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Conserved domains on  [gi|24663548|ref|NP_648609|]
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uncharacterized protein Dmel_CG10943 [Drosophila melanogaster]

Protein Classification

CALCOCO1 superfamily-containing protein( domain architecture ID 1001507)

CALCOCO1 superfamily-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CALCOCO1 super family cl37761
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
7-209 6.73e-04

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.


The actual alignment was detected with superfamily member pfam07888:

Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.03  E-value: 6.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548     7 LENKLRDMEFKLAIANEKLAIFDDKIKD---KNEIIEALKMSNNLYKSDYKDRFDAQASIIEKLEEELSTLRKAKLNSSQ 83
Cdd:pfam07888  71 WERQRRELESRVAELKEELRQSREKHEEleeKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERET 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548    84 DLETTKNKSKlrSTIFFFKESEKEKKLLISSLEAQIKEKAKTEIEnsqlIKSLKSQIGDNDVKLKDKQDLIATLEARLKE 163
Cdd:pfam07888 151 ELERMKERAK--KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE----FQELRNSLAQRDTQVLQLQDTITTLTQKLTT 224
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 24663548   164 SDSKNIENEHMIQSLSVKMCRIISEEKEYKSLIATLKNQIGQKSET 209
Cdd:pfam07888 225 AHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270
 
Name Accession Description Interval E-value
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
7-209 6.73e-04

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: 41.03  E-value: 6.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548     7 LENKLRDMEFKLAIANEKLAIFDDKIKD---KNEIIEALKMSNNLYKSDYKDRFDAQASIIEKLEEELSTLRKAKLNSSQ 83
Cdd:pfam07888  71 WERQRRELESRVAELKEELRQSREKHEEleeKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERET 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548    84 DLETTKNKSKlrSTIFFFKESEKEKKLLISSLEAQIKEKAKTEIEnsqlIKSLKSQIGDNDVKLKDKQDLIATLEARLKE 163
Cdd:pfam07888 151 ELERMKERAK--KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE----FQELRNSLAQRDTQVLQLQDTITTLTQKLTT 224
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 24663548   164 SDSKNIENEHMIQSLSVKMCRIISEEKEYKSLIATLKNQIGQKSET 209
Cdd:pfam07888 225 AHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
64-300 3.33e-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: 39.28  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548     64 IEKLEEELSTLR------KAKLNSSQDL--ETTKNKSKLRSTIFFFKESEKEKKLLISSLEAQIKEKAKTEIENSQLIKS 135
Cdd:TIGR02169  683 LEGLKRELSSLQselrriENRLDELSQElsDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548    136 LKSQIGDNDVKLKDKQDLIATLEARLKESDSKNIEN-------------------EHMIQSLSVKMCRIISEEKEYKSLI 196
Cdd:TIGR02169  763 LEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelskleeevsriearlreiEQKLNRLTLEKEYLEKEIQELQEQR 842
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548    197 ATLKNQIGQKSETLEKNKGIITSLKAQIKEKDKINGENSKVIANHKAQIKEKDDQITYLELGLNLETCKTREKDELLNDQ 276
Cdd:TIGR02169  843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
                          250       260
                   ....*....|....*....|....
gi 24663548    277 AAtimKLQSNQERVKETHKLIPSE 300
Cdd:TIGR02169  923 KA---KLEALEEELSEIEDPKGED 943
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
59-256 3.98e-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: 3.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548  59 AQASIIEKLEEELSTLRKAKLNSSQDLETTKNKsklrstifffkesekekkllISSLEAQIKEKAKTEIENSQLIKSLKS 138
Cdd:COG4942  17 AQADAAAEAEAELEQLQQEIAELEKELAALKKE--------------------EKALLKQLAALERRIAALARRIRALEQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548 139 QIGDNDVKLKDKQDLIATLEARLKE---------------------------SDSKNIEN-----EHMIQSLSVKMCRII 186
Cdd:COG4942  77 ELAALEAELAELEKEIAELRAELEAqkeelaellralyrlgrqpplalllspEDFLDAVRrlqylKYLAPARREQAEELR 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548 187 SEEKEYKSLIATLKNQIGQKSETLEKNKGIITSLKAQIKEKDKINGENSKVIANHKAQIKEKDDQITYLE 256
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
25-279 6.57e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 37.98  E-value: 6.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548   25 LAIFDDKIKDknEIIEALKMSNNLYKSDYKDRFdaQASIIEKLEEELSTLRKA--KLNSSQDLETTKNKSKLRSTIFFFK 102
Cdd:PRK05771  10 LIVTLKSYKD--EVLEALHELGVVHIEDLKEEL--SNERLRKLRSLLTKLSEAldKLRSYLPKLNPLREEKKKVSVKSLE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548  103 ESEKEKKLLISSLEAQIKEKAKTEIENSQLIKSLKSQI------GDNDVKLKDKQDL------IATLEARLKESDSKNIE 170
Cdd:PRK05771  86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIerlepwGNFDLDLSLLLGFkyvsvfVGTVPEDKLEELKLESD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548  171 NEHMIqslsvkmcrIISEEKEYK-SLIATLKNQIGQKSETLEKN---------KGIITSLKAQIKEK-DKINGENSKVia 239
Cdd:PRK05771 166 VENVE---------YISTDKGYVyVVVVVLKELSDEVEEELKKLgferleleeEGTPSELIREIKEElEEIEKERESL-- 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 24663548  240 nhKAQIKEKDDQITYLELGLNLETCKTREKDELLNDQAAT 279
Cdd:PRK05771 235 --LEELKELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
 
Name Accession Description Interval E-value
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
7-209 6.73e-04

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: 41.03  E-value: 6.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548     7 LENKLRDMEFKLAIANEKLAIFDDKIKD---KNEIIEALKMSNNLYKSDYKDRFDAQASIIEKLEEELSTLRKAKLNSSQ 83
Cdd:pfam07888  71 WERQRRELESRVAELKEELRQSREKHEEleeKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERET 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548    84 DLETTKNKSKlrSTIFFFKESEKEKKLLISSLEAQIKEKAKTEIEnsqlIKSLKSQIGDNDVKLKDKQDLIATLEARLKE 163
Cdd:pfam07888 151 ELERMKERAK--KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE----FQELRNSLAQRDTQVLQLQDTITTLTQKLTT 224
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 24663548   164 SDSKNIENEHMIQSLSVKMCRIISEEKEYKSLIATLKNQIGQKSET 209
Cdd:pfam07888 225 AHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
64-300 3.33e-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: 39.28  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548     64 IEKLEEELSTLR------KAKLNSSQDL--ETTKNKSKLRSTIFFFKESEKEKKLLISSLEAQIKEKAKTEIENSQLIKS 135
Cdd:TIGR02169  683 LEGLKRELSSLQselrriENRLDELSQElsDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548    136 LKSQIGDNDVKLKDKQDLIATLEARLKESDSKNIEN-------------------EHMIQSLSVKMCRIISEEKEYKSLI 196
Cdd:TIGR02169  763 LEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelskleeevsriearlreiEQKLNRLTLEKEYLEKEIQELQEQR 842
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548    197 ATLKNQIGQKSETLEKNKGIITSLKAQIKEKDKINGENSKVIANHKAQIKEKDDQITYLELGLNLETCKTREKDELLNDQ 276
Cdd:TIGR02169  843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
                          250       260
                   ....*....|....*....|....
gi 24663548    277 AAtimKLQSNQERVKETHKLIPSE 300
Cdd:TIGR02169  923 KA---KLEALEEELSEIEDPKGED 943
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
59-256 3.98e-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: 3.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548  59 AQASIIEKLEEELSTLRKAKLNSSQDLETTKNKsklrstifffkesekekkllISSLEAQIKEKAKTEIENSQLIKSLKS 138
Cdd:COG4942  17 AQADAAAEAEAELEQLQQEIAELEKELAALKKE--------------------EKALLKQLAALERRIAALARRIRALEQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548 139 QIGDNDVKLKDKQDLIATLEARLKE---------------------------SDSKNIEN-----EHMIQSLSVKMCRII 186
Cdd:COG4942  77 ELAALEAELAELEKEIAELRAELEAqkeelaellralyrlgrqpplalllspEDFLDAVRrlqylKYLAPARREQAEELR 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548 187 SEEKEYKSLIATLKNQIGQKSETLEKNKGIITSLKAQIKEKDKINGENSKVIANHKAQIKEKDDQITYLE 256
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
25-279 6.57e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 37.98  E-value: 6.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548   25 LAIFDDKIKDknEIIEALKMSNNLYKSDYKDRFdaQASIIEKLEEELSTLRKA--KLNSSQDLETTKNKSKLRSTIFFFK 102
Cdd:PRK05771  10 LIVTLKSYKD--EVLEALHELGVVHIEDLKEEL--SNERLRKLRSLLTKLSEAldKLRSYLPKLNPLREEKKKVSVKSLE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548  103 ESEKEKKLLISSLEAQIKEKAKTEIENSQLIKSLKSQI------GDNDVKLKDKQDL------IATLEARLKESDSKNIE 170
Cdd:PRK05771  86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIerlepwGNFDLDLSLLLGFkyvsvfVGTVPEDKLEELKLESD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663548  171 NEHMIqslsvkmcrIISEEKEYK-SLIATLKNQIGQKSETLEKN---------KGIITSLKAQIKEK-DKINGENSKVia 239
Cdd:PRK05771 166 VENVE---------YISTDKGYVyVVVVVLKELSDEVEEELKKLgferleleeEGTPSELIREIKEElEEIEKERESL-- 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 24663548  240 nhKAQIKEKDDQITYLELGLNLETCKTREKDELLNDQAAT 279
Cdd:PRK05771 235 --LEELKELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
 
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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