|
Name |
Accession |
Description |
Interval |
E-value |
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
30-437 |
6.34e-177 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 501.13 E-value: 6.34e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 30 VAVYGLGKMGLPLAAVYAETCGNVIGADIDPDVVAAINRGDCHVKrEPGlDELVSETVESGALRAVESPvEAADRASIHV 109
Cdd:COG0677 2 IAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPIL-EPG-DELLAEAVAAGRLRATTDP-EALAEADVVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 110 VIVPTPITDANQPDLAILQSVIESIADGLDQGDLVVVECTVPPGTTRDELLPLLERESDLSR-EEFGLAVCPERTSSGRA 188
Cdd:COG0677 79 IAVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKAgEDFFLAYSPERINPGNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 189 LQDIRgAYPKVVGGIDDESTRVAELVYGELTDNDVISVPNATTAEAVKVFEGVYRDVNIALANELASIADDAEISINGAI 268
Cdd:COG0677 159 LHELR-NIPKVVGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 269 ETANTQPFCDLHKPGPGVGGHCIPYYPYFLI---EQFEAPFPLLRTAREVNDSMPGFTVEKTVELLAEHGKAVADSRILV 345
Cdd:COG0677 238 EAANTKPGFLIFYPGPGVGGHCIPVDPYYLTwkaRELGYHPRLILAAREINDSMPEYVVERVVKALNEAGKSLKGARVLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 346 LGLTYRPGVEETRATPARPICADLTERGADVFAVDPMLDDAEGFDATKLAFE-DLAEHEFDAAVLVTDHDEFAGIDWAGF 424
Cdd:COG0677 318 LGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGEYGELVDlEEALEGADAVVLAVDHDEFDELDPEEL 397
|
410
....*....|....*.
gi 2339757616 425 ---DPMVVVDGRDALD 437
Cdd:COG0677 398 rlkGAKVVVDTRGVLD 413
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
30-434 |
5.22e-125 |
|
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.
Pssm-ID: 274399 [Multi-domain] Cd Length: 409 Bit Score: 368.86 E-value: 5.22e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 30 VAVYGLGKMGLPLAAVYAETCGNVIGADIDPDVVAAINRGDCHVKrEPGLDELVSETVESGALRAVESPVEAADRASIHV 109
Cdd:TIGR03026 3 IAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIY-EPGLDELLAKALKAGRLRATTDYEEAIRDADVII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 110 VIVPTPITDANQPDLAILQSVIESIADGLDQGDLVVVECTVPPGTTRDELLPLLERESDLSREEFGLAVCPERTSSGRAL 189
Cdd:TIGR03026 82 ICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDFYLAYNPEFLREGNAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 190 QDIRGAyPKVVGGIDDESTRVAELVYGELTDNdVISVPNATTAEAVKVFEGVYRDVNIALANELASIADDAEISINGAIE 269
Cdd:TIGR03026 162 HDLLHP-DRIVGGETEEAGEAVAELYSPIIDG-PVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 270 TANTQPF--CDLHKPGPGVGGHCIPYYPYFLIEQFE---APFPLLRTAREVNDSMPGFTVEKTVELLaehgKAVADSRIL 344
Cdd:TIGR03026 240 AAGTDPRigFNFLNPGPGVGGHCIPKDPLALIAKAKelgYNPELIEAAREINDSQPDYVVEKIKDLL----GPLKGKTVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 345 VLGLTYRPGVEETRATPARPICADLTERGADVFAVDP--MLDDAEGFDATKLAFEDLAehEFDAAVLVTDHDEFAGIDWA 422
Cdd:TIGR03026 316 ILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPlvPEEEVKGLPSIDDLEEALK--GADALVILTDHSEFKDLDLE 393
|
410
....*....|....*.
