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Conserved domains on  [gi|552764863|ref|WP_023016992|]
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MULTISPECIES: Ig-like domain-containing protein [Corynebacterium]

Protein Classification

L,D-transpeptidase( domain architecture ID 16057555)

L,D-transpeptidase catalyzes the formation of 3->3 peptidoglycan cross-links

CATH:  2.40.440.10|2.60.40.3780|2.60.40.3710
EC:  2.3.2.-
Gene Ontology:  GO:0018104|GO:0071972
PubMed:  18266857
SCOP:  4000465|4002015

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Big_10 pfam17964
Bacterial Ig domain; This entry represents a bacterial Ig-like domain found associated with ...
 65-241 1.18e-72

Bacterial Ig domain; This entry represents a bacterial Ig-like domain found associated with transpeptidase domains.


:

Pssm-ID: 465591 [Multi-domain]  Cd Length: 182  Bit Score: 225.20  E-value: 1.18e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863   65 AEDVDPSKPVTVESTT-ELKSVTMTNELGVEVEEKLSEDGKKWTTAEDLGYNHTYSIVASDKDGNKK----NLSFSTSQA 139
Cdd:pfam17964   1 ATGVNPGTPVTVTVAGgTLTDVTVTDSDGKEVPGKLSADGTSWTSTEPLGYGTTYTVTATAKGAGGKattqTSSFTTVSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863  140 AGVAQVAMTPIPGSEVGVGQVIGVNFGTYITDRKAAEDTITVKTNPEVEGAFYWVNNQEVRWRPKEYWEPGTKVEVKVDQ 219
Cdd:pfam17964  81 ANTTSGTLTPLDGSTVGVGMPISINFDKPVTDKAAVEKAITVTTSPAVEGAWHWFGDQRVDWRPKEYWPPGTKVTVDARL 160

                         170       180
                  ....*....|....*....|..
gi 552764863  220 YGKDLGGGIYGGENTGTDFTIG 241
Cdd:pfam17964 161 YGVDLGDGVYGQQDRTVTFTIG 182
ErfK COG1376
Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];
246-368 8.51e-30

Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440986 [Multi-domain]  Cd Length: 121  Bit Score: 111.49  E-value: 8.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863 246 ALVDNATKTMKVYKNKELLRTIPVSLGRDyQYDTPNGRYVIGDQHQSLLMDSETFGLPHDAGGYSTEV-DWATQMSYSGI 324
Cdd:COG1376    1 IVVDLSEQRLYVYEDGGLVRTYPVSVGRP-GFPTPTGTFRVLRKAENPTWTPPAEMPAGMPGGPDNPLgPYALYLSDGGY 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 552764863 325 YVHSAPWsVWAQGnSNTSHGCINVTPEAAQWFQNTVKRGDIVRV 368
Cdd:COG1376   80 GIHGTPW-PSSIG-RNVSHGCIRLSNEDAKWLYDRVPVGTPVVV 121
 
Name Accession Description Interval E-value
Big_10 pfam17964
Bacterial Ig domain; This entry represents a bacterial Ig-like domain found associated with ...
 65-241 1.18e-72

Bacterial Ig domain; This entry represents a bacterial Ig-like domain found associated with transpeptidase domains.


Pssm-ID: 465591 [Multi-domain]  Cd Length: 182  Bit Score: 225.20  E-value: 1.18e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863   65 AEDVDPSKPVTVESTT-ELKSVTMTNELGVEVEEKLSEDGKKWTTAEDLGYNHTYSIVASDKDGNKK----NLSFSTSQA 139
Cdd:pfam17964   1 ATGVNPGTPVTVTVAGgTLTDVTVTDSDGKEVPGKLSADGTSWTSTEPLGYGTTYTVTATAKGAGGKattqTSSFTTVSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863  140 AGVAQVAMTPIPGSEVGVGQVIGVNFGTYITDRKAAEDTITVKTNPEVEGAFYWVNNQEVRWRPKEYWEPGTKVEVKVDQ 219
Cdd:pfam17964  81 ANTTSGTLTPLDGSTVGVGMPISINFDKPVTDKAAVEKAITVTTSPAVEGAWHWFGDQRVDWRPKEYWPPGTKVTVDARL 160

                         170       180
                  ....*....|....*....|..
gi 552764863  220 YGKDLGGGIYGGENTGTDFTIG 241
Cdd:pfam17964 161 YGVDLGDGVYGQQDRTVTFTIG 182
LDT_IgD_like_2 cd13432
IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found ...
 145-241 1.85e-47

IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3->3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain; this model represents the repeat adjacent to the catalytic domain.


Pssm-ID: 240447  Cd Length: 99  Bit Score: 157.29  E-value: 1.85e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863 145 VAMTPIPGSEVGVGQVIGVNFGTYITDRKAAEDTITVKTNPEVEGAFYWVNNQEVRWRPKEYWEPGTKVEVKVDQYGKDL 224
Cdd:cd13432    3 ASVNPLDGETVGVGMPVIVTFDEPVTDRAAVEKALKVTTSPPVEGAWYWLSDREVHWRPKEYWPPGTKVTVDANLYGVDL 82

                         90
                 ....*....|....*..
gi 552764863 225 GGGIYGGENTGTDFTIG 241
Cdd:cd13432   83 GDGVYGQEDRSTTFTIG 99
ErfK COG1376
Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];
246-368 8.51e-30

Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440986 [Multi-domain]  Cd Length: 121  Bit Score: 111.49  E-value: 8.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863 246 ALVDNATKTMKVYKNKELLRTIPVSLGRDyQYDTPNGRYVIGDQHQSLLMDSETFGLPHDAGGYSTEV-DWATQMSYSGI 324
Cdd:COG1376    1 IVVDLSEQRLYVYEDGGLVRTYPVSVGRP-GFPTPTGTFRVLRKAENPTWTPPAEMPAGMPGGPDNPLgPYALYLSDGGY 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 552764863 325 YVHSAPWsVWAQGnSNTSHGCINVTPEAAQWFQNTVKRGDIVRV 368
Cdd:COG1376   80 GIHGTPW-PSSIG-RNVSHGCIRLSNEDAKWLYDRVPVGTPVVV 121
YkuD_like cd16913
L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like ...
 247-369 1.55e-22

L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.


Pssm-ID: 341130 [Multi-domain]  Cd Length: 121  Bit Score: 91.99  E-value: 1.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863 247 LVDNATKTMKVYKNKELLRTIPVSLGRDYqYDTPNGRYVIGDQHQSLLMDSETFGLPHDAGGYsteVDWATQMSY--SGI 324
Cdd:cd16913    3 VVDLSEQRLYLYENGKLVKTYPVSTGKPG-TPTPTGTFRITRKVKNPTWTGPPSIPPGPYNPL---GPYALRLSGpgSGI 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 552764863 325 YVHSAPWSVWaqGNSNTSHGCINVTPEAAQWFQNTVKRGDIVRVF 369
Cdd:cd16913   79 GIHGTPWPSS--IGRPASHGCIRLSNEDAKELYDWVPVGTPVVIY 121
YkuD pfam03734
L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. ...
 243-368 1.98e-13

L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. It has been shown that this domain can act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. This gives bacteria resistance to beta-lactam antibiotics that inhibit PBPs which usually carry out the cross-linking reaction. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue. Several members of this family contain peptidoglycan binding domains. The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. The two beta-sheets form a cradle capped by an alpha-helix. This family was formerly called the ErfK/YbiS/YcfS/YnhG family, but is now named after the first protein of known structure.


Pssm-ID: 461031 [Multi-domain]  Cd Length: 89  Bit Score: 65.45  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863  243 RTVALVDNATKTMK-VYKNKELLRTIPVSLGRDYqYDTPNGRYVIgdqhqsllmdsetfglphdaggystevdwatqmsy 321
Cdd:pfam03734   1 DRYIVVDLSEQRLLyLYENGGLVLRYPVSVGRGD-GPTPTGTFRI----------------------------------- 44

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 552764863  322 sgIYVHSAPWSVWAQGNSNTSHGCINVTPEAAQWFQNTVKRGDIVRV 368
Cdd:pfam03734  45 --IYIHDTGTPDLFGLGRRRSHGCIRLSNEDAKELYDRVLVGTPVVI 89
 
Name Accession Description Interval E-value
Big_10 pfam17964
Bacterial Ig domain; This entry represents a bacterial Ig-like domain found associated with ...
 65-241 1.18e-72

Bacterial Ig domain; This entry represents a bacterial Ig-like domain found associated with transpeptidase domains.


Pssm-ID: 465591 [Multi-domain]  Cd Length: 182  Bit Score: 225.20  E-value: 1.18e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863   65 AEDVDPSKPVTVESTT-ELKSVTMTNELGVEVEEKLSEDGKKWTTAEDLGYNHTYSIVASDKDGNKK----NLSFSTSQA 139
Cdd:pfam17964   1 ATGVNPGTPVTVTVAGgTLTDVTVTDSDGKEVPGKLSADGTSWTSTEPLGYGTTYTVTATAKGAGGKattqTSSFTTVSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863  140 AGVAQVAMTPIPGSEVGVGQVIGVNFGTYITDRKAAEDTITVKTNPEVEGAFYWVNNQEVRWRPKEYWEPGTKVEVKVDQ 219
Cdd:pfam17964  81 ANTTSGTLTPLDGSTVGVGMPISINFDKPVTDKAAVEKAITVTTSPAVEGAWHWFGDQRVDWRPKEYWPPGTKVTVDARL 160

                         170       180
                  ....*....|....*....|..
gi 552764863  220 YGKDLGGGIYGGENTGTDFTIG 241
Cdd:pfam17964 161 YGVDLGDGVYGQQDRTVTFTIG 182
LDT_IgD_like_2 cd13432
IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found ...
 145-241 1.85e-47

IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3->3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain; this model represents the repeat adjacent to the catalytic domain.


Pssm-ID: 240447  Cd Length: 99  Bit Score: 157.29  E-value: 1.85e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863 145 VAMTPIPGSEVGVGQVIGVNFGTYITDRKAAEDTITVKTNPEVEGAFYWVNNQEVRWRPKEYWEPGTKVEVKVDQYGKDL 224
Cdd:cd13432    3 ASVNPLDGETVGVGMPVIVTFDEPVTDRAAVEKALKVTTSPPVEGAWYWLSDREVHWRPKEYWPPGTKVTVDANLYGVDL 82

                         90
                 ....*....|....*..
gi 552764863 225 GGGIYGGENTGTDFTIG 241
Cdd:cd13432   83 GDGVYGQEDRSTTFTIG 99
ErfK COG1376
Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];
246-368 8.51e-30

Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440986 [Multi-domain]  Cd Length: 121  Bit Score: 111.49  E-value: 8.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863 246 ALVDNATKTMKVYKNKELLRTIPVSLGRDyQYDTPNGRYVIGDQHQSLLMDSETFGLPHDAGGYSTEV-DWATQMSYSGI 324
Cdd:COG1376    1 IVVDLSEQRLYVYEDGGLVRTYPVSVGRP-GFPTPTGTFRVLRKAENPTWTPPAEMPAGMPGGPDNPLgPYALYLSDGGY 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 552764863 325 YVHSAPWsVWAQGnSNTSHGCINVTPEAAQWFQNTVKRGDIVRV 368
Cdd:COG1376   80 GIHGTPW-PSSIG-RNVSHGCIRLSNEDAKWLYDRVPVGTPVVV 121
LDT_IgD_like cd13430
IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found ...
 149-240 3.66e-23

IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3->3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain.


