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Conserved domains on  [gi|612883078|gb|EZU95119|]
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hypothetical protein V148_01577 [Staphylococcus aureus 11P8]

Protein Classification

C45 family peptidase( domain architecture ID 10506331)

C45 family peptidase similar to Aspergillus nidulans acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase which converts isopenicillin N to penicillin G, and Drosophila pigment protein tan which converts N-beta-alanyl dopamine to dopamine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AAT pfam03417
Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;
80-289 8.08e-87

Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;


:

Pssm-ID: 397472  Cd Length: 223  Bit Score: 259.96  E-value: 8.08e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078   80 GKDFMVRNYDYHPATYDGRYLLYQPTDSGLAQIGPVSRVTGRMDGMNESGLTMGYNFMHRKKP-ANGFVCYMIGRLILEN 158
Cdd:pfam03417   5 NGRLLGRNEDYDPETYSHRYLLTAPEDPGFATIGYAGRLPGRTDGINEKGLAMGINFVHLRKLrGDGFPRHFITRLLLET 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078  159 CRNVKEAIQLLKEIPHRSSFSYILMDKSLNHAIVEVTPRS--IDVRYDN---ICTNHF--EILTHENRNYTKESKERLAR 231
Cdd:pfam03417  85 CSSVEEAVKLLKEIPRASSFNFILLDAAGNLAVVEVEPGSkdISVREANeylAHTNHFvhESLTAENQNITDSSISRLER 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 612883078  232 TISQTNDNLDMTTAFKLFNNPQYEIYSKL-FKSWSGTIHTSMYHPETLTAYFTLGENAP 289
Cdd:pfam03417 165 IQFLLSQKESPKDAFELLNDREDGPYSKLrYKSWEGTLHTALYDPADRKATLCLGNPRN 223
 
Name Accession Description Interval E-value
AAT pfam03417
Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;
80-289 8.08e-87

Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;


Pssm-ID: 397472  Cd Length: 223  Bit Score: 259.96  E-value: 8.08e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078   80 GKDFMVRNYDYHPATYDGRYLLYQPTDSGLAQIGPVSRVTGRMDGMNESGLTMGYNFMHRKKP-ANGFVCYMIGRLILEN 158
Cdd:pfam03417   5 NGRLLGRNEDYDPETYSHRYLLTAPEDPGFATIGYAGRLPGRTDGINEKGLAMGINFVHLRKLrGDGFPRHFITRLLLET 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078  159 CRNVKEAIQLLKEIPHRSSFSYILMDKSLNHAIVEVTPRS--IDVRYDN---ICTNHF--EILTHENRNYTKESKERLAR 231
Cdd:pfam03417  85 CSSVEEAVKLLKEIPRASSFNFILLDAAGNLAVVEVEPGSkdISVREANeylAHTNHFvhESLTAENQNITDSSISRLER 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 612883078  232 TISQTNDNLDMTTAFKLFNNPQYEIYSKL-FKSWSGTIHTSMYHPETLTAYFTLGENAP 289
Cdd:pfam03417 165 IQFLLSQKESPKDAFELLNDREDGPYSKLrYKSWEGTLHTALYDPADRKATLCLGNPRN 223
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
10-280 8.32e-85

C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.


Pssm-ID: 468523 [Multi-domain]  Cd Length: 312  Bit Score: 257.99  E-value: 8.32e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078  10 NREKEWKKRVPRFDID-VNETYQIFQTYAPQIWEELMGLQSILKMPTRQII-LNFGHYRFtdLKESGCTVFQ-----GKD 82
Cdd:NF040521  25 ALLRAWGLVSWRELRDfAKEFLAALEAFAPELWEELEGIADGLGLPFEDVLaLNARTEIL--AAPDGCSTFAvlgedGEP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078  83 FMVRNYDYHPATYDGRYLLYQPTDSGL--AQIGPVSRVTGRMDGMNESGLTMGYNFM-HRKKPANGFVCYMIGRLILENC 159
Cdd:NF040521 103 ILARNYDWHPELYDGCLLLTIRPDGGPryASIGYAGLLPGRTDGMNEAGLAVTLNFLdGRKLPGVGVPVHLLARAILENC 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078 160 RNVKEAIQLLKEIPHRSSFSYILMDKSLNHAIVEVTPRSIDVRYDN----ICTNHFEI--LTHENRNYTKESKERLARTI 233
Cdd:NF040521 183 KTVDEAIALLKEIPRASSFNLTLADASGRAASVEASPDRVVVVRPEdgllVHTNHFLSpeLEEENRIATPSSRERYERLE 262
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 612883078 234 SQTNDNLDMTTAFKLFNNP-QYEIYSKLFKSW--SGTIHTSMYHPETLTA 280
Cdd:NF040521 263 ELLKGKLDAEDAKALLSDGyPLPICRHPYPDGdrFGTLATVVFDPAAGTL 312
COG4927 COG4927
Predicted choloylglycine hydrolase [General function prediction only];
24-220 4.21e-84

