NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|296932073|gb|ADH92881|]
View 

UDP-glucose--hexose-1-phosphateuridylyl transferase [Arcanobacterium haemolyticum DSM 20595]

Protein Classification

UDP-glucose--hexose-1-phosphate uridylyltransferase( domain architecture ID 11480523)

UDP-glucose--hexose-1-phosphate uridylyltransferase catalyzes the conversion from UDP-alpha-D-glucose and alpha-D-galactose 1-phosphate to alpha-D-glucose 1-phosphate and UDP-alpha-D-galactose

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK05270 PRK05270
UDP-glucose--hexose-1-phosphate uridylyltransferase;
3-485 0e+00

UDP-glucose--hexose-1-phosphate uridylyltransferase;


:

Pssm-ID: 235382 [Multi-domain]  Cd Length: 493  Bit Score: 652.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073   3 TNVYNAVDELIDYARKNLELDPRNEDFTRNAIFAIFGLNSYAPTGATCDDRVPDAVIARFTQACVDAGLI--GVEGEAAL 80
Cdd:PRK05270   1 MTISQLIEKLIDYAIQNGLIEELDRIYLRNRLLALLGEDSYEEVDEDEDLESPIDLLDQLVDYAVENGLIedTQTERDIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073  81 ADQVMGLLTPRPAEVIDRFDEIRKRdGGTAAMAWFYQYCVANHYVKRAVLDRNPRFDV----GDLTITINLAKPEfRDAK 156
Cdd:PRK05270  81 DAQLMDLLTPRPSEVNRRFWEKYQK-SPEAATDYFYQLSKANNYIKTDAIAKNISWKVptkyGDLEITINLSKPE-KDPK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 157 K-AAAGNSVAGGYPSCTICHENEGFAGRQ----KGTLRTVPITLGGQEWFWQFSPYGYFDQHGIAVNMEHTPMHMDHGTF 231
Cdd:PRK05270 159 AiAAAKKAKASSYPKCLLCMENEGYAGRLnhpaRSNHRIIRLTLGGESWGFQYSPYAYFNEHCIVLSEKHRPMKISRKTF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 232 YRLMDFVDQFPQYFIGCNAALPRIGGSVLGHDHYQGGGEVLPMHKAATRVTYRVPGTDGVAVEIVDWHNTVVRVVGQDRD 311
Cdd:PRK05270 239 ERLLDFVEQFPHYFIGSNADLPIVGGSILSHDHYQGGRHTFPMAKAPIEEEFTLAGYPDVKAGIVKWPMSVIRLTSKNKD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 312 LVAQVSAQIADSWVAFSDLEIGIVPCDDDGVHSAVSPTCVVTGRGYEMSMIFRSNVTSEEFPDGVFHAHPEFFAIKQESI 391
Cdd:PRK05270 319 ELIDAADKILEAWRGYSDESVDILAYTDGTPHNTITPIARRRGGKYELDLVLRNNRTSEEHPDGIFHPHPEVHHIKKENI 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 392 GLIEAQGLFILPARLQRQLGELADAI-EAGDSLPAELAEFEMVDAEIRGIVgdsrDRDVIDAAIRQELGSVCERILENTA 470
Cdd:PRK05270 399 GLIEVMGLAILPGRLKEELEEVEKYLlGEANEVAAKHQEWAEQLKAKYGIT----TKENVEAIVQEEVGSVFARVLEDAG 474
                        490
                 ....*....|....*....
gi 296932073 471 VFKD----QWRFEKFIEDL 485
Cdd:PRK05270 475 VFKRteegQAAFDRFIESL 493
 
Name Accession Description Interval E-value
PRK05270 PRK05270
UDP-glucose--hexose-1-phosphate uridylyltransferase;
3-485 0e+00

UDP-glucose--hexose-1-phosphate uridylyltransferase;


Pssm-ID: 235382 [Multi-domain]  Cd Length: 493  Bit Score: 652.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073   3 TNVYNAVDELIDYARKNLELDPRNEDFTRNAIFAIFGLNSYAPTGATCDDRVPDAVIARFTQACVDAGLI--GVEGEAAL 80
Cdd:PRK05270   1 MTISQLIEKLIDYAIQNGLIEELDRIYLRNRLLALLGEDSYEEVDEDEDLESPIDLLDQLVDYAVENGLIedTQTERDIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073  81 ADQVMGLLTPRPAEVIDRFDEIRKRdGGTAAMAWFYQYCVANHYVKRAVLDRNPRFDV----GDLTITINLAKPEfRDAK 156
Cdd:PRK05270  81 DAQLMDLLTPRPSEVNRRFWEKYQK-SPEAATDYFYQLSKANNYIKTDAIAKNISWKVptkyGDLEITINLSKPE-KDPK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 157 K-AAAGNSVAGGYPSCTICHENEGFAGRQ----KGTLRTVPITLGGQEWFWQFSPYGYFDQHGIAVNMEHTPMHMDHGTF 231
Cdd:PRK05270 159 AiAAAKKAKASSYPKCLLCMENEGYAGRLnhpaRSNHRIIRLTLGGESWGFQYSPYAYFNEHCIVLSEKHRPMKISRKTF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 232 YRLMDFVDQFPQYFIGCNAALPRIGGSVLGHDHYQGGGEVLPMHKAATRVTYRVPGTDGVAVEIVDWHNTVVRVVGQDRD 311
Cdd:PRK05270 239 ERLLDFVEQFPHYFIGSNADLPIVGGSILSHDHYQGGRHTFPMAKAPIEEEFTLAGYPDVKAGIVKWPMSVIRLTSKNKD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 312 LVAQVSAQIADSWVAFSDLEIGIVPCDDDGVHSAVSPTCVVTGRGYEMSMIFRSNVTSEEFPDGVFHAHPEFFAIKQESI 391
Cdd:PRK05270 319 ELIDAADKILEAWRGYSDESVDILAYTDGTPHNTITPIARRRGGKYELDLVLRNNRTSEEHPDGIFHPHPEVHHIKKENI 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 392 GLIEAQGLFILPARLQRQLGELADAI-EAGDSLPAELAEFEMVDAEIRGIVgdsrDRDVIDAAIRQELGSVCERILENTA 470
Cdd:PRK05270 399 GLIEVMGLAILPGRLKEELEEVEKYLlGEANEVAAKHQEWAEQLKAKYGIT----TKENVEAIVQEEVGSVFARVLEDAG 474
                        490
                 ....*....|....*....
gi 296932073 471 VFKD----QWRFEKFIEDL 485
Cdd:PRK05270 475 VFKRteegQAAFDRFIESL 493
GalT2 COG4468
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
3-485 3.03e-151

Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 443565  Cd Length: 499  Bit Score: 440.79  E-value: 3.03e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073   3 TNVYNAVDELIDYARKNLELDPRNEDFTRNAIFAIFGLNSYAPTGATC-DDRVPDAVIARFTQACVDAGLIG--VEGEAA 79
Cdd:COG4468    1 MMINQAIERLVEYAIKNGLIEEEDRIYARNRLLELLGLDEPEEPEVEEeNEESLPEILDELLDYAVENGLIEdtVTERDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073  80 LADQVMGLLTPRPAEVIDRFDEIRKRDGgTAAMAWFYQYCVANHYVKRAVLDRNPRF----DVGDLTITINLAKPEfRDA 155
Cdd:COG4468   81 FDTKIMGLLTPRPSEVNRKFWELYAESP-KAATDYFYKLSKDSNYIRTDRIAKNIKWktptEYGDLEITINLSKPE-KDP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 156 KK-AAAGNSVAGGYPSCTICHENEGFAG------RQkgTLRTVPITLGGQEWFWQFSPYGYFDQHGIAVNMEHTPMHMDH 228
Cdd:COG4468  159 KAiAAAKNAKQSSYPKCLLCKENEGYAGrlnhpaRQ--NHRIIPLTLNGEDWGFQYSPYVYYNEHCIVLSEEHRPMKIDR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 229 GTFYRLMDFVDQFPQYFIGCNAALPRIGGSVLGHDHYQGGGEVLPMHKAATRVTYRVPGTDGVAVEIVDWHNTVVRVVGQ 308
Cdd:COG4468  237 ATFERLLDFVEQFPHYFIGSNADLPIVGGSILSHDHFQGGRYTFPMEKAPIEEEFTLKGFPDVEAGIVKWPMSVIRLRSE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 309 DRDLVAQVSAQIADSWVAFSDLEIGIVPCDDDGVHSAVSPTCVVTGRGYEMSMIFRSNVTSEEFPDGVFHAHPEFFAIKQ 388
Cdd:COG4468  317 DKERLVEAADKILEAWRGYSDESVDILAYTDGTPHNTITPIARRRGGKYELDLVLRNNRTSEEHPLGIFHPHAEVHHIKK 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 389 ESIGLIEAQGLFILPARLQRQLGELADAIEAGDSLPAE----------LAEFEMVDAEIrgivgdsrDRDVIDAAIRQEL 458
Cdd:COG4468  397 ENIGLIEVMGLAVLPGRLKEELEEVKKYLLGEKKDIEEnevlakhaewAEELKAKYPTL--------TKENVEEILKEEV 468
                        490       500       510
                 ....*....|....*....|....*....|.
gi 296932073 459 GSVCERILENTAVFKD----QWRFEKFIEDL 485
Cdd:COG4468  469 GKVFERVLEDAGVFKRdeegRAAFKRFIESL 499
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
85-183 6.56e-14

Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication with C-terminal domain. Both involved in Zn and Fe binding.


Pssm-ID: 426039 [Multi-domain]  Cd Length: 182  Bit Score: 70.01  E-value: 6.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073   85 MGLLTPRPAEVIDRFDEIRKrdgGT-AAMAWFYQYCVANHYVKRAVLDRNPRFDV----GDLTITINLAKPEF------- 152
Cdd:pfam01087  52 MCYLCPGPSRANGDFNPDYK---SPfVFTNDFYALSKDNPYIKTDAIAKNILFKAetvyGDCEVTCFLSKPELtlplmsp 128
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 296932073  153 RDAKK-AAAGNSV-----AGGYPSCTICHENEGFAGR 183
Cdd:pfam01087 129 KDPKAiAAAWQEKyaelgASSYPKCVLCFENEGYAMG 165
 
Name Accession Description Interval E-value
PRK05270 PRK05270
UDP-glucose--hexose-1-phosphate uridylyltransferase;
3-485 0e+00

UDP-glucose--hexose-1-phosphate uridylyltransferase;


Pssm-ID: 235382 [Multi-domain]  Cd Length: 493  Bit Score: 652.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073   3 TNVYNAVDELIDYARKNLELDPRNEDFTRNAIFAIFGLNSYAPTGATCDDRVPDAVIARFTQACVDAGLI--GVEGEAAL 80
Cdd:PRK05270   1 MTISQLIEKLIDYAIQNGLIEELDRIYLRNRLLALLGEDSYEEVDEDEDLESPIDLLDQLVDYAVENGLIedTQTERDIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073  81 ADQVMGLLTPRPAEVIDRFDEIRKRdGGTAAMAWFYQYCVANHYVKRAVLDRNPRFDV----GDLTITINLAKPEfRDAK 156
Cdd:PRK05270  81 DAQLMDLLTPRPSEVNRRFWEKYQK-SPEAATDYFYQLSKANNYIKTDAIAKNISWKVptkyGDLEITINLSKPE-KDPK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 157 K-AAAGNSVAGGYPSCTICHENEGFAGRQ----KGTLRTVPITLGGQEWFWQFSPYGYFDQHGIAVNMEHTPMHMDHGTF 231
Cdd:PRK05270 159 AiAAAKKAKASSYPKCLLCMENEGYAGRLnhpaRSNHRIIRLTLGGESWGFQYSPYAYFNEHCIVLSEKHRPMKISRKTF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 232 YRLMDFVDQFPQYFIGCNAALPRIGGSVLGHDHYQGGGEVLPMHKAATRVTYRVPGTDGVAVEIVDWHNTVVRVVGQDRD 311
Cdd:PRK05270 239 ERLLDFVEQFPHYFIGSNADLPIVGGSILSHDHYQGGRHTFPMAKAPIEEEFTLAGYPDVKAGIVKWPMSVIRLTSKNKD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 312 LVAQVSAQIADSWVAFSDLEIGIVPCDDDGVHSAVSPTCVVTGRGYEMSMIFRSNVTSEEFPDGVFHAHPEFFAIKQESI 391
Cdd:PRK05270 319 ELIDAADKILEAWRGYSDESVDILAYTDGTPHNTITPIARRRGGKYELDLVLRNNRTSEEHPDGIFHPHPEVHHIKKENI 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 392 GLIEAQGLFILPARLQRQLGELADAI-EAGDSLPAELAEFEMVDAEIRGIVgdsrDRDVIDAAIRQELGSVCERILENTA 470
Cdd:PRK05270 399 GLIEVMGLAILPGRLKEELEEVEKYLlGEANEVAAKHQEWAEQLKAKYGIT----TKENVEAIVQEEVGSVFARVLEDAG 474
                        490
                 ....*....|....*....
gi 296932073 471 VFKD----QWRFEKFIEDL 485
Cdd:PRK05270 475 VFKRteegQAAFDRFIESL 493
GalT2 COG4468
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
3-485 3.03e-151

Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 443565  Cd Length: 499  Bit Score: 440.79  E-value: 3.03e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073   3 TNVYNAVDELIDYARKNLELDPRNEDFTRNAIFAIFGLNSYAPTGATC-DDRVPDAVIARFTQACVDAGLIG--VEGEAA 79
Cdd:COG4468    1 MMINQAIERLVEYAIKNGLIEEEDRIYARNRLLELLGLDEPEEPEVEEeNEESLPEILDELLDYAVENGLIEdtVTERDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073  80 LADQVMGLLTPRPAEVIDRFDEIRKRDGgTAAMAWFYQYCVANHYVKRAVLDRNPRF----DVGDLTITINLAKPEfRDA 155
Cdd:COG4468   81 FDTKIMGLLTPRPSEVNRKFWELYAESP-KAATDYFYKLSKDSNYIRTDRIAKNIKWktptEYGDLEITINLSKPE-KDP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 156 KK-AAAGNSVAGGYPSCTICHENEGFAG------RQkgTLRTVPITLGGQEWFWQFSPYGYFDQHGIAVNMEHTPMHMDH 228
Cdd:COG4468  159 KAiAAAKNAKQSSYPKCLLCKENEGYAGrlnhpaRQ--NHRIIPLTLNGEDWGFQYSPYVYYNEHCIVLSEEHRPMKIDR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 229 GTFYRLMDFVDQFPQYFIGCNAALPRIGGSVLGHDHYQGGGEVLPMHKAATRVTYRVPGTDGVAVEIVDWHNTVVRVVGQ 308
Cdd:COG4468  237 ATFERLLDFVEQFPHYFIGSNADLPIVGGSILSHDHFQGGRYTFPMEKAPIEEEFTLKGFPDVEAGIVKWPMSVIRLRSE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 309 DRDLVAQVSAQIADSWVAFSDLEIGIVPCDDDGVHSAVSPTCVVTGRGYEMSMIFRSNVTSEEFPDGVFHAHPEFFAIKQ 388
Cdd:COG4468  317 DKERLVEAADKILEAWRGYSDESVDILAYTDGTPHNTITPIARRRGGKYELDLVLRNNRTSEEHPLGIFHPHAEVHHIKK 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 389 ESIGLIEAQGLFILPARLQRQLGELADAIEAGDSLPAE----------LAEFEMVDAEIrgivgdsrDRDVIDAAIRQEL 458
Cdd:COG4468  397 ENIGLIEVMGLAVLPGRLKEELEEVKKYLLGEKKDIEEnevlakhaewAEELKAKYPTL--------TKENVEEILKEEV 468
                        490       500       510
                 ....*....|....*....|....*....|.
gi 296932073 459 GSVCERILENTAVFKD----QWRFEKFIEDL 485
Cdd:COG4468  469 GKVFERVLEDAGVFKRdeegRAAFKRFIESL 499
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
85-183 6.56e-14

Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication with C-terminal domain. Both involved in Zn and Fe binding.


Pssm-ID: 426039 [Multi-domain]  Cd Length: 182  Bit Score: 70.01  E-value: 6.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073   85 MGLLTPRPAEVIDRFDEIRKrdgGT-AAMAWFYQYCVANHYVKRAVLDRNPRFDV----GDLTITINLAKPEF------- 152
Cdd:pfam01087  52 MCYLCPGPSRANGDFNPDYK---SPfVFTNDFYALSKDNPYIKTDAIAKNILFKAetvyGDCEVTCFLSKPELtlplmsp 128
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 296932073  153 RDAKK-AAAGNSV-----AGGYPSCTICHENEGFAGR 183
Cdd:pfam01087 129 KDPKAiAAAWQEKyaelgASSYPKCVLCFENEGYAMG 165
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
359-488 8.79e-05

Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport and metabolism, Signal transduction mechanisms]; Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440425 [Multi-domain]  Cd Length: 487  Bit Score: 44.81  E-value: 8.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296932073 359 MSMIFRsnvtseefpDGVFHA--HP-EFFAIKQESIGLIEaqglF----ILPARLQRQLGELADAIEAGDslPAELAE-- 429
Cdd:COG0661  272 LRQVFR---------DGFFHAdpHPgNIFVLPDGRLVLLD----FgmvgRLDPETREGLAELLLALLNRD--YDRVAEal 336
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 296932073 430 FEMvdaeirGIVGDSRDRDVIDAAIRQelgsVCERILENTAvfkDQWRFEKFIEDLGFV 488
Cdd:COG0661  337 LEL------GFVPPDTDVDELERALRA----VLEPYFGKPL---KDISFGELLLELFEL 382
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH