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Conserved domains on  [gi|242397425|ref|NP_001156428|]
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coiled-coil domain-containing protein 138 [Mus musculus]

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 ...
 206-337 2.12e-04

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: 44.66  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425   206 KLQYETTAQKKFAEELQKREQFLAEREQLLFSHETALSKIKGVKEEVLTRFQILKEQHGTEIEHLTEALKEKNKENKRMR 285
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 242397425   286 SSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFMTVQR 337
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 206-337 2.12e-04

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: 44.66  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425   206 KLQYETTAQKKFAEELQKREQFLAEREQLLFSHETALSKIKGVKEEVLTRFQILKEQHGTEIEHLTEALKEKNKENKRMR 285
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 242397425   286 SSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFMTVQR 337
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
191-331 8.51e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 8.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425 191 HEINQIYDELyhihMKLQYETTAQKKFAEELQKREQFLAEREQLLFSHETALSKIKGVKEEVLTRFQILKEqhgtEIEHL 270
Cdd:PRK03918 207 REINEISSEL----PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK----EIEEL 278

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242397425 271 TEALKEKnKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYE 331
Cdd:PRK03918 279 EEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 198-336 1.05e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.40  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425  198 DELYHIHMKLQYETTAQKKFAE-------ELQKREQFLAEREQLLFSH---ETALSKIKGVKEEVLTRFQIL-KEQHGTE 266
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKfknnkevELEELKKILAEDEKLLDEKkqfEKIAEELKGKEQELIFLLQAReKEIHDLE 456

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242397425  267 IEHLTEALKEKN--KENKRMRSSFDTLRELNDNLRKQLNEVSEENKK-------MEIQAKRVQARLDNLQRKYEFMTVQ 336
Cdd:pfam05483 457 IQLTAIKTSEEHylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEltqeasdMTLELKKHQEDIINCKKQEERMLKQ 535
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
211-331 1.70e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425 211 TTAQKKFAEELQKREQFLAEREQLLFSHETALSKIKGVKEEVLTRFQILKEQHgTEIEHLTEALKEKNKENKRMRSSFDT 290
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE-EELEELNEQLQAAQAELAQAQEELES 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 242397425 291 LRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYE 331
Cdd:COG4372  106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA 146
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 249-311 5.59e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.39  E-value: 5.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242397425 249 KEEVLTRFQILKEQHGTEIEHLTEALKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKK 311
Cdd:cd22887    9 LEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDE 71
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 206-337 2.12e-04

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: 44.66  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425   206 KLQYETTAQKKFAEELQKREQFLAEREQLLFSHETALSKIKGVKEEVLTRFQILKEQHGTEIEHLTEALKEKNKENKRMR 285
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 242397425   286 SSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFMTVQR 337
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
191-331 8.51e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 8.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425 191 HEINQIYDELyhihMKLQYETTAQKKFAEELQKREQFLAEREQLLFSHETALSKIKGVKEEVLTRFQILKEqhgtEIEHL 270
Cdd:PRK03918 207 REINEISSEL----PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK----EIEEL 278

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242397425 271 TEALKEKnKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYE 331
Cdd:PRK03918 279 EEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 198-336 1.05e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.40  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425  198 DELYHIHMKLQYETTAQKKFAE-------ELQKREQFLAEREQLLFSH---ETALSKIKGVKEEVLTRFQIL-KEQHGTE 266
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKfknnkevELEELKKILAEDEKLLDEKkqfEKIAEELKGKEQELIFLLQAReKEIHDLE 456

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242397425  267 IEHLTEALKEKN--KENKRMRSSFDTLRELNDNLRKQLNEVSEENKK-------MEIQAKRVQARLDNLQRKYEFMTVQ 336
Cdd:pfam05483 457 IQLTAIKTSEEHylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEltqeasdMTLELKKHQEDIINCKKQEERMLKQ 535
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
211-331 1.70e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425 211 TTAQKKFAEELQKREQFLAEREQLLFSHETALSKIKGVKEEVLTRFQILKEQHgTEIEHLTEALKEKNKENKRMRSSFDT 290
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE-EELEELNEQLQAAQAELAQAQEELES 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 242397425 291 LRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYE 331
Cdd:COG4372  106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA 146
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 211-328 1.84e-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: 41.58  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425   211 TTAQKKFAEELQKREQFLAEREQLlfshETALSKIKGVKEEVLTRF-QILKEQHGTEIEHLTEALKEKNKENKRMRSSFD 289
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERL----EARLERLEDRRERLQQEIeELLKKLEEAELKELQAELEELEEELEELQEELE 457

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 242397425   290 TLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQR 328
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
192-338 3.26e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425 192 EINQIYDELYHIHMKLQYETTAQKKFAEELQKREQFLAEREQLLFSHETALSKIKGVKEEVLTRFQILKEqhgtEIEHLT 271
Cdd:COG4372   39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE----EAEELQ 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242397425 272 EALKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFMTVQRL 338
Cdd:COG4372  115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
181-329 4.08e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425 181 KVSKKQGLLPHEINQIYDELYHIHMKLQYETT---AQKKFAEELQKREQFLAEREQLLFSHE---TALSKIKGVKEEVLT 254
Cdd:COG1340   99 KELAELNKAGGSIDKLRKEIERLEWRQQTEVLspeEEKELVEKIKELEKELEKAKKALEKNEklkELRAELKELRKEAEE 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425 255 RFQILKE------QHGTEIEHLTEALKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQR 328
Cdd:COG1340  179 IHKKIKElaeeaqELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKR 258


                 .
gi 242397425 329 K 329
Cdd:COG1340  259 E 259
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 192-333 4.58e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425  192 EINQIYDELYHIHMKLQYETTAQKKFAEELQKREQFLAEREQLLFSHETALSKIK------GVKEEVLTRFQILKEQHGT 265
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfelkkeNLEKEIDEKNKEIEELKQT 576

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242397425  266 ------EIEHLTEALKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFM 333
Cdd:TIGR04523 577 qkslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 249-311 5.59e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.39  E-value: 5.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242397425 249 KEEVLTRFQILKEQHGTEIEHLTEALKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKK 311
Cdd:cd22887    9 LEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDE 71
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 205-318 8.65e-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: 38.98  E-value: 8.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242397425 205 MKLQYETTAQKKFAEELQKREQFLAEREQLLFSHETALSKIKGVKEEVLTRFQILKEQHGTEIEHLTEALKEKNKENKRM 284
Cdd:COG4942  139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218

                         90       100       110
                 ....*....|....*....|....*....|....
gi 242397425 285 RSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKR 318
Cdd:COG4942  219 QQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
 
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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