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Conserved domains on  [gi|568973232|ref|XP_006533045|]
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synergin gamma isoform X5 [Mus musculus]

Protein Classification

ARGLU and EH domain-containing protein( domain architecture ID 13188349)

protein containing domains Med15, ARGLU, 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 ...
 398-449 3.71e-13

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: 65.32  E-value: 3.71e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568973232  398 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGRLTKEELYTVLAMVAVTQR 449
Cdd:cd00052    16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
ARGLU super family cl38471
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 97-130 2.33e-05

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: 45.81  E-value: 2.33e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568973232    97 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 130
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 14-225 5.82e-04

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: 44.23  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973232    14 AGGMRPPQGLIPMQQQGFPMVSVMQPNMQGMMGMNySSQMSQGPIAMQ---AGIPMGP---MPAAGVPFLGQPPFLSMRP 87
Cdd:pfam09606  219 MGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQ-QSQLGMGINQMQqmpQGVGGGAgqgGPGQPMGPPGQQPGAMPNV 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973232    88 AGPQYTPDMQKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKLRLLSSVKPKTGEKNRDDALEA---IKGNLDGFSRDA 164
Cdd:pfam09606  298 MSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGAnpmQRGQPGMMSSPS 377

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568973232   165 kmhPTPASHPKKQDCPTSSHSTKTVS-PSSAFPGEDEFSGFVQGPVEFPACGPSSTAPPFQS 225
Cdd:pfam09606  378 ---PVPGQQVRQVTPNQFMRQSPQPSvPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQ 436
SAP130_C super family cl25748
Histone deacetylase complex subunit SAP130 C-terminus;
452-520 2.74e-03

Histone deacetylase complex subunit SAP130 C-terminus;


The actual alignment was detected with superfamily member pfam16014:

Pssm-ID: 464973 [Multi-domain]  Cd Length: 371  Bit Score: 41.84  E-value: 2.74e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973232   452 PAMSPDALSQFPAAPIPTLsgfpMTLPTPVSQPTAMPSGPTGSMPLTLGQPIMGINLVGPVGGAAAPTS 520
Cdd:pfam16014   49 QTASASPPSQHPAQAIPTI----LAPAAPPSQPSVVLSTLPAAMAVTPPIPASMANVVAPPTQPAASST 113
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 398-449 3.71e-13

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: 65.32  E-value: 3.71e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568973232  398 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGRLTKEELYTVLAMVAVTQR 449
Cdd:cd00052    16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 398-459 1.46e-10

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: 59.21  E-value: 1.46e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568973232    398 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGRLTKEELYTVLAMVAVTQRG--VPAMSPDAL 459
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGypIPASLPPSL 90
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 97-130 2.33e-05

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: 45.81  E-value: 2.33e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568973232    97 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 130
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PRK04239 PRK04239
DNA-binding protein;
97-131 4.27e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.02  E-value: 4.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568973232   97 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL 131
Cdd:PRK04239    8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 14-225 5.82e-04

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: 44.23  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973232    14 AGGMRPPQGLIPMQQQGFPMVSVMQPNMQGMMGMNySSQMSQGPIAMQ---AGIPMGP---MPAAGVPFLGQPPFLSMRP 87
Cdd:pfam09606  219 MGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQ-QSQLGMGINQMQqmpQGVGGGAgqgGPGQPMGPPGQQPGAMPNV 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973232    88 AGPQYTPDMQKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKLRLLSSVKPKTGEKNRDDALEA---IKGNLDGFSRDA 164
Cdd:pfam09606  298 MSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGAnpmQRGQPGMMSSPS 377

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568973232   165 kmhPTPASHPKKQDCPTSSHSTKTVS-PSSAFPGEDEFSGFVQGPVEFPACGPSSTAPPFQS 225
Cdd:pfam09606  378 ---PVPGQQVRQVTPNQFMRQSPQPSvPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQ 436
SAP130_C pfam16014
Histone deacetylase complex subunit SAP130 C-terminus;
452-520 2.74e-03

Histone deacetylase complex subunit SAP130 C-terminus;