gi 2339757616 423 GFDPM----VVVDGRD 434
Cdd:TIGR03026 394 KIKDLmkgkVVVDTRN 409
|
|
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
30-431 |
8.19e-80 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 253.37 E-value: 8.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 30 VAVYGLGKMGLPLAAVYAETCGNVIGADIDPDVVAAINRGDCHVKrEPGLDELVSETVESGALRAVESPvEAADrasIHV 109
Cdd:PRK11064 6 ISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIV-EPDLDMVVKTAVEGGYLRATTTP-EPAD---AFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 110 VIVPTPITDANQPDLAILQSVIESIADGLDQGDLVVVECTVPPGTTRDELLPLLERESDLS-------REEFGLAVCPER 182
Cdd:PRK11064 81 IAVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTfpqqageQADINIAYCPER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 183 TSSGRALQDIRgAYPKVVGGIDDESTRVAELVYGELTDNDVIsVPNATTAEAVKVFEGVYRDVNIALANELASIADDAEI 262
Cdd:PRK11064 161 VLPGQVMVELI-KNDRVIGGMTPVCSARASELYKIFLEGECV-VTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 263 SINGAIETANTQPFCDLHKPGPGVGGHCIPYYPYFLIEQFEAPFPLLRTAREVNDSMPGFTVEKT----VELLAEHGKAV 338
Cdd:PRK11064 239 NVWELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVkaavADCLAATDKRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 339 ADSRILVLGLTYRPGVEETRATPARPICADLTER-GADVFAVDPMLDD--AEGFDATKLAFEDLAEHEFDAAVLVTDHDE 415
Cdd:PRK11064 319 SEVKIACFGLAFKPNIDDLRESPAMEIAELIAQWhSGETLVVEPNIHQlpKKLDGLVTLVSLDEALATADVLVMLVDHSQ 398
|
410
....*....|....*.
gi 2339757616 416 FAGIDWAGFDPMVVVD 431
Cdd:PRK11064 399 FKAINGDNVHQQWVVD 414
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
30-211 |
4.53e-41 |
|
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.
Pssm-ID: 397677 [Multi-domain] Cd Length: 186 Bit Score: 144.70 E-value: 4.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 30 VAVYGLGKMGLPLAAVYAETCGNVIGADIDPDVVAAINRGDCHVKrEPGLDELVSETVeSGALRAVESPVEAADRASIHV 109
Cdd:pfam03721 3 ISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIY-EPGLDELVKANV-SGRLSFTTDYSTAIEEADVIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 110 VIVPTP-ITDANQPDLAILQSVIESIADGLDQGDLVVVECTVPPGTTRDELLPLLERESDLSREEFGLAVCPERTSSGRA 188
Cdd:pfam03721 81 IAVGTPsKKGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFDVASNPEFLREGSA 160
|
170 180
....*....|....*....|...
gi 2339757616 189 LQDIRGAyPKVVGGIDDESTRVA 211
Cdd:pfam03721 161 VYDLFNP-DRVVIGVTEKCAEAA 182
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
344-437 |
8.93e-19 |
|
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.
Pssm-ID: 214954 [Multi-domain] Cd Length: 99 Bit Score: 81.01 E-value: 8.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 344 LVLGLTYRPGVEETRATPARPICADLTERGADVFAVDPMLDDAEGFDATKLAFEDLAE-HEFDAAVLVTDHDEFAGIDWA 422
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREYGLTYVSDLEEAlKGADAVVIATEHDEFRSLDPE 80
|
90
....*....|....*....
gi 2339757616 423 GF----DPMVVVDGRDALD 437
Cdd:smart00984 81 ELkdlmKKPVVVDGRNILD 99
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
30-437 |
6.34e-177 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 501.13 E-value: 6.34e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 30 VAVYGLGKMGLPLAAVYAETCGNVIGADIDPDVVAAINRGDCHVKrEPGlDELVSETVESGALRAVESPvEAADRASIHV 109
Cdd:COG0677 2 IAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPIL-EPG-DELLAEAVAAGRLRATTDP-EALAEADVVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 110 VIVPTPITDANQPDLAILQSVIESIADGLDQGDLVVVECTVPPGTTRDELLPLLERESDLSR-EEFGLAVCPERTSSGRA 188
Cdd:COG0677 79 IAVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKAgEDFFLAYSPERINPGNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 189 LQDIRgAYPKVVGGIDDESTRVAELVYGELTDNDVISVPNATTAEAVKVFEGVYRDVNIALANELASIADDAEISINGAI 268
Cdd:COG0677 159 LHELR-NIPKVVGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 269 ETANTQPFCDLHKPGPGVGGHCIPYYPYFLI---EQFEAPFPLLRTAREVNDSMPGFTVEKTVELLAEHGKAVADSRILV 345
Cdd:COG0677 238 EAANTKPGFLIFYPGPGVGGHCIPVDPYYLTwkaRELGYHPRLILAAREINDSMPEYVVERVVKALNEAGKSLKGARVLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 346 LGLTYRPGVEETRATPARPICADLTERGADVFAVDPMLDDAEGFDATKLAFE-DLAEHEFDAAVLVTDHDEFAGIDWAGF 424
Cdd:COG0677 318 LGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGEYGELVDlEEALEGADAVVLAVDHDEFDELDPEEL 397
|
410
....*....|....*.
