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Conserved domains on  [gi|496081127|ref|WP_008805634|]
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MULTISPECIES: endolytic peptidoglycan transglycosylase RlpA [Klebsiella]

Protein Classification

septal ring lytic transglycosylase RlpA family protein( domain architecture ID 11484865)

septal ring lytic transglycosylase RlpA family protein similar to endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A), a lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10672 PRK10672
endolytic peptidoglycan transglycosylase RlpA;
1-385 0e+00

endolytic peptidoglycan transglycosylase RlpA;


:

Pssm-ID: 236733 [Multi-domain]  Cd Length: 361  Bit Score: 558.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127   1 MRKQWLGICIAAGLLAACSSDDVQQKTVSTPQPAVCNGPTVEISGADPQYETPNATANQDYERDGKSYKIVQDPANFTQA 80
Cdd:PRK10672   1 MRKQWLGIGIAAGLLAACTSDDGQQQTVSAPQPAVCNGPVVEISGAEPRYEPYNPTANQDYQRNGKSYKIVQDPSNFSQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127  81 GFAAIYDAEPNSNLTASGETFDPTQLTAAHPTLPIPSYARITNLANGRMIVVRINDRGPYGNDRVISLSRASADRLNTSN 160
Cdd:PRK10672  81 GLAAIYDAEAGSNLTASGERFDPNALTAAHPTLPIPSYVRVTNLANGRMIVVRINDRGPYGPGRVIDLSRAAADRLNTSN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127 161 NTKVRIDPIIVAPDGSLSGPGMACTTVAKQTYALPARPNLDGGDATGMNQPAP---ADVRPISNSTLKPEDSVGAPVNSG 237
Cdd:PRK10672 161 NTKVRIDPIIVAPDGSLSGPGTAGTTVAKQSYALPARPDLSGGMGTPSVQPAPapqGDVLPVSNSTLKSEDPTGAPVTSS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127 238 GFLGAPTPLNSGVLESSEPAATTAATAAPAAAVATQTAPVTAPGSIqgsvaataataatasavaasstatssaSGNFVVQ 317
Cdd:PRK10672 241 GFLGAPTTLAPGVLEGSEPTPTAPSSAPATAPAAAAPQAAATSSSA---------------------------SGNFVVQ 293

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496081127 318 VGAVSDQARAQQYQQRLSQQFSVPGRVTQNGAVWRIQLGPFADKAQASAVQQRLQSEAQLQSFITRAN 385
Cdd:PRK10672 294 VGAVSDQQRAQQWQQSLSQRFGVPGRVTQNGAVYRVQLGPFASRQQASALQQRLQTEAQQQSFITTAQ 361
 
Name Accession Description Interval E-value
PRK10672 PRK10672
endolytic peptidoglycan transglycosylase RlpA;
1-385 0e+00

endolytic peptidoglycan transglycosylase RlpA;


Pssm-ID: 236733 [Multi-domain]  Cd Length: 361  Bit Score: 558.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127   1 MRKQWLGICIAAGLLAACSSDDVQQKTVSTPQPAVCNGPTVEISGADPQYETPNATANQDYERDGKSYKIVQDPANFTQA 80
Cdd:PRK10672   1 MRKQWLGIGIAAGLLAACTSDDGQQQTVSAPQPAVCNGPVVEISGAEPRYEPYNPTANQDYQRNGKSYKIVQDPSNFSQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127  81 GFAAIYDAEPNSNLTASGETFDPTQLTAAHPTLPIPSYARITNLANGRMIVVRINDRGPYGNDRVISLSRASADRLNTSN 160
Cdd:PRK10672  81 GLAAIYDAEAGSNLTASGERFDPNALTAAHPTLPIPSYVRVTNLANGRMIVVRINDRGPYGPGRVIDLSRAAADRLNTSN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127 161 NTKVRIDPIIVAPDGSLSGPGMACTTVAKQTYALPARPNLDGGDATGMNQPAP---ADVRPISNSTLKPEDSVGAPVNSG 237
Cdd:PRK10672 161 NTKVRIDPIIVAPDGSLSGPGTAGTTVAKQSYALPARPDLSGGMGTPSVQPAPapqGDVLPVSNSTLKSEDPTGAPVTSS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127 238 GFLGAPTPLNSGVLESSEPAATTAATAAPAAAVATQTAPVTAPGSIqgsvaataataatasavaasstatssaSGNFVVQ 317
Cdd:PRK10672 241 GFLGAPTTLAPGVLEGSEPTPTAPSSAPATAPAAAAPQAAATSSSA---------------------------SGNFVVQ 293

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496081127 318 VGAVSDQARAQQYQQRLSQQFSVPGRVTQNGAVWRIQLGPFADKAQASAVQQRLQSEAQLQSFITRAN 385
Cdd:PRK10672 294 VGAVSDQQRAQQWQQSLSQRFGVPGRVTQNGAVYRVQLGPFASRQQASALQQRLQTEAQQQSFITTAQ 361
RlpA COG0797
Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane ...
 55-176 6.99e-51

Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440560 [Multi-domain]  Cd Length: 133  Bit Score: 166.57  E-value: 6.99e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127  55 ATANQDYERDGKSYKIVQDPANFTQAGFAAIYDAEPNSNLTASGETFDPTQLTAAHPTLPIPSYARITNLANGRMIVVRI 134
Cdd:COG0797   10 GASGKPYTVRGKTYYPLAEASGYTETGLASWYGDKFHGRKTASGERYDPNALTAAHKTLPLGTYVRVTNLENGRSVVVRV 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 496081127 135 NDRGPYGNDRVISLSRASADRLNTSNNTKVRIDPIIVAPDGS 176
Cdd:COG0797   90 NDRGPFVKGRIIDLSYAAARKLGMLGKGVAPVRVEVLGPASL 131
DPBB_RlpA-like cd22268
double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar ...
 79-168 5.51e-36

double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar proteins; Endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A, RlpA) is a lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. It adopts a double-psi beta-barrel (DPBB) fold and is one of four SPOR-domain containing proteins in Escherichia coli (including FtsN, DedA and DamX) that bind peptidoglycan (PG) and are targeted to the septum during division. It directly interacts with the divisome protein FtsK in vitro, and deletion of the rlpA gene partially bypasses the requirement for functional FtsK, a large, multi-spanning membrane protein that facilitates double-stranded DNA translocation during division and sporulation in E. coli and Bacillus subtilis, respectively. In Pseudomonas aeruginosa, RlpA contributes to rod shape maintenance and daughter cell separation. The separation of daughter cells requires extensive PG remodeling. It has been suggested that amidases and RlpA work in tandem to degrade PG in the division septum and lateral wall to facilitate daughter cell separation.


Pssm-ID: 439248 [Multi-domain]  Cd Length: 92  Bit Score: 126.41  E-value: 5.51e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127  79 QAGFAAIYDAEPNSNLTASGETFDPTQLTAAHPTLPIPSYARITNLANGRMIVVRINDRGPYGNDRVISLSRASADRLN- 157
Cdd:cd22268    1 ETGKASWYGPGFHGRRTASGERYDPNALTAAHKTLPFGTKVRVTNLENGKSVVVRVNDRGPFVKGRIIDLSYAAAKKLGm 80

                         90
                 ....*....|..
gi 496081127 158 -TSNNTKVRIDP 168
Cdd:cd22268   81 lGAGVAPVRIEV 92
rlpA TIGR00413
rare lipoprotein A; This is a family of prokaryotic proteins with unknown function. ...
 81-196 5.79e-25

rare lipoprotein A; This is a family of prokaryotic proteins with unknown function. Lipoprotein annotation based on the presence of consensus lipoprotein signal sequence. Included in this family is the E. coli putative lipoprotein rlpA. [Cell envelope, Other]


Pssm-ID: 273065 [Multi-domain]  Cd Length: 208  Bit Score: 100.83  E-value: 5.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127   81 GFAAIYDAEPNSNLTASGETFDPTQLTAAHPTLPIPSYARITNLANGRMIVVRINDRGPYGNDRVISLSRASADRLN--T 158
Cdd:TIGR00413   1 GLASWYGPKFHGRKTANGEVYNMKALTAAHKTLPFNTYVKVTNLHNNRSVIVRINDRGPFSDDRIIDLSHAAAREIGliS 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 496081127  159 SNNTKVRIDPIIVAPDGSLSGPgmacttvAKQTYALPA 196
Cdd:TIGR00413  81 RGVGQVRIEVLHVAKNGNLSGA-------ATKTFNKQA 111
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 79-166 1.44e-21

Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Recent studies show that the full-length RlpA protein from Pseudomonas Aeruginosa is an outer membrane protein that is a lytic transglycolase with specificity for peptidoglycan lacking stem peptides. Residue D157 in UniProtKB:Q9X6V6 is critical for lytic activity.


Pssm-ID: 427248 [Multi-domain]  Cd Length: 82  Bit Score: 87.65  E-value: 1.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127   79 QAGFAAIYDaepnsNLTASGETFDPTQLTAAHPTLPIPSYARItnlANGRMIVVRINDRGPYGNDRVISLSRASADRLNT 158
Cdd:pfam03330   1 AAGSASLYN-----NGTACGECYDVRCLTAAHPTLPFGTYCRV---LSGRSVIVRITDRGPFPPGRHFDLSGAAFEKLAM 72


                  ....*...
gi 496081127  159 SNNTKVRI 166
Cdd:pfam03330  73 PRAGIVPV 80
 
Name Accession Description Interval E-value
PRK10672 PRK10672
endolytic peptidoglycan transglycosylase RlpA;
1-385 0e+00

endolytic peptidoglycan transglycosylase RlpA;


Pssm-ID: 236733 [Multi-domain]  Cd Length: 361  Bit Score: 558.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127   1 MRKQWLGICIAAGLLAACSSDDVQQKTVSTPQPAVCNGPTVEISGADPQYETPNATANQDYERDGKSYKIVQDPANFTQA 80
Cdd:PRK10672   1 MRKQWLGIGIAAGLLAACTSDDGQQQTVSAPQPAVCNGPVVEISGAEPRYEPYNPTANQDYQRNGKSYKIVQDPSNFSQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127  81 GFAAIYDAEPNSNLTASGETFDPTQLTAAHPTLPIPSYARITNLANGRMIVVRINDRGPYGNDRVISLSRASADRLNTSN 160
Cdd:PRK10672  81 GLAAIYDAEAGSNLTASGERFDPNALTAAHPTLPIPSYVRVTNLANGRMIVVRINDRGPYGPGRVIDLSRAAADRLNTSN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127 161 NTKVRIDPIIVAPDGSLSGPGMACTTVAKQTYALPARPNLDGGDATGMNQPAP---ADVRPISNSTLKPEDSVGAPVNSG 237
Cdd:PRK10672 161 NTKVRIDPIIVAPDGSLSGPGTAGTTVAKQSYALPARPDLSGGMGTPSVQPAPapqGDVLPVSNSTLKSEDPTGAPVTSS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127 238 GFLGAPTPLNSGVLESSEPAATTAATAAPAAAVATQTAPVTAPGSIqgsvaataataatasavaasstatssaSGNFVVQ 317
Cdd:PRK10672 241 GFLGAPTTLAPGVLEGSEPTPTAPSSAPATAPAAAAPQAAATSSSA---------------------------SGNFVVQ 293

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496081127 318 VGAVSDQARAQQYQQRLSQQFSVPGRVTQNGAVWRIQLGPFADKAQASAVQQRLQSEAQLQSFITRAN 385
Cdd:PRK10672 294 VGAVSDQQRAQQWQQSLSQRFGVPGRVTQNGAVYRVQLGPFASRQQASALQQRLQTEAQQQSFITTAQ 361
RlpA COG0797
Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane ...
 55-176 6.99e-51

Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440560 [Multi-domain]  Cd Length: 133  Bit Score: 166.57  E-value: 6.99e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127  55 ATANQDYERDGKSYKIVQDPANFTQAGFAAIYDAEPNSNLTASGETFDPTQLTAAHPTLPIPSYARITNLANGRMIVVRI 134
Cdd:COG0797   10 GASGKPYTVRGKTYYPLAEASGYTETGLASWYGDKFHGRKTASGERYDPNALTAAHKTLPLGTYVRVTNLENGRSVVVRV 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 496081127 135 NDRGPYGNDRVISLSRASADRLNTSNNTKVRIDPIIVAPDGS 176
Cdd:COG0797   90 NDRGPFVKGRIIDLSYAAARKLGMLGKGVAPVRVEVLGPASL 131
DPBB_RlpA-like cd22268
double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar ...
 79-168 5.51e-36

double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar proteins; Endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A, RlpA) is a lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. It adopts a double-psi beta-barrel (DPBB) fold and is one of four SPOR-domain containing proteins in Escherichia coli (including FtsN, DedA and DamX) that bind peptidoglycan (PG) and are targeted to the septum during division. It directly interacts with the divisome protein FtsK in vitro, and deletion of the rlpA gene partially bypasses the requirement for functional FtsK, a large, multi-spanning membrane protein that facilitates double-stranded DNA translocation during division and sporulation in E. coli and Bacillus subtilis, respectively. In Pseudomonas aeruginosa, RlpA contributes to rod shape maintenance and daughter cell separation. The separation of daughter cells requires extensive PG remodeling. It has been suggested that amidases and RlpA work in tandem to degrade PG in the division septum and lateral wall to facilitate daughter cell separation.


