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Conserved domains on  [gi|570359564|ref|NP_001275655|]
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elongator complex protein 4 isoform 3 [Homo sapiens]

Protein Classification

elongator complex protein 4( domain architecture ID 10528956)

elongator complex protein 4 is a component of the RNA polymerase II elongator complex, which is associated with the RNA polymerase II (Pol II) holoenzyme, and which is involved in transcriptional elongation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PAXNEB pfam05625
PAXNEB protein; PAXNEB or PAX6 neighbour is found in several eukaryotic organizms. PAXNED is ...
45-407 7.95e-133

PAXNEB protein; PAXNEB or PAX6 neighbour is found in several eukaryotic organizms. PAXNED is an RNA polymerase II Elongator protein subunit. It is part of the HAP subcomplex of Elongator, which is a six-subunit component of the RNA polymerase II holoenzyme. The HAP subcomplex is required for Elongator structural integrity and histone acetyltransferase activity. This protein family has a P-loop-like motif and adopts a RecA-ATPase-like fold, lacking the conserved sequence signature of ATPases.


:

Pssm-ID: 461696  Cd Length: 359  Bit Score: 390.03  E-value: 7.95e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564   45 RLVSIAGTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTVLLIEEDKYNIYSPLLFKYFLAEGIVNGHTLLVASAKEDPAN 124
Cdd:pfam05625   1 APKPIPGTRPSPHNGQLTTSTGTPSLDKLLGGGLPLGSSLLIEEDGTTDFAGVLLKYFAAEGVVQGHHVHVASLDDDPEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564  125 ILQELPAPLLDDKCKKefdEDVYNHKTPESNIKMKIAWRYQLLPKMEIGPVSSS----RFGHYYDASKRMPQELIEASNW 200
Cdd:pfam05625  81 WLRELPGPVSDDKGSS---KDRKKPKIAEEEEKMKIAWRYEKLPKVQSSLASSSneyeKFCHQFDLTKRLEPPPLSEISF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564  201 HGFFLPEKISstlkvepCSLTPGYTKLLQFIQNIIYEEGFDGSNPqkkqrnILRIGIQNLGSPLWGDDICCaenggNSHS 280
Cdd:pfam05625 158 IPLSEPQCES-------IFDSPSYASLLDQIQQILSKESFSPPTT------IHRIVIPSLLSPLWYPPDSS-----KPSD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564  281 LTKFLYVLRGLLR--TSLSACIITMPTHLI-QNKAIIARVTTLSDVVVGLESFIG-SERETNPLYK---DYHGLIHIRQI 353
Cdd:pfam05625 220 LLPFLHSLRALLRqySSNLVAMITLPSSLYpRSSGLVRWIEHLSDGVIELEPFPGeSDKELNPAYKgakDYHGLLHIHKL 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 570359564  354 PRLNNLICDESDVKDLAFKLKRKLFTIEAgvqWHdlgsrQPRLLGSSNSPASAS 407
Cdd:pfam05625 300 PVLNELGGGIPETTDLAFKLSRRKFVIEP---LH-----LPPEDGDTESSSSCG 345
 
Name Accession Description Interval E-value
PAXNEB pfam05625
PAXNEB protein; PAXNEB or PAX6 neighbour is found in several eukaryotic organizms. PAXNED is ...
45-407 7.95e-133

PAXNEB protein; PAXNEB or PAX6 neighbour is found in several eukaryotic organizms. PAXNED is an RNA polymerase II Elongator protein subunit. It is part of the HAP subcomplex of Elongator, which is a six-subunit component of the RNA polymerase II holoenzyme. The HAP subcomplex is required for Elongator structural integrity and histone acetyltransferase activity. This protein family has a P-loop-like motif and adopts a RecA-ATPase-like fold, lacking the conserved sequence signature of ATPases.


