NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462552716|ref|XP_054170845|]
View 

synergin gamma isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 416-467 1.44e-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: 66.86  E-value: 1.44e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462552716  416 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMIAVTQR 467
Cdd:cd00052     16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
ARGLU super family cl38471
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 115-148 2.48e-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: 2.48e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2462552716  115 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 148
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PABP-1234 super family cl31127
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 27-149 1.01e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


The actual alignment was detected with superfamily member TIGR01628:

Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 43.64  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716   27 FMFPVAGGIRPPQGlMPMQ-QQGFPMVSVMQPNMQ--------GIMGMNYSSQMSQGPIAmqagiPMG--PMPAAGMPYL 95
Cdd:TIGR01628  375 FMQLQPRMRQLPMG-SPMGgAMGQPPYYGQGPQQQfngqplgwPRMSMMPTPMGPGGPLR-----PNGlaPMNAVRAPSR 448

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462552716   96 GQAPFLGMRPPGP-QYTPDMQKQFAEEQQ------KRFEQQQKLLEEERKRRQFEEQKQKL 149
Cdd:TIGR01628  449 NAQNAAQKPPMQPvMYPPNYQSLPLSQDLpqpqstASQGGQNKKLAQVLASATPQMQKQVL 509
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 37-298 1.13e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716   37 PPQGLMPMQQQGFPMVSVMQPNMQGIMgmnySSQMSQGPIAMQAGIPMGPMPAAGMPY-LGQAPFLGMRPPGPQYTPDMQ 115
Cdd:pfam03154  245 PHPPLQPMTQPPPPSQVSPQPLPQPSL----HGQMPPMPHSLQTGPSHMQHPVPPQPFpLTPQSSQSQVPPGPSPAAPGQ 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716  116 KQfaeeQQKRFEQQQKLLEEERKRRQFEEQKQKLRLLSSVKPKTGEKSRddaleaikgnldgfsrdakmHPTPASH--PK 193
Cdd:pfam03154  321 SQ----QRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQ--------------------LPNPQSHkhPP 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716  194 KPDCPTSSHSTKTVSPSPAFLDEEEFSDFMQGPVEVPPCGPSSTSQPFQSfHPSTPLGQLHTQkagTQPLPPSQSPVPFA 273
Cdd:pfam03154  377 HLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP-PPAQPPVLTQSQ---SLPPPAASHPPTSG 452

                          250       260
                   ....*....|....*....|....*....
gi 2462552716  274 LHGVPGQIPY----FSTASASHSVPEAGP 298
Cdd:pfam03154  453 LHQVPSQSPFpqhpFVPGGPPPITPPSGP 481
SAP130_C super family cl25748
Histone deacetylase complex subunit SAP130 C-terminus;
470-553 7.58e-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: 40.30  E-value: 7.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716  470 PAMSPDALNQFPAAPIPTLsgfsMTLPTPVSQPTVIPSGPAGSMPLSLGQPVMGINLVGP-----VGGAAAQASSGFIPT 544
Cdd:pfam16014   49 QTASASPPSQHPAQAIPTI----LAPAAPPSQPSVVLSTLPAAMAVTPPIPASMANVVAPptqpaASSTAACAVSSVLPE 124


                   ....*....
gi 2462552716  545 YPANQVVKP 553
Cdd:pfam16014  125 IKIKQEAEP 133
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 416-467 1.44e-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: 66.86  E-value: 1.44e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462552716  416 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMIAVTQR 467
Cdd:cd00052     16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 416-477 1.14e-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: 59.60  E-value: 1.14e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462552716   416 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMIAVTQRG--VPAMSPDAL 477
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGypIPASLPPSL 90
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 115-148 2.48e-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: 2.48e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2462552716  115 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 148
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PRK04239 PRK04239
DNA-binding protein;
115-149 3.05e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.79  E-value: 3.05e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462552716  115 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL 149
Cdd:PRK04239     8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 27-149 1.01e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 43.64  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716   27 FMFPVAGGIRPPQGlMPMQ-QQGFPMVSVMQPNMQ--------GIMGMNYSSQMSQGPIAmqagiPMG--PMPAAGMPYL 95
Cdd:TIGR01628  375 FMQLQPRMRQLPMG-SPMGgAMGQPPYYGQGPQQQfngqplgwPRMSMMPTPMGPGGPLR-----PNGlaPMNAVRAPSR 448

