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Conserved domains on  [gi|189409150|ref|NP_057494|]
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charged multivesicular body protein 5 isoform 1 [Homo sapiens]

Protein Classification

SNF7 family protein( domain architecture ID 229656)

SNF7 family protein may be involved in protein sorting and transport from the endosome to the vacuole/lysosome

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00464 super family cl21588
SNF-7-like protein; Provisional
1-201 1.88e-74

SNF-7-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00464:

Pssm-ID: 473916 [Multi-domain]  Cd Length: 211  Bit Score: 223.93  E-value: 1.88e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150   1 MNRLFGKAKpKAPPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMReGPAKNMVKQKALRVLKQKRMYEQQRD 80
Cdd:PTZ00464   1 MNRLFGKKN-KTPKPTLEDASKRIGGRSEVVDARINKIDAELMKLKEQIQRTR-GMTQSRHKQRAMQLLQQKRMYQNQQD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150  81 NLAQQSFNMEQANYTIQSLKDTKTTVDAMKLGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGTPE-LD 159
Cdd:PTZ00464  79 MMMQQQFNMDQLQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDdID 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 189409150 160 EDDLEAELDALGDELLADEDSSYLDEAASAP-AIPEGVPTDTK 201
Cdd:PTZ00464 159 EDEMLGELDALDFDMEKEADASYLADALAVPgTKLPDVPTDEK 201
 
Name Accession Description Interval E-value
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
1-201 1.88e-74

SNF-7-like protein; Provisional


Pssm-ID: 240425 [Multi-domain]  Cd Length: 211  Bit Score: 223.93  E-value: 1.88e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150   1 MNRLFGKAKpKAPPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMReGPAKNMVKQKALRVLKQKRMYEQQRD 80
Cdd:PTZ00464   1 MNRLFGKKN-KTPKPTLEDASKRIGGRSEVVDARINKIDAELMKLKEQIQRTR-GMTQSRHKQRAMQLLQQKRMYQNQQD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150  81 NLAQQSFNMEQANYTIQSLKDTKTTVDAMKLGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGTPE-LD 159
Cdd:PTZ00464  79 MMMQQQFNMDQLQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDdID 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 189409150 160 EDDLEAELDALGDELLADEDSSYLDEAASAP-AIPEGVPTDTK 201
Cdd:PTZ00464 159 EDEMLGELDALDFDMEKEADASYLADALAVPgTKLPDVPTDEK 201
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
13-195 9.63e-46

Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.


Pssm-ID: 460896 [Multi-domain]  Cd Length: 168  Bit Score: 149.31  E-value: 9.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150   13 PPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMRegpaknmvkqkALRVLKQKRMYEQQRDNLAQQSFNMEQA 92
Cdd:pfam03357   2 AIRSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDA-----------ALLLLKQKKRYEKQLDQLDGQLSNLEQQ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150   93 NYTIQSLKDTKTTVDAMKLGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGT-PELDEDDLEAELDALG 171
Cdd:pfam03357  71 RMAIENAKSNQEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDaDEEDEEELDAELDALL 150
                         170       180
                  ....*....|....*....|....
gi 189409150  172 DELLAdedssylDEAASAPAIPEG 195
Cdd:pfam03357 151 DEIGD-------EESVELPSAPSG 167
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
27-189 2.09e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150   27 RAESIDKKISRLDAELVKYKDQIKKMregpaknmvkQKALRVLKQKRMYEQQRDNLAQQSFNMEQANYTIQSLKDTKTTV 106
Cdd:COG4913   611 KLAALEAELAELEEELAEAEERLEAL----------EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL 680
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150  107 DAMKLGVKEMKKAYKQVKIdQIEDLQDQLEDMMEDAN-----------EIQEALSRSYGTPELDEDDLEAELDALGDELL 175
Cdd:COG4913   681 DASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGrlekeleqaeeELDELQDRLEAAEDLARLELRALLEERFAAAL 759
                         170
                  ....*....|....
gi 189409150  176 ADEDSSYLDEAASA 189
Cdd:COG4913   760 GDAVERELRENLEE 773
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
27-173 2.72e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.50  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150    27 RAESIDKKISRLDAELVKYKDQIKKMREGPAKNmvkQKALRVLKQKRMYEQQRdnLAQQSFNMEQANYTIQSLK----DT 102
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERLEEA---EEELAEAEAEIEELEAQ--IEQLKEELKALREALDELRaeltLL 815
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189409150   103 KTTVDAMKLGVKEMKKAyKQVKIDQIEDLQDQLEDMmedaNEIQEALSRSYGTPELDEDDLEAELDALGDE 173
Cdd:TIGR02168  816 NEEAANLRERLESLERR-IAATERRLEDLEEQIEEL----SEDIESLAAEIEELEELIEELESELEALLNE 881
 
