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Conserved domains on  [gi|156120951|ref|NP_001095622|]
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synergin gamma [Bos taurus]

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 ...
385-435 4.14e-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: 4.14e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156120951  385 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYAVLAMIAATQ 435
Cdd:cd00052    16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
ARGLU super family cl38471
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
115-148 2.47e-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: 2.47e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 156120951   115 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 148
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
DUF4175 super family cl44629
Domain of unknown function (DUF4175);
39-177 2.69e-03

Domain of unknown function (DUF4175);


The actual alignment was detected with superfamily member pfam13779:

Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 42.28  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120951    39 QGLMPMQQqgfpMVSVMQPNMQGMIGMNYSSQMSQgpiAMQA-----------------GIPMGPIPAGGMP-YLGQAPF 100
Cdd:pfam13779  577 QMLSQLQQ----MLENLQAGQPQQQQQQGQSEMQQ---AMDElgdllreqqqlldetfrQLQQQGGQQQGQPgQQGQQGQ 649
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120951   101 LGMRPPGPQYTPD-MQKQFAEEQQKRFEQQQKLLeeerkRRQFEEQKQKLRLLSSVKPKTG----EKSRDDALEAI-KGN 174
Cdd:pfam13779  650 GQQPGQGGQQPGAqMPPQGGAEALGDLAERQQAL-----RRRLEELQDELKELGGKEPGQAlgdaGRAMRDAEEALgQGD 724

                   ...
gi 156120951   175 LDG 177
Cdd:pfam13779  725 LAG 727
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
385-435 4.14e-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: 4.14e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156120951  385 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYAVLAMIAATQ 435
Cdd:cd00052    16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
385-446 1.72e-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: 58.83  E-value: 1.72e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156120951    385 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYAVLAMIAATQGG--VPAMSPDAL 446
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGypIPASLPPSL 90
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
115-148 2.47e-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: 2.47e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 156120951   115 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 148
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PRK04239 PRK04239
DNA-binding protein;
115-149 3.65e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.40  E-value: 3.65e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 156120951  115 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL 149
Cdd:PRK04239    8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
DUF4175 pfam13779
Domain of unknown function (DUF4175);
39-177 2.69e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 42.28  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120951    39 QGLMPMQQqgfpMVSVMQPNMQGMIGMNYSSQMSQgpiAMQA-----------------GIPMGPIPAGGMP-YLGQAPF 100
Cdd:pfam13779  577 QMLSQLQQ----MLENLQAGQPQQQQQQGQSEMQQ---AMDElgdllreqqqlldetfrQLQQQGGQQQGQPgQQGQQGQ 649
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120951   101 LGMRPPGPQYTPD-MQKQFAEEQQKRFEQQQKLLeeerkRRQFEEQKQKLRLLSSVKPKTG----EKSRDDALEAI-KGN 174
Cdd:pfam13779  650 GQQPGQGGQQPGAqMPPQGGAEALGDLAERQQAL-----RRRLEELQDELKELGGKEPGQAlgdaGRAMRDAEEALgQGD 724

                   ...
gi 156120951   175 LDG 177
Cdd:pfam13779  725 LAG 727
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
385-435 4.14e-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: 4.14e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156120951  385 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYAVLAMIAATQ 435
Cdd:cd00052    16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
385-446 1.72e-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: 58.83  E-value: 1.72e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156120951    385 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYAVLAMIAATQGG--VPAMSPDAL 446
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGypIPASLPPSL 90
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
115-148 2.47e-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: 2.47e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 156120951   115 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 148
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PRK04239 PRK04239
DNA-binding protein;
115-149 3.65e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.40  E-value: 3.65e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 156120951  115 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL 149
Cdd:PRK04239    8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
114-150 7.83e-04

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: 41.56  E-value: 7.83e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 156120951   114 MQKQFAEEQQKRFEQQQKLleEERKRRQFEEQKQKLR 150
Cdd:pfam05672   48 LRRRAEEERARREEEARRL--EEERRREEEERQRKAE 82
DUF4175 pfam13779
Domain of unknown function (DUF4175);
39-177 2.69e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 42.28  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120951    39 QGLMPMQQqgfpMVSVMQPNMQGMIGMNYSSQMSQgpiAMQA-----------------GIPMGPIPAGGMP-YLGQAPF 100
Cdd:pfam13779  577 QMLSQLQQ----MLENLQAGQPQQQQQQGQSEMQQ---AMDElgdllreqqqlldetfrQLQQQGGQQQGQPgQQGQQGQ 649
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120951   101 LGMRPPGPQYTPD-MQKQFAEEQQKRFEQQQKLLeeerkRRQFEEQKQKLRLLSSVKPKTG----EKSRDDALEAI-KGN 174
Cdd:pfam13779  650 GQQPGQGGQQPGAqMPPQGGAEALGDLAERQQAL-----RRRLEELQDELKELGGKEPGQAlgdaGRAMRDAEEALgQGD 724

                   ...
gi 156120951   175 LDG 177
Cdd:pfam13779  725 LAG 727
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
114-151 3.98e-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: 41.48  E-value: 3.98e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 156120951   114 MQKQFAEEQQKRFEQ---QQKLLEEERKRRQFEEQKQKLRL 151
Cdd:pfam15709  374 MREELELEQQRRFEEirlRKQRLEEERQRQEEEERKQRLQL 414
 
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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