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Conserved domains on  [gi|1261325759|ref|WP_097850558.1|]
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aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
17-364 6.33e-90

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


The actual alignment was detected with superfamily member cd00616:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 352  Bit Score: 274.42  E-value: 6.33e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  17 YLDKLEQIDISHIYTNyGPINQRFEETImSEFFQNRGAVTtVANATLGLMAAIQCKKRKKGKYALMPSFTFPATPLAAIW 96
Cdd:cd00616     1 ELEAVEEVLDSGWLTL-GPKVREFEKAF-AEYLGVKYAVA-VSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  97 CGLEPYFIDISLDDWCMDKTVLLDKIdelNEEVAVVVPYATFGSWMDLKDYEEL-EKKGVPVVVDAAPGFGLMHEGVHYG 175
Cdd:cd00616    78 LGATPVFVDIDPDTYNIDPELIEAAI---TPRTKAIIPVHLYGNPADMDAIMAIaKRHGLPVIEDAAQALGATYKGRKVG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 176 qNFSGMIVYSFHATKPFGIGEGGMIYSHNEEEINQIKRMGNFGFDHNR---ECTMMGFNCKMTEYAAAIGITTINKWNHK 252
Cdd:cd00616   155 -TFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRfkyEHEILGYNYRLSEIQAAIGLAQLEKLDEI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 253 MQERNRISEWYKQLLQSTGLIKKGWQVQKTKAVIHQF-MPILGSEKINNMQIIEKLKKQKIEARSYFSPSCHQQDFFKK- 330
Cdd:cd00616   234 IARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYvIRLDPEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKLl 313
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1261325759 331 -YKSTDLTNTNKIEKRIISLPLWEGMTKEIVEKII 364
Cdd:cd00616   314 gYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVI 348
 
Name Accession Description Interval E-value
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
17-364 6.33e-90

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 274.42  E-value: 6.33e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  17 YLDKLEQIDISHIYTNyGPINQRFEETImSEFFQNRGAVTtVANATLGLMAAIQCKKRKKGKYALMPSFTFPATPLAAIW 96
Cdd:cd00616     1 ELEAVEEVLDSGWLTL-GPKVREFEKAF-AEYLGVKYAVA-VSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  97 CGLEPYFIDISLDDWCMDKTVLLDKIdelNEEVAVVVPYATFGSWMDLKDYEEL-EKKGVPVVVDAAPGFGLMHEGVHYG 175
Cdd:cd00616    78 LGATPVFVDIDPDTYNIDPELIEAAI---TPRTKAIIPVHLYGNPADMDAIMAIaKRHGLPVIEDAAQALGATYKGRKVG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 176 qNFSGMIVYSFHATKPFGIGEGGMIYSHNEEEINQIKRMGNFGFDHNR---ECTMMGFNCKMTEYAAAIGITTINKWNHK 252
Cdd:cd00616   155 -TFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRfkyEHEILGYNYRLSEIQAAIGLAQLEKLDEI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 253 MQERNRISEWYKQLLQSTGLIKKGWQVQKTKAVIHQF-MPILGSEKINNMQIIEKLKKQKIEARSYFSPSCHQQDFFKK- 330
Cdd:cd00616   234 IARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYvIRLDPEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKLl 313
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1261325759 331 -YKSTDLTNTNKIEKRIISLPLWEGMTKEIVEKII 364
Cdd:cd00616   314 gYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVI 348
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
3-364 9.61e-75

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 235.73  E-value: 9.61e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759   3 NIPFLRASIvpANEYLDKLEQIDISHIYTNyGPINQRFEETImSEFFQNRGAVTtVANATLGLMAAIQCKKRKKGKYALM 82
Cdd:COG0399     1 MIPLSRPSI--GEEEIAAVVEVLRSGWLTL-GPEVKEFEEEF-AAYLGVKHAVA-VSSGTAALHLALRALGIGPGDEVIT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  83 PSFTFPATPLAAIWCGLEPYFIDISLDDWCMDktvlLDKIDE-LNEEVAVVVPYATFGSWMDLKDYEEL-EKKGVPVVVD 160
Cdd:COG0399    76 PAFTFVATANAILYVGATPVFVDIDPDTYNID----PEALEAaITPRTKAIIPVHLYGQPADMDAIMAIaKKHGLKVIED 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 161 AAPGFGLMHEGVHYGqNFSGMIVYSFHATKPFGIGEGGMIYSHNEEEINQIKRMGNFGFDHNR--ECTMMGFNCKMTEYA 238
Cdd:COG0399   152 AAQALGATYKGKKVG-TFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAkyEHVELGYNYRMDELQ 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 239 AAIGI---TTINKWNHKmqeRNRISEWYKQLLQSTGLIKKGWQVQKTKAVIHQFmPILGSEKINNMQIIEKLKKQKIEAR 315
Cdd:COG0399   231 AAIGLaqlKRLDEFIAR---RRAIAARYREALADLPGLTLPKVPPGAEHVYHLY-VIRLDEGEDRDELIAALKARGIGTR 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1261325759 316 SYFSPSCHQQDFFKK--YKSTDLTNTNKIEKRIISLPLWEGMTKEIVEKII 364
Cdd:COG0399   307 VHYPIPLHLQPAYRDlgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVI 357
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
15-367 6.40e-69