Pssm-ID: 461696  Cd Length: 359  Bit Score: 390.03  E-value: 7.95e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564   45 RLVSIAGTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTVLLIEEDKYNIYSPLLFKYFLAEGIVNGHTLLVASAKEDPAN 124
Cdd:pfam05625   1 APKPIPGTRPSPHNGQLTTSTGTPSLDKLLGGGLPLGSSLLIEEDGTTDFAGVLLKYFAAEGVVQGHHVHVASLDDDPEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564  125 ILQELPAPLLDDKCKKefdEDVYNHKTPESNIKMKIAWRYQLLPKMEIGPVSSS----RFGHYYDASKRMPQELIEASNW 200
Cdd:pfam05625  81 WLRELPGPVSDDKGSS---KDRKKPKIAEEEEKMKIAWRYEKLPKVQSSLASSSneyeKFCHQFDLTKRLEPPPLSEISF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564  201 HGFFLPEKISstlkvepCSLTPGYTKLLQFIQNIIYEEGFDGSNPqkkqrnILRIGIQNLGSPLWGDDICCaenggNSHS 280
Cdd:pfam05625 158 IPLSEPQCES-------IFDSPSYASLLDQIQQILSKESFSPPTT------IHRIVIPSLLSPLWYPPDSS-----KPSD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564  281 LTKFLYVLRGLLR--TSLSACIITMPTHLI-QNKAIIARVTTLSDVVVGLESFIG-SERETNPLYK---DYHGLIHIRQI 353
Cdd:pfam05625 220 LLPFLHSLRALLRqySSNLVAMITLPSSLYpRSSGLVRWIEHLSDGVIELEPFPGeSDKELNPAYKgakDYHGLLHIHKL 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 570359564  354 PRLNNLICDESDVKDLAFKLKRKLFTIEAgvqWHdlgsrQPRLLGSSNSPASAS 407
Cdd:pfam05625 300 PVLNELGGGIPETTDLAFKLSRRKFVIEP---LH-----LPPEDGDTESSSSCG 345
Elp4 cd19494
Elongator subcomplex subunit Elp4; Elongator is a highly conserved multiprotein complex ...
51-330 2.63e-105

Elongator subcomplex subunit Elp4; Elongator is a highly conserved multiprotein complex involved in RNA polymerase II-mediated transcriptional elongation and many other processes, including cytoskeleton organization, exocytosis, and tRNA modification. It is composed of two subcomplexes, Elp1-3 and Elp4-6. Elp4-6 forms a heterohexameric RecA-like ring structure, although they lack the key sequence signatures of ATPases.


Pssm-ID: 410902  Cd Length: 259  Bit Score: 316.17  E-value: 2.63e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564  51 GTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTVLLIEEDKYNIYSPLLFKYFLAEGIVNGHTLLVASAKEDPANILQELP 130
Cdd:cd19494    1 GTRPSPHNSQLLTSTGIASLDDLLGGGLPLGSLLLIEEDSHSSYAKLLLKYFLAEGLVSGHHVFVASADDDPFEFLRELP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564 131 APLLDDKCKKEFDEDvyNHKTPESNIKMKIAWRYQLLPKME---IGPVSSSRFGHYYDASKRMPQELIEASNWHGFFLPE 207
Cdd:cd19494   81 GPVSDSEAAEDDEDD--ASAAAGNEEDMKIAWRYQNLKKVEtsvSSSSSSPDYCHTFDLTKRMDPEALSASELTCIDPEP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564 208 KISStlkvepcslTPGYTKLLQFIQNIIYEEGFdgsnpqKKQRNILRIGIQNLGSPLWGDDIccaenggNSHSLTKFLYV 287
Cdd:cd19494  159 LSSA---------SSPYDTLLSQIQELLSASGF------GSPKNVLRIAIPSLGSPLWGDDE-------SSSELLKFLHA 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 570359564 288 LRGLLRTSLSACIITMPTHLIQNKAIIARVTTLSDVVVGLESF 330
Cdd:cd19494  217 LRSLLRSSNAVAMITVPSHLYDSPALVARLRHLADAVIELESF 259
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
63-129 1.50e-04

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 43.37  E-value: 1.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 570359564  63 VSTGLPALDQLLGGGLAVGTVLLIeedkynIYSP-----LLFKYFLAEGIVNGHTLLVASAKEDPANILQEL 129
Cdd:COG0467    2 VPTGIPGLDELLGGGLPRGSSTLL------SGPPgtgktTLALQFLAEGLRRGEKGLYVSFEESPEQLLRRA 67
 
Name Accession Description Interval E-value
PAXNEB pfam05625
PAXNEB protein; PAXNEB or PAX6 neighbour is found in several eukaryotic organizms. PAXNED is ...
45-407 7.95e-133

PAXNEB protein; PAXNEB or PAX6 neighbour is found in several eukaryotic organizms. PAXNED is an RNA polymerase II Elongator protein subunit. It is part of the HAP subcomplex of Elongator, which is a six-subunit component of the RNA polymerase II holoenzyme. The HAP subcomplex is required for Elongator structural integrity and histone acetyltransferase activity. This protein family has a P-loop-like motif and adopts a RecA-ATPase-like fold, lacking the conserved sequence signature of ATPases.


