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Conserved domains on  [gi|1831506634|ref|NP_001367140|]
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Leucine zipper protein 1 [Caenorhabditis elegans]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1-217 1.36e-06

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.61  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634   1 MRNWPLFVFLICLVLFFYAFYVYQAQGEvLSQTNEEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNE 80
Cdd:COG4942     1 MRKLLLLALLLALAAAAQADAAAEAEAE-LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634  81 ECMTSLRNTKLRVDTLEKDGKSNTDNYTKM---------QEELSAL--KEKAEELQRNNTALNSLVSTQAQLINQLNQTI 149
Cdd:COG4942    80 ALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831506634 150 GIIQFEKEELKNAAHlnnltpKIEKPKDKQAEEQNA-EEQHKEKEVTVTTVTTQHSREEAQVKEDNQAQ 217
Cdd:COG4942   160 AELAALRAELEAERA------ELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQEA 222
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1-217 1.36e-06

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: 48.61  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634   1 MRNWPLFVFLICLVLFFYAFYVYQAQGEvLSQTNEEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNE 80
Cdd:COG4942     1 MRKLLLLALLLALAAAAQADAAAEAEAE-LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634  81 ECMTSLRNTKLRVDTLEKDGKSNTDNYTKM---------QEELSAL--KEKAEELQRNNTALNSLVSTQAQLINQLNQTI 149
Cdd:COG4942    80 ALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831506634 150 GIIQFEKEELKNAAHlnnltpKIEKPKDKQAEEQNA-EEQHKEKEVTVTTVTTQHSREEAQVKEDNQAQ 217
Cdd:COG4942   160 AELAALRAELEAERA------ELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQEA 222
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
35-193 1.22e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634  35 EEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNEECMTSLRNTKLRVDTLEKDGKSNTDNYTKMQEEL 114
Cdd:PRK02224  279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634 115 SALKEKAEELQRNNTALNSLVSTQAQLINQLNQTI---------GIIQFEKEELKNAAHLNNLTPKIEKPKDKQAEEQNA 185
Cdd:PRK02224  359 EELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438

                  ....*...
gi 1831506634 186 EEQHKEKE 193
Cdd:PRK02224  439 RERVEEAE 446
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-217 9.84e-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: 37.34  E-value: 9.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634   30 LSQTNEEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNEECMTSLRNTKLRVDTLEKDGKSNTD---- 105
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEklee 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634  106 ---NYTKMQEELSALKEKAEELQRNNTALNSLVSTQAQLINQLNQTIGIIQFEKEELKN-----AAHLNNLTPKIEKPKD 177
Cdd:TIGR02168  349 lkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEArlerlEDRRERLQQEIEELLK 428
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1831506634  178 KQAEEQNAEEQHKEKEVTVTTVTTQHSREEAQVKEDNQAQ 217
Cdd:TIGR02168  429 KLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1-217 1.36e-06

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: 48.61  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634   1 MRNWPLFVFLICLVLFFYAFYVYQAQGEvLSQTNEEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNE 80
Cdd:COG4942     1 MRKLLLLALLLALAAAAQADAAAEAEAE-LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634  81 ECMTSLRNTKLRVDTLEKDGKSNTDNYTKM---------QEELSAL--KEKAEELQRNNTALNSLVSTQAQLINQLNQTI 149
Cdd:COG4942    80 ALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831506634 150 GIIQFEKEELKNAAHlnnltpKIEKPKDKQAEEQNA-EEQHKEKEVTVTTVTTQHSREEAQVKEDNQAQ 217
Cdd:COG4942   160 AELAALRAELEAERA------ELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQEA 222
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
35-193 1.22e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634  35 EEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNEECMTSLRNTKLRVDTLEKDGKSNTDNYTKMQEEL 114
Cdd:PRK02224  279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634 115 SALKEKAEELQRNNTALNSLVSTQAQLINQLNQTI---------GIIQFEKEELKNAAHLNNLTPKIEKPKDKQAEEQNA 185
Cdd:PRK02224  359 EELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438

                  ....*...
gi 1831506634 186 EEQHKEKE 193
Cdd:PRK02224  439 RERVEEAE 446
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-217 9.84e-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: 37.34  E-value: 9.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634   30 LSQTNEEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNEECMTSLRNTKLRVDTLEKDGKSNTD---- 105
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEklee 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506634  106 ---NYTKMQEELSALKEKAEELQRNNTALNSLVSTQAQLINQLNQTIGIIQFEKEELKN-----AAHLNNLTPKIEKPKD 177
Cdd:TIGR02168  349 lkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEArlerlEDRRERLQQEIEELLK 428
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1831506634  178 KQAEEQNAEEQHKEKEVTVTTVTTQHSREEAQVKEDNQAQ 217
Cdd:TIGR02168  429 KLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
 
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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