Pssm-ID: 439248 [Multi-domain]  Cd Length: 92  Bit Score: 126.41  E-value: 5.51e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127  79 QAGFAAIYDAEPNSNLTASGETFDPTQLTAAHPTLPIPSYARITNLANGRMIVVRINDRGPYGNDRVISLSRASADRLN- 157
Cdd:cd22268    1 ETGKASWYGPGFHGRRTASGERYDPNALTAAHKTLPFGTKVRVTNLENGKSVVVRVNDRGPFVKGRIIDLSYAAAKKLGm 80

                         90
                 ....*....|..
gi 496081127 158 -TSNNTKVRIDP 168
Cdd:cd22268   81 lGAGVAPVRIEV 92
rlpA TIGR00413
rare lipoprotein A; This is a family of prokaryotic proteins with unknown function. ...
 81-196 5.79e-25

rare lipoprotein A; This is a family of prokaryotic proteins with unknown function. Lipoprotein annotation based on the presence of consensus lipoprotein signal sequence. Included in this family is the E. coli putative lipoprotein rlpA. [Cell envelope, Other]


Pssm-ID: 273065 [Multi-domain]  Cd Length: 208  Bit Score: 100.83  E-value: 5.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127   81 GFAAIYDAEPNSNLTASGETFDPTQLTAAHPTLPIPSYARITNLANGRMIVVRINDRGPYGNDRVISLSRASADRLN--T 158
Cdd:TIGR00413   1 GLASWYGPKFHGRKTANGEVYNMKALTAAHKTLPFNTYVKVTNLHNNRSVIVRINDRGPFSDDRIIDLSHAAAREIGliS 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 496081127  159 SNNTKVRIDPIIVAPDGSLSGPgmacttvAKQTYALPA 196
Cdd:TIGR00413  81 RGVGQVRIEVLHVAKNGNLSGA-------ATKTFNKQA 111
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 79-166 1.44e-21

Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Recent studies show that the full-length RlpA protein from Pseudomonas Aeruginosa is an outer membrane protein that is a lytic transglycolase with specificity for peptidoglycan lacking stem peptides. Residue D157 in UniProtKB:Q9X6V6 is critical for lytic activity.


Pssm-ID: 427248 [Multi-domain]  Cd Length: 82  Bit Score: 87.65  E-value: 1.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081127   79 QAGFAAIYDaepnsNLTASGETFDPTQLTAAHPTLPIPSYARItnlANGRMIVVRINDRGPYGNDRVISLSRASADRLNT 158
Cdd:pfam03330   1 AAGSASLYN-----NGTACGECYDVRCLTAAHPTLPFGTYCRV---LSGRSVIVRITDRGPFPPGRHFDLSGAAFEKLAM 72


                  ....*...
gi 496081127  159 SNNTKVRI 166
Cdd:pfam03330  73 PRAGIVPV 80
SPOR pfam05036
SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell ...
 312-383 1.03e-06

SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.


Pssm-ID: 461531 [Multi-domain]  Cd Length: 76  Bit Score: 45.81  E-value: 1.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496081127  312 GNFVVQVGAVSDQARAQQYQQR-LSQQFSVPGRVTQNGA-VWRIQLGPFADKAQASAVQQRLQSEAQLQSFITR 383
Cdd:pfam05036   3 GGYYVQLGAFSNEANAEALAAKlRAKGFAAYVAVTSKGGgLYRVRVGPFASREEARAALKKLKALAGLSPFVVK 76
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
 312-383 1.12e-05

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 44.77  E-value: 1.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496081127 312 GNFVVQVGAVSDQARAQQYQ----QRLSQQFSVPgRVTQNGAVWRIQLGPFADKAQASAVQQRLQSEAQLQSFITR 383
Cdd:COG3147   64 GGWVVQLGAFSNEDNAKELVaklrAAGYPAYTEP-VTTGGGTLYRVRVGPFASRAEAEAALAKLKKLTGLKGFVVR 138
 
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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