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Conserved domains on  [gi|50927086|gb|AAH79324|]
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LOC361776 [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 5.42e-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: 5.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086     17 AEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQACEA 96
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086     97 IkkktTEQEERFIKEITDFNDnyEITKKRDALMEEDIKL-----EMADLENQAEALRGEMKSMEYnsgQLQELQKLKSEL 171
Cdd:TIGR02168  745 L----EERIAQLSKELTELEA--EIEELEERLEEAEEELaeaeaEIEELEAQIEQLKEELKALRE---ALDELRAELTLL 815
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 50927086    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 5.42e-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: 5.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086     17 AEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQACEA 96
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086     97 IkkktTEQEERFIKEITDFNDnyEITKKRDALMEEDIKL-----EMADLENQAEALRGEMKSMEYnsgQLQELQKLKSEL 171
Cdd:TIGR02168  745 L----EERIAQLSKELTELEA--EIEELEERLEEAEEELaeaeaEIEELEAQIEQLKEELKALRE---ALDELRAELTLL 815
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 50927086    172 LQELFTLQKKLKVLKDEETEAICITKHLEAEKIKIRE 208
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
15-250 4.11e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 4.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086  15 HQAEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQAc 94
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER- 310
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086  95 eaiKKKTTEQEERFIKEITDFNDNYEITKKRDALMEEDIKLEMADLENQAEALRGEMKSMEYNSGQLQELQKLKSELLQE 174
Cdd:COG1196 311 ---RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50927086 175 LFTLQKKLKVLKDEETEAICITKHLEAEKIKIREKPQHDPECVRRLKRELDLYKEEDMESVCRALQIEVDLLESTL 250
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
CagA_N pfam18971
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...
37-171 6.46e-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: 6.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086    37 KIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENaleRQCSAIVserdrLLQACEAIKKKTTEQEERFIKEITDFN 116
Cdd:pfam18971 632 EVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEAN---RDARAIA-----YTQNLKGIKRELSDKLEKISKDLKDFS 703
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 50927086   117 ---DNYEITKKRDalmeedikleMADLENQAEALRGEMKSMEYNSGQLQELQKLKSEL 171
Cdd:pfam18971 704 ksfDEFKNGKNKD----------FSKAEETLKALKGSVKDLGINPEWISKVENLNAAL 751
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
17-208 5.42e-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: 5.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086     17 AEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQACEA 96
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086     97 IkkktTEQEERFIKEITDFNDnyEITKKRDALMEEDIKL-----EMADLENQAEALRGEMKSMEYnsgQLQELQKLKSEL 171
Cdd:TIGR02168  745 L----EERIAQLSKELTELEA--EIEELEERLEEAEEELaeaeaEIEELEAQIEQLKEELKALRE---ALDELRAELTLL 815
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 50927086    172 LQELFTLQKKLKVLKDEETEAICITKHLEAEKIKIRE 208
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
15-250 4.11e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 4.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086  15 HQAEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQAc 94
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER- 310
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086  95 eaiKKKTTEQEERFIKEITDFNDNYEITKKRDALMEEDIKLEMADLENQAEALRGEMKSMEYNSGQLQELQKLKSELLQE 174
Cdd:COG1196 311 ---RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50927086 175 LFTLQKKLKVLKDEETEAICITKHLEAEKIKIREKPQHDPECVRRLKRELDLYKEEDMESVCRALQIEVDLLESTL 250
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
16-225 2.74e-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: 38.59  E-value: 2.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086  16 QAEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENALERQCSAIVSERDRLLQACE 95
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086  96 AIKKKTTEQ-----------EERFIKEITDFNDNYEITKKRDALMEEDiklemadlENQAEALRGEMKSMEYNSGQLQEL 164
Cdd:COG4942 101 AQKEELAELlralyrlgrqpPLALLLSPEDFLDAVRRLQYLKYLAPAR--------REQAEELRADLAELAALRAELEAE 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50927086 165 QKLKSELLQELFTLQKKLKVLKDEETEAIcitKHLEAEKIKIREKPQHDPECVRRLKRELD 225
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIA 230
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
10-209 2.75e-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: 2.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086  10 IIFTEHQAEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLESKVQQFSEktfLLELLKTRENALERQcSAIVSERDR 89
Cdd:COG3883  18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK---LQAEIAEAEAEIEER-REELGERAR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086  90 LLQaceaIKKKTTEQEERFI--KEITDFNDNYEITKK---RDALMEEDIKLEMADLENQAEALRGEMKSMEynsGQLQEL 164
Cdd:COG3883  94 ALY----RSGGSVSYLDVLLgsESFSDFLDRLSALSKiadADADLLEELKADKAELEAKKAELEAKLAELE---ALKAEL 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 50927086 165 QKLKSELLQELFTLQKKLKVLKDEETEAICITKHLEAEKIKIREK 209
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
CagA_N pfam18971
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...
37-171 6.46e-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: 6.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086    37 KIKKATEDLNEEKIKLESKVQQFSEKTFLLELLKTRENaleRQCSAIVserdrLLQACEAIKKKTTEQEERFIKEITDFN 116
Cdd:pfam18971 632 EVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEAN---RDARAIA-----YTQNLKGIKRELSDKLEKISKDLKDFS 703
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 50927086   117 ---DNYEITKKRDalmeedikleMADLENQAEALRGEMKSMEYNSGQLQELQKLKSEL 171
Cdd:pfam18971 704 ksfDEFKNGKNKD----------FSKAEETLKALKGSVKDLGINPEWISKVENLNAAL 751
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
12-175 8.38e-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: 8.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086   12 FTEHQAEESRRVMREVRSEIARCRGKIKKATEDLNEEKIKLES-KVQQFSEKTFLLELLKTRENALERQCSAIVSERDRL 90
Cdd:COG4913  285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARL 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50927086   91 LQACEAIKKKTTEQEERF---IKEITDFNDNYEITKKRDALMEEDIKLEMADLENQAEALRGEMKSMEYNSGQL-QELQK 166
Cdd:COG4913  365 EALLAALGLPLPASAEEFaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIpARLLA 444

                 ....*....
gi 50927086  167 LKSELLQEL 175
Cdd:COG4913  445 LRDALAEAL 453
 
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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