Pssm-ID: 464973 [Multi-domain]  Cd Length: 371  Bit Score: 41.84  E-value: 2.74e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973232   452 PAMSPDALSQFPAAPIPTLsgfpMTLPTPVSQPTAMPSGPTGSMPLTLGQPIMGINLVGPVGGAAAPTS 520
Cdd:pfam16014   49 QTASASPPSQHPAQAIPTI----LAPAAPPSQPSVVLSTLPAAMAVTPPIPASMANVVAPPTQPAASST 113
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 398-449 3.71e-13

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: 65.32  E-value: 3.71e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568973232  398 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGRLTKEELYTVLAMVAVTQR 449
Cdd:cd00052    16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 398-459 1.46e-10

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: 59.21  E-value: 1.46e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568973232    398 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGRLTKEELYTVLAMVAVTQRG--VPAMSPDAL 459
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGypIPASLPPSL 90
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 97-130 2.33e-05

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: 45.81  E-value: 2.33e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568973232    97 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 130
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PRK04239 PRK04239
DNA-binding protein;
97-131 4.27e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.02  E-value: 4.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568973232   97 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL 131
Cdd:PRK04239    8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 14-225 5.82e-04

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: 44.23  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973232    14 AGGMRPPQGLIPMQQQGFPMVSVMQPNMQGMMGMNySSQMSQGPIAMQ---AGIPMGP---MPAAGVPFLGQPPFLSMRP 87
Cdd:pfam09606  219 MGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQ-QSQLGMGINQMQqmpQGVGGGAgqgGPGQPMGPPGQQPGAMPNV 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973232    88 AGPQYTPDMQKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKLRLLSSVKPKTGEKNRDDALEA---IKGNLDGFSRDA 164
Cdd:pfam09606  298 MSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGAnpmQRGQPGMMSSPS 377

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568973232   165 kmhPTPASHPKKQDCPTSSHSTKTVS-PSSAFPGEDEFSGFVQGPVEFPACGPSSTAPPFQS 225
Cdd:pfam09606  378 ---PVPGQQVRQVTPNQFMRQSPQPSvPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQ 436
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 96-132 1.01e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 41.18  E-value: 1.01e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568973232    96 MQKQFAEEQQKRFEQQQKLleEERKRRQFEEQKQKLR 132
Cdd:pfam05672   48 LRRRAEEERARREEEARRL--EEERRREEEERQRKAE 82
SAP130_C pfam16014
Histone deacetylase complex subunit SAP130 C-terminus;
452-520 2.74e-03

Histone deacetylase complex subunit SAP130 C-terminus;


Pssm-ID: 464973 [Multi-domain]  Cd Length: 371  Bit Score: 41.84  E-value: 2.74e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973232   452 PAMSPDALSQFPAAPIPTLsgfpMTLPTPVSQPTAMPSGPTGSMPLTLGQPIMGINLVGPVGGAAAPTS 520
Cdd:pfam16014   49 QTASASPPSQHPAQAIPTI----LAPAAPPSQPSVVLSTLPAAMAVTPPIPASMANVVAPPTQPAASST 113
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 14-114 4.95e-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: 41.15  E-value: 4.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973232    14 AGGMRPPQGLIPMQQQGFPMVSVMQPNMQGMMGMNYSSQ---MSQGPIAMQAGIPMGPMPAAGVPFLGQPPFLSMRPAGP 90
Cdd:pfam09606  155 AGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQgpmGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQM 234

                           90       100
                   ....*....|....*....|....
gi 568973232    91 QYTPdMQKQFAEEQQKRFEQQQKL 114
Cdd:pfam09606  235 GGAP-NQVAMQQQQPQQQGQQSQL 257
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 96-133 5.28e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.09  E-value: 5.28e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568973232    96 MQKQFAEEQQKRFEQ---QQKLLEEERKRRQFEEQKQKLRL 133
Cdd:pfam15709  374 MREELELEQQRRFEEirlRKQRLEEERQRQEEEERKQRLQL 414
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 91-154 9.15e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 9.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568973232   91 QYTPDMQKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL---RLLSSVKPKTGEKNRDDALEAIK 154
Cdd:PRK09510   80 QRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAeeaAKQAALKQKQAEEAAAKAAAAAK 146
 
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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