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Conserved domains on  [gi|254587986|ref|NP_942583|]
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synergin gamma isoform 3 [Homo sapiens]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 10040948)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

CATH:  1.10.238.10
Gene Ontology:  GO:0005509
PubMed:  2479149|10191494
SCOP:  3001983

Graphical summary

 Zoom to residue level

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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 ...
 238-289 1.88e-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: 66.47  E-value: 1.88e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 254587986  238 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMIAVTQR 289
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 2.23e-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: 2.23e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 254587986   116 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 149
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PABP-1234 super family cl31127
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 27-150 5.10e-04

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: 44.41  E-value: 5.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986    27 FMFPVAGGIRPPQAGLM-------PMQQQGFPMVSVMQPNMQGIMGMNYSSQMSQGPIAmqagiPMG--PMPAAGMPYLG 97
Cdd:TIGR01628  375 FMQLQPRMRQLPMGSPMggamgqpPYYGQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLR-----PNGlaPMNAVRAPSRN 449

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986    98 QAPFLGMRPPGP-QYTPDMQKQFAEEQQ------KRFEQQQKLLEEERKRRQFEEQKQKL 150
Cdd:TIGR01628  450 AQNAAQKPPMQPvMYPPNYQSLPLSQDLpqpqstASQGGQNKKLAQVLASATPQMQKQVL 509
SAP130_C super family cl25748
Histone deacetylase complex subunit SAP130 C-terminus;
292-375 4.83e-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: 40.69  E-value: 4.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986   292 PAMSPDALNQFPAAPIPTLsgfsMTLPTPVSQPTVIPSGPAGSMPLSLGQPVMGINLVGP-----VGGAAAQASSGFIPT 366
Cdd:pfam16014   49 QTASASPPSQHPAQAIPTI----LAPAAPPSQPSVVLSTLPAAMAVTPPIPASMANVVAPptqpaASSTAACAVSSVLPE 124


                   ....*....
gi 254587986   367 YPANQVVKP 375
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 ...
 238-289 1.88e-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: 66.47  E-value: 1.88e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 254587986  238 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMIAVTQR 289
Cdd:cd00052    16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 238-299 1.11e-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: 1.11e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254587986    238 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMIAVTQRG--VPAMSPDAL 299
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGypIPASLPPSL 90
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 116-149 2.23e-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: 2.23e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 254587986   116 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 149
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PRK04239 PRK04239
DNA-binding protein;
116-150 4.05e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.02  E-value: 4.05e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 254587986  116 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL 150
Cdd:PRK04239    8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 27-150 5.10e-04

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: 44.41  E-value: 5.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986    27 FMFPVAGGIRPPQAGLM-------PMQQQGFPMVSVMQPNMQGIMGMNYSSQMSQGPIAmqagiPMG--PMPAAGMPYLG 97
Cdd:TIGR01628  375 FMQLQPRMRQLPMGSPMggamgqpPYYGQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLR-----PNGlaPMNAVRAPSRN 449

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986    98 QAPFLGMRPPGP-QYTPDMQKQFAEEQQ------KRFEQQQKLLEEERKRRQFEEQKQKL 150
Cdd:TIGR01628  450 AQNAAQKPPMQPvMYPPNYQSLPLSQDLpqpqstASQGGQNKKLAQVLASATPQMQKQVL 509
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 41-338 6.04e-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: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986    41 GLMPMQQQGFPM----VSVMQP--NMQGIMGMNYSSQMSQGPIAM----QAGIPM--GPMPAAGMPYLGQAPfLGMRPPG 108
Cdd:pfam09606  130 PQMPMGGAGFPSqmsrVGRMQPggQAGGMMQPSSGQPGSGTPNQMgpngGPGQGQagGMNGGQQGPMGGQMP-PQMGVPG 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986   109 PQYTPDMQKQFAEEQQKRFE---QQQKLLEEERKRRQFEEQKQ----KLRLLSSVKPKTGEKSRDDALEAIKGNLDGFSR 181
Cdd:pfam09606  209 MPGPADAGAQMGQQAQANGGmnpQQMGGAPNQVAMQQQQPQQQgqqsQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPG 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986   182 DAKMHPTPASHPKKPGVGVFPSQDPAQPRMppwiynESLVPDAYKKILETTMTPTGIDTAKLYPILMSSGLPRETLGQIW 261
Cdd:pfam09606  289 QQPGAMPNVMSIGDQNNYQQQQTRQQQQQQ------GGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGA 362

