NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|949496168|ref|WP_056938714|]
View 

glucosaminidase domain-containing protein [Lentilactobacillus buchneri]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK06347 super family cl32140
1,4-beta-N-acetylmuramoylhydrolase;
19-208 5.70e-42

1,4-beta-N-acetylmuramoylhydrolase;


The actual alignment was detected with superfamily member PRK06347:

Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 151.00  E-value: 5.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  19 ANHSHASVETdFINQLKTPVVKISKANHLYPSVMMAQAIVESDFGRSELSLDAN-NYFGVKGAYNGQSVTMSTGEYTSKG 97
Cdd:PRK06347 143 ALRSGATVQS-FIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNyNLFGIKGAYNGQSYTKQTLEDDGKG 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  98 KHYMTAAAFKKYPSVEASIKDNAYLLRHGTLSDPNYYEGTWTTNAISSSDAAMALSLTYATDMNYGNKLNAIITKYDLNK 177
Cdd:PRK06347 222 NYYTITAKFRKYPSYHQSLEDYAQVIRKGPSWNPNYYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQ 301

                        170       180       190
                 ....*....|....*....|....*....|.
gi 949496168 178 LDGSVSTGDIGSKIDASLNKQLAGDSKKSAL 208
Cdd:PRK06347 302 YDSGKTTGGNSGSTGNSSNSSNTGNTSNAKI 332
 
Name Accession Description Interval E-value
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
19-208 5.70e-42

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 151.00  E-value: 5.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  19 ANHSHASVETdFINQLKTPVVKISKANHLYPSVMMAQAIVESDFGRSELSLDAN-NYFGVKGAYNGQSVTMSTGEYTSKG 97
Cdd:PRK06347 143 ALRSGATVQS-FIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNyNLFGIKGAYNGQSYTKQTLEDDGKG 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  98 KHYMTAAAFKKYPSVEASIKDNAYLLRHGTLSDPNYYEGTWTTNAISSSDAAMALSLTYATDMNYGNKLNAIITKYDLNK 177
Cdd:PRK06347 222 NYYTITAKFRKYPSYHQSLEDYAQVIRKGPSWNPNYYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQ 301

                        170       180       190
                 ....*....|....*....|....*....|.
gi 949496168 178 LDGSVSTGDIGSKIDASLNKQLAGDSKKSAL 208
Cdd:PRK06347 302 YDSGKTTGGNSGSTGNSSNSSNTGNTSNAKI 332
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 29-177 1.53e-39

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 138.18  E-value: 1.53e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  29 DFINQLKTPVVKISKANHLYPSVMMAQAIVESDFGRSELS-LDANNYFGVKGAYN--GQSVTMSTGEYtSKGKHYMTAAA 105
Cdd:COG1705  131 EFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELDgSPSNNLFGIKAGGSwqGKSVEVTTTEY-VNGKAVKIKAR 209

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949496168 106 FKKYPSVEASIKDNAYLLRHgtlsdPNYYEGTWtTNAISSSDAAMALSL-TYATDMNYGNKLNAIITKYDLNK 177
Cdd:COG1705  210 FRAYDSYAESFRDYARLLKN-----NPRYAGAL-ANAKDYEAFAKALQKaGYATDPKYADKLISIIESYNLTQ 276
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 29-180 6.55e-29

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 106.75  E-value: 6.55e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168    29 DFINQLKTPVVKISKANHLYPSVMMAQAIVESDFGRSELSLDANNYFGVKGAYNGQSVTMSTGEYTSKGKHYMTaAAFKK 108
Cdd:smart00047  10 EFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKGAYDGRPVRMGTLEYLNGGWVTVK-AAFRG 88

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949496168   109 YPSveASIKDNAYLLRHGTLsdpnYYEGTWTTNAIsssdaamaLSLTYATDMNYGNKLNAIITKYDLnKLDG 180
Cdd:smart00047  89 YFG--EKFIDYAYVLRGQNP----LYKKRWGSNAL--------QTAGYATDPDYAKKLIRIIALYDE-KLKG 145
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 39-118 8.24e-21

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 83.78  E-value: 8.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168   39 VKISKANHLYPSVMMAQAIVESDFGRSELSLDANNYFGVKGAYNGQsVTMSTGEYTSKgkhymtaAAFKKYPSVEASIKD 118
Cdd:pfam01832   5 IEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKASWKGK-VAYDTDEVTVA-------ARFRKYDSVEESIRD 76
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 50-179 3.64e-17

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 79.40  E-value: 3.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  50 SVMMAQAIVESDFGRSELSLDANNYFGVK--GAYNGQSV---TMSTGEYTSKGKHYMTAAAFKKYPSVEASIKDNAYLLR 124
Cdd:NF038016 183 SVTIAQAILESGWGRSGLTREDHNYFGIKcfGSPGPIAVgcrSYATFECSPTGGCFDTTATFRAYASAADSFRDHGRFLS 262