gi 2339757616 425 ---DPMVVVDGRDALD 437
Cdd:COG0677 398 rlkGAKVVVDTRGVLD 413
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
30-434 |
5.22e-125 |
|
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.
Pssm-ID: 274399 [Multi-domain] Cd Length: 409 Bit Score: 368.86 E-value: 5.22e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 30 VAVYGLGKMGLPLAAVYAETCGNVIGADIDPDVVAAINRGDCHVKrEPGLDELVSETVESGALRAVESPVEAADRASIHV 109
Cdd:TIGR03026 3 IAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIY-EPGLDELLAKALKAGRLRATTDYEEAIRDADVII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 110 VIVPTPITDANQPDLAILQSVIESIADGLDQGDLVVVECTVPPGTTRDELLPLLERESDLSREEFGLAVCPERTSSGRAL 189
Cdd:TIGR03026 82 ICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDFYLAYNPEFLREGNAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 190 QDIRGAyPKVVGGIDDESTRVAELVYGELTDNdVISVPNATTAEAVKVFEGVYRDVNIALANELASIADDAEISINGAIE 269
Cdd:TIGR03026 162 HDLLHP-DRIVGGETEEAGEAVAELYSPIIDG-PVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 270 TANTQPF--CDLHKPGPGVGGHCIPYYPYFLIEQFE---APFPLLRTAREVNDSMPGFTVEKTVELLaehgKAVADSRIL 344
Cdd:TIGR03026 240 AAGTDPRigFNFLNPGPGVGGHCIPKDPLALIAKAKelgYNPELIEAAREINDSQPDYVVEKIKDLL----GPLKGKTVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 345 VLGLTYRPGVEETRATPARPICADLTERGADVFAVDP--MLDDAEGFDATKLAFEDLAehEFDAAVLVTDHDEFAGIDWA 422
Cdd:TIGR03026 316 ILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPlvPEEEVKGLPSIDDLEEALK--GADALVILTDHSEFKDLDLE 393
|
410
....*....|....*.
gi 2339757616 423 GFDPM----VVVDGRD 434
Cdd:TIGR03026 394 KIKDLmkgkVVVDTRN 409
|
|
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
30-431 |
8.19e-80 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 253.37 E-value: 8.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 30 VAVYGLGKMGLPLAAVYAETCGNVIGADIDPDVVAAINRGDCHVKrEPGLDELVSETVESGALRAVESPvEAADrasIHV 109
Cdd:PRK11064 6 ISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIV-EPDLDMVVKTAVEGGYLRATTTP-EPAD---AFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 110 VIVPTPITDANQPDLAILQSVIESIADGLDQGDLVVVECTVPPGTTRDELLPLLERESDLS-------REEFGLAVCPER 182
Cdd:PRK11064 81 IAVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTfpqqageQADINIAYCPER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 183 TSSGRALQDIRgAYPKVVGGIDDESTRVAELVYGELTDNDVIsVPNATTAEAVKVFEGVYRDVNIALANELASIADDAEI 262
Cdd:PRK11064 161 VLPGQVMVELI-KNDRVIGGMTPVCSARASELYKIFLEGECV-VTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 263 SINGAIETANTQPFCDLHKPGPGVGGHCIPYYPYFLIEQFEAPFPLLRTAREVNDSMPGFTVEKT----VELLAEHGKAV 338
Cdd:PRK11064 239 NVWELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVkaavADCLAATDKRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 339 ADSRILVLGLTYRPGVEETRATPARPICADLTER-GADVFAVDPMLDD--AEGFDATKLAFEDLAEHEFDAAVLVTDHDE 415
Cdd:PRK11064 319 SEVKIACFGLAFKPNIDDLRESPAMEIAELIAQWhSGETLVVEPNIHQlpKKLDGLVTLVSLDEALATADVLVMLVDHSQ 398
|
410
....*....|....*.
gi 2339757616 416 FAGIDWAGFDPMVVVD 431
Cdd:PRK11064 399 FKAINGDNVHQQWVVD 414
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
30-437 |
7.78e-58 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 196.40 E-value: 7.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 30 VAVYGLGKMGLPLAAVYAETCGNVIGADIDPDVVAAINRGDCHVKrEPGLDELVSETVESGALRAVESPVEAADRASIHV 109
Cdd:COG1004 3 IAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIY-EPGLEELVARNVAAGRLRFTTDLAEAVAEADVVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 110 VIVPTPITDANQPDLAILQSVIESIADGLDQGDLVVVECTVPPGTTrDELLPLLERESDLSREEFGLAVCPERTSSGRAL 189
Cdd:COG1004 82 IAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTA-DRVRAIIAEELRGAGVDFDVVSNPEFLREGSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 190 QDIRgaYPK--VVGGIDDESTRVAELVYGELTDNDV-ISVPNATTAEAVKVfegvyrDVN------IALANELASIADDA 260
Cdd:COG1004 161 EDFL--RPDriVIGVDSERAAEVLRELYAPFVRNGTpIIVTDLRSAELIKY------AANaflatkISFINEIANLCEKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 261 EISIN------GAietantqpfcD-------LHkPGPGVGGHCipyypyF------LI---EQFEAPFPLLRTAREVNDS 318
Cdd:COG1004 233 GADVEevargiGL----------DsrigpkfLY-AGIGYGGSC------FpkdvraLIataRELGYDLRLLEAVEEVNER 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 319 MPGFTVEKTVELLaehGKAVADSRILVLGLTYRPGVEETRATPARPICADLTERGADVFAVDPM-LDDAEGFDATKLAFE 397
Cdd:COG1004 296 QKRRLVEKIREHL---GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVaMENARRLLPDDITYA 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2339757616 398 DLAE---HEFDAAVLVTDHDEFAGIDWAG-FDPM---VVVDGRDALD 437
Cdd:COG1004 373 DDAYealEGADALVILTEWPEFRALDFARlKALMkgpVIFDGRNLLD 419
|
|
| PRK15182 |
PRK15182 |
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB; |
27-445 |
2.36e-46 |
|
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
Pssm-ID: 185104 [Multi-domain] Cd Length: 425 Bit Score: 165.63 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 27 EIPVAVYGLGKMGLPLAAVYAETcGNVIGADIDPDVVAAINRG-DCHVkrepgldELVSETVESGALRAVESPVEAADRA 105
Cdd:PRK15182 6 EVKIAIIGLGYVGLPLAVEFGKS-RQVVGFDVNKKRILELKNGvDVNL-------ETTEEELREARYLKFTSEIEKIKEC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 106 SIHVVIVPTPITDANQPDLAILQSVIESIADGLDQGDLVVVECTVPPGTTRDELLPLLERESDLS-REEFGLAVCPERTS 184
Cdd:PRK15182 78 NFYIITVPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEECVPILARMSGMTfNQDFYVGYSPERIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 185 SG---RALQDIRgaypKVVGGIDDESTRVAELVYGELTDNDVISVPNATTAEAVKVFEGVYRDVNIALANELASIAD--- 258
Cdd:PRK15182 158 PGdkkHRLTNIK----KITSGSTAQIAELIDEVYQQIISAGTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNrln 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 259 -DAEISINGAIETANTQPFcdlhKPGPgVGGHCIPYYPYFLIEQFEAP--FP-LLRTAREVNDSMPGFTVEKTVELLAEH 334
Cdd:PRK15182 234 iDTEAVLRAAGSKWNFLPF----RPGL-VGGHCIGVDPYYLTHKSQGIgyYPeIILAGRRLNDNMGNYVSEQLIKAMIKK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 335 GKAVADSRILVLGLTYRPGVEETRATPARPICADLTERGADVFAVDPMLDDAE-GFDATKLAFEDLAEHEFDAAVLVTDH 413
Cdd:PRK15182 309 GINVEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEvRREYGIIPVSEVKSSHYDAIIVAVGH 388
|
410 420 430
....*....|....*....|....*....|....*..