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254587986   262 ALANRTTPGKLTKEELYTVLAMIAVTQRGVPAMSPDALNQFPAAP--IPTLSGFSMTLPTPVSQPTviPSGPAGSMPLS 338
Cdd:pfam09606  363 NPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPgsQPPQSHPGGMIPSPALIPS--PSPQMSQQPAQ 439
DUF4175 pfam13779
Domain of unknown function (DUF4175);
42-178 3.42e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 41.90  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986    42 LMPMQQqgfpMVSVMQPNMQGIMGMNYSSQMSQgpiAM----------------------QAGIPMGPMPAAGmpylGQA 99
Cdd:pfam13779  579 LSQLQQ----MLENLQAGQPQQQQQQGQSEMQQ---AMdelgdllreqqqlldetfrqlqQQGGQQQGQPGQQ----GQQ 647

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986   100 PFLGMRPPGPQYTPD-MQKQFAEEQQKRFEQQQKLLeeerkRRQFEEQKQKLRLLSSVKPKTG----EKSRDDALEAI-K 173
Cdd:pfam13779  648 GQGQQPGQGGQQPGAqMPPQGGAEALGDLAERQQAL-----RRRLEELQDELKELGGKEPGQAlgdaGRAMRDAEEALgQ 722


                   ....*
gi 254587986   174 GNLDG 178
Cdd:pfam13779  723 GDLAG 727
SAP130_C pfam16014
Histone deacetylase complex subunit SAP130 C-terminus;
292-375 4.83e-03

Histone deacetylase complex subunit SAP130 C-terminus;


Pssm-ID: 464973 [Multi-domain]  Cd Length: 371  Bit Score: 40.69  E-value: 4.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986   292 PAMSPDALNQFPAAPIPTLsgfsMTLPTPVSQPTVIPSGPAGSMPLSLGQPVMGINLVGP-----VGGAAAQASSGFIPT 366
Cdd:pfam16014   49 QTASASPPSQHPAQAIPTI----LAPAAPPSQPSVVLSTLPAAMAVTPPIPASMANVVAPptqpaASSTAACAVSSVLPE 124


                   ....*....
gi 254587986   367 YPANQVVKP 375
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 ...
 238-289 1.88e-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: 66.47  E-value: 1.88e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 254587986  238 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMIAVTQR 289
Cdd:cd00052    16 ISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 238-299 1.11e-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: 1.11e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254587986    238 IDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMIAVTQRG--VPAMSPDAL 299
Cdd:smart00027   27 VTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGypIPASLPPSL 90
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 116-149 2.23e-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: 2.23e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 254587986   116 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQK 149
Cdd:pfam15346   98 QRKEAEERLAMLEEQRRMKEERQRREKEEEEREK 131
PRK04239 PRK04239
DNA-binding protein;
116-150 4.05e-04

DNA-binding protein;


Pssm-ID: 179798  Cd Length: 110  Bit Score: 41.02  E-value: 4.05e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 254587986  116 QKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL 150
Cdd:PRK04239    8 RRKLEELQKQAQEQQQAQEEQEEAQAQAEAQKQAI 42
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 27-150 5.10e-04

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: 44.41  E-value: 5.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986    27 FMFPVAGGIRPPQAGLM-------PMQQQGFPMVSVMQPNMQGIMGMNYSSQMSQGPIAmqagiPMG--PMPAAGMPYLG 97
Cdd:TIGR01628  375 FMQLQPRMRQLPMGSPMggamgqpPYYGQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLR-----PNGlaPMNAVRAPSRN 449

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986    98 QAPFLGMRPPGP-QYTPDMQKQFAEEQQ------KRFEQQQKLLEEERKRRQFEEQKQKL 150
Cdd:TIGR01628  450 AQNAAQKPPMQPvMYPPNYQSLPLSQDLpqpqstASQGGQNKKLAQVLASATPQMQKQVL 509
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 41-338 6.04e-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: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986    41 GLMPMQQQGFPM----VSVMQP--NMQGIMGMNYSSQMSQGPIAM----QAGIPM--GPMPAAGMPYLGQAPfLGMRPPG 108
Cdd:pfam09606  130 PQMPMGGAGFPSqmsrVGRMQPggQAGGMMQPSSGQPGSGTPNQMgpngGPGQGQagGMNGGQQGPMGGQMP-PQMGVPG 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986   109 PQYTPDMQKQFAEEQQKRFE---QQQKLLEEERKRRQFEEQKQ----KLRLLSSVKPKTGEKSRDDALEAIKGNLDGFSR 181
Cdd:pfam09606  209 MPGPADAGAQMGQQAQANGGmnpQQMGGAPNQVAMQQQQPQQQgqqsQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPG 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986   182 DAKMHPTPASHPKKPGVGVFPSQDPAQPRMppwiynESLVPDAYKKILETTMTPTGIDTAKLYPILMSSGLPRETLGQIW 261
Cdd:pfam09606  289 QQPGAMPNVMSIGDQNNYQQQQTRQQQQQQ------GGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGA 362

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254587986   262 ALANRTTPGKLTKEELYTVLAMIAVTQRGVPAMSPDALNQFPAAP--IPTLSGFSMTLPTPVSQPTviPSGPAGSMPLS 338
Cdd:pfam09606  363 NPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPgsQPPQSHPGGMIPSPALIPS--PSPQMSQQPAQ 439
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 115-151 7.08e-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: 7.08e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 254587986   115 MQKQFAEEQQKRFEQQQKLleEERKRRQFEEQKQKLR 151
Cdd:pfam05672   48 LRRRAEEERARREEEARRL--EEERRREEEERQRKAE 82
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 115-152 3.20e-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: 3.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 254587986   115 MQKQFAEEQQKRFEQ---QQKLLEEERKRRQFEEQKQKLRL 152
Cdd:pfam15709  374 MREELELEQQRRFEEirlRKQRLEEERQRQEEEERKQRLQL 414
DUF4175 pfam13779
Domain of unknown function (DUF4175);
42-178 3.42e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 41.90  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986    42 LMPMQQqgfpMVSVMQPNMQGIMGMNYSSQMSQgpiAM----------------------QAGIPMGPMPAAGmpylGQA 99
Cdd:pfam13779  579 LSQLQQ----MLENLQAGQPQQQQQQGQSEMQQ---AMdelgdllreqqqlldetfrqlqQQGGQQQGQPGQQ----GQQ 647

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986   100 PFLGMRPPGPQYTPD-MQKQFAEEQQKRFEQQQKLLeeerkRRQFEEQKQKLRLLSSVKPKTG----EKSRDDALEAI-K 173
Cdd:pfam13779  648 GQGQQPGQGGQQPGAqMPPQGGAEALGDLAERQQAL-----RRRLEELQDELKELGGKEPGQAlgdaGRAMRDAEEALgQ 722


                   ....*
gi 254587986   174 GNLDG 178
Cdd:pfam13779  723 GDLAG 727
SAP130_C pfam16014
Histone deacetylase complex subunit SAP130 C-terminus;
292-375 4.83e-03

Histone deacetylase complex subunit SAP130 C-terminus;


Pssm-ID: 464973 [Multi-domain]  Cd Length: 371  Bit Score: 40.69  E-value: 4.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587986   292 PAMSPDALNQFPAAPIPTLsgfsMTLPTPVSQPTVIPSGPAGSMPLSLGQPVMGINLVGP-----VGGAAAQASSGFIPT 366
Cdd:pfam16014   49 QTASASPPSQHPAQAIPTI----LAPAAPPSQPSVVLSTLPAAMAVTPPIPASMANVVAPptqpaASSTAACAVSSVLPE 124


                   ....*....
gi 254587986   367 YPANQVVKP 375
Cdd:pfam16014  125 IKIKQEAEP 133
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 110-173 5.33e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 5.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254587986  110 QYTPDMQKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKL---RLLSSVKPKTGEKSRDDALEAIK 173
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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