Predicted choloylglycine hydrolase [General function prediction only];


Pssm-ID: 443955 [Multi-domain]  Cd Length: 242  Bit Score: 253.72  E-value: 4.21e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078  24 IDVNETYQIFQTYAPQIWEELMGLQSILKMPTRQIILNFGHYRFTDlkeSGCTVF----QGKDFMVRNYDYHPATYDGRY 99
Cdd:COG4927   40 PFLAEARAALRRYMPELWEELEGLADGLDVPLEELLLLNGGYYLPL---SGCSQFavapEGEPLLARNYDFHPDLYEGRL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078 100 LLYQPTDSGLAQIGPVSRVTGRMDGMNESGLTMGYNFMHRKKPANGFVCYMIGRLILENCRNVKEAIQLLKEIPHRSSFS 179
Cdd:COG4927  117 LLTVQPDGGYAFIGVTDGLIGRLDGMNEKGLAVGLNFVGRKVAGPGFPIPLLIRYILETCSTVDEAIALLKEIPHASSYN 196
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 612883078 180 YILMDKSLNHAIVEVTPRSIDVRYDN---ICTNHFEILT--HENRN 220
Cdd:COG4927  197 LTLADASGNAAVVEVSPRGVEVREPNgflVCTNHFQSLEmaEENRN 242
Ntn_CGH_like cd01935
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins ...
75-273 1.45e-32

Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins includes conjugated bile acid hydrolase (CBAH), penicillin V acylase (PVA), acid ceramidase (AC), and N-acylethanolamine-hydrolyzing acid amidase (NAAA) which cleave non-peptide carbon-nitrogen bonds in bile salt constituents. These enzymes have an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which they belong. This nucleophilic cysteine is exposed by post-translational prossessing of the precursor protein.


Pssm-ID: 238910  Cd Length: 229  Bit Score: 120.54  E-value: 1.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078  75 CT--VFQGKD---FMVRNYDYHPAT------------YDGRYLLYQPTDSGLAQIGPVSRVTGRMDGMNESGLTMGYNFM 137
Cdd:cd01935    1 CTsiVAQTKDggvYLGRNMDFSFDYelrllvfprgyqRNGQTGDKSKWYAKYGSGGTSAGYIGLVDGMNEKGLSVSLLYF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078 138 HR--------KKPANGFVCYMIGRLILENCRNVKEAIQLLKEIPH----------RSSFSYILMDKSLNHAIVEVTPRSI 199
Cdd:cd01935   81 PGyayypagiKEGKDGLPAFELIRWVLENCDSVEEVKEALKKIPIvdfpiplggpAAPLHYILSDKSGDSAVIEPIDGGL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612883078 200 DVRYD---NICTNHFEILTHENRnytkeskerlaRTISqtndnldmtTAFKLFNNPQYEIYSKLFKSWSGTIHTSMY 273
Cdd:cd01935  161 KIYDNpwfGVMTNHPTFDWHLPR-----------RFVR---------VAYLKNTAQKNKETVEDVKNLFHILESVPI 217
 
Name Accession Description Interval E-value
AAT pfam03417
Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;
80-289 8.08e-87

Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;


Pssm-ID: 397472  Cd Length: 223  Bit Score: 259.96  E-value: 8.08e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078   80 GKDFMVRNYDYHPATYDGRYLLYQPTDSGLAQIGPVSRVTGRMDGMNESGLTMGYNFMHRKKP-ANGFVCYMIGRLILEN 158
Cdd:pfam03417   5 NGRLLGRNEDYDPETYSHRYLLTAPEDPGFATIGYAGRLPGRTDGINEKGLAMGINFVHLRKLrGDGFPRHFITRLLLET 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078  159 CRNVKEAIQLLKEIPHRSSFSYILMDKSLNHAIVEVTPRS--IDVRYDN---ICTNHF--EILTHENRNYTKESKERLAR 231
Cdd:pfam03417  85 CSSVEEAVKLLKEIPRASSFNFILLDAAGNLAVVEVEPGSkdISVREANeylAHTNHFvhESLTAENQNITDSSISRLER 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 612883078  232 TISQTNDNLDMTTAFKLFNNPQYEIYSKL-FKSWSGTIHTSMYHPETLTAYFTLGENAP 289
Cdd:pfam03417 165 IQFLLSQKESPKDAFELLNDREDGPYSKLrYKSWEGTLHTALYDPADRKATLCLGNPRN 223
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
10-280 8.32e-85

C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.


Pssm-ID: 468523 [Multi-domain]  Cd Length: 312  Bit Score: 257.99  E-value: 8.32e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078  10 NREKEWKKRVPRFDID-VNETYQIFQTYAPQIWEELMGLQSILKMPTRQII-LNFGHYRFtdLKESGCTVFQ-----GKD 82
Cdd:NF040521  25 ALLRAWGLVSWRELRDfAKEFLAALEAFAPELWEELEGIADGLGLPFEDVLaLNARTEIL--AAPDGCSTFAvlgedGEP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078  83 FMVRNYDYHPATYDGRYLLYQPTDSGL--AQIGPVSRVTGRMDGMNESGLTMGYNFM-HRKKPANGFVCYMIGRLILENC 159
Cdd:NF040521 103 ILARNYDWHPELYDGCLLLTIRPDGGPryASIGYAGLLPGRTDGMNEAGLAVTLNFLdGRKLPGVGVPVHLLARAILENC 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078 160 RNVKEAIQLLKEIPHRSSFSYILMDKSLNHAIVEVTPRSIDVRYDN----ICTNHFEI--LTHENRNYTKESKERLARTI 233
Cdd:NF040521 183 KTVDEAIALLKEIPRASSFNLTLADASGRAASVEASPDRVVVVRPEdgllVHTNHFLSpeLEEENRIATPSSRERYERLE 262
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 612883078 234 SQTNDNLDMTTAFKLFNNP-QYEIYSKLFKSW--SGTIHTSMYHPETLTA 280
Cdd:NF040521 263 ELLKGKLDAEDAKALLSDGyPLPICRHPYPDGdrFGTLATVVFDPAAGTL 312
COG4927 COG4927
Predicted choloylglycine hydrolase [General function prediction only];
24-220 4.21e-84

Predicted choloylglycine hydrolase [General function prediction only];


Pssm-ID: 443955 [Multi-domain]  Cd Length: 242  Bit Score: 253.72  E-value: 4.21e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078  24 IDVNETYQIFQTYAPQIWEELMGLQSILKMPTRQIILNFGHYRFTDlkeSGCTVF----QGKDFMVRNYDYHPATYDGRY 99
Cdd:COG4927   40 PFLAEARAALRRYMPELWEELEGLADGLDVPLEELLLLNGGYYLPL---SGCSQFavapEGEPLLARNYDFHPDLYEGRL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078 100 LLYQPTDSGLAQIGPVSRVTGRMDGMNESGLTMGYNFMHRKKPANGFVCYMIGRLILENCRNVKEAIQLLKEIPHRSSFS 179
Cdd:COG4927  117 LLTVQPDGGYAFIGVTDGLIGRLDGMNEKGLAVGLNFVGRKVAGPGFPIPLLIRYILETCSTVDEAIALLKEIPHASSYN 196
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 612883078 180 YILMDKSLNHAIVEVTPRSIDVRYDN---ICTNHFEILT--HENRN 220
Cdd:COG4927  197 LTLADASGNAAVVEVSPRGVEVREPNgflVCTNHFQSLEmaEENRN 242
Ntn_CGH_like cd01935
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins ...
75-273 1.45e-32

Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins includes conjugated bile acid hydrolase (CBAH), penicillin V acylase (PVA), acid ceramidase (AC), and N-acylethanolamine-hydrolyzing acid amidase (NAAA) which cleave non-peptide carbon-nitrogen bonds in bile salt constituents. These enzymes have an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which they belong. This nucleophilic cysteine is exposed by post-translational prossessing of the precursor protein.


