|
Name |
Accession |
Description |
Interval |
E-value |
| ThuA |
pfam06283 |
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA ... |
29-241 |
4.30e-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: 312.64 E-value: 4.30e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 29 KVLVFSKTMGFKHASIPAGIAALQKMGQENGFAVDTTKNAEMFTDDNLKQYSAVVFLSTTGNVLDQFQEAAFERYIQAGG 108
Cdd:pfam06283 1 RVLVFSGTAGWRHESIPAGIEAIRKLGAENGFEVDATEDAAVFTDENLAQYDVVVFLNTTGDVLDEEQEAAFQRYVQAGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 109 GYVGIHAAADTEYDWGWYNDLAGAQFLSHPRGTPNADFIIKDKNFIATEFFKDSvWNRDDELYNYKNINPDVNVVMTLDE 188
Cdd:pfam06283 81 GFVGLHSAADTEYDWPWYGKLVGARFVAHDPAPQQATVDVEDRSHPITAGLPAE-WERTDEWYNFKPNPPGNHVLATTDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1273388195 189 STYEGGQ-NGDFHPIAWYHDFDGGRAFYTGGGHTDESFSEDLFLKHVLGGIKYA 241
Cdd:pfam06283 160 SSYDGGGnMGVDHPVAWTREDGAGRVFYTALGHTTESYEDPEFRKHLLGGIRWA 213
|
|
| YliI |
COG2133 |
Glucose/arabinose dehydrogenase, beta-propeller fold [Carbohydrate transport and metabolism]; |
258-691 |
4.66e-92 |
|
Glucose/arabinose dehydrogenase, beta-propeller fold [Carbohydrate transport and metabolism];
:
Pssm-ID: 441736 [Multi-domain] Cd Length: 365 Bit Score: 299.54 E-value: 4.66e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 258 PPDTDRFSKLVLSEGqFFEPTEMAVLPNNDVLIAQRRGEIVLYNDETQELKEVAKLDVYwktletpgVNAEEGVMGLQKD 337
Cdd:COG2133 21 PTLPPGFTVEVVADG-LDHPWGLAFLPDGRLLVTERAGRIRLLDDDGKLSTPVADLPVF--------AGGEGGLLGVALD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 338 PDYANNNWIYVYYAPTGDKwVNRLSRLKYADGNFdLGSEQVILEVDSQREiCCHTGGSIAFGPDNLLYLSTGDNSTPFne 417
Cdd:COG2133 92 PDFATNGYLYVAYTDPGGA-GTRVARFTLSDGDT-LTSEEVILDGLPAGG-GNHNGGRLAFGPDGKLYVSVGDRGNAC-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 418 rgekyvnngfaplndtpgheqyDARRSSGNTNDLRGKILRIKVneDGSydIPEGNLFpVGTEKTRPEIYTMGHRNPYRIS 497
Cdd:COG2133 167 ----------------------EARGNAQDLNSLRGKILRIDP--DGS--IPADNPF-VGTPGARPEIYAYGHRNPQGLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 498 VDVKRGYVYWGDVGPDaradsletrgprGYDEMNQARKPGNFGWPLFIGDNyaykEYNyetgesgeafdpqkPMNTSRNN 577
Cdd:COG2133 220 FDPETGELWATEHGPD------------GGDELNRIEPGGNYGWPYCEGGQ----NYD--------------PIGDSTPD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 578 TGLTElppamPAYVFypydessqfpqttTGGRNAMAGPtyysdLYTGqDKLPDYYDGKVIIYDWMRGWMFAVHLKEDGSF 657
Cdd:COG2133 270 AGLTD-----PVATW-------------PPGHAPSGLA-----FYTG-DAFPAEYRGGLFVADLGSRRVVRVPLDGDGKV 325
|
410 420 430
....*....|....*....|....*....|....
