NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958758704|ref|XP_038955156|]
View 

coiled-coil domain-containing protein 138 isoform X4 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 44-187 6.73e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 6.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704   44 LLPHQINQIYDELFHIHMKLQNETAAQQKFAEELQKREQFLAEREQLLfrhETALSKIKGVKEEVLTRFQILKEQHSTEI 123
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL---EELNKKIKDLGEEEQLRVKEKIGELEAEI 303

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758704  124 EHLTETLKEKNKENKRMRssfDTLRELNDNLRKQLNEVSEENKKMEIQAKR---VQARLDNLQRKYE 187
Cdd:TIGR02169  304 ASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEIEELEREIEEERKRrdkLTEEYAELKEELE 367
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 44-187 6.73e-05

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: 45.83  E-value: 6.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704   44 LLPHQINQIYDELFHIHMKLQNETAAQQKFAEELQKREQFLAEREQLLfrhETALSKIKGVKEEVLTRFQILKEQHSTEI 123
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL---EELNKKIKDLGEEEQLRVKEKIGELEAEI 303

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758704  124 EHLTETLKEKNKENKRMRssfDTLRELNDNLRKQLNEVSEENKKMEIQAKR---VQARLDNLQRKYE 187
Cdd:TIGR02169  304 ASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEIEELEREIEEERKRrdkLTEEYAELKEELE 367
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-192 4.65e-04

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: 43.17  E-value: 4.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  54 DELFHIHMKLQNETAAQQKFAE-------ELQKREQFLAEREQLLFRH---ETALSKIKGVKEEVLTRFQIL-KEQHSTE 122
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKfknnkevELEELKKILAEDEKLLDEKkqfEKIAEELKGKEQELIFLLQAReKEIHDLE 456

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758704 123 IEHLTETLKEKN--KENKRMRSSFDTLRELNDNLRKQLNEVSEENKK-------MEIQAKRVQARLDNLQRKYEFMTVQ 192
Cdd:pfam05483 457 IQLTAIKTSEEHylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEltqeasdMTLELKKHQEDIINCKKQEERMLKQ 535
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 105-167 1.36e-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: 37.93  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958758704 105 KEEVLTRFQILKEQHSTEIEHLTETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKK 167
Cdd:cd22887     9 LEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDE 71
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
48-194 1.45e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  48 QINQIYDELFHIHMKLQNETAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEVLTRFQILKEQHSTeiehLT 127
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE----LQ 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758704 128 ETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFMTVQRL 194
Cdd:COG4372   115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
PRK12704 PRK12704
phosphodiesterase; Provisional
 49-180 1.91e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  49 INQIYDELFHIHMKLQNETAAQQKfaeELQKREQFLAEREQLLFRHETALSKikgvKEEVLtrfqilkEQHSTEIEHLTE 128
Cdd:PRK12704   59 LLEAKEEIHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDRKLELLEK----REEEL-------EKKEKELEQKQQ 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758704 129 TLKEKNKEnkrmrssfdtLRELNDNLRKQLNEVS----EENKKMEIQAKRVQARLD 180
Cdd:PRK12704  125 ELEKKEEE----------LEELIEEQLQELERISgltaEEAKEILLEKVEEEARHE 170
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 44-187 6.73e-05

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: 45.83  E-value: 6.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704   44 LLPHQINQIYDELFHIHMKLQNETAAQQKFAEELQKREQFLAEREQLLfrhETALSKIKGVKEEVLTRFQILKEQHSTEI 123
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL---EELNKKIKDLGEEEQLRVKEKIGELEAEI 303

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758704  124 EHLTETLKEKNKENKRMRssfDTLRELNDNLRKQLNEVSEENKKMEIQAKR---VQARLDNLQRKYE 187
Cdd:TIGR02169  304 ASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEIEELEREIEEERKRrdkLTEEYAELKEELE 367
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 48-193 1.11e-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: 45.05  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704   48 QINQIYDELFHI---HMKLQNETAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEVLTRFQILKEQHSTEIE 124
Cdd:TIGR02168  790 QIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758704  125 HLTETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFMTVQR 193
Cdd:TIGR02168  870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-192 4.65e-04

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: 43.17  E-value: 4.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  54 DELFHIHMKLQNETAAQQKFAE-------ELQKREQFLAEREQLLFRH---ETALSKIKGVKEEVLTRFQIL-KEQHSTE 122
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKfknnkevELEELKKILAEDEKLLDEKkqfEKIAEELKGKEQELIFLLQAReKEIHDLE 456

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758704 123 IEHLTETLKEKN--KENKRMRSSFDTLRELNDNLRKQLNEVSEENKK-------MEIQAKRVQARLDNLQRKYEFMTVQ 192
Cdd:pfam05483 457 IQLTAIKTSEEHylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEltqeasdMTLELKKHQEDIINCKKQEERMLKQ 535
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 48-187 5.63e-04

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: 42.75  E-value: 5.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704   48 QINQIYDELfhIHMKLQNETAAQQKFAEELQKREQFLAEREQ----LLFRHETALSKIKGVKEEVL----TRFQILKEQH 119
Cdd:TIGR02169  780 ALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrLTLEKEYLEKEIQELQEQRIdlkeQIKSIEKEIE 857

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  120 S--TEIEHLTETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYE 187
Cdd:TIGR02169  858 NlnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 67-184 9.66e-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: 41.97  E-value: 9.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704   67 TAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEVLTRfqiLKEQHSTEIEHLTETLKEKNKENKRMRSSFDT 146
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL---LKKLEEAELKELQAELEELEEELEELQEELER 458

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1958758704  147 LRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQR 184
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 105-167 1.36e-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: 37.93  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958758704 105 KEEVLTRFQILKEQHSTEIEHLTETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKK 167
Cdd:cd22887     9 LEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDE 71
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
48-194 1.45e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  48 QINQIYDELFHIHMKLQNETAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEVLTRFQILKEQHSTeiehLT 127
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE----LQ 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758704 128 ETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFMTVQRL 194
Cdd:COG4372   115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
PRK12704 PRK12704
phosphodiesterase; Provisional
 49-180 1.91e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  49 INQIYDELFHIHMKLQNETAAQQKfaeELQKREQFLAEREQLLFRHETALSKikgvKEEVLtrfqilkEQHSTEIEHLTE 128
Cdd:PRK12704   59 LLEAKEEIHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDRKLELLEK----REEEL-------EKKEKELEQKQQ 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758704 129 TLKEKNKEnkrmrssfdtLRELNDNLRKQLNEVS----EENKKMEIQAKRVQARLD 180
Cdd:PRK12704  125 ELEKKEEE----------LEELIEEQLQELERISgltaEEAKEILLEKVEEEARHE 170
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
40-185 2.19e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.28  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  40 KKQGLLPHQINQIYDELFHIHMKLQNE---TAAQQKFAEELQKREQFLAEREQLLFRHE---TALSKIKGVKEEVLTRFQ 113
Cdd:COG1340   102 AELNKAGGSIDKLRKEIERLEWRQQTEvlsPEEEKELVEKIKELEKELEKAKKALEKNEklkELRAELKELRKEAEEIHK 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758704 114 ILKE------QHSTEIEHLTETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRK 185
Cdd:COG1340   182 KIKElaeeaqELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKRE 259
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
67-187 2.44e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  67 TAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEvLTRFQILKEQHSTEIEHLTETLKEKNKENKRMRSSFDT 146
Cdd:COG4372    27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE-LEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958758704 147 LRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYE 187
Cdd:COG4372   106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA 146
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 50-187 2.83e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.49  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  50 NQIYDELFHI--HMKLQNETAAQQKF---------------AEELQKREQF-----------------LAEREQLLFRHE 95
Cdd:pfam17380 268 NEFLNQLLHIvqHQKAVSERQQQEKFekmeqerlrqekeekAREVERRRKLeeaekarqaemdrqaaiYAEQERMAMERE 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  96 TALSKIKgVKEEVLTRFQILKEQHSTEIEHLTETLK---EKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKME-IQ 171
Cdd:pfam17380 348 RELERIR-QEERKRELERIRQEEIAMEISRMRELERlqmERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEqIR 426

                         170
                  ....*....|....*.
gi 1958758704 172 AKRVQARLDNLQRKYE 187
Cdd:pfam17380 427 AEQEEARQREVRRLEE 442
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 70-225 3.59e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.88  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  70 QQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEVLTRFQILKEQHSTEIEHLTEtLKEKNKENKRMRSS----FD 145
Cdd:pfam07888  40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEE-LEEKYKELSASSEElseeKD 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704 146 TLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFMTVQRlkGDSHAAHE-----VKSSKQEKVPASKPFKA 220
Cdd:pfam07888 119 ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR--KEEEAERKqlqakLQQTEEELRSLSKEFQE 196


                  ....*
gi 1958758704 221 ALNGQ 225
Cdd:pfam07888 197 LRNSL 201
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 40-189 4.31e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  40 KKQGLLPHQINQIYDELFHIHMKLQNETAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKE-EVLTR-FQILKE 117
Cdd:COG1579    24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyEALQKeIESLKR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704 118 QHST----------EIEHLTETLKEKNKENKRMRSSFDTLRElndNLRKQLNEVSEENKKMEIQAKRVQARLD-NLQRKY 186
Cdd:COG1579   104 RISDledeilelmeRIEELEEELAELEAELAELEAELEEKKA---ELDEELAELEAELEELEAEREELAAKIPpELLALY 180


                  ...
gi 1958758704 187 EFM 189
Cdd:COG1579   181 ERI 183
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
47-187 5.20e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758704  47 HQINQIYDELfhihMKLQNETAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEVLTRFQILKEqhstEIEHL 126
Cdd:PRK03918  207 REINEISSEL----PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK----EIEEL 278

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958758704 127 TETLKEKnKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYE 187
Cdd:PRK03918  279 EEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH