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Conserved domains on  [gi|530376515|ref|XP_005262724|]
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UDP-glucose 6-dehydrogenase isoform X1 [Homo sapiens]

Protein Classification

UDP-glucose 6-dehydrogenase( domain architecture ID 11476687)

UDP-glucose 6-dehydrogenase is involved in the biosynthesis of glycosaminoglycans, hyaluronan, chondroitin sulfate, and heparan sulfate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
17-477 0e+00

probable UDP-glucose 6-dehydrogenase


:

Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 786.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  17 IKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEAD 96
Cdd:PLN02353   1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  97 LVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKpNLNLQVLSNPEFL 176
Cdd:PLN02353  81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSK-GINFQILSNPEFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 177 AEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEA 256
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 257 TGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLF 336
Cdd:PLN02353 240 TGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMF 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 337 NTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQV---------SRL 407
Cdd:PLN02353 320 NTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRhlqpmsptaVKQ 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 408 VTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDglHNELQTIGFQIETIGK 477
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLD--HEKLREIGFIVYSIGK 467
 
Name Accession Description Interval E-value
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
17-477 0e+00

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 786.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  17 IKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEAD 96
Cdd:PLN02353   1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  97 LVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKpNLNLQVLSNPEFL 176
Cdd:PLN02353  81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSK-GINFQILSNPEFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 177 AEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEA 256
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 257 TGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLF 336
Cdd:PLN02353 240 TGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMF 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 337 NTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQV---------SRL 407
Cdd:PLN02353 320 NTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRhlqpmsptaVKQ 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 408 VTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDglHNELQTIGFQIETIGK 477
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLD--HEKLREIGFIVYSIGK 467
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
19-478 0e+00

UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 563.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  19 KICCIGAGYVGGPTCSVIAHMCPEirVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCR-GKNLFFSTNIDDAIKEADL 97
Cdd:COG1004    2 KIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  98 VFISVNTPTKTYGmgkgrAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIF-DANTKPNLNLQVLSNPEFL 176
Cdd:COG1004   80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIaEELRGAGVDFDVVSNPEFL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 177 AEGTAIKDLKNPDRVLIGGDetpeGQRAVQALCAVYEHWVPRE-KILTTNTWSSELSKLAANAFLAQRISSINSISALCE 255
Cdd:COG1004  155 REGSAVEDFLRPDRIVIGVD----SERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 256 ATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPevARYWQQVIDMNDYQRRRFASRIIDSL 335
Cdd:COG1004  231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 336 FNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPreqivvdlshpgvsedDQVSRL----VTIS 411
Cdd:COG1004  309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAM----------------ENARRLlpddITYA 372
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530376515 412 KDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAfIFDGRRVLDglHNELQTIGFQIETIGKK 478
Cdd:COG1004  373 DDAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLD--PEELRAAGFTYYGIGRP 436
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
18-456 1.20e-115

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: 346.91  E-value: 1.20e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515   18 KKICCIGAGYVGGPTCSVIAHMcpEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLF-FSTNIDDAIKEAD 96
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDAD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515   97 LVFISVNTPTKTYGMgkgraADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRR--IFDANTKPNLNLQVLSNPE 174
Cdd:TIGR03026  79 VIIICVPTPLKEDGS-----PDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpiLERSGLKLGEDFYLAYNPE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  175 FLAEGTAIKDLKNPDRVLIGgdETPEGQRAVQALcavYEHWVpREKILTTNTWSSELSKLAANAFLAQRISSINSISALC 254
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRIVGG--ETEEAGEAVAEL---YSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARIC 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  255 EATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPevARYWQQVIDMNDYQRRRFASRIIDS 334
Cdd:TIGR03026 228 EALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDL 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  335 LFNtVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPgvseddqvsrlvtiskDP 414
Cdd:TIGR03026 306 LGP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSID----------------DL 368
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 530376515  415 YEACDGAHAVVICTEWDMFKELDYERIhKKMLKPAFIFDGRR 456
Cdd:TIGR03026 369 EEALKGADALVILTDHSEFKDLDLEKI-KDLMKGKVVVDTRN 409
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
18-204 1.75e-71

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: 225.59  E-value: 1.75e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515   18 KKICCIGAGYVGGPTCSVIAHMCpeIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADL 97
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515   98 VFISVNTPTKTygmgKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESI--RRIFDANTKPNLNLQVLSNPEF 175
Cdd:pfam03721  79 IFIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLvkPIIEEGGKKVGVDFDVASNPEF 154
                         170       180
                  ....*....|....*....|....*....
gi 530376515  176 LAEGTAIKDLKNPDRVLIGGDETPEGQRA 204
Cdd:pfam03721 155 LREGSAVYDLFNPDRVVIGVTEKCAEAAL 183
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
345-459 3.56e-33

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: 121.46  E-value: 3.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515   345 AILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIvvdlshpgvseddqvSRLVTISKDPYEACDGAHAV 424
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAR---------------EYGLTYVSDLEEALKGADAV 65
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 530376515   425 VICTEWDMFKELDYERIhKKMLKPAFIFDGRRVLD 459
Cdd:smart00984  66 VIATEHDEFRSLDPEEL-KDLMKKPVVVDGRNILD 99
 
Name Accession Description Interval E-value
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
17-477 0e+00

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 786.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  17 IKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEAD 96
Cdd:PLN02353   1 MVKICCIGAGYVGGPTMAVIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKNLFFSTDVEKHVAEAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  97 LVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKpNLNLQVLSNPEFL 176
Cdd:PLN02353  81 IVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSK-GINFQILSNPEFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 177 AEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEA 256
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAANAFLAQRISSVNAMSALCEA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 257 TGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLF 336
Cdd:PLN02353 240 TGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKMNDYQKSRFVNRVVSSMF 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 337 NTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQV---------SRL 407
Cdd:PLN02353 320 NTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNKFDWDHPRhlqpmsptaVKQ 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 408 VTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDglHNELQTIGFQIETIGK 477
Cdd:PLN02353 400 VSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPAFVFDGRNVLD--HEKLREIGFIVYSIGK 467
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
19-478 0e+00

UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 563.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  19 KICCIGAGYVGGPTCSVIAHMCPEirVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCR-GKNLFFSTNIDDAIKEADL 97
Cdd:COG1004    2 KIAVIGTGYVGLVTAACLAELGHE--VTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVaAGRLRFTTDLAEAVAEADV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  98 VFISVNTPTKTYGmgkgrAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIF-DANTKPNLNLQVLSNPEFL 176
Cdd:COG1004   80 VFIAVGTPSDEDG-----SADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIaEELRGAGVDFDVVSNPEFL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 177 AEGTAIKDLKNPDRVLIGGDetpeGQRAVQALCAVYEHWVPRE-KILTTNTWSSELSKLAANAFLAQRISSINSISALCE 255
Cdd:COG1004  155 REGSAVEDFLRPDRIVIGVD----SERAAEVLRELYAPFVRNGtPIIVTDLRSAELIKYAANAFLATKISFINEIANLCE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 256 ATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPevARYWQQVIDMNDYQRRRFASRIIDSL 335
Cdd:COG1004  231 KVGADVEEVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYD--LRLLEAVEEVNERQKRRLVEKIREHL 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 336 FNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPreqivvdlshpgvsedDQVSRL----VTIS 411
Cdd:COG1004  309 GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAM----------------ENARRLlpddITYA 372
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530376515 412 KDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAfIFDGRRVLDglHNELQTIGFQIETIGKK 478
Cdd:COG1004  373 DDAYEALEGADALVILTEWPEFRALDFARLKALMKGPV-IFDGRNLLD--PEELRAAGFTYYGIGRP 436
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
18-456 1.20e-115

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: 346.91  E-value: 1.20e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515   18 KKICCIGAGYVGGPTCSVIAHMcpEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLF-FSTNIDDAIKEAD 96
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADL--GHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLrATTDYEEAIRDAD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515   97 LVFISVNTPTKTYGMgkgraADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRR--IFDANTKPNLNLQVLSNPE 174
Cdd:TIGR03026  79 VIIICVPTPLKEDGS-----PDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKpiLERSGLKLGEDFYLAYNPE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  175 FLAEGTAIKDLKNPDRVLIGgdETPEGQRAVQALcavYEHWVpREKILTTNTWSSELSKLAANAFLAQRISSINSISALC 254
Cdd:TIGR03026 154 FLREGNAVHDLLHPDRIVGG--ETEEAGEAVAEL---YSPII-DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARIC 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  255 EATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPevARYWQQVIDMNDYQRRRFASRIIDS 334
Cdd:TIGR03026 228 EALGIDVYEVIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYN--PELIEAAREINDSQPDYVVEKIKDL 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  335 LFNtVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPgvseddqvsrlvtiskDP 414
Cdd:TIGR03026 306 LGP-LKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSID----------------DL 368
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 530376515  415 YEACDGAHAVVICTEWDMFKELDYERIhKKMLKPAFIFDGRR 456
Cdd:TIGR03026 369 EEALKGADALVILTDHSEFKDLDLEKI-KDLMKGKVVVDTRN 409
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
18-204 1.75e-71

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: 225.59  E-value: 1.75e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515   18 KKICCIGAGYVGGPTCSVIAHMCpeIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADL 97
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIG--HDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGRLSFTTDYSTAIEEADV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515   98 VFISVNTPTKTygmgKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESI--RRIFDANTKPNLNLQVLSNPEF 175
Cdd:pfam03721  79 IFIAVGTPSKK----GGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLvkPIIEEGGKKVGVDFDVASNPEF 154
                         170       180
                  ....*....|....*....|....*....
gi 530376515  176 LAEGTAIKDLKNPDRVLIGGDETPEGQRA 204
Cdd:pfam03721 155 LREGSAVYDLFNPDRVVIGVTEKCAEAAL 183
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
19-459 1.73e-54

UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 188.35  E-value: 1.73e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  19 KICCIGAGYVGGPTCSVIAHMCpeIRVTVVDVNESRINAWNSPTLPIYEPG---LKEVVESCRgknLFFSTNIDdAIKEA 95
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKAG--FRVIGFDINPERVEELNAGEDPILEPGdelLAEAVAAGR---LRATTDPE-ALAEA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  96 DLVFISVNTPTKtygmgKGRAADLKYIEACARRIVQN-SNGYKIVTEkSTVPVRAAESI-RRIFDANT--KPNLNLQVLS 171
Cdd:COG0677   75 DVVIIAVPTPLD-----EDKEPDLSYLESASETIAPHlKPGDLVVLE-STVYPGTTEEVcVPILEKRSglKAGEDFFLAY 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 172 NPEFLAEGTAIKDLKNPDRVlIGGDeTPEGQRAVQALcavYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSIS 251
Cdd:COG0677  149 SPERINPGNKLHELRNIPKV-VGGI-TPESAERAAAL---YGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 252 ALCEATGADVEEVATAIGMDQRIgNKFlKASVGFGGSCFQKDVLNLVYLCEALNLP----EVARywqqviDMNDYQRRRF 327
Cdd:COG0677  224 LICDRLGIDVWEVIEAANTKPGF-LIF-YPGPGVGGHCIPVDPYYLTWKARELGYHprliLAAR------EINDSMPEYV 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 328 ASRIIDSLFN---TVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPreqivvdlshpgvseDDQV 404
Cdd:COG0677  296 VERVVKALNEagkSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVD---------------EEEV 360
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530376515 405 SRLVTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKmlKPAFIFDGRRVLD 459
Cdd:COG0677  361 EGEYGELVDLEEALEGADAVVLAVDHDEFDELDPEELRLK--GAKVVVDTRGVLD 413
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
228-321 3.80e-43

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: 147.91  E-value: 3.80e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  228 SSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLP 307
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
                          90
                  ....*....|....
gi 530376515  308 evARYWQQVIDMND 321
Cdd:pfam00984  81 --ARLLEAAREVNE 92
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
345-459 8.69e-38

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: 133.86  E-value: 8.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  345 AILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHpgvseddqvsrlVTISKDPYEACDGAHAV 424
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALGDG------------VTLVDDLEEALKGADAI 68
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 530376515  425 VICTEWDMFKELDYERIhKKMLKPAFIFDGRRVLD 459
Cdd:pfam03720  69 VILTDHDEFKSLDWEKL-KKLMKPPVVFDGRNVLD 102
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
345-459 3.56e-33

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: 121.46  E-value: 3.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515   345 AILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIvvdlshpgvseddqvSRLVTISKDPYEACDGAHAV 424
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAR---------------EYGLTYVSDLEEALKGADAV 65
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 530376515   425 VICTEWDMFKELDYERIhKKMLKPAFIFDGRRVLD 459
Cdd:smart00984  66 VIATEHDEFRSLDPEEL-KDLMKKPVVVDGRNILD 99
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
19-382 2.61e-29

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 118.97  E-value: 2.61e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  19 KICCIGAGYVGGPTCSVIAHmcpEIRVTVVDVNESRINAWNSPTLPIYEpglKEVVESCRGKNLFFSTNID--DAIKEAD 96
Cdd:PRK15057   2 KITISGTGYVGLSNGLLIAQ---NHEVVALDILPSRVAMLNDRISPIVD---KEIQQFLQSDKIHFNATLDknEAYRDAD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  97 LVFISvnTPTKtYGmGKGRAADLKYIEACARRIVQnSNGYKIVTEKSTVPVRAAESIRRIFdaNTKpnlnlQVLSNPEFL 176
Cdd:PRK15057  76 YVIIA--TPTD-YD-PKTNYFNTSSVESVIKDVVE-INPYAVMVIKSTVPVGFTAAMHKKY--RTE-----NIIFSPEFL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 177 AEGTAIKDLKNPDRVLIGgdetPEGQRAvQALCAVYEHWVPREKILT--TNTWSSELSKLAANAFLAQRISSINSISALC 254
Cdd:PRK15057 144 REGKALYDNLHPSRIVIG----ERSERA-ERFAALLQEGAIKQNIPTlfTDSTEAEAIKLFANTYLAMRVAYFNELDSYA 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 255 EATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLvyLCEALNLPEvaRYWQQVIDMNDYQRRRFASRIIDS 334
Cdd:PRK15057 219 ESLGLNTRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQL--LANYQSVPN--NLISAIVDANRTRKDFIADAILSR 294
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 530376515 335 lfntvTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDP 382
Cdd:PRK15057 295 -----KPQVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEP 337
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
18-372 1.18e-21

UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 96.98  E-value: 1.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  18 KKICCIGAGYVGGPTCSVIAHMcpEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESC-RGKNLFFSTniddAIKEAD 96
Cdd:PRK11064   4 ETISVIGLGYIGLPTAAAFASR--QKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAvEGGYLRATT----TPEPAD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  97 LVFISVNTPTKtygmgKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFdANTKPNL----------N 166
Cdd:PRK11064  78 AFLIAVPTPFK-----GDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWL-AEARPDLtfpqqageqaD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 167 LQVLSNPEFLAEGTAIKDLKNPDRVlIGGdETPE-GQRAVqalcAVYEHWVPREKILTtNTWSSELSKLAANAFLAQRIS 245
Cdd:PRK11064 152 INIAYCPERVLPGQVMVELIKNDRV-IGG-MTPVcSARAS----ELYKIFLEGECVVT-NSRTAEMCKLTENSFRDVNIA 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 246 SINSISALCEATGADVEEVAtaigmdqRIGNK-----FLKASVGFGGSCFQKDVLNLVYLCealnlPEVARYWQQVIDMN 320
Cdd:PRK11064 225 FANELSLICADQGINVWELI-------RLANRhprvnILQPGPGVGGHCIAVDPWFIVAQN-----PQQARLIRTAREVN 292
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530376515 321 D----YQRRRFASRIIDSLFNT---VTDKKIAILGFAFKKDTGDTRESSSIYISKYLMD 372
Cdd:PRK11064 293 DgkphWVIDQVKAAVADCLAATdkrASEVKIACFGLAFKPNIDDLRESPAMEIAELIAQ 351
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
14-389 4.27e-11

Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 64.71  E-value: 4.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  14 MFEIK--KICCIGAGYVGGPtcsVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVEScrgKNLFFSTNIDDa 91
Cdd:PRK15182   1 MFGIDevKIAIIGLGYVGLP---LAVEFGKSRQVVGFDVNKKRILELKNGVDVNLETTEEELREA---RYLKFTSEIEK- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  92 IKEADLVFISVNTPTKTYgmgkgRAADLKYIEACARRI----------VQNSNGYKIVTEKSTVPVRAAESirrifdaNT 161
Cdd:PRK15182  74 IKECNFYIITVPTPINTY-----KQPDLTPLIKASETVgtvlnrgdivVYESTVYPGCTEEECVPILARMS-------GM 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 162 KPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDetpegQRAVQALCAVYEhwvpreKILTTNTWSSELSKLAANAFL- 240
Cdd:PRK15182 142 TFNQDFYVGYSPERINPGDKKHRLTNIKKITSGST-----AQIAELIDEVYQ------QIISAGTYKAESIKVAEAAKVi 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515 241 --AQR---ISSINSISALCEATGADVEEVATAIGMDQrignKFLKASVGF-GGSCFQKDVLNLVYLCEALNL-PEVARYW 313
Cdd:PRK15182 211 enTQRdlnIALVNELAIIFNRLNIDTEAVLRAAGSKW----NFLPFRPGLvGGHCIGVDPYYLTHKSQGIGYyPEIILAG 286
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530376515 314 QQVID-MNDYQRRRFASRIIDSLFNtVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQI 389
Cdd:PRK15182 287 RRLNDnMGNYVSEQLIKAMIKKGIN-VEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEV 362
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
18-102 8.78e-03

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 38.12  E-value: 8.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376515  18 KKICCIGAG-----YVGGptcsVIAHMCPEIRVTVVDVNESRINAWNSptlpiyEPGLKevvescrgknlfFSTNIDDAI 92
Cdd:COG0345    3 MKIGFIGAGnmgsaIIKG----LLKSGVPPEDIIVSDRSPERLEALAE------RYGVR------------VTTDNAEAA 60
                         90
                 ....*....|
gi 530376515  93 KEADLVFISV 102
Cdd:COG0345   61 AQADVVVLAV 70
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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