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Conserved domains on  [gi|624389464|gb|KBT48301|]
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allophanate hydrolase [Mycobacterium tuberculosis 2233BH]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CT_A_B super family cl00865
Carboxyltransferase domain, subdomain A and B; Urea carboxylase (UC) catalyzes a two-step, ...
3-300 2.45e-159

Carboxyltransferase domain, subdomain A and B; Urea carboxylase (UC) catalyzes a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the A and B subdomains of the CT domain. This domain covers the whole length of KipA (kinase A) from Bacillus subtilis. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity.


The actual alignment was detected with superfamily member TIGR00724:

Pssm-ID: 469961  Cd Length: 314  Bit Score: 446.54  E-value: 2.45e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464    3 TLEILRSGPLALVEDLGRAGLAHLGVGRSGAADRRSHTLANRLVANPDDWATVEVTFGGFSARVRGgDVDIAVTGADTDP 82
Cdd:TIGR00724   1 MIEILRAGSHTLIQDLGRVGYRRIGVPHSGAMDAYSLRLANRLVGNPDDTPAIEVTLGGPTIRFHC-DVIFAVTGADTDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464   83 TVNGIMVGT-NSIHHVRDGQVISLGTPRAGLRTYLAVRGGVCVEPVLGSRSYDVMSAIGP---SPLRAGDVLPVGEHTDD 158
Cdd:TIGR00724  80 CLNDGQVIPqWRPYEVKRGQILSLGRLKSGMRGYLAVRGGIDVPPVLGSCSTDLRANIGGyegRPLKAGDVLPLGSNELD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464  159 YPELDQAPVAaIEEHLVELRVVPGPRDDWLVDP--DALVHTIWMASNRSDRVGMRLQGRPLQHRWPDRQLPGEGVTRGAI 236
Cdd:TIGR00724 160 LNEPQGLIPQ-IPEWRIEIRVLPGPEYDFFKREsiEAFWRSEWKVSSNSDRMGYRLQGPKLKHARPNRELLTHGIVYGSI 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 624389464  237 QVPPNGLPVILGPDHPITGSYPVVGVITDEDIDKVAQIRPGQYVRLHWARPRSRLPGQGVTQAW 300
Cdd:TIGR00724 239 QVPPNGQPIILMADAQTTGGYPKIAVVIEADLWKVAQVRPGQSIKFVPLSLEEALKLRESQERY 302
 
Name Accession Description Interval E-value
urea_amlyse_rel TIGR00724
biotin-dependent carboxylase uncharacterized domain; Urea amidolyase of Saccharomyces ...
3-300 2.45e-159

biotin-dependent carboxylase uncharacterized domain; Urea amidolyase of Saccharomyces cerevisiae is a 1835 amino acid protein with an amidase domain, a biotin/lipoyl cofactor attachment domain, a carbamoyl-phosphate synthase L chain-like domain, and uncharacterized regions. It has both urea carboxylase and allophanate hydrolase activities. This model models a domain that represents uncharacterized prokaryotic proteins of about 300 amino acids, regions of prokaryotic urea carboxylase and of the urea carboxylase region of yeast urea amidolyase, and regions of other biotin-containing proteins. [Unknown function, General]