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949496168 125 hgtlsdpnyyegTWttnaiSSSDAAMALS------------LTYATDMNYGNKLNAIITKYDLNKLD 179
Cdd:NF038016 263 ------------VN-----SRYAPAFAYTddpdqfareihkAGYATDPTYADKLIGLMKQYNLYQYD 312
 
Name Accession Description Interval E-value
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
19-208 5.70e-42

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 151.00  E-value: 5.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  19 ANHSHASVETdFINQLKTPVVKISKANHLYPSVMMAQAIVESDFGRSELSLDAN-NYFGVKGAYNGQSVTMSTGEYTSKG 97
Cdd:PRK06347 143 ALRSGATVQS-FIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNyNLFGIKGAYNGQSYTKQTLEDDGKG 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  98 KHYMTAAAFKKYPSVEASIKDNAYLLRHGTLSDPNYYEGTWTTNAISSSDAAMALSLTYATDMNYGNKLNAIITKYDLNK 177
Cdd:PRK06347 222 NYYTITAKFRKYPSYHQSLEDYAQVIRKGPSWNPNYYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQ 301

                        170       180       190
                 ....*....|....*....|....*....|.
gi 949496168 178 LDGSVSTGDIGSKIDASLNKQLAGDSKKSAL 208
Cdd:PRK06347 302 YDSGKTTGGNSGSTGNSSNSSNTGNTSNAKI 332
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 29-177 1.53e-39

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 138.18  E-value: 1.53e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  29 DFINQLKTPVVKISKANHLYPSVMMAQAIVESDFGRSELS-LDANNYFGVKGAYN--GQSVTMSTGEYtSKGKHYMTAAA 105
Cdd:COG1705  131 EFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELDgSPSNNLFGIKAGGSwqGKSVEVTTTEY-VNGKAVKIKAR 209

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949496168 106 FKKYPSVEASIKDNAYLLRHgtlsdPNYYEGTWtTNAISSSDAAMALSL-TYATDMNYGNKLNAIITKYDLNK 177
Cdd:COG1705  210 FRAYDSYAESFRDYARLLKN-----NPRYAGAL-ANAKDYEAFAKALQKaGYATDPKYADKLISIIESYNLTQ 276
PRK08581 PRK08581
amidase domain-containing protein;
28-179 3.22e-39

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 143.77  E-value: 3.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  28 TDFINQLKTPVVKISKANHLYPSVMMAQAIVESDFGRSELSLDAN-NYFGVKGAYNGQSVTMSTGEYTSkGKHYMTAAAF 106
Cdd:PRK08581 321 RQFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAKSPNhNLFGIKGAYEGNSVSFNTLEADG-NQLYSINAGF 399

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949496168 107 KKYPSVEASIKDNAYLLRHGTLSDPNYYEGTWTTNAISSSDAAMALSLTYATDMNYGNKLNAIITKYDLNKLD 179
Cdd:PRK08581 400 RKYPSTKESLEDYADLIKNGIDGNSTIYKPTWKSEAKSYKDATSHLSKTYATDPNYAKKLNSIIKHYNLTQFD 472
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 29-180 6.55e-29

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 106.75  E-value: 6.55e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168    29 DFINQLKTPVVKISKANHLYPSVMMAQAIVESDFGRSELSLDANNYFGVKGAYNGQSVTMSTGEYTSKGKHYMTaAAFKK 108
Cdd:smart00047  10 EFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKGAYDGRPVRMGTLEYLNGGWVTVK-AAFRG 88

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949496168   109 YPSveASIKDNAYLLRHGTLsdpnYYEGTWTTNAIsssdaamaLSLTYATDMNYGNKLNAIITKYDLnKLDG 180
Cdd:smart00047  89 YFG--EKFIDYAYVLRGQNP----LYKKRWGSNAL--------QTAGYATDPDYAKKLIRIIALYDE-KLKG 145
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 39-118 8.24e-21

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 83.78  E-value: 8.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168   39 VKISKANHLYPSVMMAQAIVESDFGRSELSLDANNYFGVKGAYNGQsVTMSTGEYTSKgkhymtaAAFKKYPSVEASIKD 118
Cdd:pfam01832   5 IEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKASWKGK-VAYDTDEVTVA-------ARFRKYDSVEESIRD 76
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 50-179 3.64e-17

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 79.40  E-value: 3.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  50 SVMMAQAIVESDFGRSELSLDANNYFGVK--GAYNGQSV---TMSTGEYTSKGKHYMTAAAFKKYPSVEASIKDNAYLLR 124
Cdd:NF038016 183 SVTIAQAILESGWGRSGLTREDHNYFGIKcfGSPGPIAVgcrSYATFECSPTGGCFDTTATFRAYASAADSFRDHGRFLS 262

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949496168 125 hgtlsdpnyyegTWttnaiSSSDAAMALS------------LTYATDMNYGNKLNAIITKYDLNKLD 179
Cdd:NF038016 263 ------------VN-----SRYAPAFAYTddpdqfareihkAGYATDPTYADKLIGLMKQYNLYQYD 312
flgJ PRK12712
flagellar rod assembly protein/muramidase FlgJ; Provisional
 22-172 1.73e-11

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139172 [Multi-domain]  Cd Length: 344  Bit Score: 63.10  E-value: 1.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  22 SHASVetdFINQLKTPVVKISKANHLYPSVMMAQAIVESDFGRSELS-LDAN---NYFGVKGAYN--GQSVTMSTGEYTS 95
Cdd:PRK12712 195 AHVSA---FVARMAGPAEAASRASGVPARLIVGQAALESGWGRREIThADGSttfNVFGIKAGANwkGRVAEVTTTEYVD 271

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949496168  96 kGKHYMTAAAFKKYPSVEASIKDNAYLLRhgtlSDPNYyegTWTTNAISSSDAAMALSLT-YATDMNYGNKLNAIITK 172
Cdd:PRK12712 272 -GQPQKVRARFRAYGSYDEACADYARLLT----SNPRY---AGVVSAASADEAAHGLQRAgYATDPAYGHKLVKIMKK 341
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
29-170 3.29e-10

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 59.12  E-value: 3.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  29 DFINQLKTPVVKISKANHLYPSVMMAQAIVESDFGRSEL-------SldaNNYFGVK--GAYNGQSVTMSTGEYtSKGKH 99
Cdd:PRK05684 154 DFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREIrtadgspS---HNLFGIKadGSWKGPVTEITTTEY-ENGVA 229

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949496168 100 YMTAAAFKKYPSVEASIKDNAYLLRHGtlsdPNYyegTWTTNAISSSDAAMAL-SLTYATDMNYGNKLNAII 170
Cdd:PRK05684 230 VKVKAAFRVYDSYLESFNDYVSLLTNN----PRY---AAVTQAASPEQFARALqDAGYATDPNYARKLVSVI 294
flgJ PRK12711
flagellar assembly peptidoglycan hydrolase FlgJ;
49-169 1.83e-07

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 237180 [Multi-domain]  Cd Length: 392  Bit Score: 51.50  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  49 PSVMMAQAIVESDFGRSEL--SLDANNYFGVKG-AYNGQSVTMSTGEYTSKGKHYMTaAAFKKYPSVEASIKDNAYLLRh 125
Cdd:PRK12711 237 PRALVAQAALETGWGRRGIgnGGDSNNLFGIKAtGWNGDKVTTGTHEYVNGVKTTET-ADFRAYGSAEESFADYVRLLK- 314

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 949496168 126 gtlSDPNYYEGTWTTNAISSSDAAMALSlTYATDMNYGNKLNAI 169
Cdd:PRK12711 315 ---NNSRYQQALQAGTDIKGFARGLQQA-GYATDPGYAAKIAAI 354
flgJ PRK12710
flagellar rod assembly protein/muramidase FlgJ; Provisional
 25-177 3.21e-06

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139170 [Multi-domain]  Cd Length: 291  Bit Score: 47.48  E-value: 3.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  25 SVETDFINQLKTPVVKISKANHLYPSVMMAQAIVESDFG----RSELSLDANNYFGVKGAYNGQ--SVTMSTGEYTSKGK 98
Cdd:PRK12710 128 SVVDDFVKSVWPTAKQAASLIGLDPKLLVAQAALETGWGkfvtRDADGSSSNNLFNIKTGSHSEveSIQVKTTEYIADTP 207

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949496168  99 HYMTAAaFKKYPSVEASIKDNAYLLRhgtlsDPNYYEGTWTTNAISSSDAAMALSLTYATDMNYGNKLNAIITKYDLNK 177
Cdd:PRK12710 208 IKINAS-FRKYPSIEHSFHDYVSLIK-----GSERYQMALANAENPEIYVSELNKAGYATDPNYSNKILSIYHGDELNQ 280
Bax COG2992
Uncharacterized FlgJ-related protein [General function prediction only];
49-125 2.88e-04

Uncharacterized FlgJ-related protein [General function prediction only];


Pssm-ID: 442231  Cd Length: 253  Bit Score: 41.06  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496168  49 PSVMMAQAIVESDFGRSELSLDANNYFG----VKGayNGqSVTMSTGEytsKGKHYmtaaaFKKYPSVEASIKdnAYLL- 123
Cdd:COG2992  121 PSLVLAQAANESGWGTSRFAREGNNLFGqwcfSKG--CG-LVPKQRDE---GANHE-----VAKFDSPQASVR--SYMLn 187


                 ....
gi 949496168 124 --RH 125
Cdd:COG2992  188 lnTH 191
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH