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Conserved domains on  [gi|115532338|ref|NP_001040684|]
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Si:ch211-1a19.3 [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, ...
21-237 4.95e-07

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: 50.15  E-value: 4.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338  21 MRNWPLFVFLICLVLFFYAFYVYQAQGEvLSQTNEEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNE 100
Cdd:COG4942    1 MRKLLLLALLLALAAAAQADAAAEAEAE-LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338 101 ECMTSLRNTKLRVDTLEKDGKSNTDNYTKM---------QEELSAL--KEKAEELQRNNTALNSLVSTQAQLINQLNQTI 169
Cdd:COG4942   80 ALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115532338 170 GIIQFEKEELKNAAHlnnltpKIEKPKDKQAEEQNA-EEQHKEKEVTVTTVTTQHSREEAQVKEDNQAQ 237
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, ...
21-237 4.95e-07

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: 50.15  E-value: 4.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338  21 MRNWPLFVFLICLVLFFYAFYVYQAQGEvLSQTNEEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNE 100
Cdd:COG4942    1 MRKLLLLALLLALAAAAQADAAAEAEAE-LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338 101 ECMTSLRNTKLRVDTLEKDGKSNTDNYTKM---------QEELSAL--KEKAEELQRNNTALNSLVSTQAQLINQLNQTI 169
Cdd:COG4942   80 ALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115532338 170 GIIQFEKEELKNAAHlnnltpKIEKPKDKQAEEQNA-EEQHKEKEVTVTTVTTQHSREEAQVKEDNQAQ 237
Cdd:COG4942  160 AELAALRAELEAERA------ELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQEA 222
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
55-213 8.63e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 8.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338  55 EEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNEECMTSLRNTKLRVDTLEKDGKSNTDNYTKMQEEL 134
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338 135 SALKEKAEELQRNNTALNSLVSTQAQLINQLNQTI---------GIIQFEKEELKNAAHLNNLTPKIEKPKDKQAEEQNA 205
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438

                 ....*...
gi 115532338 206 EEQHKEKE 213
Cdd:PRK02224 439 RERVEEAE 446
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
50-237 5.39e-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: 38.11  E-value: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338    50 LSQTNEEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNEECMTSLRNTKLRVDTLEKDGKSNTD---- 125
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEklee 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338   126 ---NYTKMQEELSALKEKAEELQRNNTALNSLVSTQAQLINQLNQTIGIIQFEKEELKN-----AAHLNNLTPKIEKPKD 197
Cdd:TIGR02168  349 lkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEArlerlEDRRERLQQEIEELLK 428
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 115532338   198 KQAEEQNAEEQHKEKEVTVTTVTTQHSREEAQVKEDNQAQ 237
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, ...
21-237 4.95e-07

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: 50.15  E-value: 4.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338  21 MRNWPLFVFLICLVLFFYAFYVYQAQGEvLSQTNEEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNE 100
Cdd:COG4942    1 MRKLLLLALLLALAAAAQADAAAEAEAE-LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338 101 ECMTSLRNTKLRVDTLEKDGKSNTDNYTKM---------QEELSAL--KEKAEELQRNNTALNSLVSTQAQLINQLNQTI 169
Cdd:COG4942   80 ALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115532338 170 GIIQFEKEELKNAAHlnnltpKIEKPKDKQAEEQNA-EEQHKEKEVTVTTVTTQHSREEAQVKEDNQAQ 237
Cdd:COG4942  160 AELAALRAELEAERA------ELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQEA 222
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
55-213 8.63e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 8.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338  55 EEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNEECMTSLRNTKLRVDTLEKDGKSNTDNYTKMQEEL 134
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338 135 SALKEKAEELQRNNTALNSLVSTQAQLINQLNQTI---------GIIQFEKEELKNAAHLNNLTPKIEKPKDKQAEEQNA 205
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438

                 ....*...
gi 115532338 206 EEQHKEKE 213
Cdd:PRK02224 439 RERVEEAE 446
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
50-268 3.79e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.34  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338  50 LSQTNEEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNEECMTSLRNTKLRVDTLEKDGKSNTDNYTK 129
Cdd:COG4372   40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338 130 MQEELSALKEKAEELQRNNTALNSLVSTQAQLINQLNQTigiIQFEKEELKNAAHLNNLTPKIEKPKDKQAEEQNAEEQH 209
Cdd:COG4372  120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ---LESLQEELAALEQELQALSEAEAEQALDELLKEANRNA 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 115532338 210 KEKEVTVTTVTTQHSREEAQVKEDNQAQSTTTVTSTESPVGKLDEKNPEIEEPEPIVAE 268
Cdd:COG4372  197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
50-237 5.39e-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: 38.11  E-value: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338    50 LSQTNEEVRQLSAQLSLTKGKLVGSMADLESANSEKKSVSIQLDDITKKNEECMTSLRNTKLRVDTLEKDGKSNTD---- 125
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEklee 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338   126 ---NYTKMQEELSALKEKAEELQRNNTALNSLVSTQAQLINQLNQTIGIIQFEKEELKN-----AAHLNNLTPKIEKPKD 197
Cdd:TIGR02168  349 lkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEArlerlEDRRERLQQEIEELLK 428
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 115532338   198 KQAEEQNAEEQHKEKEVTVTTVTTQHSREEAQVKEDNQAQ 237
Cdd:TIGR02168  429 KLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
50-236 8.22e-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: 37.74  E-value: 8.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338    50 LSQTNEEVRQLSAQLSLTKGKlvgsMADLESANSEKKSVSIQLDDITKKNEECMTSLRNtklRVDTLEKDGKSNTDNYTK 129
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAE----IEELEREIEEERKRRDKLTEEYAELKEELEDLRA---ELEEVDKEFAETRDELKD 389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532338   130 MQEELSALKEKAEELQRNNTALNSLVSTQAQLINQLNQTI-----GIIQFEKEELKNAAHLNNLTPKIEKPKDKQAEEQN 204
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIagieaKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
                          170       180       190
                   ....*....|....*....|....*....|..
gi 115532338   205 AEEQHKEKEVTVTTVTTQHSREEAQVKEDNQA 236
Cdd:TIGR02169  470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
 
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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