gi 2339757616 414 DEFAGI---DWAGF--DPMVVVDGRDALDLSWTDHRI 445
Cdd:PRK15182 389 QQFKQMgseDIRGFgkDKHVLYDLKYVLPAEQSDVRL 425
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
30-211 |
4.53e-41 |
|
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.
Pssm-ID: 397677 [Multi-domain] Cd Length: 186 Bit Score: 144.70 E-value: 4.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 30 VAVYGLGKMGLPLAAVYAETCGNVIGADIDPDVVAAINRGDCHVKrEPGLDELVSETVeSGALRAVESPVEAADRASIHV 109
Cdd:pfam03721 3 ISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIY-EPGLDELVKANV-SGRLSFTTDYSTAIEEADVIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 110 VIVPTP-ITDANQPDLAILQSVIESIADGLDQGDLVVVECTVPPGTTRDELLPLLERESDLSREEFGLAVCPERTSSGRA 188
Cdd:pfam03721 81 IAVGTPsKKGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFDVASNPEFLREGSA 160
|
170 180
....*....|....*....|...
gi 2339757616 189 LQDIRGAyPKVVGGIDDESTRVA 211
Cdd:pfam03721 161 VYDLFNP-DRVVIGVTEKCAEAA 182
|
|
| UDPG_MGDP_dh |
pfam00984 |
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ... |
231-317 |
2.04e-27 |
|
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.
Pssm-ID: 460015 [Multi-domain] Cd Length: 92 Bit Score: 104.77 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 231 TAEAVKVFEGVYRDVNIALANELASIADDAEISINGAIETANTQPF--CDLHKPGPGVGGHCIPYYPYFLI---EQFEAP 305
Cdd:pfam00984 1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRigPKFLYPGPGVGGSCLPKDPRALIylaRELGVP 80
|
90
....*....|..
gi 2339757616 306 FPLLRTAREVND 317
Cdd:pfam00984 81 ARLLEAAREVNE 92
|
|
| UDPG_MGDP_dh_C |
pfam03720 |
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ... |
344-437 |
5.04e-20 |
|
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.
Pssm-ID: 427462 [Multi-domain] Cd Length: 103 Bit Score: 84.55 E-value: 5.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 344 LVLGLTYRPGVEETRATPARPICADLTERGADVFAVDPMLDD----AEGFDATKLAFEDLAEHEFDAAVLVTDHDEFAGI 419
Cdd:pfam03720 1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEeaieALGDGVTLVDDLEEALKGADAIVILTDHDEFKSL 80
|
90 100
....*....|....*....|..
gi 2339757616 420 DWAGFDPM----VVVDGRDALD 437
Cdd:pfam03720 81 DWEKLKKLmkppVVFDGRNVLD 102
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
344-437 |
8.93e-19 |
|
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.
Pssm-ID: 214954 [Multi-domain] Cd Length: 99 Bit Score: 81.01 E-value: 8.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 344 LVLGLTYRPGVEETRATPARPICADLTERGADVFAVDPMLDDAEGFDATKLAFEDLAE-HEFDAAVLVTDHDEFAGIDWA 422
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREYGLTYVSDLEEAlKGADAVVIATEHDEFRSLDPE 80
|
90
....*....|....*....
gi 2339757616 423 GF----DPMVVVDGRDALD 437
Cdd:smart00984 81 ELkdlmKKPVVVDGRNILD 99
|
|
| PRK15057 |
PRK15057 |
UDP-glucose 6-dehydrogenase; Provisional |
30-412 |
8.88e-16 |
|
UDP-glucose 6-dehydrogenase; Provisional
Pssm-ID: 185017 [Multi-domain] Cd Length: 388 Bit Score: 78.53 E-value: 8.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 30 VAVYGLGKMGLPLAAVYAETcGNVIGADIDPDVVAAINRgdchvKREPGLDELVSETVESGAL--RAVESPVEAADRASi 107
Cdd:PRK15057 3 ITISGTGYVGLSNGLLIAQN-HEVVALDILPSRVAMLND-----RISPIVDKEIQQFLQSDKIhfNATLDKNEAYRDAD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 108 hVVIVPTPiTD----ANQPDLAILQSVIESIADgLDQGDLVVVECTVPPGTTrdellPLLERESDLSREEFGlavcPERT 183
Cdd:PRK15057 76 -YVIIATP-TDydpkTNYFNTSSVESVIKDVVE-INPYAVMVIKSTVPVGFT-----AAMHKKYRTENIIFS----PEFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 184 SSGRALQDirGAYPK--VVGGIDDESTRVAELVYGELTDNDVISV-PNATTAEAVKVFEGVYRDVNIALANELASIADDA 260
Cdd:PRK15057 144 REGKALYD--NLHPSriVIGERSERAERFAALLQEGAIKQNIPTLfTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 261 EISINGAIETANTQPFCDLH--KPGPGVGGHCIPYYPYFLIEQFEA-PFPLLRTAREVNDSMPGFTVEKtveLLAEHGKA 337
Cdd:PRK15057 222 GLNTRQIIEGVCLDPRIGNHynNPSFGYGGYCLPKDTKQLLANYQSvPNNLISAIVDANRTRKDFIADA---ILSRKPQV 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2339757616 338 VADSRILVlgltyRPGVEETRATPARPICADLTERGADVFAVDPMLDDAEGFDaTKLAfEDLAEHEFDAAVLVTD 412
Cdd:PRK15057 299 VGIYRLIM-----KSGSDNFRASSIQGIMKRIKAKGVEVIIYEPVMKEDSFFN-SRLE-RDLATFKQQADVIISN 366
|
|
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
34-437 |
4.24e-07 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 51.99 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 34 GLGKMGLPLAAVYAETCGN--VIGADIDPDVVAAINRGDCHVkREPGLDELVSETvesgalRA--------VESPVEAAD 103
Cdd:PLN02353 8 GAGYVGGPTMAVIALKCPDieVVVVDISVPRIDAWNSDQLPI-YEPGLDEVVKQC------RGknlffstdVEKHVAEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 104 rasIHVVIVPTP-----ITDANQPDLAILQSVIESIADgLDQGDLVVVECTVPPGTTRDELLPLLERESDLSReeFGLAV 178
Cdd:PLN02353 81 ---IVFVSVNTPtktrgLGAGKAADLTYWESAARMIAD-VSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGIN--FQILS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 179 CPERTSSGRALQDIRGAYPKVVGGIDDESTR--VAEL--VYGELTDNDVISVPNATTAEAVKVfegvyrDVNIALANELA 254
Cdd:PLN02353 155 NPEFLAEGTAIEDLFKPDRVLIGGRETPEGQkaVQALkdVYAHWVPEERIITTNLWSAELSKL------AANAFLAQRIS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 255 SI-----------ADDAEISINGAIETANTQPFCDlhkPGPGVGGHCIPYYPYFLIEQFEApFPLLRTAR------EVND 317
Cdd:PLN02353 229 SVnamsalceatgADVSQVSHAVGKDSRIGPKFLN---ASVGFGGSCFQKDILNLVYICEC-NGLPEVAEywkqviKMND 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 318 SMPGFTVEKTVellAEHGKAVADSRILVLGLTYRPGVEETRATPARPICADLTERGADVFAVDPMLDDAEgfdatklAFE 397
Cdd:PLN02353 305 YQKSRFVNRVV---SSMFNTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQ-------IQR 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2339757616 398 DLAEHEFD---------------AAVLV-----------------TDHDEFAGIDWAG-FDPMV----VVDGRDALD 437
Cdd:PLN02353 375 DLSMNKFDwdhprhlqpmsptavKQVSVvwdayeatkgahgicilTEWDEFKTLDYQKiYDNMQkpafVFDGRNVLD 451
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
29-157 |
1.21e-05 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 46.65 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 29 PVAVYGLGKMGLPLAAVYAETCGNVIGADIDPDVVAAInrgdchvkrepgldelvsetVESGAlRAVESPVEAADRASIH 108
Cdd:COG2084 3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEAL--------------------VAAGA-RVAASPAEAAAAADVV 61
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2339757616 109 VVIVPTPitdanqpdlAILQSVI---ESIADGLDQGDLVVVECTVPPGTTRD 157
Cdd:COG2084 62 ITMLPDD---------AAVEEVLlgeDGLLAALRPGAVVVDMSTISPETARE 104
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
30-249 |
1.93e-05 |
|
sulfolactaldehyde 3-reductase;
Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 46.39 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 30 VAVYGLGKMGLPLAAVYAETCGNVIGADIDPDVVAAInrgdchvkrepgldelvsetVESGALRAVeSPVEAADRASIHV 109
Cdd:PRK15461 4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDAL--------------------VDKGATPAA-SPAQAAAGAEFVI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 110 VIVPTPitdanqpdlAILQSVIE---SIADGLDQGDLVVVECTVPPGTTrDELLpllereSDLSREEFGLAVCPERTSSG 186
Cdd:PRK15461 63 TMLPNG---------DLVRSVLFgenGVCEGLSRDALVIDMSTIHPLQT-DKLI------ADMQAKGFSMMDVPVGRTSD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 187 RAlqdIRGAYPKVVGGIDDESTRVAELVY---GELTD-------------NDVISVP-NATTAEAVKVFEGVYRDVNIAL 249
Cdd:PRK15461 127 NA---ITGTLLLLAGGTAEQVERATPILMamgNELINaggpgmgirvkliNNYMSIAlNALSAEAAVLCEALGLSFDVAL 203
|
|
| NAD_Gly3P_dh_N |
pfam01210 |
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ... |
29-114 |
6.11e-04 |
|
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain.
Pssm-ID: 395967 [Multi-domain] Cd Length: 158 Bit Score: 40.25 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 29 PVAVYGLGKMGLPLAAVYAETCGNVIGADIDPDVVAAINRGDCHVKREPGLDelVSETvesgaLRAVESPVEAADRASIH 108
Cdd:pfam01210 1 KIAVLGAGSWGTALAKVLADNGHEVRLWGRDEELIEEINTTHENVRYLPGIK--LPEN-----LKATTDLAEALKGADII 73
|
....*.
gi 2339757616 109 VVIVPT 114
Cdd:pfam01210 74 VIVVPS 79
|
|
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
29-169 |
1.25e-03 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 41.38 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 29 PVAVYGLGKMGLPLAAVYAetcgnvigadidpdvvaainRGDCHVKREPGLDELVSETVESGALRAvESPVEAADRASIH 108
Cdd:PLN02858 6 VVGFVGLDSLSFELASSLL--------------------RSGFKVQAFEISTPLMEKFCELGGHRC-DSPAEAAKDAAAL 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2339757616 109 VVIvptpITDANQPDLAILQSviESIADGLDQGDLVVVECTVPPGTTRDELLPLLERESDL 169
Cdd:PLN02858 65 VVV----LSHPDQVDDVFFGD--EGAAKGLQKGAVILIRSTILPLQLQKLEKKLTERKEQI 119
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
30-157 |
2.68e-03 |
|
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.
Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 38.22 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2339757616 30 VAVYGLGKMGLPLAavyaetcGNVIGADIDpdvVAAINRGdchvkrepglDELVSETVESGAlRAVESPVEAADRASIHV 109
Cdd:pfam03446 2 IGFIGLGVMGSPMA-------LNLLKAGYT---VTVYNRT----------PEKVEELVAAGA-IAAASPAEFVAGLDVVI 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2339757616 110 VIVPTPitdanqpdlAILQSVIES--IADGLDQGDLVVVECTVPPGTTRD 157
Cdd:pfam03446 61 TMVPAG---------AAVDAVIFGegLLPGLKPGDIIIDGSTSSPEDARR 101
|
|
| |