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462552716   96 GQAPFLGMRPPGP-QYTPDMQKQFAEEQQ------KRFEQQQKLLEEERKRRQFEEQKQKL 149
Cdd:TIGR01628  449 NAQNAAQKPPMQPvMYPPNYQSLPLSQDLpqpqstASQGGQNKKLAQVLASATPQMQKQVL 509
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 28-269 1.05e-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: 43.46  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716   28 MFPVAGGIRPPQglMPMQQQGfPMVSVMQPNMQgiMGMNYSSQMSQG-PIAMQAGIP---MGPMPaagmpylgQAPFLGM 103
Cdd:pfam09606  229 MNPQQMGGAPNQ--VAMQQQQ-PQQQGQQSQLG--MGINQMQQMPQGvGGGAGQGGPgqpMGPPG--------QQPGAMP 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716  104 RPPGPQYTPDMQKQFAEEQQKRFEQQQklleeerkrrqfeEQKQKLRLLSSVkpktGEKSRDDALEAIKGNLDGFSRDAK 183
Cdd:pfam09606  296 NVMSIGDQNNYQQQQTRQQQQQQGGNH-------------PAAHQQQMNQSV----GQGGQVVALGGLNHLETWNPGNFG 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716  184 MHPTPASHPKKPDCPTSShstktvSPSPAFLDEEEFSD-FMQGP--VEVP-PCGPSSTSQPFQS--FHPSTPLGQLHTQK 257
Cdd:pfam09606  359 GLGANPMQRGQPGMMSSP------SPVPGQQVRQVTPNqFMRQSpqPSVPsPQGPGSQPPQSHPggMIPSPALIPSPSPQ 432

                          250
                   ....*....|....*.
gi 2462552716  258 AGTQP----LPPSQSP 269
Cdd:pfam09606  433 MSQQPaqqrTIGQDSP 448
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 37-298 1.13e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716   37 PPQGLMPMQQQGFPMVSVMQPNMQGIMgmnySSQMSQGPIAMQAGIPMGPMPAAGMPY-LGQAPFLGMRPPGPQYTPDMQ 115
Cdd:pfam03154  245 PHPPLQPMTQPPPPSQVSPQPLPQPSL----HGQMPPMPHSLQTGPSHMQHPVPPQPFpLTPQSSQSQVPPGPSPAAPGQ 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716  116 KQfaeeQQKRFEQQQKLLEEERKRRQFEEQKQKLRLLSSVKPKTGEKSRddaleaikgnldgfsrdakmHPTPASH--PK 193
Cdd:pfam03154  321 SQ----QRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQ--------------------LPNPQSHkhPP 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716  194 KPDCPTSSHSTKTVSPSPAFLDEEEFSDFMQGPVEVPPCGPSSTSQPFQSfHPSTPLGQLHTQkagTQPLPPSQSPVPFA 273
Cdd:pfam03154  377 HLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP-PPAQPPVLTQSQ---SLPPPAASHPPTSG 452

                          250       260
                   ....*....|....*....|....*....
gi 2462552716  274 LHGVPGQIPY----FSTASASHSVPEAGP 298
Cdd:pfam03154  453 LHQVPSQSPFpqhpFVPGGPPPITPPSGP 481
SAP130_C pfam16014
Histone deacetylase complex subunit SAP130 C-terminus;
470-553 7.58e-03

Histone deacetylase complex subunit SAP130 C-terminus;


Pssm-ID: 464973 [Multi-domain]  Cd Length: 371  Bit Score: 40.30  E-value: 7.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716  470 PAMSPDALNQFPAAPIPTLsgfsMTLPTPVSQPTVIPSGPAGSMPLSLGQPVMGINLVGP-----VGGAAAQASSGFIPT 544
Cdd:pfam16014   49 QTASASPPSQHPAQAIPTI----LAPAAPPSQPSVVLSTLPAAMAVTPPIPASMANVVAPptqpaASSTAACAVSSVLPE 124


                   ....*....
gi 2462552716  545 YPANQVVKP 553
Cdd:pfam16014  125 IKIKQEAEP 133
 
Name Accession Description Interval E-value
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 416-467 1.44e-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: 66.86  E-value: 1.44e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462552716  416 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMIAVTQR 467
Cdd:cd00052     16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 416-477 1.14e-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: 59.60  E-value: 1.14e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462552716   416 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMIAVTQRG--VPAMSPDAL 477
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGypIPASLPPSL 90
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 115-148 2.48e-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: 2.48e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2462552716  115 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 148
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PRK04239 PRK04239
DNA-binding protein;
115-149 3.05e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.79  E-value: 3.05e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462552716  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 7.88e-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: 7.88e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2462552716  114 MQKQFAEEQQKRFEQQQKLleEERKRRQFEEQKQKLR 150
Cdd:pfam05672   48 LRRRAEEERARREEEARRL--EEERRREEEERQRKAE 82
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 27-149 1.01e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 43.64  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716   27 FMFPVAGGIRPPQGlMPMQ-QQGFPMVSVMQPNMQ--------GIMGMNYSSQMSQGPIAmqagiPMG--PMPAAGMPYL 95
Cdd:TIGR01628  375 FMQLQPRMRQLPMG-SPMGgAMGQPPYYGQGPQQQfngqplgwPRMSMMPTPMGPGGPLR-----PNGlaPMNAVRAPSR 448

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462552716   96 GQAPFLGMRPPGP-QYTPDMQKQFAEEQQ------KRFEQQQKLLEEERKRRQFEEQKQKL 149
Cdd:TIGR01628  449 NAQNAAQKPPMQPvMYPPNYQSLPLSQDLpqpqstASQGGQNKKLAQVLASATPQMQKQVL 509
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 28-269 1.05e-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: 43.46  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716   28 MFPVAGGIRPPQglMPMQQQGfPMVSVMQPNMQgiMGMNYSSQMSQG-PIAMQAGIP---MGPMPaagmpylgQAPFLGM 103
Cdd:pfam09606  229 MNPQQMGGAPNQ--VAMQQQQ-PQQQGQQSQLG--MGINQMQQMPQGvGGGAGQGGPgqpMGPPG--------QQPGAMP 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716  104 RPPGPQYTPDMQKQFAEEQQKRFEQQQklleeerkrrqfeEQKQKLRLLSSVkpktGEKSRDDALEAIKGNLDGFSRDAK 183
Cdd:pfam09606  296 NVMSIGDQNNYQQQQTRQQQQQQGGNH-------------PAAHQQQMNQSV----GQGGQVVALGGLNHLETWNPGNFG 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716  184 MHPTPASHPKKPDCPTSShstktvSPSPAFLDEEEFSD-FMQGP--VEVP-PCGPSSTSQPFQS--FHPSTPLGQLHTQK 257
Cdd:pfam09606  359 GLGANPMQRGQPGMMSSP------SPVPGQQVRQVTPNqFMRQSpqPSVPsPQGPGSQPPQSHPggMIPSPALIPSPSPQ 432

