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Conserved domains on  [gi|528501451|ref|XP_005157497|]
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synergin gamma isoform X3 [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 1.88e-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: 1.88e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528501451  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 2.16e-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: 2.16e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 528501451   102 QKQMAEEHQKRLEQQQRMLEEDRKRRQFEEQKQK 135
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PHA03247 super family cl33720
large tegument protein UL36; Provisional
173-704 4.27e-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: 48.40  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  173 PTPSSQSKKPDSSPSHSSvtshslpPAFPDDDdefSDFVQGPVDAFSSFPSPPHPPSSPSLRAAHANQPLETGPGQHPSS 252
Cdd:PHA03247 2580 PAVTSRARRPDAPPQSAR-------PRAPVDD---RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP 2649
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  253 TLPHSVPSSLPVSP-----AIQHSSVISSSQSAFQGPSLEEKMFSSCDLtADKkaqvsfKPRQALSELNPRAQVTAqfhs 327
Cdd:PHA03247 2650 ERPRDDPAPGRVSRprrarRLGRAAQASSPPQRPRRRAARPTVGSLTSL-ADP------PPPPPTPEPAPHALVSA---- 2718
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  328 sTKARNWAQTQDDFHSAFMTGMAPEPLPATQAPPVADNPPIQPTRASGvgayPQQDMQPMVPTWLYNDSLIPELFKKVLE 407
Cdd:PHA03247 2719 -TPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG----PPAPAPPAAPAAGPPRRLTRPAVASLSE 2793
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  408 FTMT------PAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIG-VAQSGltvmslDILSQFP 480
Cdd:PHA03247 2794 SRESlpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsVAPGG------DVRRRPP 2867
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  481 SPPVPNLPAMTMAIPAvlPQHQQPIMTQPPVSMPMPtaaPPVMSMTPNPPAQPPATfITNFPPVQATKADDDDFQDFQEA 560
Cdd:PHA03247 2868 SRSPAAKPAAPARPPV--RRLARPAVSRSTESFALP---PDQPERPPQPQAPPPPQ-PQPQPPPPPQPQPPPPPPPRPQP 2941
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  561 PKAgvgddSFTDFQGETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDkyavfkqlSVEQPAEPTPAVSDSGDK------ 634
Cdd:PHA03247 2942 PLA-----PTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP--------SREAPASSTPPLTGHSLSrvsswa 3008
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  635 -------------YSVFRELEPPSERkpvgEGFADFKSVSADDGFTDFKTADTVSPlDPPDQAKFQPTFPPPFASSQSLS 701
Cdd:PHA03247 3009 sslalheetdpppVSLKQTLWPPDDT----EDSDADSLFDSDSERSDLEALDPLPP-EPHDPFAHEPDPATPEAGARESP 3083

                  ...
gi 528501451  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 1.48e-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: 43.07  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451    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 1.88e-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: 1.88e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528501451  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 1.51e-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: 1.51e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528501451    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 2.16e-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: 2.16e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 528501451   102 QKQMAEEHQKRLEQQQRMLEEDRKRRQFEEQKQK 135
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PHA03247 PHA03247
large tegument protein UL36; Provisional
173-704 4.27e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  173 PTPSSQSKKPDSSPSHSSvtshslpPAFPDDDdefSDFVQGPVDAFSSFPSPPHPPSSPSLRAAHANQPLETGPGQHPSS 252
Cdd:PHA03247 2580 PAVTSRARRPDAPPQSAR-------PRAPVDD---RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP 2649
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  253 TLPHSVPSSLPVSP-----AIQHSSVISSSQSAFQGPSLEEKMFSSCDLtADKkaqvsfKPRQALSELNPRAQVTAqfhs 327
Cdd:PHA03247 2650 ERPRDDPAPGRVSRprrarRLGRAAQASSPPQRPRRRAARPTVGSLTSL-ADP------PPPPPTPEPAPHALVSA---- 2718
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  328 sTKARNWAQTQDDFHSAFMTGMAPEPLPATQAPPVADNPPIQPTRASGvgayPQQDMQPMVPTWLYNDSLIPELFKKVLE 407
Cdd:PHA03247 2719 -TPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG----PPAPAPPAAPAAGPPRRLTRPAVASLSE 2793
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  408 FTMT------PAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIG-VAQSGltvmslDILSQFP 480
Cdd:PHA03247 2794 SRESlpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsVAPGG------DVRRRPP 2867
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  481 SPPVPNLPAMTMAIPAvlPQHQQPIMTQPPVSMPMPtaaPPVMSMTPNPPAQPPATfITNFPPVQATKADDDDFQDFQEA 560
Cdd:PHA03247 2868 SRSPAAKPAAPARPPV--RRLARPAVSRSTESFALP---PDQPERPPQPQAPPPPQ-PQPQPPPPPQPQPPPPPPPRPQP 2941
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  561 PKAgvgddSFTDFQGETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDkyavfkqlSVEQPAEPTPAVSDSGDK------ 634
Cdd:PHA03247 2942 PLA-----PTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP--------SREAPASSTPPLTGHSLSrvsswa 3008
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  635 -------------YSVFRELEPPSERkpvgEGFADFKSVSADDGFTDFKTADTVSPlDPPDQAKFQPTFPPPFASSQSLS 701
Cdd:PHA03247 3009 sslalheetdpppVSLKQTLWPPDDT----EDSDADSLFDSDSERSDLEALDPLPP-EPHDPFAHEPDPATPEAGARESP 3083

                  ...
gi 528501451  702 HSQ 704
Cdd:PHA03247 3084 SSQ 3086
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
454-549 1.73e-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: 45.30  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451   454 LYTVLALIGVAQSGLTVMSLDILSQ---FPSPPVPNLPAMTMAIPAVLPQHQQPIMTQPPVSMPMPTAAPPvmSMTPNPP 530
Cdd:pfam07174   14 LWATLAIAAVAGASAVAVALPAVAHadpEPAPPPPSTATAPPAPPPPPPAPAAPAPPPPPAAPNAPNAPPP--PADPNAP 91
                           90
                   ....*....|....*....
gi 528501451   531 AQPPATFITNFPPVQATKA 549
Cdd:pfam07174   92 PPPPADPNAPPPPAVDPNA 110
PRK04239 PRK04239
DNA-binding protein;
102-136 3.41e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.40  E-value: 3.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528501451  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 1.48e-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: 43.07  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451    40 MVQVMQPNMQGMMGMNFGAQMPGAMPIQGGMAMGMQTPGMQFMGQPQFMGMRAPGPQFPADIQKQMAEEHQKRLEQQQRM 119
Cdd:pfam09606  170 TPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQ 249
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
99-181 4.62e-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: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451    99 ADIQKQMAEEHQKRLEQQQRMLEEDRKRRqfEEQKQKL--RLLSSVKP--KTGEKSRDDAL---EAIKGNLDGFSRDAKM 171
Cdd:pfam06391   96 EELLELEKREKEERRKEEKQEEEEEKEKK--EKAKQELidELMTSNKDaeEIIAQHKKTAKkrkSERRRKLEELNRVLEQ 173
                           90
                   ....*....|
gi 528501451   172 HPTPSSQSKK 181
Cdd:pfam06391  174 KPTQFSTGIK 183
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
482-548 5.26e-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: 39.39  E-value: 5.26e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528501451    482 PPVPNLPAMTMAIPavlPQHQQPIMTQPPVSMPMP----TAAPPVMSMTPNPPAqPPATFITNFPPVQATK 548
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 ...
398-466 1.88e-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: 1.88e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528501451  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 1.51e-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: 1.51e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528501451    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 2.16e-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: 2.16e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 528501451   102 QKQMAEEHQKRLEQQQRMLEEDRKRRQFEEQKQK 135
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PHA03247 PHA03247
large tegument protein UL36; Provisional
173-704 4.27e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  173 PTPSSQSKKPDSSPSHSSvtshslpPAFPDDDdefSDFVQGPVDAFSSFPSPPHPPSSPSLRAAHANQPLETGPGQHPSS 252
Cdd:PHA03247 2580 PAVTSRARRPDAPPQSAR-------PRAPVDD---RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP 2649
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  253 TLPHSVPSSLPVSP-----AIQHSSVISSSQSAFQGPSLEEKMFSSCDLtADKkaqvsfKPRQALSELNPRAQVTAqfhs 327
Cdd:PHA03247 2650 ERPRDDPAPGRVSRprrarRLGRAAQASSPPQRPRRRAARPTVGSLTSL-ADP------PPPPPTPEPAPHALVSA---- 2718
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  328 sTKARNWAQTQDDFHSAFMTGMAPEPLPATQAPPVADNPPIQPTRASGvgayPQQDMQPMVPTWLYNDSLIPELFKKVLE 407
Cdd:PHA03247 2719 -TPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG----PPAPAPPAAPAAGPPRRLTRPAVASLSE 2793
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  408 FTMT------PAGIDTAKLYPILISSGLPREALGQIWALANRTTPGKLTKEELYTVLALIG-VAQSGltvmslDILSQFP 480
Cdd:PHA03247 2794 SRESlpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsVAPGG------DVRRRPP 2867
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  481 SPPVPNLPAMTMAIPAvlPQHQQPIMTQPPVSMPMPtaaPPVMSMTPNPPAQPPATfITNFPPVQATKADDDDFQDFQEA 560
Cdd:PHA03247 2868 SRSPAAKPAAPARPPV--RRLARPAVSRSTESFALP---PDQPERPPQPQAPPPPQ-PQPQPPPPPQPQPPPPPPPRPQP 2941
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  561 PKAgvgddSFTDFQGETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDkyavfkqlSVEQPAEPTPAVSDSGDK------ 634
Cdd:PHA03247 2942 PLA-----PTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP--------SREAPASSTPPLTGHSLSrvsswa 3008
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  635 -------------YSVFRELEPPSERkpvgEGFADFKSVSADDGFTDFKTADTVSPlDPPDQAKFQPTFPPPFASSQSLS 701
Cdd:PHA03247 3009 sslalheetdpppVSLKQTLWPPDDT----EDSDADSLFDSDSERSDLEALDPLPP-EPHDPFAHEPDPATPEAGARESP 3083

                  ...
gi 528501451  702 HSQ 704
Cdd:PHA03247 3084 SSQ 3086
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
493-734 1.12e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.79  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  493 AIPAvlPQHQQPIMTQPPVSMPmPTAAPPVMSMTPNPPAQPPATFITNFPPVQATKADDDDFQDFQEAPKAGVGddsftd 572
Cdd:PRK12323  372 AGPA--TAAAAPVAQPAPAAAA-PAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASAR------ 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  573 fqgetGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVSDSgdkysvfrelePPSERKPvgE 652
Cdd:PRK12323  443 -----GPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP-----------PPWEELP--P 504
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  653 GFADFKSVSADDGFTDFKTADTVSPLDPPDQAKFQPTFPPPFASSQSLSHSQPASLAQPRNPlnmadlDLFTTMAPPTST 732
Cdd:PRK12323  505 EFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPP------RASASGLPDMFD 578

                  ..
gi 528501451  733 AD 734
Cdd:PRK12323  579 GD 580
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
454-549 1.73e-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: 45.30  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451   454 LYTVLALIGVAQSGLTVMSLDILSQ---FPSPPVPNLPAMTMAIPAVLPQHQQPIMTQPPVSMPMPTAAPPvmSMTPNPP 530
Cdd:pfam07174   14 LWATLAIAAVAGASAVAVALPAVAHadpEPAPPPPSTATAPPAPPPPPPAPAAPAPPPPPAAPNAPNAPPP--PADPNAP 91
                           90
                   ....*....|....*....
gi 528501451   531 AQPPATFITNFPPVQATKA 549
Cdd:pfam07174   92 PPPPADPNAPPPPAVDPNA 110
PRK04239 PRK04239
DNA-binding protein;
102-136 3.41e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.40  E-value: 3.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528501451  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 1.48e-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: 43.07  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451    40 MVQVMQPNMQGMMGMNFGAQMPGAMPIQGGMAMGMQTPGMQFMGQPQFMGMRAPGPQFPADIQKQMAEEHQKRLEQQQRM 119
Cdd:pfam09606  170 TPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQ 249
PHA03247 PHA03247
large tegument protein UL36; Provisional
483-784 2.68e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  483 PVPNLPAMTM--AIPAVLPQHQQPIM----TQPPVSMPMPTAAPPVmSMTPNPPAQPPATFITNFPPVQATKADDDDFQD 556
Cdd:PHA03247 2575 PRPSEPAVTSraRRPDAPPQSARPRApvddRGDPRGPAPPSPLPPD-THAPDPPPPSPSPAANEPDPHPPPTVPPPERPR 2653
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  557 FQEAPKAgVGDDSFTDFQGETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVSDSGdkys 636
Cdd:PHA03247 2654 DDPAPGR-VSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAA---- 2728
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  637 vfRELEPPSERKPVGEGFADFKSVSADDG--FTDFKTADTVSPLDPPDQAKF-QPTFPPPFASSQSLSH---------SQ 704
Cdd:PHA03247 2729 --RQASPALPAAPAPPAVPAGPATPGGPArpARPPTTAGPPAPAPPAAPAAGpPRRLTRPAVASLSESReslpspwdpAD 2806
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  705 PASLAQPRNPLNMADLDLFTTMAPPTSTAdsklnlfPSAPPSLVLPSAVVKPPSMGGDDFGDFALFGSSSSSEVAPTTSA 784
Cdd:PHA03247 2807 PPAAVLAPAAALPPAASPAGPLPPPTSAQ-------PTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPA 2879
PHA03247 PHA03247
large tegument protein UL36; Provisional
348-745 2.87e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  348 GMAPEPLPATQAPPVADN--PPIQP----------TRASGVGAYPQQDmQPMVPTWLYNDSLIPElfkkvlefTMTPAGI 415
Cdd:PHA03247 2549 GDPPPPLPPAAPPAAPDRsvPPPRPaprpsepavtSRARRPDAPPQSA-RPRAPVDDRGDPRGPA--------PPSPLPP 2619
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  416 DTAKLYPILIS-SGLPREALGQIWALA-------NRTTPGKLTKEELYTVLALIGVAQSGL----------TVMSLDILS 477
Cdd:PHA03247 2620 DTHAPDPPPPSpSPAANEPDPHPPPTVppperprDDPAPGRVSRPRRARRLGRAAQASSPPqrprrraarpTVGSLTSLA 2699
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  478 QFPSPPVPNLPAMTMAIPAV----LPQHQQPIMTQPPVS-MPMPTAAPPVMSMTPNPPAQPPATfitnFPPVQATKADDD 552
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALVSATplppGPAAARQASPALPAApAPPAVPAGPATPGGPARPARPPTT----AGPPAPAPPAAP 2775
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  553 DFQDFQEAPKAGVGDDSftdfqgETGGTFPsmTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVsdsg 632
Cdd:PHA03247 2776 AAGPPRRLTRPAVASLS------ESRESLP--SPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP---- 2843
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  633 dkysvfrelEPPSERKPVGEGFADFKSVSAdDGFTDFKTADTVSPLDPPDQAKFQPTFPPPfASSQSLSHSQPASLAQPR 712
Cdd:PHA03247 2844 ---------GPPPPSLPLGGSVAPGGDVRR-RPPSRSPAAKPAAPARPPVRRLARPAVSRS-TESFALPPDQPERPPQPQ 2912
                         410       420       430
                  ....*....|....*....|....*....|...
gi 528501451  713 NPlnmadldlfttmAPPTSTADSKLNLFPSAPP 745
Cdd:PHA03247 2913 AP------------PPPQPQPQPPPPPQPQPPP 2933
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
99-181 4.62e-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: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451    99 ADIQKQMAEEHQKRLEQQQRMLEEDRKRRqfEEQKQKL--RLLSSVKP--KTGEKSRDDAL---EAIKGNLDGFSRDAKM 171
Cdd:pfam06391   96 EELLELEKREKEERRKEEKQEEEEEKEKK--EKAKQELidELMTSNKDaeEIIAQHKKTAKkrkSERRRKLEELNRVLEQ 173
                           90
                   ....*....|
gi 528501451   172 HPTPSSQSKK 181
Cdd:pfam06391  174 KPTQFSTGIK 183
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
482-548 5.26e-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: 39.39  E-value: 5.26e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528501451    482 PPVPNLPAMTMAIPavlPQHQQPIMTQPPVSMPMP----TAAPPVMSMTPNPPAqPPATFITNFPPVQATK 548
Cdd:smart00818   94 QPAQQPFQPQPLQP---PQPQQPMQPQPPVHPIPPlppqPPLPPMFPMQPLPPL-LPDLPLEAWPATDKTK 160
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
96-159 7.20e-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: 7.20e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451    96 QFPADIQKQMAEEHQKRLEQQQRMLEEDRKRRQF------EEQKQKLRLLSSVKpktgeKSRDDALEAIK 159
Cdd:pfam13868   73 RYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIveriqeEDQAEAEEKLEKQR-----QLREEIDEFNE 137
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
498-549 7.31e-03

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 39.82  E-value: 7.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 528501451  498 LPQHQQP---IMTQPPVSMPMPTAAPPVMSMTPNPPAQPPATFITNFPPVQATKA 549
Cdd:PLN02983  141 LPQPPPPapvVMMQPPPPHAMPPASPPAAQPAPSAPASSPPPTPASPPPAKAPKS 195
PRK10263 PRK10263
DNA translocase FtsK; Provisional
503-706 9.13e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 9.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  503 QPIMTQPPVSMPMPTAAPPVMSMTPNPPAQPPATFIT----NFPPVQATKADDDDFQDFQEAP----KAGVGDDSFTDFQ 574
Cdd:PRK10263  338 EPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIApapeGYPQQSQYAQPAVQYNEPLQQPvqpqQPYYAPAAEQPAQ 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501451  575 GETGGTFPSMTSSSQSSVPAMLTPVSGSSSSSSDKYAVFKQLSVEQPAEPTPAVSDSGDKYSVFRELEPPS--------- 645
Cdd:PRK10263  418 QPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPvvepepvve 497
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528501451  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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