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Conserved domains on  [gi|916680925|ref|WP_051288016|]
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N-acetylmuramoyl-L-alanine amidase [Alkalicoccus chagannorensis]

Protein Classification

N-acetylmuramoyl-L-alanine amidase( domain architecture ID 10159408)

N-acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides; contains a peptidoglycan binding domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 22-138 1.50e-22

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


:

Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 88.57  E-value: 1.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916680925   22 NVRMVTLHHSATKRGNAAAFAAYHVDHLGWPGIGYHYVIRRDGTVEVCWDDWTISYHT--KNRNTGNIGICLVGSGS--- 96
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPYAACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIELEGNFGgdp 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 916680925   97 FTVSQKASALDLAAEKCAVHRLSEQAF-QGHRDhpGQQTACPG 138
Cdd:pfam01510  81 PTDAQYEALARLLADLCKRYGIPPDRRiVGHRD--VGRKTDPG 121
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 150-212 2.00e-17

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 73.40  E-value: 2.00e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 916680925 150 PTLRKGGSNLRVRALQERLLHAGsvLPLYGADGVFGKETEQAVRSFQQQASAAVDGVVGKETW 212
Cdd:COG3409    4 PTLRLGDSGEDVRELQQRLNALG--YYPGPVDGIFGPATEAAVRAFQRANGLPVDGIVGPATW 64
 
Name Accession Description Interval E-value
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 22-138 1.50e-22

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 88.57  E-value: 1.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916680925   22 NVRMVTLHHSATKRGNAAAFAAYHVDHLGWPGIGYHYVIRRDGTVEVCWDDWTISYHT--KNRNTGNIGICLVGSGS--- 96
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPYAACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIELEGNFGgdp 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 916680925   97 FTVSQKASALDLAAEKCAVHRLSEQAF-QGHRDhpGQQTACPG 138
Cdd:pfam01510  81 PTDAQYEALARLLADLCKRYGIPPDRRiVGHRD--VGRKTDPG 121
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 22-138 4.63e-19

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 79.64  E-value: 4.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916680925  22 NVRMVTLHHSATKRGNAAA-----FAAYHVdhLGWPGIGYHYVIRRDGTVEVCWDDWTISYHTKNR-NTGNIGICLVGSG 95
Cdd:cd06583    1 PVKYVVIHHTANPNCYTAAaavryLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGNyNSYSIGIELIGNF 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 916680925  96 S---FTVSQKASALDLAAEKCAVHRLSEQA-FQGHRDHPGqQTACPG 138
Cdd:cd06583   79 DggpPTAAQLEALAELLAYLVKRYGIPPDYrIVGHRDVSP-GTECPG 124
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 150-212 2.00e-17

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 73.40  E-value: 2.00e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 916680925 150 PTLRKGGSNLRVRALQERLLHAGsvLPLYGADGVFGKETEQAVRSFQQQASAAVDGVVGKETW 212
Cdd:COG3409    4 PTLRLGDSGEDVRELQQRLNALG--YYPGPVDGIFGPATEAAVRAFQRANGLPVDGIVGPATW 64
PHA00447 PHA00447
lysozyme
 17-144 2.48e-17

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 75.58  E-value: 2.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916680925  17 YRKTTNVRMVTLHHSATKRGNAAAFAAYHVDHL--GWPGIGYHYVIRRDGTVEVCWDDWTISYHTKNRNTGNIGICLVG- 93
Cdd:PHA00447   4 FKPRSSTKAIFVHCSATKPSMDVGVREIRQWHKeqGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGg 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 916680925  94 -------SGSFTVSQKASALDLAAEKCAVHrlSEQAFQGHRDHPGQqtACPGVHARSW 144
Cdd:PHA00447  84 iddkgkfDANFTPAQMQSLKSLLVTLKAKY--PGAEIKAHHDVAPK--ACPSFDLQRW 137
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 161-212 2.14e-12

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 59.84  E-value: 2.14e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 916680925  161 VRALQERLLHAGSVLPlyGADGVFGKETEQAVRSFQQQASAAVDGVVGKETW 212
Cdd:pfam01471   5 VKELQRYLNRLGYYPG--PVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETL 54
Ami_2 smart00644
Ami_2 domain;
22-137 9.35e-10

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 54.67  E-value: 9.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916680925    22 NVRMVTLHHSATKRGNAAAFAAYHVDHlGWPGIGYHYVIRRDGTVEVC--WDDWtiSYHTKNRNTGN-----IGICLVGS 94
Cdd:smart00644   2 PPRGIVIHHTANSNASCANEARYMQNN-HMNDIGYHFLVGGDGRVYQGvgWNYV--AWHAGGAHTPGyndisIGIEFIGS 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 916680925    95 G-----SFTVSQKAsALDLAAEKCAVHRLSE---QAFQGHRDHPGqqTACP 137
Cdd:smart00644  79 FdsddePFAEALYA-ALDLLAKLLKGAGLPPdgrYRIVGHRDVAP--TEDP 126
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
18-138 7.51e-07

N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442259  Cd Length: 167  Bit Score: 47.55  E-value: 7.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916680925  18 RKTTNVRMVTLHHSATKRGNAAafaayhVDHLGWPGIG--YHYVIRRDGTVE--VCWDDwtISYH-----TKNRNTGN-- 86
Cdd:COG3023   22 PAGAEIDLIVIHYTAGPPGGGA------LDWLTDPALRvsAHYLIDRDGEIYqlVPEDD--RAWHagvssWRGRTNLNdf 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 916680925  87 -IGICLVGSGS----FTVSQKASALDLAAEKCAVHRLSEQAFQGHRDHPGQQTACPG 138
Cdd:COG3023   94 sIGIELENPGHgwapFTEAQYEALAALLRDLCARYGIPPDHIVGHSDIAPGRKTDPG 150
 
Name Accession Description Interval E-value
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 22-138 1.50e-22

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 88.57  E-value: 1.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916680925   22 NVRMVTLHHSATKRGNAAAFAAYHVDHLGWPGIGYHYVIRRDGTVEVCWDDWTISYHT--KNRNTGNIGICLVGSGS--- 96
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPYAACIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAgnGGGNDRSIGIELEGNFGgdp 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 916680925   97 FTVSQKASALDLAAEKCAVHRLSEQAF-QGHRDhpGQQTACPG 138
Cdd:pfam01510  81 PTDAQYEALARLLADLCKRYGIPPDRRiVGHRD--VGRKTDPG 121
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 22-138 4.63e-19

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 79.64  E-value: 4.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916680925  22 NVRMVTLHHSATKRGNAAA-----FAAYHVdhLGWPGIGYHYVIRRDGTVEVCWDDWTISYHTKNR-NTGNIGICLVGSG 95
Cdd:cd06583    1 PVKYVVIHHTANPNCYTAAaavryLQNYHM--RGWSDISYHFLVGGDGRIYQGRGWNYVGWHAGGNyNSYSIGIELIGNF 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 916680925  96 S---FTVSQKASALDLAAEKCAVHRLSEQA-FQGHRDHPGqQTACPG 138
Cdd:cd06583   79 DggpPTAAQLEALAELLAYLVKRYGIPPDYrIVGHRDVSP-GTECPG 124
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 150-212 2.00e-17

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 73.40  E-value: 2.00e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 916680925 150 PTLRKGGSNLRVRALQERLLHAGsvLPLYGADGVFGKETEQAVRSFQQQASAAVDGVVGKETW 212
Cdd:COG3409    4 PTLRLGDSGEDVRELQQRLNALG--YYPGPVDGIFGPATEAAVRAFQRANGLPVDGIVGPATW 64
PHA00447 PHA00447
lysozyme
 17-144 2.48e-17

lysozyme


Pssm-ID: 177282 [Multi-domain]  Cd Length: 142  Bit Score: 75.58  E-value: 2.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916680925  17 YRKTTNVRMVTLHHSATKRGNAAAFAAYHVDHL--GWPGIGYHYVIRRDGTVEVCWDDWTISYHTKNRNTGNIGICLVG- 93
Cdd:PHA00447   4 FKPRSSTKAIFVHCSATKPSMDVGVREIRQWHKeqGWLDVGYHFIIRRDGTVEEGRPEDVVGSHVKGYNSNSVGVCLVGg 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 916680925  94 -------SGSFTVSQKASALDLAAEKCAVHrlSEQAFQGHRDHPGQqtACPGVHARSW 144
Cdd:PHA00447  84 iddkgkfDANFTPAQMQSLKSLLVTLKAKY--PGAEIKAHHDVAPK--ACPSFDLQRW 137
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 161-212 2.14e-12

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 59.84  E-value: 2.14e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 916680925  161 VRALQERLLHAGSVLPlyGADGVFGKETEQAVRSFQQQASAAVDGVVGKETW 212
Cdd:pfam01471   5 VKELQRYLNRLGYYPG--PVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETL 54
Ami_2 smart00644
Ami_2 domain;
22-137 9.35e-10

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 54.67  E-value: 9.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916680925    22 NVRMVTLHHSATKRGNAAAFAAYHVDHlGWPGIGYHYVIRRDGTVEVC--WDDWtiSYHTKNRNTGN-----IGICLVGS 94
Cdd:smart00644   2 PPRGIVIHHTANSNASCANEARYMQNN-HMNDIGYHFLVGGDGRVYQGvgWNYV--AWHAGGAHTPGyndisIGIEFIGS 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 916680925    95 G-----SFTVSQKAsALDLAAEKCAVHRLSE---QAFQGHRDHPGqqTACP 137
Cdd:smart00644  79 FdsddePFAEALYA-ALDLLAKLLKGAGLPPdgrYRIVGHRDVAP--TEDP 126
YcbB COG2989
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
150-212 2.97e-09

Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442228 [Multi-domain]  Cd Length: 529  Bit Score: 56.10  E-value: 2.97e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 916680925 150 PTLRKGGSNLRVRALQERLLHAGSVLPLYGADG-VFGKETEQAVRSFQQQASAAVDGVVGKETW 212
Cdd:COG2989  202 PTLRPGDSDPRVPALRERLAALGDLPADAPSDSdVYDAELVEAVKRFQARHGLKADGVIGPATL 265
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
 20-129 1.18e-08

Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The bacteriophage molecule, but not its moth homologue, has been shown to have N-acetylmuramoyl-L-alanine amidase activity. One member of this family, Tag7, is a cytokine.


Pssm-ID: 128941  Cd Length: 142  Bit Score: 51.91  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916680925    20 TTNVRMVTLHHSATKRGNAAAFAA--------YHVDHLGWPGIGYHYVIRRDGTVE--VCWDdwTISYHTKNRNTGNIGI 89
Cdd:smart00701  21 TRPVRYVIIHHTATPNCYTDAQCAqilrniqaYHMEELGWCDIGYNFLVGGDGKVYegRGWN--VVGAHTGGYNDISLGI 98

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 916680925    90 CLVG--SGSFTVSQKASAL-DLAAEKCAVHRLSEQAFQ-GHRDH 129
Cdd:smart00701  99 AFIGnfTDKLPTDAALDAAqDLLACAVQRGHLSPDYKLvGHRQV 142
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
18-138 7.51e-07

N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442259  Cd Length: 167  Bit Score: 47.55  E-value: 7.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916680925  18 RKTTNVRMVTLHHSATKRGNAAafaayhVDHLGWPGIG--YHYVIRRDGTVE--VCWDDwtISYH-----TKNRNTGN-- 86
Cdd:COG3023   22 PAGAEIDLIVIHYTAGPPGGGA------LDWLTDPALRvsAHYLIDRDGEIYqlVPEDD--RAWHagvssWRGRTNLNdf 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 916680925  87 -IGICLVGSGS----FTVSQKASALDLAAEKCAVHRLSEQAFQGHRDHPGQQTACPG 138
Cdd:COG3023   94 sIGIELENPGHgwapFTEAQYEALAALLRDLCARYGIPPDHIVGHSDIAPGRKTDPG 150
 
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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