                          250
                   ....*....|....*.
gi 2462552716  258 AGTQP----LPPSQSP 269
Cdd:pfam09606  433 MSQQPaqqrTIGQDSP 448
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 37-298 1.13e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716   37 PPQGLMPMQQQGFPMVSVMQPNMQGIMgmnySSQMSQGPIAMQAGIPMGPMPAAGMPY-LGQAPFLGMRPPGPQYTPDMQ 115
Cdd:pfam03154  245 PHPPLQPMTQPPPPSQVSPQPLPQPSL----HGQMPPMPHSLQTGPSHMQHPVPPQPFpLTPQSSQSQVPPGPSPAAPGQ 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716  116 KQfaeeQQKRFEQQQKLLEEERKRRQFEEQKQKLRLLSSVKPKTGEKSRddaleaikgnldgfsrdakmHPTPASH--PK 193
Cdd:pfam03154  321 SQ----QRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQ--------------------LPNPQSHkhPP 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716  194 KPDCPTSSHSTKTVSPSPAFLDEEEFSDFMQGPVEVPPCGPSSTSQPFQSfHPSTPLGQLHTQkagTQPLPPSQSPVPFA 273
Cdd:pfam03154  377 HLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP-PPAQPPVLTQSQ---SLPPPAASHPPTSG 452

                          250       260
                   ....*....|....*....|....*....
gi 2462552716  274 LHGVPGQIPY----FSTASASHSVPEAGP 298
Cdd:pfam03154  453 LHQVPSQSPFpqhpFVPGGPPPITPPSGP 481
DUF4175 pfam13779
Domain of unknown function (DUF4175);
39-177 2.64e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 42.28  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716   39 QGLMPMQQqgfpMVSVMQPNMQGIMGMNYSSQMSQgpiAM----------------------QAGIPMGPMPAAGmpylG 96
Cdd:pfam13779  577 QMLSQLQQ----MLENLQAGQPQQQQQQGQSEMQQ---AMdelgdllreqqqlldetfrqlqQQGGQQQGQPGQQ----G 645

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716   97 QAPFLGMRPPGPQYTPD-MQKQFAEEQQKRFEQQQKLLeeerkRRQFEEQKQKLRLLSSVKPKTG----EKSRDDALEAI 171
Cdd:pfam13779  646 QQGQGQQPGQGGQQPGAqMPPQGGAEALGDLAERQQAL-----RRRLEELQDELKELGGKEPGQAlgdaGRAMRDAEEAL 720


                   ....*..
gi 2462552716  172 -KGNLDG 177
Cdd:pfam13779  721 gQGDLAG 727
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 114-151 3.07e-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: 41.86  E-value: 3.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2462552716  114 MQKQFAEEQQKRFEQ---QQKLLEEERKRRQFEEQKQKLRL 151
Cdd:pfam15709  374 MREELELEQQRRFEEirlRKQRLEEERQRQEEEERKQRLQL 414
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 109-172 5.20e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 5.20e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462552716  109 QYTPDMQKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL---RLLSSVKPKTGEKSRDDALEAIK 172
Cdd:PRK09510    80 QRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAeeaAKQAALKQKQAEEAAAKAAAAAK 146
SAP130_C pfam16014
Histone deacetylase complex subunit SAP130 C-terminus;
470-553 7.58e-03

Histone deacetylase complex subunit SAP130 C-terminus;


Pssm-ID: 464973 [Multi-domain]  Cd Length: 371  Bit Score: 40.30  E-value: 7.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462552716  470 PAMSPDALNQFPAAPIPTLsgfsMTLPTPVSQPTVIPSGPAGSMPLSLGQPVMGINLVGP-----VGGAAAQASSGFIPT 544
Cdd:pfam16014   49 QTASASPPSQHPAQAIPTI----LAPAAPPSQPSVVLSTLPAAMAVTPPIPASMANVVAPptqpaASSTAACAVSSVLPE 124


                   ....*....
gi 2462552716  545 YPANQVVKP 553
Cdd:pfam16014  125 IKIKQEAEP 133
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH