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Conserved domains on  [gi|1958661249|ref|XP_038942907|]
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synergin gamma isoform X14 [Rattus norvegicus]

Protein Classification

ARGLU and EH domain-containing protein( domain architecture ID 11865368)

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 ...
235-286 2.19e-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: 2.19e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958661249  235 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMVAVTQR 286
Cdd:cd00052     16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
30-331 2.12e-05

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: 48.85  E-value: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661249   30 AGGMRPPQGLIPMQQQGFPMVSVMQPNMQGMMGMNYSSQ---MSQGPIAMQAGIPMGPMPAAGVPFLGQPPFLGMRPAap 106
Cdd:pfam09606  155 AGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQgpmGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQ-- 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661249  107 qytpdmQKQFAEEQQKRFEQQQklleeerkrrQFEEQKQKLRLLSSVKPKTGEKNRDDALEAIKGNLDGFSRDAKMHPTP 186
Cdd:pfam09606  233 ------QMGGAPNQVAMQQQQP----------QQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPN 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661249  187 ASHPKKPGVGVFPSQDPVQPRMppwiynESLVPDAYKKILETTMTPTGIDTAKLYPILMSSGLPRETLGQIWALANRTTP 266
Cdd:pfam09606  297 VMSIGDQNNYQQQQTRQQQQQQ------GGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQP 370
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661249  267 GKLTKEELYTVLAMVAVTQRGVPAMSPDTLNQFPAAP--IPTLSGFPMTLPTPVSQPTA---MTSGPAGS 331
Cdd:pfam09606  371 GMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPgsQPPQSHPGGMIPSPALIPSPspqMSQQPAQQ 440
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
235-286 2.19e-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: 2.19e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958661249  235 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMVAVTQR 286
Cdd:cd00052     16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
235-296 1.64e-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: 1.64e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661249   235 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMVAVTQRG--VPAMSPDTL 296
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGypIPASLPPSL 90
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
30-331 2.12e-05

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: 48.85  E-value: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661249   30 AGGMRPPQGLIPMQQQGFPMVSVMQPNMQGMMGMNYSSQ---MSQGPIAMQAGIPMGPMPAAGVPFLGQPPFLGMRPAap 106
Cdd:pfam09606  155 AGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQgpmGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQ-- 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661249  107 qytpdmQKQFAEEQQKRFEQQQklleeerkrrQFEEQKQKLRLLSSVKPKTGEKNRDDALEAIKGNLDGFSRDAKMHPTP 186
Cdd:pfam09606  233 ------QMGGAPNQVAMQQQQP----------QQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPN 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661249  187 ASHPKKPGVGVFPSQDPVQPRMppwiynESLVPDAYKKILETTMTPTGIDTAKLYPILMSSGLPRETLGQIWALANRTTP 266
Cdd:pfam09606  297 VMSIGDQNNYQQQQTRQQQQQQ------GGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQP 370
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661249  267 GKLTKEELYTVLAMVAVTQRGVPAMSPDTLNQFPAAP--IPTLSGFPMTLPTPVSQPTA---MTSGPAGS 331
Cdd:pfam09606  371 GMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPgsQPPQSHPGGMIPSPALIPSPspqMSQQPAQQ 440
PRK04239 PRK04239
DNA-binding protein;
113-147 4.83e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 40.63  E-value: 4.83e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958661249  113 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL 147
Cdd:PRK04239     8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
235-286 2.19e-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: 2.19e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958661249  235 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMVAVTQR 286
Cdd:cd00052     16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
235-296 1.64e-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: 1.64e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661249   235 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMVAVTQRG--VPAMSPDTL 296
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGypIPASLPPSL 90
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
30-331 2.12e-05

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: 48.85  E-value: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661249   30 AGGMRPPQGLIPMQQQGFPMVSVMQPNMQGMMGMNYSSQ---MSQGPIAMQAGIPMGPMPAAGVPFLGQPPFLGMRPAap 106
Cdd:pfam09606  155 AGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQgpmGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQ-- 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661249  107 qytpdmQKQFAEEQQKRFEQQQklleeerkrrQFEEQKQKLRLLSSVKPKTGEKNRDDALEAIKGNLDGFSRDAKMHPTP 186
Cdd:pfam09606  233 ------QMGGAPNQVAMQQQQP----------QQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPN 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661249  187 ASHPKKPGVGVFPSQDPVQPRMppwiynESLVPDAYKKILETTMTPTGIDTAKLYPILMSSGLPRETLGQIWALANRTTP 266
Cdd:pfam09606  297 VMSIGDQNNYQQQQTRQQQQQQ------GGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQP 370
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661249  267 GKLTKEELYTVLAMVAVTQRGVPAMSPDTLNQFPAAP--IPTLSGFPMTLPTPVSQPTA---MTSGPAGS 331
Cdd:pfam09606  371 GMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPgsQPPQSHPGGMIPSPALIPSPspqMSQQPAQQ 440
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
113-146 2.14e-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: 2.14e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958661249  113 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 146
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PRK04239 PRK04239
DNA-binding protein;
113-147 4.83e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 40.63  E-value: 4.83e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958661249  113 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL 147
Cdd:PRK04239     8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
112-148 1.26e-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: 40.79  E-value: 1.26e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958661249  112 MQKQFAEEQQKRFEQQQKLleEERKRRQFEEQKQKLR 148
Cdd:pfam05672   48 LRRRAEEERARREEEARRL--EEERRREEEERQRKAE 82
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
100-170 2.84e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 2.84e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661249  100 GMRPAAPQYTPDMQKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL---RLLSSVKPKTGEKNRDDALEAIK 170
Cdd:PRK09510    73 SAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAeeaAKQAALKQKQAEEAAAKAAAAAK 146
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
112-149 4.03e-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: 4.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958661249  112 MQKQFAEEQQKRFEQ---QQKLLEEERKRRQFEEQKQKLRL 149
Cdd:pfam15709  374 MREELELEQQRRFEEirlRKQRLEEERQRQEEEERKQRLQL 414
DUF4175 pfam13779
Domain of unknown function (DUF4175);
42-175 5.77e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 40.74  E-value: 5.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661249   42 MQQqgfpMVSVMQPNMQGMMGMNYSSQMSQgpiAMQAgipMGPM---------------PAAGVPFLGQPPFLGMRPAAP 106
Cdd:pfam13779  582 LQQ----MLENLQAGQPQQQQQQGQSEMQQ---AMDE---LGDLlreqqqlldetfrqlQQQGGQQQGQPGQQGQQGQGQ 651
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661249  107 QYTPDMQKQFAEEQQKRFEQQQKLLEEERK--RRQFEEQKQKLRLLSSVKPKTG----EKNRDDALEAI-KGNLDG 175
Cdd:pfam13779  652 QPGQGGQQPGAQMPPQGGAEALGDLAERQQalRRRLEELQDELKELGGKEPGQAlgdaGRAMRDAEEALgQGDLAG 727
 
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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