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Conserved domains on  [gi|1207191284|ref|XP_021328593|]
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synergin gamma isoform X1 [Danio rerio]

Protein Classification

ARGLU and EH domain-containing protein( domain architecture ID 13598847)

protein containing domains PABP-1234, ARGLU, Caldesmon, and EH

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 ...
398-466 2.05e-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: 2.05e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207191284  398 IPELFKKVLefTMTPAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIGVAQS 466
Cdd:cd00052      1 YDQIFRSLD--PDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
ARGLU super family cl38471
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
102-135 2.20e-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.


The actual alignment was detected with superfamily member pfam15346:

Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 48.89  E-value: 2.20e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1207191284  102 QKQMAEEHQKRLEQQQRMLEEDRKRRQFEEQKQK 135
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PHA03247 super family cl33720
large tegument protein UL36; Provisional
173-704 3.33e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 3.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  173 PTPSSQSKKPDSSPSHSSvtshslpPAFPDDDdefSDFVQGPVDAFSSFPSPPHPPSSPSLRAAHANQPLETGPGQHPSS 252
Cdd:PHA03247  2580 PAVTSRARRPDAPPQSAR-------PRAPVDD---RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP 2649
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  253 TLPHSVPSSLPVSP-----AIQHSSVISSSQSAFQGPSLEEKMFSSCDLtADKkaqvsfKPRQALSELNPRAQVTAqfhs 327
Cdd:PHA03247  2650 ERPRDDPAPGRVSRprrarRLGRAAQASSPPQRPRRRAARPTVGSLTSL-ADP------PPPPPTPEPAPHALVSA---- 2718
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  328 sTKARNWAQTQDDFHSAFMTGMAPEPLPATQAPPVADNPPIQPTRASGvgayPQQDMQPMVPTWLYNDSLIPELFKKVLE 407
Cdd:PHA03247  2719 -TPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG----PPAPAPPAAPAAGPPRRLTRPAVASLSE 2793
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  408 FTMT------PAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIG-VAQSGltvmslDILSQFP 480
Cdd:PHA03247  2794 SRESlpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsVAPGG------DVRRRPP 2867
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  481 SPPVPNLPAMTMAIPAvlPQHQQPIMTQPPVSMPMPtaaPPVMSMTPNPPAQPPATfITNFPPVQATKADDDDFQDFQEA 560
Cdd:PHA03247  2868 SRSPAAKPAAPARPPV--RRLARPAVSRSTESFALP---PDQPERPPQPQAPPPPQ-PQPQPPPPPQPQPPPPPPPRPQP 2941
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  561 PKAgvgddSFTDFQGETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDkyavfkqlSVEQPAEPTPAVSDSGDK------ 634
Cdd:PHA03247  2942 PLA-----PTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP--------SREAPASSTPPLTGHSLSrvsswa 3008
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  635 -------------YSVFRELEPPSERkpvgEGFADFKSVSADDGFTDFKTADTVSPlDPPDQAKFQPTFPPPFASSQSLS 701
Cdd:PHA03247  3009 sslalheetdpppVSLKQTLWPPDDT----EDSDADSLFDSDSERSDLEALDPLPP-EPHDPFAHEPDPATPEAGARESP 3083

                   ...
gi 1207191284  702 HSQ 704
Cdd:PHA03247  3084 SSQ 3086
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
40-119 1.21e-03