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 220.62  E-value: 6.40e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  15 NEYLDKLEQIDISHIYTNyGPINQRFEETImSEFFQNRGAVTtVANATLGLMAAIQCKKRKKGKYALMPSFTFPATPLAA 94
Cdd:pfam01041   5 EEELAAVREVLKSGWLTT-GPYVREFERAF-AAYLGVKHAIA-VSSGTAALHLALRALGVGPGDEVITPSFTFVATANAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  95 IWCGLEPYFIDISLDDWCMDktvlLDKIDEL-NEEVAVVVPYATFGSWMDLKDYEELEKK-GVPVVVDAAPGFGLMHEGV 172
Cdd:pfam01041  82 LRLGAKPVFVDIDPDTYNID----PEAIEAAiTPRTKAIIPVHLYGQPADMDAIRAIAARhGLPVIEDAAHALGATYQGK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 173 HYGqNFSGMIVYSFHATKPFGIGEGGMIYSHNEEEINQIKRMGNFGFDHNREC----TMMGFNCKMTEYAAAIGITTINK 248
Cdd:pfam01041 158 KVG-TLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKrywhEVLGYNYRMTEIQAAIGLAQLER 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 249 WNHKMQERNRISEWYKQLLQS-TGLIKKGWQVQKTKAVIHQFMPILGSEKINNMQIIEKLKKQKIEARSYFSPSCHQQDF 327
Cdd:pfam01041 237 LDEFIARRREIAALYQTLLADlPGFTPLTTPPEADVHAWHLFPILVPEEAINRDELVEALKEAGIGTRVHYPIPLHLQPY 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1261325759 328 FKK---YKSTDLTNTNKIEKRIISLPLWEGMTKEIVEKIIMCL 367
Cdd:pfam01041 317 YRDlfgYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
34-364 1.79e-41

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.


Pssm-ID: 274662  Cd Length: 380  Bit Score: 149.40  E-value: 1.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  34 GPINQRFEETImSEFFQNRGAVTtVANATLGLMAAIQCKKRKKGKYALMPSFTFPATPLAAIWCGLEPYFIDISLDDWCM 113
Cdd:TIGR03588  28 GPTVPAFEEAL-AEYVGAKYAVA-FNSATSALHIACLALGVGPGDRVWTTPITFVATANCALYCGAKVDFVDIDPDTGNI 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 114 DKTVLLDKIDELNEE---VAVVVPYAtfGSWMDLKDYEELEKK-GVPVVVDAAPGFGLMHEGVHYG-QNFSGMIVYSFHA 188
Cdd:TIGR03588 106 DEDALEKKLAAAKGKlpkAIVPVDFA--GKSVDMQAIAALAKKhGLKIIEDASHALGAEYGGKPVGnCRYADATVFSFHP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 189 TKPFGIGEGGMIYSHNEEEINQIKRMGNFGFDHNR-------------ECTMMGFNCKMTEYAAAIGITTINKWNHKMQE 255
Cdd:TIGR03588 184 VKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPllfekqdegpwyyEQQELGFNYRMTDIQAALGLSQLKKLDRFVAK 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 256 RNRISEWYKQLLQSTGLIKKGWQVQKTKAVIHQFmPIL--GSEKINNMQIIEKLKKQKIEARSYFSPsCHQQDFFKK-YK 332
Cdd:TIGR03588 264 RREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLY-PILldQEFGCTRKEVFEALRAAGIGVQVHYIP-VHLQPYYRQgFG 341
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1261325759 333 STDLTNTNKIEKRIISLPLWEGMTKEIVEKII 364
Cdd:TIGR03588 342 DGDLPSAENFYLAEISLPLHPALTLEQQQRVV 373
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
4-369 7.83e-23