gi 1273388195 658 NKMEPFAPEVkLNNLIDMEMGPDGRVYLLEYGSG 691
Cdd:COG2133 326 VGEEDFLTGA-GGRPRDVAQGPDGALYVLDDNDG 358
|
|
| CytC552 |
COG4654 |
Cytochrome c551/c552 [Energy production and conversion]; |
864-950 |
2.44e-33 |
|
Cytochrome c551/c552 [Energy production and conversion];
:
Pssm-ID: 443692 [Multi-domain] Cd Length: 88 Bit Score: 123.47 E-value: 2.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 864 SAAVTGKALAQSMDCKTCHKEAEASIGPNYMDVAQKYKNRRDAMSYLQTRIKTGGNGVWGEVTMPAHPKITSDETRQIAL 943
Cdd:COG4654 2 ADAAAGKALAKKSGCLACHAVDKKLVGPSYKDVAKKYKGKADAVAKLAKKIKKGGSGVWGDVPMPPHPQLSDAEAKALVK 81
|
....*..
gi 1273388195 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 |
1.19e-14 |
|
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: 69.72 E-value: 1.19e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1273388195 723 TAGKTPLAISASVV--AKDREGDNITYTWDFGNGETKETTEPNVSYTYADAGSYNLSVTVADDKGESA 788
Cdd:pfam00801 2 SASGTVVAAGQPVTftATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSAN 69
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThuA |
pfam06283 |
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA ... |
29-241 |
4.30e-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: 312.64 E-value: 4.30e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 29 KVLVFSKTMGFKHASIPAGIAALQKMGQENGFAVDTTKNAEMFTDDNLKQYSAVVFLSTTGNVLDQFQEAAFERYIQAGG 108
Cdd:pfam06283 1 RVLVFSGTAGWRHESIPAGIEAIRKLGAENGFEVDATEDAAVFTDENLAQYDVVVFLNTTGDVLDEEQEAAFQRYVQAGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 109 GYVGIHAAADTEYDWGWYNDLAGAQFLSHPRGTPNADFIIKDKNFIATEFFKDSvWNRDDELYNYKNINPDVNVVMTLDE 188
Cdd:pfam06283 81 GFVGLHSAADTEYDWPWYGKLVGARFVAHDPAPQQATVDVEDRSHPITAGLPAE-WERTDEWYNFKPNPPGNHVLATTDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1273388195 189 STYEGGQ-NGDFHPIAWYHDFDGGRAFYTGGGHTDESFSEDLFLKHVLGGIKYA 241
Cdd:pfam06283 160 SSYDGGGnMGVDHPVAWTREDGAGRVFYTALGHTTESYEDPEFRKHLLGGIRWA 213
|
|
| YliI |
COG2133 |
Glucose/arabinose dehydrogenase, beta-propeller fold [Carbohydrate transport and metabolism]; |
258-691 |
4.66e-92 |
|
Glucose/arabinose dehydrogenase, beta-propeller fold [Carbohydrate transport and metabolism];
Pssm-ID: 441736 [Multi-domain] Cd Length: 365 Bit Score: 299.54 E-value: 4.66e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 258 PPDTDRFSKLVLSEGqFFEPTEMAVLPNNDVLIAQRRGEIVLYNDETQELKEVAKLDVYwktletpgVNAEEGVMGLQKD 337
Cdd:COG2133 21 PTLPPGFTVEVVADG-LDHPWGLAFLPDGRLLVTERAGRIRLLDDDGKLSTPVADLPVF--------AGGEGGLLGVALD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 338 PDYANNNWIYVYYAPTGDKwVNRLSRLKYADGNFdLGSEQVILEVDSQREiCCHTGGSIAFGPDNLLYLSTGDNSTPFne 417
Cdd:COG2133 92 PDFATNGYLYVAYTDPGGA-GTRVARFTLSDGDT-LTSEEVILDGLPAGG-GNHNGGRLAFGPDGKLYVSVGDRGNAC-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 418 rgekyvnngfaplndtpgheqyDARRSSGNTNDLRGKILRIKVneDGSydIPEGNLFpVGTEKTRPEIYTMGHRNPYRIS 497
Cdd:COG2133 167 ----------------------EARGNAQDLNSLRGKILRIDP--DGS--IPADNPF-VGTPGARPEIYAYGHRNPQGLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 498 VDVKRGYVYWGDVGPDaradsletrgprGYDEMNQARKPGNFGWPLFIGDNyaykEYNyetgesgeafdpqkPMNTSRNN 577
Cdd:COG2133 220 FDPETGELWATEHGPD------------GGDELNRIEPGGNYGWPYCEGGQ----NYD--------------PIGDSTPD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 578 TGLTElppamPAYVFypydessqfpqttTGGRNAMAGPtyysdLYTGqDKLPDYYDGKVIIYDWMRGWMFAVHLKEDGSF 657
Cdd:COG2133 270 AGLTD-----PVATW-------------PPGHAPSGLA-----FYTG-DAFPAEYRGGLFVADLGSRRVVRVPLDGDGKV 325
|
410 420 430
....*....|....*....|....*....|....
gi 1273388195 658 NKMEPFAPEVkLNNLIDMEMGPDGRVYLLEYGSG 691
Cdd:COG2133 326 VGEEDFLTGA-GGRPRDVAQGPDGALYVLDDNDG 358
|
|
| COG3828 |
COG3828 |
Type 1 glutamine amidotransferase (GATase1)-like domain [General function prediction only]; |
23-246 |
1.22e-89 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain [General function prediction only];
Pssm-ID: 443040 [Multi-domain] Cd Length: 222 Bit Score: 287.18 E-value: 1.22e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 23 KREGEPKVLVFSKtmGFKHAsIPAGIAALQKMGQENGFAVDTTKNAEMFTDDNLKQYSAVVFLSTTGNVLDQFQEAAFER 102
Cdd:COG3828 2 KAAKKKKVLVFSG--GFRHD-IEAGVPALKELLEENGFEVDVTEDAADFTPENLAKYDLVVFNNTTGDVLTDEQQAALED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 103 YIQAGGGYVGIHAAADTEYDWGWYNDLAGAQFLSHPRGTPnADFIIKDKNFIATEFFKDSvWNRDDELYNYK-NINPDVN 181
Cdd:COG3828 79 YVEAGGGFVGIHAATDTFRDWPWYGELVGGQFVSHPPIQE-ATVTVEDPDHPITKGLPDE-FTVTDEWYNFLrDPRPDVT 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1273388195 182 VVMTLDESTYEGGQNGDFHPIAWYHDFDGGRAFYTGGGHTDESFSEDLFLKHVLGGIKYAIGENE 246
Cdd:COG3828 157 VLATTDESTYPGGGMGGDHPVAWTREYGKGRVFYTALGHDEESFEDPGFRTLLLRGILWAAGGKV 221
|
|
| GSDH |
pfam07995 |
Glucose / Sorbosone dehydrogenase; Members of this family are glucose/sorbosone dehydrogenases ... |
276-549 |
8.00e-39 |
|
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: 147.70 E-value: 8.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 276 EPTEMAVLPNNDVLIAQRRGEIVLYNDETQELKEVAkldvywktlETPGVNAEE--GVMGLQKDPDYANNNWIYVYYA-P 352
Cdd:pfam07995 3 HPWGLAFLPDGRMLVTERPGRLRIVDADGKLSTPIA---------GVPEVAARGqgGLLDVALHPDFAENRWVYLSYAeA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 353 TGDKWVNRLSRLKYADGNFDLGSEQVILEVDSQREICCHTGGSIAFGPDNLLYLSTGDNSTpfnergekyvnngfaplnd 432
Cdd:pfam07995 74 GGGGAGTAVARARLSDDGTALEDVEVIFRQIPKVSGGGHFGSRLVFGPDGTLFVTTGDRGD------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 433 tpgheqydaRRSSGNTNDLRGKILRIkvNEDGSydIPEGNLFpVGTEKTRPEIYTMGHRNPYRISVDVKRGYVYwgdvgp 512
Cdd:pfam07995 135 ---------RDLAQDLDSHLGKILRL--NPDGS--IPADNPF-VGRPGALPEIWSYGHRNPQGLAFDPDTGRLW------ 194
|
250 260 270
....*....|....*....|....*....|....*...
gi 1273388195 513 daradSLEtRGPRGYDEMNQARKPGNFGWPLFI-GDNY 549
Cdd:pfam07995 195 -----EHE-HGPRGGDEINLIEAGKNYGWPVVSyGDNY 226
|
|
| CytC552 |
COG4654 |
Cytochrome c551/c552 [Energy production and conversion]; |
864-950 |
2.44e-33 |
|
Cytochrome c551/c552 [Energy production and conversion];
Pssm-ID: 443692 [Multi-domain] Cd Length: 88 Bit Score: 123.47 E-value: 2.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 864 SAAVTGKALAQSMDCKTCHKEAEASIGPNYMDVAQKYKNRRDAMSYLQTRIKTGGNGVWGEVTMPAHPKITSDETRQIAL 943
Cdd:COG4654 2 ADAAAGKALAKKSGCLACHAVDKKLVGPSYKDVAKKYKGKADAVAKLAKKIKKGGSGVWGDVPMPPHPQLSDAEAKALVK 81
|
....*..