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.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 43.46  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284   40 MVQVMQPNMQGMMGMNFGAQMPGAMPIQGGMAMGMQTPGMQFMGQPQFMGMRAPGPQFPADIQKQMAEEHQKRLEQQQRM 119
Cdd:pfam09606  170 TPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQ 249
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
398-466 2.05e-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: 2.05e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207191284  398 IPELFKKVLefTMTPAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIGVAQS 466
Cdd:cd00052      1 YDQIFRSLD--PDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
415-474 1.49e-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: 53.44  E-value: 1.49e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207191284   415 IDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIGVAQSGLTV-MSLD 474
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIpASLP 87
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
102-135 2.20e-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: 2.20e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1207191284  102 QKQMAEEHQKRLEQQQRMLEEDRKRRQFEEQKQK 135
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PHA03247 PHA03247
large tegument protein UL36; Provisional
173-704 3.33e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 3.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  173 PTPSSQSKKPDSSPSHSSvtshslpPAFPDDDdefSDFVQGPVDAFSSFPSPPHPPSSPSLRAAHANQPLETGPGQHPSS 252
Cdd:PHA03247  2580 PAVTSRARRPDAPPQSAR-------PRAPVDD---RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP 2649
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  253 TLPHSVPSSLPVSP-----AIQHSSVISSSQSAFQGPSLEEKMFSSCDLtADKkaqvsfKPRQALSELNPRAQVTAqfhs 327
Cdd:PHA03247  2650 ERPRDDPAPGRVSRprrarRLGRAAQASSPPQRPRRRAARPTVGSLTSL-ADP------PPPPPTPEPAPHALVSA---- 2718
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  328 sTKARNWAQTQDDFHSAFMTGMAPEPLPATQAPPVADNPPIQPTRASGvgayPQQDMQPMVPTWLYNDSLIPELFKKVLE 407
Cdd:PHA03247  2719 -TPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG----PPAPAPPAAPAAGPPRRLTRPAVASLSE 2793
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  408 FTMT------PAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIG-VAQSGltvmslDILSQFP 480
Cdd:PHA03247  2794 SRESlpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsVAPGG------DVRRRPP 2867
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  481 SPPVPNLPAMTMAIPAvlPQHQQPIMTQPPVSMPMPtaaPPVMSMTPNPPAQPPATfITNFPPVQATKADDDDFQDFQEA 560
Cdd:PHA03247  2868 SRSPAAKPAAPARPPV--RRLARPAVSRSTESFALP---PDQPERPPQPQAPPPPQ-PQPQPPPPPQPQPPPPPPPRPQP 2941
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  561 PKAgvgddSFTDFQGETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDkyavfkqlSVEQPAEPTPAVSDSGDK------ 634
Cdd:PHA03247  2942 PLA-----PTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP--------SREAPASSTPPLTGHSLSrvsswa 3008
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  635 -------------YSVFRELEPPSERkpvgEGFADFKSVSADDGFTDFKTADTVSPlDPPDQAKFQPTFPPPFASSQSLS 701
Cdd:PHA03247  3009 sslalheetdpppVSLKQTLWPPDDT----EDSDADSLFDSDSERSDLEALDPLPP-EPHDPFAHEPDPATPEAGARESP 3083

                   ...
gi 1207191284  702 HSQ 704
Cdd:PHA03247  3084 SSQ 3086
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
454-549 1.32e-04

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: 45.69  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  454 LYTVLALIGVAQSGLTVMSLDILSQ---FPSPPVPNLPAMTMAIPAVLPQHQQPIMTQPPVSMPMPTAAPPvmSMTPNPP 530
Cdd:pfam07174   14 LWATLAIAAVAGASAVAVALPAVAHadpEPAPPPPSTATAPPAPPPPPPAPAAPAPPPPPAAPNAPNAPPP--PADPNAP 91
                           90
                   ....*....|....*....
gi 1207191284  531 AQPPATFITNFPPVQATKA 549
Cdd:pfam07174   92 PPPPADPNAPPPPAVDPNA 110
PRK04239 PRK04239
DNA-binding protein;
102-136 3.86e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.40  E-value: 3.86e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1207191284  102 QKQMAEEHQKRLEQQQRMLEEDRKRRQFEEQKQKL 136
Cdd:PRK04239     8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
40-119 1.21e-03

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: 43.46  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284   40 MVQVMQPNMQGMMGMNFGAQMPGAMPIQGGMAMGMQTPGMQFMGQPQFMGMRAPGPQFPADIQKQMAEEHQKRLEQQQRM 119
Cdd:pfam09606  170 TPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQ 249
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
482-548 3.51e-03

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: 39.77  E-value: 3.51e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207191284   482 PPVPNLPAMTMAIPavlPQHQQPIMTQPPVSMPMP----TAAPPVMSMTPNPPAqPPATFITNFPPVQATK 548
Cdd:smart00818   94 QPAQQPFQPQPLQP---PQPQQPMQPQPPVHPIPPlppqPPLPPMFPMQPLPPL-LPDLPLEAWPATDKTK 160
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
99-181 4.70e-03

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: 39.92  E-value: 4.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284   99 ADIQKQMAEEHQKRLEQQQRMLEEDRKRRqfEEQKQKL--RLLSSVKP--KTGEKSRDDAL---EAIKGNLDGFSRDAKM 171
Cdd:pfam06391   96 EELLELEKREKEERRKEEKQEEEEEKEKK--EKAKQELidELMTSNKDaeEIIAQHKKTAKkrkSERRRKLEELNRVLEQ 173
                           90
                   ....*....|
gi 1207191284  172 HPTPSSQSKK 181
Cdd:pfam06391  174 KPTQFSTGIK 183
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
398-466 2.05e-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: 2.05e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207191284  398 IPELFKKVLefTMTPAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIGVAQS 466
Cdd:cd00052      1 YDQIFRSLD--PDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
415-474 1.49e-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: 53.44  E-value: 1.49e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207191284   415 IDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIGVAQSGLTV-MSLD 474
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIpASLP 87
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
102-135 2.20e-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: 2.20e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1207191284  102 QKQMAEEHQKRLEQQQRMLEEDRKRRQFEEQKQK 135
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PHA03247 PHA03247
large tegument protein UL36; Provisional
173-704 3.33e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 3.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  173 PTPSSQSKKPDSSPSHSSvtshslpPAFPDDDdefSDFVQGPVDAFSSFPSPPHPPSSPSLRAAHANQPLETGPGQHPSS 252
Cdd:PHA03247  2580 PAVTSRARRPDAPPQSAR-------PRAPVDD---RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP 2649
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  253 TLPHSVPSSLPVSP-----AIQHSSVISSSQSAFQGPSLEEKMFSSCDLtADKkaqvsfKPRQALSELNPRAQVTAqfhs 327
Cdd:PHA03247  2650 ERPRDDPAPGRVSRprrarRLGRAAQASSPPQRPRRRAARPTVGSLTSL-ADP------PPPPPTPEPAPHALVSA---- 2718
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  328 sTKARNWAQTQDDFHSAFMTGMAPEPLPATQAPPVADNPPIQPTRASGvgayPQQDMQPMVPTWLYNDSLIPELFKKVLE 407
Cdd:PHA03247  2719 -TPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG----PPAPAPPAAPAAGPPRRLTRPAVASLSE 2793
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  408 FTMT------PAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIG-VAQSGltvmslDILSQFP 480
Cdd:PHA03247  2794 SRESlpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsVAPGG------DVRRRPP 2867
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  481 SPPVPNLPAMTMAIPAvlPQHQQPIMTQPPVSMPMPtaaPPVMSMTPNPPAQPPATfITNFPPVQATKADDDDFQDFQEA 560
Cdd:PHA03247  2868 SRSPAAKPAAPARPPV--RRLARPAVSRSTESFALP---PDQPERPPQPQAPPPPQ-PQPQPPPPPQPQPPPPPPPRPQP 2941
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  561 PKAgvgddSFTDFQGETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDkyavfkqlSVEQPAEPTPAVSDSGDK------ 634
Cdd:PHA03247  2942 PLA-----PTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP--------SREAPASSTPPLTGHSLSrvsswa 3008
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  635 -------------YSVFRELEPPSERkpvgEGFADFKSVSADDGFTDFKTADTVSPlDPPDQAKFQPTFPPPFASSQSLS 701
Cdd:PHA03247  3009 sslalheetdpppVSLKQTLWPPDDT----EDSDADSLFDSDSERSDLEALDPLPP-EPHDPFAHEPDPATPEAGARESP 3083

                   ...
gi 1207191284  702 HSQ 704
Cdd:PHA03247  3084 SSQ 3086
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
493-734 9.65e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.79  E-value: 9.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  493 AIPAvlPQHQQPIMTQPPVSMPmPTAAPPVMSMTPNPPAQPPATFITNFPPVQATKADDDDFQDFQEAPKAGVGddsftd 572
Cdd:PRK12323   372 AGPA--TAAAAPVAQPAPAAAA-PAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASAR------ 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  573 fqgetGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVSDSgdkysvfrelePPSERKPvgE 652
Cdd:PRK12323   443 -----GPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP-----------PPWEELP--P 504
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  653 GFADFKSVSADDGFTDFKTADTVSPLDPPDQAKFQPTFPPPFASSQSLSHSQPASLAQPRNPlnmadlDLFTTMAPPTST 732
Cdd:PRK12323   505 EFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPP------RASASGLPDMFD 578

                   ..
gi 1207191284  733 AD 734
Cdd:PRK12323   579 GD 580
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
454-549 1.32e-04

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: 45.69  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  454 LYTVLALIGVAQSGLTVMSLDILSQ---FPSPPVPNLPAMTMAIPAVLPQHQQPIMTQPPVSMPMPTAAPPvmSMTPNPP 530
Cdd:pfam07174   14 LWATLAIAAVAGASAVAVALPAVAHadpEPAPPPPSTATAPPAPPPPPPAPAAPAPPPPPAAPNAPNAPPP--PADPNAP 91
                           90
                   ....*....|....*....
gi 1207191284  531 AQPPATFITNFPPVQATKA 549
Cdd:pfam07174   92 PPPPADPNAPPPPAVDPNA 110
PRK04239 PRK04239
DNA-binding protein;
102-136 3.86e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.40  E-value: 3.86e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1207191284  102 QKQMAEEHQKRLEQQQRMLEEDRKRRQFEEQKQKL 136
Cdd:PRK04239     8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
40-119 1.21e-03

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: 43.46  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284   40 MVQVMQPNMQGMMGMNFGAQMPGAMPIQGGMAMGMQTPGMQFMGQPQFMGMRAPGPQFPADIQKQMAEEHQKRLEQQQRM 119
Cdd:pfam09606  170 TPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQ 249
PHA03247 PHA03247
large tegument protein UL36; Provisional
348-745 2.33e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  348 GMAPEPLPATQAPPVADN--PPIQP----------TRASGVGAYPQQDmQPMVPTWLYNDSLIPElfkkvlefTMTPAGI 415
Cdd:PHA03247  2549 GDPPPPLPPAAPPAAPDRsvPPPRPaprpsepavtSRARRPDAPPQSA-RPRAPVDDRGDPRGPA--------PPSPLPP 2619
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  416 DTAKLYPILIS-SGLPREALGQIWALA-------NRTTPGKLTKEELYTVLALIGVAQSGL----------TVMSLDILS 477
Cdd:PHA03247  2620 DTHAPDPPPPSpSPAANEPDPHPPPTVppperprDDPAPGRVSRPRRARRLGRAAQASSPPqrprrraarpTVGSLTSLA 2699
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  478 QFPSPPVPNLPAMTMAIPAV----LPQHQQPIMTQPPVS-MPMPTAAPPVMSMTPNPPAQPPATfitnFPPVQATKADDD 552
Cdd:PHA03247  2700 DPPPPPPTPEPAPHALVSATplppGPAAARQASPALPAApAPPAVPAGPATPGGPARPARPPTT----AGPPAPAPPAAP 2775
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  553 DFQDFQEAPKAGVGDDSftdfqgETGGTFPsmTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVsdsg 632
Cdd:PHA03247  2776 AAGPPRRLTRPAVASLS------ESRESLP--SPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP---- 2843
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  633 dkysvfrelEPPSERKPVGEGFADFKSVSAdDGFTDFKTADTVSPLDPPDQAKFQPTFPPPfASSQSLSHSQPASLAQPR 712
Cdd:PHA03247  2844 ---------GPPPPSLPLGGSVAPGGDVRR-RPPSRSPAAKPAAPARPPVRRLARPAVSRS-TESFALPPDQPERPPQPQ 2912
                          410       420       430
                   ....*....|....*....|....*....|...
gi 1207191284  713 NPlnmadldlfttmAPPTSTADSKLNLFPSAPP 745
Cdd:PHA03247  2913 AP------------PPPQPQPQPPPPPQPQPPP 2933
PHA03247 PHA03247
large tegument protein UL36; Provisional
480-784 2.45e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  480 PSP---PVPNLPAMTM--AIPAVLPQHQQPIM----TQPPVSMPMPTAAPPVmSMTPNPPAQPPATFITNFPPVQATKAD 550
Cdd:PHA03247  2569 PPPrpaPRPSEPAVTSraRRPDAPPQSARPRApvddRGDPRGPAPPSPLPPD-THAPDPPPPSPSPAANEPDPHPPPTVP 2647
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  551 DDDFQDFQEAPKAgVGDDSFTDFQGETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVSD 630
Cdd:PHA03247  2648 PPERPRDDPAPGR-VSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPA 2726
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  631 SGdkysvfRELEPPSERKPVGEGFADFKSVSADDG--FTDFKTADTVSPLDPPDQAKF-QPTFPPPFASSQSLSH----- 702
Cdd:PHA03247  2727 AA------RQASPALPAAPAPPAVPAGPATPGGPArpARPPTTAGPPAPAPPAAPAAGpPRRLTRPAVASLSESReslps 2800
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  703 ----SQPASLAQPRNPLNMADLDLFTTMAPPTSTAdsklnlfPSAPPSLVLPSAVVKPPSMGGDDFGDFALFGSSSSSEV 778
Cdd:PHA03247  2801 pwdpADPPAAVLAPAAALPPAASPAGPLPPPTSAQ-------PTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAA 2873

                   ....*.
gi 1207191284  779 APTTSA 784
Cdd:PHA03247  2874 KPAAPA 2879
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
482-548 3.51e-03

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: 39.77  E-value: 3.51e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207191284   482 PPVPNLPAMTMAIPavlPQHQQPIMTQPPVSMPMP----TAAPPVMSMTPNPPAqPPATFITNFPPVQATK 548
Cdd:smart00818   94 QPAQQPFQPQPLQP---PQPQQPMQPQPPVHPIPPlppqPPLPPMFPMQPLPPL-LPDLPLEAWPATDKTK 160
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
99-181 4.70e-03

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: 39.92  E-value: 4.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284   99 ADIQKQMAEEHQKRLEQQQRMLEEDRKRRqfEEQKQKL--RLLSSVKP--KTGEKSRDDAL---EAIKGNLDGFSRDAKM 171
Cdd:pfam06391   96 EELLELEKREKEERRKEEKQEEEEEKEKK--EKAKQELidELMTSNKDaeEIIAQHKKTAKkrkSERRRKLEELNRVLEQ 173
                           90
                   ....*....|
gi 1207191284  172 HPTPSSQSKK 181
Cdd:pfam06391  174 KPTQFSTGIK 183
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
498-549 6.41e-03

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 40.21  E-value: 6.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207191284  498 LPQHQQP---IMTQPPVSMPMPTAAPPVMSMTPNPPAQPPATFITNFPPVQATKA 549
Cdd:PLN02983   141 LPQPPPPapvVMMQPPPPHAMPPASPPAAQPAPSAPASSPPPTPASPPPAKAPKS 195
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
96-159 7.34e-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: 7.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284   96 QFPADIQKQMAEEHQKRLEQQQRMLEEDRKRRQF------EEQKQKLRLLSSVKpktgeKSRDDALEAIK 159
Cdd:pfam13868   73 RYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIveriqeEDQAEAEEKLEKQR-----QLREEIDEFNE 137
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
477-548 8.84e-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: 40.52  E-value: 8.84e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207191284  477 SQFPSPPVPNLPAMTMAIPAVLPQHQQPIMTQPPVSMPMPTAAPPVMSMTPnppaqPPATFITNFPPVQATK 548
Cdd:pfam03154  307 SQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKP-----PPTTPIPQLPNPQSHK 373
PRK10263 PRK10263
DNA translocase FtsK; Provisional
503-706 9.15e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 9.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  503 QPIMTQPPVSMPMPTAAPPVMSMTPNPPAQPPATFIT----NFPPVQATKADDDDFQDFQEAP----KAGVGDDSFTDFQ 574
Cdd:PRK10263   338 EPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIApapeGYPQQSQYAQPAVQYNEPLQQPvqpqQPYYAPAAEQPAQ 417
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207191284  575 GETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVSDSGDKYSVFRELEPPS--------- 645
Cdd:PRK10263   418 QPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPvvepepvve 497
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207191284  646 ERKPVGEGFADFKSVSADDGFTDFKTADTVSPLDPPDQAK--FQPTFPPPFASSQSLSHSQPA 706
Cdd:PRK10263   498 ETKPARPPLYYFEEVEEKRAREREQLAAWYQPIPEPVKEPepIKSSLKAPSVAAVPPVEAAAA 560
 
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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