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 98.56  E-value: 7.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759   4 IPFLRASIvpANEYLDKLEQIDISHIYTNyGPINQRFEETImSEFFQNRGAVTtVANATLGLMAAIQCKKRKKGKYALMP 83
Cdd:PRK11658    5 LPFSRPAM--GDEELAAVKEVLRSGWITT-GPKNQALEQAF-CQLTGNQHAIA-VSSATAGMHITLMALGIGPGDEVITP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  84 SFTFPATPLAAIWCGLEPYFIDISLDDwCMDKTVLLDKIDELNEEVAVVVPYAtfGSWMDLKDYEEL-EKKGVPVVVDAA 162
Cdd:PRK11658   80 SLTWVSTLNMIVLLGATPVMVDVDRDT-LMVTPEAIEAAITPRTKAIIPVHYA--GAPADLDAIRAIgERYGIPVIEDAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 163 PGFGLMHEGVHYGQnfSGMIVYSFHATKPFGIGEGGMIYSHNEEEINQIKRMGNFG-----FD---HNR----ECTMMGF 230
Cdd:PRK11658  157 HAVGTYYKGRHIGA--RGTAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGlgvdaFDrqtQGRapqaEVLTPGY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 231 NCKMTEYAAAIGITTINKWNHKMQERNRISEWYKQLLQSTG---LIKKGWQVQKTKaviHQFMPILGSEK--INNMQIIE 305
Cdd:PRK11658  235 KYNLADINAAIALVQLAKLEALNARRREIAARYLQALADLPfqpLSLPAWPHQHAW---HLFIIRVDEERcgISRDALME 311
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261325759 306 KLKKQKIEARSYFSpSCHQQDFFK-KYKSTDLTNTNKIEKRIISLPLWEGMTKEIVEKIIMCLMQ 369
Cdd:PRK11658  312 ALKERGIGTGLHFR-AAHTQKYYReRFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQ 375
 
Name Accession Description Interval E-value
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
17-364 6.33e-90

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 274.42  E-value: 6.33e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  17 YLDKLEQIDISHIYTNyGPINQRFEETImSEFFQNRGAVTtVANATLGLMAAIQCKKRKKGKYALMPSFTFPATPLAAIW 96
Cdd:cd00616     1 ELEAVEEVLDSGWLTL-GPKVREFEKAF-AEYLGVKYAVA-VSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  97 CGLEPYFIDISLDDWCMDKTVLLDKIdelNEEVAVVVPYATFGSWMDLKDYEEL-EKKGVPVVVDAAPGFGLMHEGVHYG 175
Cdd:cd00616    78 LGATPVFVDIDPDTYNIDPELIEAAI---TPRTKAIIPVHLYGNPADMDAIMAIaKRHGLPVIEDAAQALGATYKGRKVG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 176 qNFSGMIVYSFHATKPFGIGEGGMIYSHNEEEINQIKRMGNFGFDHNR---ECTMMGFNCKMTEYAAAIGITTINKWNHK 252
Cdd:cd00616   155 -TFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRfkyEHEILGYNYRLSEIQAAIGLAQLEKLDEI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 253 MQERNRISEWYKQLLQSTGLIKKGWQVQKTKAVIHQF-MPILGSEKINNMQIIEKLKKQKIEARSYFSPSCHQQDFFKK- 330
Cdd:cd00616   234 IARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYvIRLDPEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKLl 313
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1261325759 331 -YKSTDLTNTNKIEKRIISLPLWEGMTKEIVEKII 364
Cdd:cd00616   314 gYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVI 348
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
3-364 9.61e-75

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 235.73  E-value: 9.61e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759   3 NIPFLRASIvpANEYLDKLEQIDISHIYTNyGPINQRFEETImSEFFQNRGAVTtVANATLGLMAAIQCKKRKKGKYALM 82
Cdd:COG0399     1 MIPLSRPSI--GEEEIAAVVEVLRSGWLTL-GPEVKEFEEEF-AAYLGVKHAVA-VSSGTAALHLALRALGIGPGDEVIT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  83 PSFTFPATPLAAIWCGLEPYFIDISLDDWCMDktvlLDKIDE-LNEEVAVVVPYATFGSWMDLKDYEEL-EKKGVPVVVD 160
Cdd:COG0399    76 PAFTFVATANAILYVGATPVFVDIDPDTYNID----PEALEAaITPRTKAIIPVHLYGQPADMDAIMAIaKKHGLKVIED 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 161 AAPGFGLMHEGVHYGqNFSGMIVYSFHATKPFGIGEGGMIYSHNEEEINQIKRMGNFGFDHNR--ECTMMGFNCKMTEYA 238
Cdd:COG0399   152 AAQALGATYKGKKVG-TFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAkyEHVELGYNYRMDELQ 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 239 AAIGI---TTINKWNHKmqeRNRISEWYKQLLQSTGLIKKGWQVQKTKAVIHQFmPILGSEKINNMQIIEKLKKQKIEAR 315
Cdd:COG0399   231 AAIGLaqlKRLDEFIAR---RRAIAARYREALADLPGLTLPKVPPGAEHVYHLY-VIRLDEGEDRDELIAALKARGIGTR 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1261325759 316 SYFSPSCHQQDFFKK--YKSTDLTNTNKIEKRIISLPLWEGMTKEIVEKII 364
Cdd:COG0399   307 VHYPIPLHLQPAYRDlgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVI 357
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
15-367 6.40e-69

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 220.62  E-value: 6.40e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  15 NEYLDKLEQIDISHIYTNyGPINQRFEETImSEFFQNRGAVTtVANATLGLMAAIQCKKRKKGKYALMPSFTFPATPLAA 94
Cdd:pfam01041   5 EEELAAVREVLKSGWLTT-GPYVREFERAF-AAYLGVKHAIA-VSSGTAALHLALRALGVGPGDEVITPSFTFVATANAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  95 IWCGLEPYFIDISLDDWCMDktvlLDKIDEL-NEEVAVVVPYATFGSWMDLKDYEELEKK-GVPVVVDAAPGFGLMHEGV 172
Cdd:pfam01041  82 LRLGAKPVFVDIDPDTYNID----PEAIEAAiTPRTKAIIPVHLYGQPADMDAIRAIAARhGLPVIEDAAHALGATYQGK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 173 HYGqNFSGMIVYSFHATKPFGIGEGGMIYSHNEEEINQIKRMGNFGFDHNREC----TMMGFNCKMTEYAAAIGITTINK 248
Cdd:pfam01041 158 KVG-TLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKrywhEVLGYNYRMTEIQAAIGLAQLER 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 249 WNHKMQERNRISEWYKQLLQS-TGLIKKGWQVQKTKAVIHQFMPILGSEKINNMQIIEKLKKQKIEARSYFSPSCHQQDF 327
Cdd:pfam01041 237 LDEFIARRREIAALYQTLLADlPGFTPLTTPPEADVHAWHLFPILVPEEAINRDELVEALKEAGIGTRVHYPIPLHLQPY 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1261325759 328 FKK---YKSTDLTNTNKIEKRIISLPLWEGMTKEIVEKIIMCL 367
Cdd:pfam01041 317 YRDlfgYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
34-364 1.79e-41

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.


Pssm-ID: 274662  Cd Length: 380  Bit Score: 149.40  E-value: 1.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  34 GPINQRFEETImSEFFQNRGAVTtVANATLGLMAAIQCKKRKKGKYALMPSFTFPATPLAAIWCGLEPYFIDISLDDWCM 113
Cdd:TIGR03588  28 GPTVPAFEEAL-AEYVGAKYAVA-FNSATSALHIACLALGVGPGDRVWTTPITFVATANCALYCGAKVDFVDIDPDTGNI 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 114 DKTVLLDKIDELNEE---VAVVVPYAtfGSWMDLKDYEELEKK-GVPVVVDAAPGFGLMHEGVHYG-QNFSGMIVYSFHA 188
Cdd:TIGR03588 106 DEDALEKKLAAAKGKlpkAIVPVDFA--GKSVDMQAIAALAKKhGLKIIEDASHALGAEYGGKPVGnCRYADATVFSFHP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 189 TKPFGIGEGGMIYSHNEEEINQIKRMGNFGFDHNR-------------ECTMMGFNCKMTEYAAAIGITTINKWNHKMQE 255
Cdd:TIGR03588 184 VKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPllfekqdegpwyyEQQELGFNYRMTDIQAALGLSQLKKLDRFVAK 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 256 RNRISEWYKQLLQSTGLIKKGWQVQKTKAVIHQFmPIL--GSEKINNMQIIEKLKKQKIEARSYFSPsCHQQDFFKK-YK 332
Cdd:TIGR03588 264 RREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLY-PILldQEFGCTRKEVFEALRAAGIGVQVHYIP-VHLQPYYRQgFG 341
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1261325759 333 STDLTNTNKIEKRIISLPLWEGMTKEIVEKII 364
Cdd:TIGR03588 342 DGDLPSAENFYLAEISLPLHPALTLEQQQRVV 373
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
4-369 7.83e-23

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 98.56  E-value: 7.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759   4 IPFLRASIvpANEYLDKLEQIDISHIYTNyGPINQRFEETImSEFFQNRGAVTtVANATLGLMAAIQCKKRKKGKYALMP 83
Cdd:PRK11658    5 LPFSRPAM--GDEELAAVKEVLRSGWITT-GPKNQALEQAF-CQLTGNQHAIA-VSSATAGMHITLMALGIGPGDEVITP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  84 SFTFPATPLAAIWCGLEPYFIDISLDDwCMDKTVLLDKIDELNEEVAVVVPYAtfGSWMDLKDYEEL-EKKGVPVVVDAA 162
Cdd:PRK11658   80 SLTWVSTLNMIVLLGATPVMVDVDRDT-LMVTPEAIEAAITPRTKAIIPVHYA--GAPADLDAIRAIgERYGIPVIEDAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 163 PGFGLMHEGVHYGQnfSGMIVYSFHATKPFGIGEGGMIYSHNEEEINQIKRMGNFG-----FD---HNR----ECTMMGF 230
Cdd:PRK11658  157 HAVGTYYKGRHIGA--RGTAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGlgvdaFDrqtQGRapqaEVLTPGY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 231 NCKMTEYAAAIGITTINKWNHKMQERNRISEWYKQLLQSTG---LIKKGWQVQKTKaviHQFMPILGSEK--INNMQIIE 305
Cdd:PRK11658  235 KYNLADINAAIALVQLAKLEALNARRREIAARYLQALADLPfqpLSLPAWPHQHAW---HLFIIRVDEERcgISRDALME 311
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261325759 306 KLKKQKIEARSYFSpSCHQQDFFK-KYKSTDLTNTNKIEKRIISLPLWEGMTKEIVEKIIMCLMQ 369
Cdd:PRK11658  312 ALKERGIGTGLHFR-AAHTQKYYReRFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQ 375
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
4-364 2.06e-12

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 67.55  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759   4 IPFLRASIVpANEyLDKLEQ-IDISHIYTNyGPINQRFEETIMSEFFQNRGAVTTVANATLGlMAAIQCKKrKKGKYALM 82
Cdd:PRK11706    2 IPFNKPPVV-GTE-LDYIQQaMSSGKLCGD-GGFTRRCQQWLEQRFGSAKVLLTPSCTAALE-MAALLLDI-QPGDEVIM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  83 PSFTFPATPLAAIWCGLEPYFIDISLDDWCMDKTVLLDKIDElNEEVAVVVPYATFGSWMDlkDYEELEKK-GVPVVVDA 161
Cdd:PRK11706   77 PSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITP-KTRAIVPVHYAGVACEMD--TIMALAKKhNLFVVEDA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 162 APGFGLMHEGV------HYGqnfsgmiVYSFHATKPFGIGEGGMIYSHNEEEINQ---IKRMGNfgfdhNRECTMMGFNC 232
Cdd:PRK11706  154 AQGVMSTYKGRalgtigHIG-------CFSFHETKNYTAGEGGALLINDPALIERaeiIREKGT-----NRSQFFRGQVD 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 233 K-----------MTEYAAAI------GITTINkwnhkmQERNRISEWYKQLLQStgLIKKGwqvQKTKAVI--------H 287
Cdd:PRK11706  222 KytwvdigssylPSELQAAYlwaqleAADRIN------QRRLALWQRYYDALAP--LAEAG---RIELPSIpddckhnaH 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261325759 288 QFMPILGSEKINNmQIIEKLKKQKIEARSYFSPsCHQQDFFKKY--KSTDLTNTNKIEKRIISLPLWEGMTKEIVEKII 364
Cdd:PRK11706  291 MFYIKLRDLEDRS-ALINFLKEAGIMAVFHYIP-LHSSPAGERFgrFHGEDRYTTKESERLLRLPLFYNLTDVEQRTVI 367
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
14-311 9.91e-09

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 56.16  E-value: 9.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  14 ANEYLD--------KLEQIDISHIYTNYGPI--NQRFEETIMsEFFQNRGAVTTVANATL--------GLMAAIQCKKrK 75
Cdd:pfam00155   8 SNEYLGdtlpavakAEKDALAGGTRNLYGPTdgHPELREALA-KFLGRSPVLKLDREAAVvfgsgagaNIEALIFLLA-N 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  76 KGKYALMPSFTFPATPLAAIWCGLEPYFIDI-SLDDWCMDKTVLLDKIDELNEEVAVVVPYATFGSWMDLKDYEEL---- 150
Cdd:pfam00155  86 PGDAILVPAPTYASYIRIARLAGGEVVRYPLyDSNDFHLDFDALEAALKEKPKVVLHTSPHNPTGTVATLEELEKLldla 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 151 EKKGVPVVVDAAPGfGLMHEGVHYGQNFSGM-------IVYSFhaTKPFGI-GE-GGMIYShNEEEINQIKRMGNFGFdh 221
Cdd:pfam00155 166 KEHNILLLVDEAYA-GFVFGSPDAVATRALLaegpnllVVGSF--SKAFGLaGWrVGYILG-NAAVISQLRKLARPFY-- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 222 nrectmmgFNCKMTEYAAAIGITTINKWNHKMQERNRISEWYKQLLQstGLIKKGWQVQKTKAvihQFMPILGSEKINNM 301
Cdd:pfam00155 240 --------SSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRD--GLQAAGLSVLPSQA---GFFLLTGLDPETAK 306
                         330
                  ....*....|
gi 1261325759 302 QIIEKLKKQK 311
Cdd:pfam00155 307 ELAQVLLEEV 316
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
13-258 5.23e-06

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 47.72  E-value: 5.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  13 PANEYLDKLEQIDISHIYTNYGPI--NQRFEETImSEFFQNRGAVTTVAN-------ATLGLMAAIQCKKRKkGKYALMP 83
Cdd:cd00609    12 PPPEVLEALAAAALRAGLLGYYPDpgLPELREAI-AEWLGRRGGVDVPPEeivvtngAQEALSLLLRALLNP-GDEVLVP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  84 SFTFPATPLAAIWCGLEPYFIDISLDDWCMDKTVLLDKIdeLNEEVAVVV------PyaTfGSWMDLKDYEEL----EKK 153
Cdd:cd00609    90 DPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLEAA--KTPKTKLLYlnnpnnP--T-GAVLSEEELEELaelaKKH 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759 154 GVPVVVDAAPGfGLMHEGVHY------GQNFSGMIVYSFhaTKPFGI-GE-GGMIYSHNEEEINQIKRMGNFGFDHnrec 225
Cdd:cd00609   165 GILIISDEAYA-ELVYDGEPPpalallDAYERVIVLRSF--SKTFGLpGLrIGYLIAPPEELLERLKKLLPYTTSG---- 237
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1261325759 226 tmmgfNCKMTEYAAAIGITTINKWNHKMQERNR 258
Cdd:cd00609   238 -----PSTLSQAAAAAALDDGEEHLEELRERYR 265
GDC-P pfam02347
Glycine cleavage system P-protein; This family consists of Glycine cleavage system P-proteins ...
30-198 4.93e-05

Glycine cleavage system P-protein; This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalyzed by this protein is:- Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2


Pssm-ID: 396772 [Multi-domain]  Cd Length: 428  Bit Score: 45.06  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  30 YTNYGP-INQRFEETIMSefFQNRGAVTT---VANATL---------GLMAAIQCKKRKKGKYaLMPSFTFPATpLAAIW 96
Cdd:pfam02347  97 YTPYQPeISQGRLEALLN--FQTMICDLTgldIANASLldegtaaaeAMALAARASKKKGKKF-VVDKDVHPQT-LEVLK 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261325759  97 CGLEPYFIDISLDDWCMDKTVLLDKIdelneeVAVVVPY-ATFGSWMDLKDYEELEKK-GVPVVVDAAP-GFGLMHEGVH 173
Cdd:pfam02347 173 TRAKPFGIEIVEVDYTEEGVTDLKDV------FGVLVQYpNTDGRIEDYKELIELAHQrKSLVVVAADLlALTLLKPPGE 246
                         170       180
                  ....*....|....*....|....*..
gi 1261325759 174 YGQNfsgmIVysFHATKPFGI--GEGG 198
Cdd:pfam02347 247 FGAD----IA--VGSAQRFGVplGYGG 267
 
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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