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Conserved domains on  [gi|1958648070|ref|XP_038940666|]
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coiled-coil domain-containing protein 172 isoform X5 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
17-208 4.94e-07

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 4.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070   17 AEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQACEA 96
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070   97 IkkktTEQEERFIKEITDFNDnyEITKKRDALMEEDIKL-----EMADLENQAEALRGEMKSMEYnsgQLQELQKLKSEL 171
Cdd:TIGR02168  745 L----EERIAQLSKELTELEA--EIEELEERLEEAEEELaeaeaEIEELEAQIEQLKEELKALRE---ALDELRAELTLL 815
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1958648070  172 LQELFTLQKKLKVLKDEETEAICITKHLEAEKIKIRE 208
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
17-208 4.94e-07

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: 50.44  E-value: 4.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070   17 AEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQACEA 96
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070   97 IkkktTEQEERFIKEITDFNDnyEITKKRDALMEEDIKL-----EMADLENQAEALRGEMKSMEYnsgQLQELQKLKSEL 171
Cdd:TIGR02168  745 L----EERIAQLSKELTELEA--EIEELEERLEEAEEELaeaeaEIEELEAQIEQLKEELKALRE---ALDELRAELTLL 815
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1958648070  172 LQELFTLQKKLKVLKDEETEAICITKHLEAEKIKIRE 208
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
15-208 1.02e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070  15 HQAEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQAc 94
Cdd:COG1196   232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER- 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070  95 eaiKKKTTEQEERFIKEITDFNDNYEITKKRDALMEEDIKLEMADLENQAEALRGEMKSMEYNSGQLQELQKLKSELLQE 174
Cdd:COG1196   311 ---RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958648070 175 LFTLQKKLKVLKDEETEAICITKHLEAEKIKIRE 208
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
CagA_N pfam18971
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...
37-171 6.41e-03

CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.


Pssm-ID: 408741 [Multi-domain]  Cd Length: 876  Bit Score: 37.83  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070  37 KIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENaleRQCSAIVserdrLLQACEAIKKKTTEQEERFIKEITDFN 116
Cdd:pfam18971 632 EVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEAN---RDARAIA-----YTQNLKGIKRELSDKLEKISKDLKDFS 703
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958648070 117 ---DNYEITKKRDalmeedikleMADLENQAEALRGEMKSMEYNSGQLQELQKLKSEL 171
Cdd:pfam18971 704 ksfDEFKNGKNKD----------FSKAEETLKALKGSVKDLGINPEWISKVENLNAAL 751
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
43-209 9.10e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.35  E-value: 9.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070  43 EDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQACEAIKKKTTEQEERFIKEITDFNDNY--- 119
Cdd:PRK03918  528 EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYlel 607
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070 120 -------EITKKRDALMEEDIKL---EMADLENQAEALRGEMKSME--YNSGQLQELQKLKSELLQELFTLQKKLKVLKD 187
Cdd:PRK03918  608 kdaekelEREEKELKKLEEELDKafeELAETEKRLEELRKELEELEkkYSEEEYEELREEYLELSRELAGLRAELEELEK 687
                         170       180
                  ....*....|....*....|..
gi 1958648070 188 EETEAICITKHLEAEKIKIREK 209
Cdd:PRK03918  688 RREEIKKTLEKLKEELEEREKA 709
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
17-208 4.94e-07

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: 50.44  E-value: 4.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070   17 AEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQACEA 96
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070   97 IkkktTEQEERFIKEITDFNDnyEITKKRDALMEEDIKL-----EMADLENQAEALRGEMKSMEYnsgQLQELQKLKSEL 171
Cdd:TIGR02168  745 L----EERIAQLSKELTELEA--EIEELEERLEEAEEELaeaeaEIEELEAQIEQLKEELKALRE---ALDELRAELTLL 815
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1958648070  172 LQELFTLQKKLKVLKDEETEAICITKHLEAEKIKIRE 208
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
15-208 1.02e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070  15 HQAEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQAc 94
Cdd:COG1196   232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER- 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070  95 eaiKKKTTEQEERFIKEITDFNDNYEITKKRDALMEEDIKLEMADLENQAEALRGEMKSMEYNSGQLQELQKLKSELLQE 174
Cdd:COG1196   311 ---RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958648070 175 LFTLQKKLKVLKDEETEAICITKHLEAEKIKIRE 208
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
10-209 2.83e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070  10 IIFTEHQAEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEktfLLELLKTRENALERQcSAIVSERDR 89
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK---LQAEIAEAEAEIEER-REELGERAR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070  90 LLQaceaIKKKTTEQEERFI--KEITDFNDNYEITKK---RDALMEEDIKLEMADLENQAEALRGEMKSMEynsGQLQEL 164
Cdd:COG3883    94 ALY----RSGGSVSYLDVLLgsESFSDFLDRLSALSKiadADADLLEELKADKAELEAKKAELEAKLAELE---ALKAEL 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958648070 165 QKLKSELLQELFTLQKKLKVLKDEETEAICITKHLEAEKIKIREK 209
Cdd:COG3883   167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
26-233 4.80e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.13  E-value: 4.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070   26 EVRSEIARCRGKIKKATEDLNEEKIKLES-----KVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQACEAIKKK 100
Cdd:TIGR02169  755 NVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070  101 TTEQEERF------IKEITDFNDNYEITKKRDALMEEDIKLEMADLENQAEALRGEMKSMEYnsgQLQELQKLKSELLQE 174
Cdd:TIGR02169  835 IQELQEQRidlkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA---QLRELERKIEELEAQ 911
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958648070  175 LFTLQKKLKVLKDEETEAICITKHLEAEKIKIREKPQHDPECVRLKRELDlYKEEDMES 233
Cdd:TIGR02169  912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQ-RVEEEIRA 969
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
16-193 5.38e-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: 37.82  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070  16 QAEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQACE 95
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070  96 AIKKKTTEQ-----------EERFIKEITDFNDNYEITKKRDALMEEDiklemadlENQAEALRGEMKSMEYNSGQLQEL 164
Cdd:COG4942   101 AQKEELAELlralyrlgrqpPLALLLSPEDFLDAVRRLQYLKYLAPAR--------REQAEELRADLAELAALRAELEAE 172
                         170       180
                  ....*....|....*....|....*....
gi 1958648070 165 QKLKSELLQELFTLQKKLKVLKDEETEAI 193
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLL 201
CagA_N pfam18971
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...
37-171 6.41e-03

CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.


Pssm-ID: 408741 [Multi-domain]  Cd Length: 876  Bit Score: 37.83  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070  37 KIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENaleRQCSAIVserdrLLQACEAIKKKTTEQEERFIKEITDFN 116
Cdd:pfam18971 632 EVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEAN---RDARAIA-----YTQNLKGIKRELSDKLEKISKDLKDFS 703
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958648070 117 ---DNYEITKKRDalmeedikleMADLENQAEALRGEMKSMEYNSGQLQELQKLKSEL 171
Cdd:pfam18971 704 ksfDEFKNGKNKD----------FSKAEETLKALKGSVKDLGINPEWISKVENLNAAL 751
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
12-175 8.03e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.59  E-value: 8.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070   12 FTEHQAEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLES-KVQQFSEKTFLLELLKTRENALERQCSAIVSERDRL 90
Cdd:COG4913    285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARL 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070   91 LQACEAIKKKTTEQEERF---IKEITDFNDNYEITKKRDALMEEDIKLEMADLENQAEALRGEMKSMEYNSGQL-QELQK 166
Cdd:COG4913    365 EALLAALGLPLPASAEEFaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIpARLLA 444

                   ....*....
gi 1958648070  167 LKSELLQEL 175
Cdd:COG4913    445 LRDALAEAL 453
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
43-209 9.10e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.35  E-value: 9.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070  43 EDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQACEAIKKKTTEQEERFIKEITDFNDNY--- 119
Cdd:PRK03918  528 EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYlel 607
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648070 120 -------EITKKRDALMEEDIKL---EMADLENQAEALRGEMKSME--YNSGQLQELQKLKSELLQELFTLQKKLKVLKD 187
Cdd:PRK03918  608 kdaekelEREEKELKKLEEELDKafeELAETEKRLEELRKELEELEkkYSEEEYEELREEYLELSRELAGLRAELEELEK 687
                         170       180
                  ....*....|....*....|..
gi 1958648070 188 EETEAICITKHLEAEKIKIREK 209
Cdd:PRK03918  688 RREEIKKTLEKLKEELEEREKA 709
 
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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