Pssm-ID: 240445  Cd Length: 98  Bit Score: 92.78  E-value: 3.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863 149 PIPGSEVGVGQVIGVNFGTYITDRKAAEDTITVKTNPEVEGAFYWVNN-QEVRWRPKEYWEPGTKVEVKVDQYGKDLGGG 227
Cdd:cd13430    6 PGDGEVVGVGAPVAIRFDENIADRGAAEKAITITTDPPVEGAFYWLPDgRRVRWRPEHFWKPGTAVDVAANTYGLDLGEG 85

                         90
                 ....*....|...
gi 552764863 228 IYGGENTGTDFTI 240
Cdd:cd13430   86 MFGADNVQLHFQI 98
YkuD_like cd16913
L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like ...
 247-369 1.55e-22

L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.


Pssm-ID: 341130 [Multi-domain]  Cd Length: 121  Bit Score: 91.99  E-value: 1.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863 247 LVDNATKTMKVYKNKELLRTIPVSLGRDYqYDTPNGRYVIGDQHQSLLMDSETFGLPHDAGGYsteVDWATQMSY--SGI 324
Cdd:cd16913    3 VVDLSEQRLYLYENGKLVKTYPVSTGKPG-TPTPTGTFRITRKVKNPTWTGPPSIPPGPYNPL---GPYALRLSGpgSGI 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 552764863 325 YVHSAPWSVWaqGNSNTSHGCINVTPEAAQWFQNTVKRGDIVRVF 369
Cdd:cd16913   79 GIHGTPWPSS--IGRPASHGCIRLSNEDAKELYDWVPVGTPVVIY 121
LDT_IgD_like_1 cd13431
IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found ...
 142-217 9.22e-16

IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3->3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain; this model represents the first (N-terminal) repeat in LdtMt2 and related proteins.


Pssm-ID: 240446  Cd Length: 95  Bit Score: 72.35  E-value: 9.22e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552764863 142 VAQVAMTPIPGSEVGVGQVIGVNFGTYITDRKAAEDTITVKTNPEVEGAFYWVNNQEVRWRPKEYWEPGTKVEVKV 217
Cdd:cd13431    8 VPVATVSPADGAVVGVAHPVVVTFADPVADRAAAENAIGITVAGPVAGGFSWTDDEPLGWTPTYFWPAHATVTVGA 83
YkuD pfam03734
L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. ...
 243-368 1.98e-13

L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. It has been shown that this domain can act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. This gives bacteria resistance to beta-lactam antibiotics that inhibit PBPs which usually carry out the cross-linking reaction. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue. Several members of this family contain peptidoglycan binding domains. The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. The two beta-sheets form a cradle capped by an alpha-helix. This family was formerly called the ErfK/YbiS/YcfS/YnhG family, but is now named after the first protein of known structure.


Pssm-ID: 461031 [Multi-domain]  Cd Length: 89  Bit Score: 65.45  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863  243 RTVALVDNATKTMK-VYKNKELLRTIPVSLGRDYqYDTPNGRYVIgdqhqsllmdsetfglphdaggystevdwatqmsy 321
Cdd:pfam03734   1 DRYIVVDLSEQRLLyLYENGGLVLRYPVSVGRGD-GPTPTGTFRI----------------------------------- 44

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 552764863  322 sgIYVHSAPWSVWAQGNSNTSHGCINVTPEAAQWFQNTVKRGDIVRV 368
Cdd:pfam03734  45 --IYIHDTGTPDLFGLGRRRSHGCIRLSNEDAKELYDRVLVGTPVVI 89
LDT_IgD_like_1 cd13431
IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found ...
 56-139 4.04e-03

IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3->3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain; this model represents the first (N-terminal) repeat in LdtMt2 and related proteins.


Pssm-ID: 240446  Cd Length: 95  Bit Score: 36.52  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764863  56 KLSASVKDGAeDVDPSKPVTVESTTE-LKSVTMTNELGVEVEEKLSeDGKKWTTAEDLGYNHTYSIVAS---DKDGNKKN 131
Cdd:cd13431   10 VATVSPADGA-VVGVAHPVVVTFADPvADRAAAENAIGITVAGPVA-GGFSWTDDEPLGWTPTYFWPAHatvTVGAGGTR 87


                 ....*...
gi 552764863 132 LSFSTSQA 139
Cdd:cd13431   88 TSFRTGDA 95
 
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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