Pssm-ID: 129807  Cd Length: 314  Bit Score: 446.54  E-value: 2.45e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464    3 TLEILRSGPLALVEDLGRAGLAHLGVGRSGAADRRSHTLANRLVANPDDWATVEVTFGGFSARVRGgDVDIAVTGADTDP 82
Cdd:TIGR00724   1 MIEILRAGSHTLIQDLGRVGYRRIGVPHSGAMDAYSLRLANRLVGNPDDTPAIEVTLGGPTIRFHC-DVIFAVTGADTDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464   83 TVNGIMVGT-NSIHHVRDGQVISLGTPRAGLRTYLAVRGGVCVEPVLGSRSYDVMSAIGP---SPLRAGDVLPVGEHTDD 158
Cdd:TIGR00724  80 CLNDGQVIPqWRPYEVKRGQILSLGRLKSGMRGYLAVRGGIDVPPVLGSCSTDLRANIGGyegRPLKAGDVLPLGSNELD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464  159 YPELDQAPVAaIEEHLVELRVVPGPRDDWLVDP--DALVHTIWMASNRSDRVGMRLQGRPLQHRWPDRQLPGEGVTRGAI 236
Cdd:TIGR00724 160 LNEPQGLIPQ-IPEWRIEIRVLPGPEYDFFKREsiEAFWRSEWKVSSNSDRMGYRLQGPKLKHARPNRELLTHGIVYGSI 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 624389464  237 QVPPNGLPVILGPDHPITGSYPVVGVITDEDIDKVAQIRPGQYVRLHWARPRSRLPGQGVTQAW 300
Cdd:TIGR00724 239 QVPPNGQPIILMADAQTTGGYPKIAVVIEADLWKVAQVRPGQSIKFVPLSLEEALKLRESQERY 302
PxpC COG1984
5-oxoprolinase subunit C/Allophanate hydrolase subunit 2 [Amino acid transport and metabolism]; ...
2-284 1.56e-114

5-oxoprolinase subunit C/Allophanate hydrolase subunit 2 [Amino acid transport and metabolism];


Pssm-ID: 441587  Cd Length: 285  Bit Score: 331.67  E-value: 1.56e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464   2 TTLEILRSGPLALVEDLGRAGLAHLGVGRSGAADRRSHTLANRLVANPDDWATVEVTFGGFSARVRGgDVDIAVTGADTD 81
Cdd:COG1984    1 MMLEVLKPGLLTTVQDLGRPGYQHLGVPPSGAMDRLALRLANRLVGNPEGAAALEITLGGPTLRFEE-DTVIALTGADMP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464  82 PTVNGIMVGTNSIHHVRDGQVISLGTPRAGLRTYLAVRGGVCVEPVLGSRSYDVMSAIG---PSPLRAGDVLPVGEHTDD 158
Cdd:COG1984   80 ATLDGRPVPPWRPVAVKAGDVLTLGAPRAGARAYLAVAGGIDVPPVLGSRSTDLRAGLGgleGRALQAGDVLPLGAPAAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464 159 YPELdQAPVAAIEEHLVELRVVPGPRDDWLVDP--DALVHTIWMASNRSDRVGMRLQGRPLQHRwPDRQLPGEGVTRGAI 236
Cdd:COG1984  160 APGR-GLPAELLPGEEVTLRVVPGPQDDWFTEEaiERFFSSEWTVTPQSDRMGYRLEGPPLERA-HPSEILSEGIVPGAI 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 624389464 237 QVPPNGLPVILGPDHPITGSYPVVGVITDEDIDKVAQIRPGQYVRLHW 284
Cdd:COG1984  238 QVPPDGQPIVLLADRQTTGGYPKIATVISADLPRLAQLRPGDTVRFVP 285
AHS2 smart00797
Allophanate hydrolase subunit 2; This domain represents subunit 2 of allophanate hydrolase ...
25-284 4.02e-109

Allophanate hydrolase subunit 2; This domain represents subunit 2 of allophanate hydrolase (AHS2).


Pssm-ID: 214821  Cd Length: 280  Bit Score: 317.89  E-value: 4.02e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464    25 HLGVGRSGAADRRSHTLANRLVANPDDWATVEVTFGGFSARVRGGDVdIAVTGADTDPTVNGIMVGTNSIHHVRDGQVIS 104
Cdd:smart00797   1 HLGVPPSGAMDQLALRLANRLVGNPENAAALEITLGGPTLRFTADAV-IALTGADFPATLDGQPVPPWKPFAVRAGQVLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464   105 LGTPRAGLRTYLAVRGGVCVEPVLGSRSYDVMSAIG---PSPLRAGDVLPVGEHTDDYPELDQAPVAAIE--EHLVELRV 179
Cdd:smart00797  80 LGAPKAGARAYLAVRGGIDVPPVLGSRSTDTRGGFGgfeGRALKAGDVLPLGAAPAAAPAGAALPAALIPdyGKEWVIRV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464   180 VPGPRDDWLVDPD--ALVHTIWMASNRSDRVGMRLQGRPLQHRWPdRQLPGEGVTRGAIQVPPNGLPVILGPDHPITGSY 257
Cdd:smart00797 160 IPGPHPDFFTEESieRFFSSEWKVTPNSDRMGYRLEGPKLEWLHP-SNIISEGVAIGAIQVPPDGQPIILLADRQTTGGY 238
                          250       260
                   ....*....|....*....|....*..
gi 624389464   258 PVVGVITDEDIDKVAQIRPGQYVRLHW 284
Cdd:smart00797 239 PKIATVISADLWKLAQLRPGDKVRFVP 265
CT_A_B pfam02626
Carboxyltransferase domain, subdomain A and B; Urea carboxylase (UC) catalyzes a two-step, ...
26-284 4.49e-103

Carboxyltransferase domain, subdomain A and B; Urea carboxylase (UC) catalyzes a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the A and B subdomains of the CT domain. This domain covers the whole length of KipA (kinase A) from Bacillus subtilis. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity.


Pssm-ID: 460627  Cd Length: 264  Bit Score: 301.65  E-value: 4.49e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464   26 LGVGRSGAADRRSHTLANRLVANPDDWATVEVTFGGFSARVRGgDVDIAVTGADTDPTVNGIMVGTNSIHHVRDGQVISL 105
Cdd:pfam02626   1 LGVPPSGAMDPLALRLANRLVGNPEGAAALEITLGGPTLRFHA-DAVIAVTGADMPATLDGKPVPMWTPVAVKAGDVLSF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464  106 GTPRAGLRTYLAVRGGVCVEPVLGSRSYDVMSAIGP---SPLRAGDVLPVGEHTDDYPELDQAPVAAI--EEHLVELRVV 180
Cdd:pfam02626  80 GAPRGGLRAYLAVAGGFDVPPVLGSRSTDLLGGLGGhegRPLRAGDVLPLGPPAAPAPALAPLPPAPPppDTPEWVIRVV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464  181 PGPRDDWLVDPD--ALVHTIWMASNRSDRVGMRLQGRPLqHRWPDRQLPGEGVTRGAIQVPPNGLPVILGPDHPITGSYP 258
Cdd:pfam02626 160 PGPQDDWFTPEAleTFFSTEWTVSPNSDRMGYRLDGEAL-HPARGSNILSEGYVPGAIQVPPGGQPIILLADGQTTGGYP 238
                         250       260
                  ....*....|....*....|....*.
gi 624389464  259 VVGVITDEDIDKVAQIRPGQYVRLHW 284
Cdd:pfam02626 239 KIATVISADLWKLAQLRPGDKVRFVP 264
 
Name Accession Description Interval E-value
urea_amlyse_rel TIGR00724
biotin-dependent carboxylase uncharacterized domain; Urea amidolyase of Saccharomyces ...
3-300 2.45e-159

biotin-dependent carboxylase uncharacterized domain; Urea amidolyase of Saccharomyces cerevisiae is a 1835 amino acid protein with an amidase domain, a biotin/lipoyl cofactor attachment domain, a carbamoyl-phosphate synthase L chain-like domain, and uncharacterized regions. It has both urea carboxylase and allophanate hydrolase activities. This model models a domain that represents uncharacterized prokaryotic proteins of about 300 amino acids, regions of prokaryotic urea carboxylase and of the urea carboxylase region of yeast urea amidolyase, and regions of other biotin-containing proteins. [Unknown function, General]


Pssm-ID: 129807  Cd Length: 314  Bit Score: 446.54  E-value: 2.45e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464    3 TLEILRSGPLALVEDLGRAGLAHLGVGRSGAADRRSHTLANRLVANPDDWATVEVTFGGFSARVRGgDVDIAVTGADTDP 82
Cdd:TIGR00724   1 MIEILRAGSHTLIQDLGRVGYRRIGVPHSGAMDAYSLRLANRLVGNPDDTPAIEVTLGGPTIRFHC-DVIFAVTGADTDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464   83 TVNGIMVGT-NSIHHVRDGQVISLGTPRAGLRTYLAVRGGVCVEPVLGSRSYDVMSAIGP---SPLRAGDVLPVGEHTDD 158
Cdd:TIGR00724  80 CLNDGQVIPqWRPYEVKRGQILSLGRLKSGMRGYLAVRGGIDVPPVLGSCSTDLRANIGGyegRPLKAGDVLPLGSNELD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464  159 YPELDQAPVAaIEEHLVELRVVPGPRDDWLVDP--DALVHTIWMASNRSDRVGMRLQGRPLQHRWPDRQLPGEGVTRGAI 236
Cdd:TIGR00724 160 LNEPQGLIPQ-IPEWRIEIRVLPGPEYDFFKREsiEAFWRSEWKVSSNSDRMGYRLQGPKLKHARPNRELLTHGIVYGSI 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 624389464  237 QVPPNGLPVILGPDHPITGSYPVVGVITDEDIDKVAQIRPGQYVRLHWARPRSRLPGQGVTQAW 300
Cdd:TIGR00724 239 QVPPNGQPIILMADAQTTGGYPKIAVVIEADLWKVAQVRPGQSIKFVPLSLEEALKLRESQERY 302
PxpC COG1984
5-oxoprolinase subunit C/Allophanate hydrolase subunit 2 [Amino acid transport and metabolism]; ...
2-284 1.56e-114

5-oxoprolinase subunit C/Allophanate hydrolase subunit 2 [Amino acid transport and metabolism];


Pssm-ID: 441587  Cd Length: 285  Bit Score: 331.67  E-value: 1.56e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464   2 TTLEILRSGPLALVEDLGRAGLAHLGVGRSGAADRRSHTLANRLVANPDDWATVEVTFGGFSARVRGgDVDIAVTGADTD 81
Cdd:COG1984    1 MMLEVLKPGLLTTVQDLGRPGYQHLGVPPSGAMDRLALRLANRLVGNPEGAAALEITLGGPTLRFEE-DTVIALTGADMP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464  82 PTVNGIMVGTNSIHHVRDGQVISLGTPRAGLRTYLAVRGGVCVEPVLGSRSYDVMSAIG---PSPLRAGDVLPVGEHTDD 158
Cdd:COG1984   80 ATLDGRPVPPWRPVAVKAGDVLTLGAPRAGARAYLAVAGGIDVPPVLGSRSTDLRAGLGgleGRALQAGDVLPLGAPAAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464 159 YPELdQAPVAAIEEHLVELRVVPGPRDDWLVDP--DALVHTIWMASNRSDRVGMRLQGRPLQHRwPDRQLPGEGVTRGAI 236
Cdd:COG1984  160 APGR-GLPAELLPGEEVTLRVVPGPQDDWFTEEaiERFFSSEWTVTPQSDRMGYRLEGPPLERA-HPSEILSEGIVPGAI 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 624389464 237 QVPPNGLPVILGPDHPITGSYPVVGVITDEDIDKVAQIRPGQYVRLHW 284
Cdd:COG1984  238 QVPPDGQPIVLLADRQTTGGYPKIATVISADLPRLAQLRPGDTVRFVP 285
AHS2 smart00797
Allophanate hydrolase subunit 2; This domain represents subunit 2 of allophanate hydrolase ...
25-284 4.02e-109

Allophanate hydrolase subunit 2; This domain represents subunit 2 of allophanate hydrolase (AHS2).


Pssm-ID: 214821  Cd Length: 280  Bit Score: 317.89  E-value: 4.02e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464    25 HLGVGRSGAADRRSHTLANRLVANPDDWATVEVTFGGFSARVRGGDVdIAVTGADTDPTVNGIMVGTNSIHHVRDGQVIS 104
Cdd:smart00797   1 HLGVPPSGAMDQLALRLANRLVGNPENAAALEITLGGPTLRFTADAV-IALTGADFPATLDGQPVPPWKPFAVRAGQVLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464   105 LGTPRAGLRTYLAVRGGVCVEPVLGSRSYDVMSAIG---PSPLRAGDVLPVGEHTDDYPELDQAPVAAIE--EHLVELRV 179
Cdd:smart00797  80 LGAPKAGARAYLAVRGGIDVPPVLGSRSTDTRGGFGgfeGRALKAGDVLPLGAAPAAAPAGAALPAALIPdyGKEWVIRV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464   180 VPGPRDDWLVDPD--ALVHTIWMASNRSDRVGMRLQGRPLQHRWPdRQLPGEGVTRGAIQVPPNGLPVILGPDHPITGSY 257
Cdd:smart00797 160 IPGPHPDFFTEESieRFFSSEWKVTPNSDRMGYRLEGPKLEWLHP-SNIISEGVAIGAIQVPPDGQPIILLADRQTTGGY 238
                          250       260
                   ....*....|....*....|....*..
gi 624389464   258 PVVGVITDEDIDKVAQIRPGQYVRLHW 284
Cdd:smart00797 239 PKIATVISADLWKLAQLRPGDKVRFVP 265
CT_A_B pfam02626
Carboxyltransferase domain, subdomain A and B; Urea carboxylase (UC) catalyzes a two-step, ...
26-284 4.49e-103

Carboxyltransferase domain, subdomain A and B; Urea carboxylase (UC) catalyzes a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the A and B subdomains of the CT domain. This domain covers the whole length of KipA (kinase A) from Bacillus subtilis. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity.


Pssm-ID: 460627  Cd Length: 264  Bit Score: 301.65  E-value: 4.49e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464   26 LGVGRSGAADRRSHTLANRLVANPDDWATVEVTFGGFSARVRGgDVDIAVTGADTDPTVNGIMVGTNSIHHVRDGQVISL 105
Cdd:pfam02626   1 LGVPPSGAMDPLALRLANRLVGNPEGAAALEITLGGPTLRFHA-DAVIAVTGADMPATLDGKPVPMWTPVAVKAGDVLSF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464  106 GTPRAGLRTYLAVRGGVCVEPVLGSRSYDVMSAIGP---SPLRAGDVLPVGEHTDDYPELDQAPVAAI--EEHLVELRVV 180
Cdd:pfam02626  80 GAPRGGLRAYLAVAGGFDVPPVLGSRSTDLLGGLGGhegRPLRAGDVLPLGPPAAPAPALAPLPPAPPppDTPEWVIRVV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389464  181 PGPRDDWLVDPD--ALVHTIWMASNRSDRVGMRLQGRPLqHRWPDRQLPGEGVTRGAIQVPPNGLPVILGPDHPITGSYP 258
Cdd:pfam02626 160 PGPQDDWFTPEAleTFFSTEWTVSPNSDRMGYRLDGEAL-HPARGSNILSEGYVPGAIQVPPGGQPIILLADGQTTGGYP 238
                         250       260
                  ....*....|....*....|....*.
gi 624389464  259 VVGVITDEDIDKVAQIRPGQYVRLHW 284
Cdd:pfam02626 239 KIATVISADLWKLAQLRPGDKVRFVP 264
 
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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