGS--IPADNPF-VGRPGALPEIWSYGHRNPQGLAFDPDTGRLWEHE--- 197
|
250 260 270
....*....|....*....|....*....|....*...
gi 1532357307 513 darvdslktRGPRGYDEMNQARQPGNFGWPLFI-GDNY 549
Cdd:pfam07995 198 ---------HGPRGGDEINLIEAGKNYGWPVVSyGDNY 226
|
|
| CytC552 |
COG4654 |
Cytochrome c551/c552 [Energy production and conversion]; |
864-950 |
2.01e-33 |
|
Cytochrome c551/c552 [Energy production and conversion];
Pssm-ID: 443692 [Multi-domain] Cd Length: 88 Bit Score: 123.86 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 864 SAAVTGKALAQSMDCKTCHKEAEASIGPNYMDVAQKYKNRRDALSYLQTRIKTGGNGVWGEVTMPAHPKITSDETRQIAL 943
Cdd:COG4654 2 ADAAAGKALAKKSGCLACHAVDKKLVGPSYKDVAKKYKGKADAVAKLAKKIKKGGSGVWGDVPMPPHPQLSDAEAKALVK 81
|
....*..
gi 1532357307 944 YILSLAG 950
Cdd:COG4654 82 WILSLKK 88
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
723-788 |
3.29e-15 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 71.26 E-value: 3.29e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1532357307 723 TAGKTPLAINASVV--ASDREGDNITYTWDFGNGETKETTEPNVSYTYTDAGAYNLSVTVGDDKGESA 788
Cdd:pfam00801 2 SASGTVVAAGQPVTftATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSAN 69
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
729-796 |
3.40e-13 |
|
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.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 65.98 E-value: 3.40e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1532357307 729 LAINASVVASDR-EGDNITYTWDFGNGETKETTEPNVSYTYTDAGAYNLSVTVGDDKGESAVSESTGIV 796
Cdd:cd00146 13 LGASVTFSASDSsGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
737-787 |
2.71e-11 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 60.54 E-value: 2.71e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1532357307 737 ASDREGDNITYTWDFGNGETkeTTEPNVSYTYTDAGAYNLSVTVGDDKGES 787
Cdd:smart00089 22 TSSDDGSIVSYTWDFGDGTS--STGPTVTHTYTKPGTYTVTLTVTNAVGSA 70
|
|
| PKD_4 |
pfam18911 |
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
710-796 |
7.24e-11 |
|
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 59.59 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 710 NRPPVIDNMIVETTAGKTPLAINASVvASDREGDNITYTWDFGNGETkeTTEPNVSYTYTDAGAYNLSVTVGDDKGESAV 789
Cdd:pfam18911 1 NAAPVADAGGDRIVAEGETVTFDASA-SDDPDGDILSYRWDFGDGTT--ATGANVSHTYAAPGTYTVTLTVTDDSGASNS 77
|
....*..
gi 1532357307 790 SESTGIV 796
Cdd:pfam18911 78 TATDTVT 84
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
720-855 |
7.35e-09 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 58.91 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 720 VETTAGKTPLAINASVVASdreGDNITYTWDFGNGETkeTTEPNVSYTYTDAGAYNLSVTVGDDKGESAVSESTGIVAGN 799
Cdd:COG3291 3 ATPTSGCAPLTVQFTDTSS---GNATSYEWDFGDGTT--STEANPSHTYTTPGTYTVTLTVTDAAGCSDTTTKTITVGAP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1532357307 800 SRPEVTINLNGGTPAFYLPGQKIAYEVSVTDPDGGTVDESNVFVSVDYLEGLDKVT 855
Cdd:COG3291 78 NPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTT 133
|
|
| PCC |
TIGR00864 |
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
720-791 |
6.02e-06 |
|
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.
Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 50.85 E-value: 6.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1532357307 720 VETTAGKTPLAINASV--VASDREGDNITYTWDFGNGETKETTEPNVSYTYTDAGAYNLSVTVGDDKGESAVSE 791
Cdd:TIGR00864 1700 LMLAASDNPAAVNALInlSAELAEGSGLQYRWFLEEGDDLETSEPFMSHSFPSAGLHLVTMKAFNELGSANASE 1773
|
|
| Cytochrom_C |
pfam00034 |
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ... |
869-948 |
4.99e-05 |
|
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.
Pssm-ID: 459641 [Multi-domain] Cd Length: 89 Bit Score: 42.91 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 869 GKALAQsMDCKTCHKEAEASIGPNYMDVAQKYKnrRDALSYLQTRIKTGGNGVWGEVT---------MPAHPKITSDETR 939
Cdd:pfam00034 3 GKKLFA-ANCAACHGVNGEGAGAGGPDLAGLAA--RYPGDALGAIRENKHAIGGGGVDraggppgtgMPAFDGLTDEEIA 79
|
....*....
gi 1532357307 940 QIALYILSL 948
Cdd:pfam00034 80 DLVAYLLSL 88
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
710-835 |
1.04e-03 |
|
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 43.49 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 710 NRPPVIDNMIVETTAGKTPLAINASvvASDREGDNITYTWDFGNGETKETTEPNV---SYTYTDAGA---YNLSVTVGDD 783
Cdd:NF038112 1373 NRAPVANAGADQTVDERSTVTLSGS--ATDPDGDALTYAWTQTAGPTVTLTGADTataSFTAPEVAAdteLTFQLTVSAD 1450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1532357307 784 KGESAVSESTGIVAG-NSRPEVtinlNGGTPAFYLPGQKIAYEVSVTDPDGGT 835
Cdd:NF038112 1451 GQASADVTVTVTVRNvNRAPVA----HAGESITVDEGSTVTLDASATDPDGDT 1499
|
|
| PCC |
TIGR00864 |
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
693-810 |
1.43e-03 |
|
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.
Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 43.15 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532357307 693 FSQNANSGLSYIEFNGGNRPPVIDNMIVETTAGKTPLAINASVVASDREGD---------NITYTWDFGNGETKETTE-- 761
Cdd:TIGR00864 1310 FRGNGTFPLALTISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQfqacaepefNYRYEWDFGGEEAAPLPAag 1389
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1532357307 762 PNVSYTYTDAGAYNLSVTVGDDKgeSAVSESTGIVAGNSRPEVTINLNG 810
Cdd:TIGR00864 1390 AEVTFIYNDPGCYLVTVAASNNI--SAANDSALIEVLEPVGATSFKHNG 1436
|
|
| PCC |
TIGR00864 |
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
735-781 |
1.95e-03 |
|
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.
Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 42.76 E-value: 1.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1532357307 735 VVASDREGDNITYTWDFGNGETKETTEPNVSYTYTDAGayNLSVTVG 781
Cdd:TIGR00864 1192 VRAALQSGDNITWTFDMGDGKSLSGPEATVEHKYAKAG--NCTVNIG 1236
|
|
| |
