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Conserved domains on  [gi|528994289|ref|XP_005220067|]
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synergin gamma isoform X1 [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 ...
 386-437 2.42e-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: 66.09  E-value: 2.42e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528994289  386 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYAVLAMIAATQR 437
Cdd:cd00052    16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
ARGLU super family cl38471
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 116-149 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 528994289   116 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 149
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
DUF4175 super family cl44629
Domain of unknown function (DUF4175);
42-178 3.97e-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: 41.51  E-value: 3.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528994289    42 LMPMQQqgfpMVSVMQPNMQGMIGMNYSSQMSQgpiAMQA-----------------GIPMGPIPAGGMP-YLGQAPFLG 103
Cdd:pfam13779  579 LSQLQQ----MLENLQAGQPQQQQQQGQSEMQQ---AMDElgdllreqqqlldetfrQLQQQGGQQQGQPgQQGQQGQGQ 651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528994289   104 MRPPGPQYTPD-MQKQFAEEQQKRFEQQQKLLeeerkRRQFEEQKQKLRLLSSVKPKTG----EKSRDDALEAI-KGNLD 177
Cdd:pfam13779  652 QPGQGGQQPGAqMPPQGGAEALGDLAERQQAL-----RRRLEELQDELKELGGKEPGQAlgdaGRAMRDAEEALgQGDLA 726


                   .
gi 528994289   178 G 178
Cdd:pfam13779  727 G 727
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 386-437 2.42e-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: 66.09  E-value: 2.42e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528994289  386 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYAVLAMIAATQR 437
Cdd:cd00052    16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 386-447 4.18e-11

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: 60.75  E-value: 4.18e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528994289    386 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYAVLAMIAATQRG--VPAMSPDAL 447
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGypIPASLPPSL 90
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 116-149 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 528994289   116 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 149
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PRK04239 PRK04239
DNA-binding protein;
116-150 3.76e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.40  E-value: 3.76e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528994289  116 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL 150
Cdd:PRK04239    8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
DUF4175 pfam13779
Domain of unknown function (DUF4175);
42-178 3.97e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 41.51  E-value: 3.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528994289    42 LMPMQQqgfpMVSVMQPNMQGMIGMNYSSQMSQgpiAMQA-----------------GIPMGPIPAGGMP-YLGQAPFLG 103
Cdd:pfam13779  579 LSQLQQ----MLENLQAGQPQQQQQQGQSEMQQ---AMDElgdllreqqqlldetfrQLQQQGGQQQGQPgQQGQQGQGQ 651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528994289   104 MRPPGPQYTPD-MQKQFAEEQQKRFEQQQKLLeeerkRRQFEEQKQKLRLLSSVKPKTG----EKSRDDALEAI-KGNLD 177
Cdd:pfam13779  652 QPGQGGQQPGAqMPPQGGAEALGDLAERQQAL-----RRRLEELQDELKELGGKEPGQAlgdaGRAMRDAEEALgQGDLA 726


                   .
gi 528994289   178 G 178
Cdd:pfam13779  727 G 727
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 386-437 2.42e-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: 66.09  E-value: 2.42e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528994289  386 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYAVLAMIAATQR 437
Cdd:cd00052    16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 386-447 4.18e-11

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: 60.75  E-value: 4.18e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528994289    386 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYAVLAMIAATQRG--VPAMSPDAL 447
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGypIPASLPPSL 90
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 116-149 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 528994289   116 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 149
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PRK04239 PRK04239
DNA-binding protein;
116-150 3.76e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.40  E-value: 3.76e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528994289  116 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL 150
Cdd:PRK04239    8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 115-151 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 528994289   115 MQKQFAEEQQKRFEQQQKLleEERKRRQFEEQKQKLR 151
Cdd:pfam05672   48 LRRRAEEERARREEEARRL--EEERRREEEERQRKAE 82
DUF4175 pfam13779
Domain of unknown function (DUF4175);
42-178 3.97e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 41.51  E-value: 3.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528994289    42 LMPMQQqgfpMVSVMQPNMQGMIGMNYSSQMSQgpiAMQA-----------------GIPMGPIPAGGMP-YLGQAPFLG 103
Cdd:pfam13779  579 LSQLQQ----MLENLQAGQPQQQQQQGQSEMQQ---AMDElgdllreqqqlldetfrQLQQQGGQQQGQPgQQGQQGQGQ 651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528994289   104 MRPPGPQYTPD-MQKQFAEEQQKRFEQQQKLLeeerkRRQFEEQKQKLRLLSSVKPKTG----EKSRDDALEAI-KGNLD 177
Cdd:pfam13779  652 QPGQGGQQPGAqMPPQGGAEALGDLAERQQAL-----RRRLEELQDELKELGGKEPGQAlgdaGRAMRDAEEALgQGDLA 726


                   .
gi 528994289   178 G 178
Cdd:pfam13779  727 G 727
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 115-152 4.30e-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: 4.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 528994289   115 MQKQFAEEQQKRFEQ---QQKLLEEERKRRQFEEQKQKLRL 152
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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