Pssm-ID: 238910  Cd Length: 229  Bit Score: 120.54  E-value: 1.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078  75 CT--VFQGKD---FMVRNYDYHPAT------------YDGRYLLYQPTDSGLAQIGPVSRVTGRMDGMNESGLTMGYNFM 137
Cdd:cd01935    1 CTsiVAQTKDggvYLGRNMDFSFDYelrllvfprgyqRNGQTGDKSKWYAKYGSGGTSAGYIGLVDGMNEKGLSVSLLYF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078 138 HR--------KKPANGFVCYMIGRLILENCRNVKEAIQLLKEIPH----------RSSFSYILMDKSLNHAIVEVTPRSI 199
Cdd:cd01935   81 PGyayypagiKEGKDGLPAFELIRWVLENCDSVEEVKEALKKIPIvdfpiplggpAAPLHYILSDKSGDSAVIEPIDGGL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612883078 200 DVRYD---NICTNHFEILTHENRnytkeskerlaRTISqtndnldmtTAFKLFNNPQYEIYSKLFKSWSGTIHTSMY 273
Cdd:cd01935  161 KIYDNpwfGVMTNHPTFDWHLPR-----------RFVR---------VAYLKNTAQKNKETVEDVKNLFHILESVPI 217
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
123-205 8.85e-05

Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) EC:3.5.1.24, penicillin acylase EC:3.5.1.11 and acid ceramidase EC:3.5.1.23. This domain forms the alpha-subunit for members from vertebral species, see family NAAA-beta, pfam15508.


Pssm-ID: 396726  Cd Length: 316  Bit Score: 43.66  E-value: 8.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078  123 DGMNESGLTM-GYNFMH-------RKKPANGFVCYMIGRLILENCRNVKEAIQLLKEI----------PHRSSFSYILMD 184
Cdd:pfam02275  68 DGLNEKGLGIaGLYFPGyafyskgPKKDKVNIQPGELILWVLGNFTSVEEVKELLTKLnivnealdilGGKAPLHWIISD 147
                          90       100
                  ....*....|....*....|.
gi 612883078  185 KSLNHAIVEVTPRSIDVrYDN 205
Cdd:pfam02275 148 ASGESIVIEPRKEGLKV-YDN 167
Ntn_PVA cd00542
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
123-222 1.38e-04

Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), catalyzes the hydrolysis of penicillin V to yield 6-amino penicillanic acid (6-APA), an important key intermediate of semisynthetic penicillins. PVA has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which PVA belongs. This nucleophilic cysteine is exposed by post-translational prossessing of the PVA precursor. PVA forms a homotetramer.


Pssm-ID: 238303  Cd Length: 303  Bit Score: 42.97  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078 123 DGMNESGLTM-GYNFMH----RKKPANGFV---CYMIGRLILENCRNVKEAIQLLKEI----------PHRSSFSYILMD 184
Cdd:cd00542   68 DGVNEKGLAIaGLYFPGyasySKETKEGKTniaPFEFITWVLGNFASVEEVKEALKNInvvddpinllGPVPPLHWIISD 147
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 612883078 185 KSLNHAIVEVTPRSIDVrYDN---ICTNHFEILTHEN--RNYT 222
Cdd:cd00542  148 KSGRSIVVEPTKGGLKV-YDNpvgVLTNSPDFDWHLTnlRNYI 189
Ntn_CGH cd01902
Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide ...
120-193 2.20e-03

Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide carbon-nitrogen bonds in choloylglycine and choloyltaurine, both of which are present in bile. CGH is present in a number of probiotic microbial organisms that inhabit the gut. CGH has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which CGH belongs.


Pssm-ID: 238885  Cd Length: 291  Bit Score: 39.24  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612883078 120 GRMDGMNESGLTMG---YNFMH-----RKKPANGFVCYmiGRLILENCRNVKEAIQLLKEIP-----------HRSSFSY 180
Cdd:cd01902   65 GTVDGMNEKGLVANllyLTESDygpadPNKPTLSAGAW--GQYLLDNYATVEEAVKALAKEPfvivasvpgdgREATLHL 142
                         90
                 ....*....|...
gi 612883078 181 ILMDKSLNHAIVE 193
Cdd:cd01902  143 SISDATGDSAIIE 155
 
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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