Name Accession Description Interval E-value
PTZ00464 PTZ00464
SNF-7-like protein; Provisional
1-201 1.88e-74

SNF-7-like protein; Provisional


Pssm-ID: 240425 [Multi-domain]  Cd Length: 211  Bit Score: 223.93  E-value: 1.88e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150   1 MNRLFGKAKpKAPPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMReGPAKNMVKQKALRVLKQKRMYEQQRD 80
Cdd:PTZ00464   1 MNRLFGKKN-KTPKPTLEDASKRIGGRSEVVDARINKIDAELMKLKEQIQRTR-GMTQSRHKQRAMQLLQQKRMYQNQQD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150  81 NLAQQSFNMEQANYTIQSLKDTKTTVDAMKLGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGTPE-LD 159
Cdd:PTZ00464  79 MMMQQQFNMDQLQFTTESVKDTKVQVDAMKQAAKTLKKQFKKLNVDKVEDLQDELADLYEDTQEIQEIMGRAYDVPDdID 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 189409150 160 EDDLEAELDALGDELLADEDSSYLDEAASAP-AIPEGVPTDTK 201
Cdd:PTZ00464 159 EDEMLGELDALDFDMEKEADASYLADALAVPgTKLPDVPTDEK 201
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
13-195 9.63e-46

Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.


Pssm-ID: 460896 [Multi-domain]  Cd Length: 168  Bit Score: 149.31  E-value: 9.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150   13 PPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMRegpaknmvkqkALRVLKQKRMYEQQRDNLAQQSFNMEQA 92
Cdd:pfam03357   2 AIRSLRKAIRKLDKKQESLEKKIEKLELEIKKLAKKGNKDA-----------ALLLLKQKKRYEKQLDQLDGQLSNLEQQ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150   93 NYTIQSLKDTKTTVDAMKLGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGT-PELDEDDLEAELDALG 171
Cdd:pfam03357  71 RMAIENAKSNQEVLNAMKQGAKAMKAMNKLMDIDKIDKLMDEIEDQMEKADEISEMLSDPLDDaDEEDEEELDAELDALL 150
                         170       180
                  ....*....|....*....|....
gi 189409150  172 DELLAdedssylDEAASAPAIPEG 195
Cdd:pfam03357 151 DEIGD-------EESVELPSAPSG 167
PTZ00446 PTZ00446
vacuolar sorting protein SNF7-like; Provisional
35-178 5.31e-05

vacuolar sorting protein SNF7-like; Provisional


Pssm-ID: 240422 [Multi-domain]  Cd Length: 191  Bit Score: 42.40  E-value: 5.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150  35 ISRLDAELVKYKDQIKKMrEGPAKNMVKQKALR----VLKQKRMYEQQRDNLAQQSFNMEQANYTIQSLKDTKTTVDAMK 110
Cdd:PTZ00446  36 IDALEKKQVQVEKKIKQL-EIEAKQKVEQNQMSnakiLLKRKKLYEQEIENILNNRLTLEDNMINLENMHLHKIAVNALS 114
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189409150 111 LGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYgTPELDEDDLEAELDALGDELLADE 178
Cdd:PTZ00446 115 YAANTHKKLNNEINTQKVEKIIDTIQENKDIQEEINQALSFNL-LNNVDDDEIDKELDLLKEQTMEEK 181
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
27-189 2.09e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150   27 RAESIDKKISRLDAELVKYKDQIKKMregpaknmvkQKALRVLKQKRMYEQQRDNLAQQSFNMEQANYTIQSLKDTKTTV 106
Cdd:COG4913   611 KLAALEAELAELEEELAEAEERLEAL----------EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL 680
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150  107 DAMKLGVKEMKKAYKQVKIdQIEDLQDQLEDMMEDAN-----------EIQEALSRSYGTPELDEDDLEAELDALGDELL 175
Cdd:COG4913   681 DASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGrlekeleqaeeELDELQDRLEAAEDLARLELRALLEERFAAAL 759
                         170
                  ....*....|....
gi 189409150  176 ADEDSSYLDEAASA 189
Cdd:COG4913   760 GDAVERELRENLEE 773
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
27-173 2.72e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.50  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150    27 RAESIDKKISRLDAELVKYKDQIKKMREGPAKNmvkQKALRVLKQKRMYEQQRdnLAQQSFNMEQANYTIQSLK----DT 102
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERLEEA---EEELAEAEAEIEELEAQ--IEQLKEELKALREALDELRaeltLL 815
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189409150   103 KTTVDAMKLGVKEMKKAyKQVKIDQIEDLQDQLEDMmedaNEIQEALSRSYGTPELDEDDLEAELDALGDE 173
Cdd:TIGR02168  816 NEEAANLRERLESLERR-IAATERRLEDLEEQIEEL----SEDIESLAAEIEELEELIEELESELEALLNE 881
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
33-192 6.84e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.05  E-value: 6.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150  33 KKISRLDAELVKYKDQIKKMREGPAKNMVKQKALRVLKQKRMYEQQRDNLAQQsfnMEQANYTIQSLKDTKTTVDAMKLG 112
Cdd:COG4717   95 EELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER---LEELEERLEELRELEEELEELEAE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150 113 VKEMKKA-------YKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSygtpELDEDDLEAELDALGDELLADEDSSYLDE 185
Cdd:COG4717  172 LAELQEEleelleqLSLATEEELQDLAEELEELQQRLAELEEELEEA----QEELEELEEELEQLENELEAAALEERLKE 247

                 ....*..
gi 189409150 186 AASAPAI 192
Cdd:COG4717  248 ARLLLLI 254
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
21-174 6.97e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 36.67  E-value: 6.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150  21 IGTVDSRAESIDKKISRLDAELVKYKDQIKKMREGPAKNMVKQKALRVLKQKR----------MYEQQRDNLAQQSFNME 90
Cdd:COG4942   50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQkeelaellraLYRLGRQPPLALLLSPE 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150  91 QANYTIQSLKDTKTTVDAMKLGVKEMKKAYKQV--KIDQIEDLQDQLEDMMEDANEIQEALSRSYGTPELDEDDLEAELD 168
Cdd:COG4942  130 DFLDAVRRLQYLKYLAPARREQAEELRADLAELaaLRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209

                 ....*.
gi 189409150 169 ALGDEL 174
Cdd:COG4942  210 ELAAEL 215
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
21-203 7.09e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 36.73  E-value: 7.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150  21 IGTVDSRAESIDKKISRLDAELVKYKDQIKKMREGPAKNMVKQKALRVLKQKR---MYEQQRDN------LAQQSFN--- 88
Cdd:COG3883   39 LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraLYRSGGSVsyldvlLGSESFSdfl 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409150  89 ---------MEQANYTIQSLKDTKTTVDAMKLGVKEmKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGTPELD 159
Cdd:COG3883  119 drlsalskiADADADLLEELKADKAELEAKKAELEA-KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQ 197
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 189409150 160 EDDLEAELDALGDELLADEDSSYLDEAASAPAIPEGVPTDTKNK 203
Cdd:COG3883  198 LAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
 
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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