gi 1273388195 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 |
1.19e-14 |
|
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: 69.72 E-value: 1.19e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1273388195 723 TAGKTPLAISASVV--AKDREGDNITYTWDFGNGETKETTEPNVSYTYADAGSYNLSVTVADDKGESA 788
Cdd:pfam00801 2 SASGTVVAAGQPVTftATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSAN 69
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
742-796 |
3.97e-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: 65.60 E-value: 3.97e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1273388195 742 GDNITYTWDFGNGETKETTEPNVSYTYADAGSYNLSVTVADDKGESAVSESTGIV 796
Cdd:cd00146 27 GSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
741-787 |
3.96e-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: 60.16 E-value: 3.96e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1273388195 741 EGDNITYTWDFGNGETkeTTEPNVSYTYADAGSYNLSVTVADDKGES 787
Cdd:smart00089 26 DGSIVSYTWDFGDGTS--STGPTVTHTYTKPGTYTVTLTVTNAVGSA 70
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
720-850 |
5.00e-09 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 59.30 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 720 VETTAGKTPLAISASVVAkdrEGDNITYTWDFGNGETkeTTEPNVSYTYADAGSYNLSVTVADDKGESAVSESTGIVAGN 799
Cdd:COG3291 3 ATPTSGCAPLTVQFTDTS---SGNATSYEWDFGDGTT--STEANPSHTYTTPGTYTVTLTVTDAAGCSDTTTKTITVGAP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1273388195 800 SRPEVTINLNGGTPAFYLPGQKIAYEVSVTDPDGGTVDESNVFVSVDYLEG 850
Cdd:COG3291 78 NPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGG 128
|
|
| PCC |
TIGR00864 |
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
727-790 |
7.73e-05 |
|
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: 47.38 E-value: 7.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1273388195 727 TPLAISASVvakdREGDNITYTWDFGNGETKETTEPNVSYTYADAGSYNLSVTVADDKGESAVS 790
Cdd:TIGR00864 1188 AATTVRAAL----QSGDNITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARI 1247
|
|
| Cytochrom_C |
pfam00034 |
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ... |
869-948 |
1.46e-04 |
|
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: 41.76 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 869 GKALAQsMDCKTCHKEAEASIGPNYMDVAQKY-KNRRDAMSYLQTRIKTGGNGVWGEVT------MPAHPKITSDETRQI 941
Cdd:pfam00034 3 GKKLFA-ANCAACHGVNGEGAGAGGPDLAGLAaRYPGDALGAIRENKHAIGGGGVDRAGgppgtgMPAFDGLTDEEIADL 81
|
....*..
gi 1273388195 942 ALYILSL 948
Cdd:pfam00034 82 VAYLLSL 88
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
710-835 |
2.38e-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: 42.34 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 710 NRPPVIDDMIVETTAGKTPLAISASvvAKDREGDNITYTWDFGNGETKETTEPNVSYTYADAGSYN------LSVTVADD 783
Cdd:NF038112 1373 NRAPVANAGADQTVDERSTVTLSGS--ATDPDGDALTYAWTQTAGPTVTLTGADTATASFTAPEVAadteltFQLTVSAD 1450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1273388195 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 |
4.30e-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: 312.64 E-value: 4.30e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 29 KVLVFSKTMGFKHASIPAGIAALQKMGQENGFAVDTTKNAEMFTDDNLKQYSAVVFLSTTGNVLDQFQEAAFERYIQAGG 108
Cdd:pfam06283 1 RVLVFSGTAGWRHESIPAGIEAIRKLGAENGFEVDATEDAAVFTDENLAQYDVVVFLNTTGDVLDEEQEAAFQRYVQAGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 109 GYVGIHAAADTEYDWGWYNDLAGAQFLSHPRGTPNADFIIKDKNFIATEFFKDSvWNRDDELYNYKNINPDVNVVMTLDE 188
Cdd:pfam06283 81 GFVGLHSAADTEYDWPWYGKLVGARFVAHDPAPQQATVDVEDRSHPITAGLPAE-WERTDEWYNFKPNPPGNHVLATTDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1273388195 189 STYEGGQ-NGDFHPIAWYHDFDGGRAFYTGGGHTDESFSEDLFLKHVLGGIKYA 241
Cdd:pfam06283 160 SSYDGGGnMGVDHPVAWTREDGAGRVFYTALGHTTESYEDPEFRKHLLGGIRWA 213
|
|
| YliI |
COG2133 |
Glucose/arabinose dehydrogenase, beta-propeller fold [Carbohydrate transport and metabolism]; |
258-691 |
4.66e-92 |
|
Glucose/arabinose dehydrogenase, beta-propeller fold [Carbohydrate transport and metabolism];
Pssm-ID: 441736 [Multi-domain] Cd Length: 365 Bit Score: 299.54 E-value: 4.66e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 258 PPDTDRFSKLVLSEGqFFEPTEMAVLPNNDVLIAQRRGEIVLYNDETQELKEVAKLDVYwktletpgVNAEEGVMGLQKD 337
Cdd:COG2133 21 PTLPPGFTVEVVADG-LDHPWGLAFLPDGRLLVTERAGRIRLLDDDGKLSTPVADLPVF--------AGGEGGLLGVALD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 338 PDYANNNWIYVYYAPTGDKwVNRLSRLKYADGNFdLGSEQVILEVDSQREiCCHTGGSIAFGPDNLLYLSTGDNSTPFne 417
Cdd:COG2133 92 PDFATNGYLYVAYTDPGGA-GTRVARFTLSDGDT-LTSEEVILDGLPAGG-GNHNGGRLAFGPDGKLYVSVGDRGNAC-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 418 rgekyvnngfaplndtpgheqyDARRSSGNTNDLRGKILRIKVneDGSydIPEGNLFpVGTEKTRPEIYTMGHRNPYRIS 497
Cdd:COG2133 167 ----------------------EARGNAQDLNSLRGKILRIDP--DGS--IPADNPF-VGTPGARPEIYAYGHRNPQGLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 498 VDVKRGYVYWGDVGPDaradsletrgprGYDEMNQARKPGNFGWPLFIGDNyaykEYNyetgesgeafdpqkPMNTSRNN 577
Cdd:COG2133 220 FDPETGELWATEHGPD------------GGDELNRIEPGGNYGWPYCEGGQ----NYD--------------PIGDSTPD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 578 TGLTElppamPAYVFypydessqfpqttTGGRNAMAGPtyysdLYTGqDKLPDYYDGKVIIYDWMRGWMFAVHLKEDGSF 657
Cdd:COG2133 270 AGLTD-----PVATW-------------PPGHAPSGLA-----FYTG-DAFPAEYRGGLFVADLGSRRVVRVPLDGDGKV 325
|
410 420 430
....*....|....*....|....*....|....
gi 1273388195 658 NKMEPFAPEVkLNNLIDMEMGPDGRVYLLEYGSG 691
Cdd:COG2133 326 VGEEDFLTGA-GGRPRDVAQGPDGALYVLDDNDG 358
|
|
| COG3828 |
COG3828 |
Type 1 glutamine amidotransferase (GATase1)-like domain [General function prediction only]; |
23-246 |
1.22e-89 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain [General function prediction only];
Pssm-ID: 443040 [Multi-domain] Cd Length: 222 Bit Score: 287.18 E-value: 1.22e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 23 KREGEPKVLVFSKtmGFKHAsIPAGIAALQKMGQENGFAVDTTKNAEMFTDDNLKQYSAVVFLSTTGNVLDQFQEAAFER 102
Cdd:COG3828 2 KAAKKKKVLVFSG--GFRHD-IEAGVPALKELLEENGFEVDVTEDAADFTPENLAKYDLVVFNNTTGDVLTDEQQAALED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 103 YIQAGGGYVGIHAAADTEYDWGWYNDLAGAQFLSHPRGTPnADFIIKDKNFIATEFFKDSvWNRDDELYNYK-NINPDVN 181
Cdd:COG3828 79 YVEAGGGFVGIHAATDTFRDWPWYGELVGGQFVSHPPIQE-ATVTVEDPDHPITKGLPDE-FTVTDEWYNFLrDPRPDVT 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1273388195 182 VVMTLDESTYEGGQNGDFHPIAWYHDFDGGRAFYTGGGHTDESFSEDLFLKHVLGGIKYAIGENE 246
Cdd:COG3828 157 VLATTDESTYPGGGMGGDHPVAWTREYGKGRVFYTALGHDEESFEDPGFRTLLLRGILWAAGGKV 221
|
|
| GSDH |
pfam07995 |
Glucose / Sorbosone dehydrogenase; Members of this family are glucose/sorbosone dehydrogenases ... |
276-549 |
8.00e-39 |
|
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: 147.70 E-value: 8.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 276 EPTEMAVLPNNDVLIAQRRGEIVLYNDETQELKEVAkldvywktlETPGVNAEE--GVMGLQKDPDYANNNWIYVYYA-P 352
Cdd:pfam07995 3 HPWGLAFLPDGRMLVTERPGRLRIVDADGKLSTPIA---------GVPEVAARGqgGLLDVALHPDFAENRWVYLSYAeA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 353 TGDKWVNRLSRLKYADGNFDLGSEQVILEVDSQREICCHTGGSIAFGPDNLLYLSTGDNSTpfnergekyvnngfaplnd 432
Cdd:pfam07995 74 GGGGAGTAVARARLSDDGTALEDVEVIFRQIPKVSGGGHFGSRLVFGPDGTLFVTTGDRGD------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 433 tpgheqydaRRSSGNTNDLRGKILRIkvNEDGSydIPEGNLFpVGTEKTRPEIYTMGHRNPYRISVDVKRGYVYwgdvgp 512
Cdd:pfam07995 135 ---------RDLAQDLDSHLGKILRL--NPDGS--IPADNPF-VGRPGALPEIWSYGHRNPQGLAFDPDTGRLW------ 194
|
250 260 270
....*....|....*....|....*....|....*...
gi 1273388195 513 daradSLEtRGPRGYDEMNQARKPGNFGWPLFI-GDNY 549
Cdd:pfam07995 195 -----EHE-HGPRGGDEINLIEAGKNYGWPVVSyGDNY 226
|
|
| CytC552 |
COG4654 |
Cytochrome c551/c552 [Energy production and conversion]; |
864-950 |
2.44e-33 |
|
Cytochrome c551/c552 [Energy production and conversion];
Pssm-ID: 443692 [Multi-domain] Cd Length: 88 Bit Score: 123.47 E-value: 2.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 864 SAAVTGKALAQSMDCKTCHKEAEASIGPNYMDVAQKYKNRRDAMSYLQTRIKTGGNGVWGEVTMPAHPKITSDETRQIAL 943
Cdd:COG4654 2 ADAAAGKALAKKSGCLACHAVDKKLVGPSYKDVAKKYKGKADAVAKLAKKIKKGGSGVWGDVPMPPHPQLSDAEAKALVK 81
|
....*..
gi 1273388195 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 |
1.19e-14 |
|
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: 69.72 E-value: 1.19e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1273388195 723 TAGKTPLAISASVV--AKDREGDNITYTWDFGNGETKETTEPNVSYTYADAGSYNLSVTVADDKGESA 788
Cdd:pfam00801 2 SASGTVVAAGQPVTftATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSAN 69
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
742-796 |
3.97e-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: 65.60 E-value: 3.97e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1273388195 742 GDNITYTWDFGNGETKETTEPNVSYTYADAGSYNLSVTVADDKGESAVSESTGIV 796
Cdd:cd00146 27 GSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
|
|
| PKD_4 |
pfam18911 |
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
710-796 |
3.76e-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: 60.36 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 710 NRPPVIDDMIVETTAGKTPLAISASVvAKDREGDNITYTWDFGNGETkeTTEPNVSYTYADAGSYNLSVTVADDKGESAV 789
Cdd:pfam18911 1 NAAPVADAGGDRIVAEGETVTFDASA-SDDPDGDILSYRWDFGDGTT--ATGANVSHTYAAPGTYTVTLTVTDDSGASNS 77
|
....*..
gi 1273388195 790 SESTGIV 796
Cdd:pfam18911 78 TATDTVT 84
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
741-787 |
3.96e-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: 60.16 E-value: 3.96e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1273388195 741 EGDNITYTWDFGNGETkeTTEPNVSYTYADAGSYNLSVTVADDKGES 787
Cdd:smart00089 26 DGSIVSYTWDFGDGTS--STGPTVTHTYTKPGTYTVTLTVTNAVGSA 70
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
720-850 |
5.00e-09 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 59.30 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 720 VETTAGKTPLAISASVVAkdrEGDNITYTWDFGNGETkeTTEPNVSYTYADAGSYNLSVTVADDKGESAVSESTGIVAGN 799
Cdd:COG3291 3 ATPTSGCAPLTVQFTDTS---SGNATSYEWDFGDGTT--STEANPSHTYTTPGTYTVTLTVTDAAGCSDTTTKTITVGAP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1273388195 800 SRPEVTINLNGGTPAFYLPGQKIAYEVSVTDPDGGTVDESNVFVSVDYLEG 850
Cdd:COG3291 78 NPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGG 128
|
|
| PCC |
TIGR00864 |
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
727-790 |
7.73e-05 |
|
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: 47.38 E-value: 7.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1273388195 727 TPLAISASVvakdREGDNITYTWDFGNGETKETTEPNVSYTYADAGSYNLSVTVADDKGESAVS 790
Cdd:TIGR00864 1188 AATTVRAAL----QSGDNITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARI 1247
|
|
| Cytochrom_C |
pfam00034 |
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ... |
869-948 |
1.46e-04 |
|
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: 41.76 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 869 GKALAQsMDCKTCHKEAEASIGPNYMDVAQKY-KNRRDAMSYLQTRIKTGGNGVWGEVT------MPAHPKITSDETRQI 941
Cdd:pfam00034 3 GKKLFA-ANCAACHGVNGEGAGAGGPDLAGLAaRYPGDALGAIRENKHAIGGGGVDRAGgppgtgMPAFDGLTDEEIADL 81
|
....*..
gi 1273388195 942 ALYILSL 948
Cdd:pfam00034 82 VAYLLSL 88
|
|
| PCC |
TIGR00864 |
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
693-810 |
3.62e-04 |
|
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: 45.07 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 693 FSQNANSGLSYIEFNGGNRPPVIDDMIVETTAGKTPLAISASVVAKDREGD---------NITYTWDFGNGETKETTE-- 761
Cdd:TIGR00864 1310 FRGNGTFPLALTISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQfqacaepefNYRYEWDFGGEEAAPLPAag 1389
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1273388195 762 PNVSYTYADAGSYnlSVTVADDKGESAVSESTGIVAGNSRPEVTINLNG 810
Cdd:TIGR00864 1390 AEVTFIYNDPGCY--LVTVAASNNISAANDSALIEVLEPVGATSFKHNG 1436
|
|
| PCC |
TIGR00864 |
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
720-791 |
4.43e-04 |
|
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: 44.69 E-value: 4.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1273388195 720 VETTAGKTPLAISASV--VAKDREGDNITYTWDFGNGETKETTEPNVSYTYADAGSYNLSVTVADDKGESAVSE 791
Cdd:TIGR00864 1700 LMLAASDNPAAVNALInlSAELAEGSGLQYRWFLEEGDDLETSEPFMSHSFPSAGLHLVTMKAFNELGSANASE 1773
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
710-835 |
2.38e-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: 42.34 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273388195 710 NRPPVIDDMIVETTAGKTPLAISASvvAKDREGDNITYTWDFGNGETKETTEPNVSYTYADAGSYN------LSVTVADD 783
Cdd:NF038112 1373 NRAPVANAGADQTVDERSTVTLSGS--ATDPDGDALTYAWTQTAGPTVTLTGADTATASFTAPEVAadteltFQLTVSAD 1450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1273388195 784 KGESAVSESTGIVAG-NSRPEVtinlNGGTPAFYLPGQKIAYEVSVTDPDGGT 835
Cdd:NF038112 1451 GQASADVTVTVTVRNvNRAPVA----HAGESITVDEGSTVTLDASATDPDGDT 1499
|
|
| |