Pssm-ID: 461696  Cd Length: 359  Bit Score: 390.03  E-value: 7.95e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564   45 RLVSIAGTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTVLLIEEDKYNIYSPLLFKYFLAEGIVNGHTLLVASAKEDPAN 124
Cdd:pfam05625   1 APKPIPGTRPSPHNGQLTTSTGTPSLDKLLGGGLPLGSSLLIEEDGTTDFAGVLLKYFAAEGVVQGHHVHVASLDDDPEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564  125 ILQELPAPLLDDKCKKefdEDVYNHKTPESNIKMKIAWRYQLLPKMEIGPVSSS----RFGHYYDASKRMPQELIEASNW 200
Cdd:pfam05625  81 WLRELPGPVSDDKGSS---KDRKKPKIAEEEEKMKIAWRYEKLPKVQSSLASSSneyeKFCHQFDLTKRLEPPPLSEISF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564  201 HGFFLPEKISstlkvepCSLTPGYTKLLQFIQNIIYEEGFDGSNPqkkqrnILRIGIQNLGSPLWGDDICCaenggNSHS 280
Cdd:pfam05625 158 IPLSEPQCES-------IFDSPSYASLLDQIQQILSKESFSPPTT------IHRIVIPSLLSPLWYPPDSS-----KPSD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564  281 LTKFLYVLRGLLR--TSLSACIITMPTHLI-QNKAIIARVTTLSDVVVGLESFIG-SERETNPLYK---DYHGLIHIRQI 353
Cdd:pfam05625 220 LLPFLHSLRALLRqySSNLVAMITLPSSLYpRSSGLVRWIEHLSDGVIELEPFPGeSDKELNPAYKgakDYHGLLHIHKL 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 570359564  354 PRLNNLICDESDVKDLAFKLKRKLFTIEAgvqWHdlgsrQPRLLGSSNSPASAS 407
Cdd:pfam05625 300 PVLNELGGGIPETTDLAFKLSRRKFVIEP---LH-----LPPEDGDTESSSSCG 345
Elp4 cd19494
Elongator subcomplex subunit Elp4; Elongator is a highly conserved multiprotein complex ...
51-330 2.63e-105

Elongator subcomplex subunit Elp4; Elongator is a highly conserved multiprotein complex involved in RNA polymerase II-mediated transcriptional elongation and many other processes, including cytoskeleton organization, exocytosis, and tRNA modification. It is composed of two subcomplexes, Elp1-3 and Elp4-6. Elp4-6 forms a heterohexameric RecA-like ring structure, although they lack the key sequence signatures of ATPases.


Pssm-ID: 410902  Cd Length: 259  Bit Score: 316.17  E-value: 2.63e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564  51 GTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTVLLIEEDKYNIYSPLLFKYFLAEGIVNGHTLLVASAKEDPANILQELP 130
Cdd:cd19494    1 GTRPSPHNSQLLTSTGIASLDDLLGGGLPLGSLLLIEEDSHSSYAKLLLKYFLAEGLVSGHHVFVASADDDPFEFLRELP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564 131 APLLDDKCKKEFDEDvyNHKTPESNIKMKIAWRYQLLPKME---IGPVSSSRFGHYYDASKRMPQELIEASNWHGFFLPE 207
Cdd:cd19494   81 GPVSDSEAAEDDEDD--ASAAAGNEEDMKIAWRYQNLKKVEtsvSSSSSSPDYCHTFDLTKRMDPEALSASELTCIDPEP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359564 208 KISStlkvepcslTPGYTKLLQFIQNIIYEEGFdgsnpqKKQRNILRIGIQNLGSPLWGDDIccaenggNSHSLTKFLYV 287
Cdd:cd19494  159 LSSA---------SSPYDTLLSQIQELLSASGF------GSPKNVLRIAIPSLGSPLWGDDE-------SSSELLKFLHA 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 570359564 288 LRGLLRTSLSACIITMPTHLIQNKAIIARVTTLSDVVVGLESF 330
Cdd:cd19494  217 LRSLLRSSNAVAMITVPSHLYDSPALVARLRHLADAVIELESF 259
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
63-129 1.50e-04

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 43.37  E-value: 1.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 570359564  63 VSTGLPALDQLLGGGLAVGTVLLIeedkynIYSP-----LLFKYFLAEGIVNGHTLLVASAKEDPANILQEL 129
Cdd:COG0467    2 VPTGIPGLDELLGGGLPRGSSTLL------SGPPgtgktTLALQFLAEGLRRGEKGLYVSFEESPEQLLRRA 67
 
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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