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Conserved domains on  [gi|1207191292|ref|XP_021328597|]
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synergin gamma isoform X7 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 206-274 2.03e-12

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


:

Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 63.39  E-value: 2.03e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207191292  206 IPELFKKVLefTMTPAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIGVAQS 274
Cdd:cd00052      1 YDQIFRSLD--PDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
MAT1 super family cl44421
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
 99-197 5.65e-07

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


The actual alignment was detected with superfamily member pfam06391:

Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 51.47  E-value: 5.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292   99 ADIQKQMAEEHQKRLEQQQRMLEEDRKRRqfEEQKQKL--RLLSSVKP--KTGEKSRDDAL---EAIKGNLDGFSRDAKM 171
Cdd:pfam06391   96 EELLELEKREKEERRKEEKQEEEEEKEKK--EKAKQELidELMTSNKDaeEIIAQHKKTAKkrkSERRRKLEELNRVLEQ 173

                           90       100
                   ....*....|....*....|....*.
gi 1207191292  172 HPTPSSQSKKPGVGAYPQQDMQPMVP 197
Cdd:pfam06391  174 KPTQFSTGIKFGQLPVPKIEEGPLYP 199
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
233-542 3.14e-05

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK12323:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 700  Bit Score: 48.33  E-value: 3.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  233 ISSGLPREALGQI--------WALAN--RTTPGKLTKEE---LYTV-------LALIGVAQSGLTVMSLDILSQFPSPPV 292
Cdd:PRK12323   290 LASLLQKIALAQVvpaavqddWPEADdiRRLAGRFDAQEvqlFYQIanlgrseLALAPDEYAGFTMTLLRMLAFRPGQSG 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  293 PNlpamtmAIPAvlPQHQQPIMTQPPVSMPmPTAAPPVMSMTPNPPAQPPATFITNFPPVQATKADDDDFQDFQEAPKAG 372
Cdd:PRK12323   370 GG------AGPA--TAAAAPVAQPAPAAAA-PAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQAS 440

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  373 VGddsftdfqgetGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVSDSgdkysvfrelePP 452
Cdd:PRK12323   441 AR-----------GPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP-----------PP 498

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  453 SERKPvgEGFADFKSVSADDGFTDFKTADTVSPLDPPDQAKFQPTFPPPFASSQSLSHSQPASLAQPRNPlnmadlDLFT 532
Cdd:PRK12323   499 WEELP--PEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPP------RASA 570

                          330
                   ....*....|
gi 1207191292  533 TMAPPTSTAD 542
Cdd:PRK12323   571 SGLPDMFDGD 580
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 206-274 2.03e-12

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 63.39  E-value: 2.03e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207191292  206 IPELFKKVLefTMTPAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIGVAQS 274
Cdd:cd00052      1 YDQIFRSLD--PDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 223-282 1.00e-08

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 53.82  E-value: 1.00e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207191292   223 IDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIGVAQSGLTV-MSLD 282
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIpASLP 87
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
 99-197 5.65e-07

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 51.47  E-value: 5.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292   99 ADIQKQMAEEHQKRLEQQQRMLEEDRKRRqfEEQKQKL--RLLSSVKP--KTGEKSRDDAL---EAIKGNLDGFSRDAKM 171
Cdd:pfam06391   96 EELLELEKREKEERRKEEKQEEEEEKEKK--EKAKQELidELMTSNKDaeEIIAQHKKTAKkrkSERRRKLEELNRVLEQ 173

                           90       100
                   ....*....|....*....|....*.
gi 1207191292  172 HPTPSSQSKKPGVGAYPQQDMQPMVP 197
Cdd:pfam06391  174 KPTQFSTGIKFGQLPVPKIEEGPLYP 199
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 40-341 7.05e-07

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 53.47  E-value: 7.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292   40 MVQVMQPNMQGMMGMNFGAQMPGAMPIQGGMAMGMQTPGMQFMGQPQFMGMRAPGPQFPADIQKQMAEEHQKRLEQQQRM 119
Cdd:pfam09606  170 TPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQ 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  120 LeedrkrrqfEEQKQKLRLLSSVKPKTGEKSRDDALEAIKGNLDGFSRDAKMHPTPSSQSKKPGV-----GAYPQQDMQP 194
Cdd:pfam09606  250 Q---------QGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNyqqqqTRQQQQQQGG 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  195 MVPTWLYNDSLIPelfkkvleftMTPAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIGVAQS 274
Cdd:pfam09606  321 NHPAAHQQQMNQS----------VGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPN 390

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207191292  275 GLTVMSLDILSQFPSPPVPNLPAMTMA----IPAVLPQHQQPIMTQPPVSMPMPTAAPPVMSMTP-----NPPAQP 341
Cdd:pfam09606  391 QFMRQSPQPSVPSPQGPGSQPPQSHPGgmipSPALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPgqsavNSPLNP 466
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
233-542 3.14e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 48.33  E-value: 3.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  233 ISSGLPREALGQI--------WALAN--RTTPGKLTKEE---LYTV-------LALIGVAQSGLTVMSLDILSQFPSPPV 292
Cdd:PRK12323   290 LASLLQKIALAQVvpaavqddWPEADdiRRLAGRFDAQEvqlFYQIanlgrseLALAPDEYAGFTMTLLRMLAFRPGQSG 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  293 PNlpamtmAIPAvlPQHQQPIMTQPPVSMPmPTAAPPVMSMTPNPPAQPPATFITNFPPVQATKADDDDFQDFQEAPKAG 372
Cdd:PRK12323   370 GG------AGPA--TAAAAPVAQPAPAAAA-PAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQAS 440

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  373 VGddsftdfqgetGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVSDSgdkysvfrelePP 452
Cdd:PRK12323   441 AR-----------GPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP-----------PP 498

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  453 SERKPvgEGFADFKSVSADDGFTDFKTADTVSPLDPPDQAKFQPTFPPPFASSQSLSHSQPASLAQPRNPlnmadlDLFT 532
Cdd:PRK12323   499 WEELP--PEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPP------RASA 570

                          330
                   ....*....|
gi 1207191292  533 TMAPPTSTAD 542
Cdd:PRK12323   571 SGLPDMFDGD 580
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 262-357 3.50e-05

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 47.23  E-value: 3.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  262 LYTVLALIGVAQSGLTVMSLDILSQ---FPSPPVPNLPAMTMAIPAVLPQHQQPIMTQPPVSMPMPTAAPPvmSMTPNPP 338
Cdd:pfam07174   14 LWATLAIAAVAGASAVAVALPAVAHadpEPAPPPPSTATAPPAPPPPPPAPAAPAPPPPPAAPNAPNAPPP--PADPNAP 91

                           90
                   ....*....|....*....
gi 1207191292  339 AQPPATFITNFPPVQATKA 357
Cdd:pfam07174   92 PPPPADPNAPPPPAVDPNA 110
PRK04239 PRK04239
DNA-binding protein;
102-136 3.35e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.40  E-value: 3.35e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1207191292  102 QKQMAEEHQKRLEQQQRMLEEDRKRRQFEEQKQKL 136
Cdd:PRK04239     8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 290-356 7.89e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 41.70  E-value: 7.89e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207191292   290 PPVPNLPAMTMAIPavlPQHQQPIMTQPPVSMPMP----TAAPPVMSMTPNPPAqPPATFITNFPPVQATK 356
Cdd:smart00818   94 QPAQQPFQPQPLQP---PQPQQPMQPQPPVHPIPPlppqPPLPPMFPMQPLPPL-LPDLPLEAWPATDKTK 160
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 206-274 2.03e-12

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 63.39  E-value: 2.03e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207191292  206 IPELFKKVLefTMTPAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIGVAQS 274
Cdd:cd00052      1 YDQIFRSLD--PDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 223-282 1.00e-08

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 53.82  E-value: 1.00e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207191292   223 IDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIGVAQSGLTV-MSLD 282
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIpASLP 87
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
 99-197 5.65e-07

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 51.47  E-value: 5.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292   99 ADIQKQMAEEHQKRLEQQQRMLEEDRKRRqfEEQKQKL--RLLSSVKP--KTGEKSRDDAL---EAIKGNLDGFSRDAKM 171
Cdd:pfam06391   96 EELLELEKREKEERRKEEKQEEEEEKEKK--EKAKQELidELMTSNKDaeEIIAQHKKTAKkrkSERRRKLEELNRVLEQ 173

                           90       100
                   ....*....|....*....|....*.
gi 1207191292  172 HPTPSSQSKKPGVGAYPQQDMQPMVP 197
Cdd:pfam06391  174 KPTQFSTGIKFGQLPVPKIEEGPLYP 199
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 40-341 7.05e-07

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 53.47  E-value: 7.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292   40 MVQVMQPNMQGMMGMNFGAQMPGAMPIQGGMAMGMQTPGMQFMGQPQFMGMRAPGPQFPADIQKQMAEEHQKRLEQQQRM 119
Cdd:pfam09606  170 TPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQ 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  120 LeedrkrrqfEEQKQKLRLLSSVKPKTGEKSRDDALEAIKGNLDGFSRDAKMHPTPSSQSKKPGV-----GAYPQQDMQP 194
Cdd:pfam09606  250 Q---------QGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNyqqqqTRQQQQQQGG 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  195 MVPTWLYNDSLIPelfkkvleftMTPAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIGVAQS 274
Cdd:pfam09606  321 NHPAAHQQQMNQS----------VGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPN 390

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207191292  275 GLTVMSLDILSQFPSPPVPNLPAMTMA----IPAVLPQHQQPIMTQPPVSMPMPTAAPPVMSMTP-----NPPAQP 341
Cdd:pfam09606  391 QFMRQSPQPSVPSPQGPGSQPPQSHPGgmipSPALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPgqsavNSPLNP 466
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 102-135 1.88e-06

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 48.89  E-value: 1.88e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1207191292  102 QKQMAEEHQKRLEQQQRMLEEDRKRRQFEEQKQK 135
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
233-542 3.14e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 48.33  E-value: 3.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  233 ISSGLPREALGQI--------WALAN--RTTPGKLTKEE---LYTV-------LALIGVAQSGLTVMSLDILSQFPSPPV 292
Cdd:PRK12323   290 LASLLQKIALAQVvpaavqddWPEADdiRRLAGRFDAQEvqlFYQIanlgrseLALAPDEYAGFTMTLLRMLAFRPGQSG 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  293 PNlpamtmAIPAvlPQHQQPIMTQPPVSMPmPTAAPPVMSMTPNPPAQPPATFITNFPPVQATKADDDDFQDFQEAPKAG 372
Cdd:PRK12323   370 GG------AGPA--TAAAAPVAQPAPAAAA-PAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQAS 440

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  373 VGddsftdfqgetGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVSDSgdkysvfrelePP 452
Cdd:PRK12323   441 AR-----------GPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP-----------PP 498

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  453 SERKPvgEGFADFKSVSADDGFTDFKTADTVSPLDPPDQAKFQPTFPPPFASSQSLSHSQPASLAQPRNPlnmadlDLFT 532
Cdd:PRK12323   499 WEELP--PEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPP------RASA 570

                          330
                   ....*....|
gi 1207191292  533 TMAPPTSTAD 542
Cdd:PRK12323   571 SGLPDMFDGD 580
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 262-357 3.50e-05

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 47.23  E-value: 3.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  262 LYTVLALIGVAQSGLTVMSLDILSQ---FPSPPVPNLPAMTMAIPAVLPQHQQPIMTQPPVSMPMPTAAPPvmSMTPNPP 338
Cdd:pfam07174   14 LWATLAIAAVAGASAVAVALPAVAHadpEPAPPPPSTATAPPAPPPPPPAPAAPAPPPPPAAPNAPNAPPP--PADPNAP 91

                           90
                   ....*....|....*....
gi 1207191292  339 AQPPATFITNFPPVQATKA 357
Cdd:pfam07174   92 PPPPADPNAPPPPAVDPNA 110
PRK04239 PRK04239
DNA-binding protein;
102-136 3.35e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.40  E-value: 3.35e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1207191292  102 QKQMAEEHQKRLEQQQRMLEEDRKRRQFEEQKQKL 136
Cdd:PRK04239     8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
PHA03247 PHA03247
large tegument protein UL36; Provisional
 288-592 5.57e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 5.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  288 PSP---PVPNLPAMTM--AIPAVLPQHQQPIM----TQPPVSMPMPTAAPPVmSMTPNPPAQPPATFITNFPPVQATKAD 358
Cdd:PHA03247  2569 PPPrpaPRPSEPAVTSraRRPDAPPQSARPRApvddRGDPRGPAPPSPLPPD-THAPDPPPPSPSPAANEPDPHPPPTVP 2647

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  359 DDDFQDFQEAPKAgVGDDSFTDFQGETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVSD 438
Cdd:PHA03247  2648 PPERPRDDPAPGR-VSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPA 2726

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  439 SGdkysvfRELEPPSERKPVGEGFADFKSVSADDG--FTDFKTADTVSPLDPPDQAKF-QPTFPPPFASSQSLSH----- 510
Cdd:PHA03247  2727 AA------RQASPALPAAPAPPAVPAGPATPGGPArpARPPTTAGPPAPAPPAAPAAGpPRRLTRPAVASLSESReslps 2800

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  511 ----SQPASLAQPRNPLNMADLDLFTTMAPPTSTAdsklnlfPSAPPSLVLPSAVVKPPSMGGDDFGDFALFGSSSSSEV 586
Cdd:PHA03247  2801 pwdpADPPAAVLAPAAALPPAASPAGPLPPPTSAQ-------PTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAA 2873


                   ....*.
gi 1207191292  587 APTTSA 592
Cdd:PHA03247  2874 KPAAPA 2879
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 290-356 7.89e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 41.70  E-value: 7.89e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207191292   290 PPVPNLPAMTMAIPavlPQHQQPIMTQPPVSMPMP----TAAPPVMSMTPNPPAqPPATFITNFPPVQATK 356
Cdd:smart00818   94 QPAQQPFQPQPLQP---PQPQQPMQPQPPVHPIPPlppqPPLPPMFPMQPLPPL-LPDLPLEAWPATDKTK 160
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 285-640 1.44e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  285 SQFPSPPVPNLPAMTMAIPAVLPQHQQPIMTQPPVSMPMPTAAPPVMSMTPnppaqPPATFITNFPPVQATKADDddfqd 364
Cdd:pfam03154  307 SQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKP-----PPTTPIPQLPNPQSHKHPP----- 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  365 fqeapkagvgddsftdfqgETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVSDSGDKYS 444
Cdd:pfam03154  377 -------------------HLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQS 437

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  445 vfRELEPPSERKPVGEGFADFKSVS--ADDGFTDFKTADTVSPLDPPDQA-KFQPTFPPPFASSQSLSHSQPASLAQPRN 521
Cdd:pfam03154  438 --QSLPPPAASHPPTSGLHQVPSQSpfPQHPFVPGGPPPITPPSGPPTSTsSAMPGIQPPSSASVSSSGPVPAAVSCPLP 515

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  522 PLNMADLDLFTTMAPPTStadsklnlfPSAPPSLVLPSAVVKPPsmggddfgdfalfgsSSSSEVAPTTSAAGRGASTTV 601
Cdd:pfam03154  516 PVQIKEEALDEAEEPESP---------PPPPRSPSPEPTVVNTP---------------SHASQSARFYKHLDRGYNSCA 571

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1207191292  602 QDDFAdFMAFGSS-----RDQRSETSSREGNSEGQTETSQQRHQ 640
Cdd:pfam03154  572 RTDLY-FMPLAGSklakkREEALEKAKREAEQKAREEKEREKEK 614
PHA03247 PHA03247
large tegument protein UL36; Provisional
 277-564 1.61e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  277 TVMSLDILSQFPSPPVPNLPAMTMAIPAV----LPQHQQPIMTQPPVS-MPMPTAAPPVMSMTPNPPAQPPATfitnFPP 351
Cdd:PHA03247  2691 TVGSLTSLADPPPPPPTPEPAPHALVSATplppGPAAARQASPALPAApAPPAVPAGPATPGGPARPARPPTT----AGP 2766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  352 VQATKADDDDFQDFQEAPKAGVGDDSftdfqgETGGTFPsmTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAE 431
Cdd:PHA03247  2767 PAPAPPAAPAAGPPRRLTRPAVASLS------ESRESLP--SPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  432 PTPAVsdsgdkysvfrelEPPSERKPVGEGFADFKSVSAdDGFTDFKTADTVSPLDPPDQAKFQPTFPPPfASSQSLSHS 511
Cdd:PHA03247  2839 PPPPP-------------GPPPPSLPLGGSVAPGGDVRR-RPPSRSPAAKPAAPARPPVRRLARPAVSRS-TESFALPPD 2903

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207191292  512 QPASLAQPRNPlnmadldlfttmAPPTSTADSKLNLFPS-APPSLVLPSAVVKP 564
Cdd:PHA03247  2904 QPERPPQPQAP------------PPPQPQPQPPPPPQPQpPPPPPPRPQPPLAP 2945
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 306-357 3.23e-03

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 40.98  E-value: 3.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207191292  306 LPQHQQP---IMTQPPVSMPMPTAAPPVMSMTPNPPAQPPATFITNFPPVQATKA 357
Cdd:PLN02983   141 LPQPPPPapvVMMQPPPPHAMPPASPPAAQPAPSAPASSPPPTPASPPPAKAPKS 195
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 311-672 4.22e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.61  E-value: 4.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  311 QPIMTQPPVSMPMPTAAPPVMSMTPNPPAQPPATFIT----NFPPVQATKADDDDFQDFQEAP----KAGVGDDSFTDFQ 382
Cdd:PRK10263   338 EPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIApapeGYPQQSQYAQPAVQYNEPLQQPvqpqQPYYAPAAEQPAQ 417

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  383 GETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVSDSGDKYSVFRELEPPS--------- 453
Cdd:PRK10263   418 QPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPvvepepvve 497

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  454 ERKPVGEGFADFKSVSADDGFTDFKTADTVSPLDPPDQAK--FQPTFPPPFASSQSLSHSQP--ASLAQPRNPLNMADLD 529
Cdd:PRK10263   498 ETKPARPPLYYFEEVEEKRAREREQLAAWYQPIPEPVKEPepIKSSLKAPSVAAVPPVEAAAavSPLASGVKKATLATGA 577

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  530 LFTTMAPPTSTADS---KLNLFPSAPPSLVLPSAVVKPPSMGGDDFGdFALFGSSSSSEVAPTTSAAGRGASTTVQDDFA 606
Cdd:PRK10263   578 AATVAAPVFSLANSggpRPQVKEGIGPQLPRPKRIRVPTRRELASYG-IKLPSQRAAEEKAREAQRNQYDSGDQYNDDEI 656

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207191292  607 DFMAFGSSRDQRSETSSREGNSEGQTETSQQRHQIGT-DKYDVFKQLSLEGGLAYDDNKESGGGSFS 672
Cdd:PRK10263   657 DAMQQDELARQFAQTQQQRYGEQYQHDVPVNAEDADAaAEAELARQFAQTQQQRYSGEQPAGANPFS 723
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 96-159 6.23e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 6.23e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292   96 QFPADIQKQMAEEHQKRLEQQQRMLEEDRKRRQF------EEQKQKLRLLSSVKpktgeKSRDDALEAIK 159
Cdd:pfam13868   73 RYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIveriqeEDQAEAEEKLEKQR-----QLREEIDEFNE 137
PHA03247 PHA03247
large tegument protein UL36; Provisional
 285-512 9.04e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 9.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  285 SQFPSPPVPNlPAMTMAIPAVLPQHQQPIMTQPPVSMPMPTAAPPVMSMTPNPPAQPPatfitnfPPVQATKADDDDFQD 364
Cdd:PHA03247  2884 RRLARPAVSR-STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ-------PPLAPTTDPAGAGEP 2955

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  365 FQEAPKAGVGddsftdfqGETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDKYAVF----KQLSVEQPAEPTPAvsdsg 440
Cdd:PHA03247  2956 SGAVPQPWLG--------ALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVsswaSSLALHEETDPPPV----- 3022

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207191292  441 dkySVFRELEPPSERkpvgEGFADFKSVSADDGFTDFKTADTVSPlDPPDQAKFQPTFPPPFASSQSLSHSQ 512
Cdd:PHA03247  3023 ---SLKQTLWPPDDT----EDSDADSLFDSDSERSDLEALDPLPP-EPHDPFAHEPDPATPEAGARESPSSQ 3086
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 251-375 9.23e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.18  E-value: 9.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191292  251 RTTPGKLTKEELYTVLALIGVAQSGLTVMSLdilSQFPSPPVPNL-PAMTMAIPAVLPQHQQPIMTQPPVsmPMPTAAPP 329
Cdd:PRK14950   342 RTTSYGQLPLELAVIEALLVPVPAPQPAKPT---AAAPSPVRPTPaPSTRPKAAAAANIPPKEPVRETAT--PPPVPPRP 416

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1207191292  330 VMSMTPNPPAQPPATFITNFPPVQATKADDDDFQDFQEAPKAGVGD 375
Cdd:PRK14950   417 VAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPPKEEEKALIADGD 462
 
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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