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Conserved domains on  [gi|2007537679|ref|NP_981960|]
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elongator complex protein 5 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Elp5 cd19496
Elongator subcomplex subunit Elp5; Elongator is a highly conserved multiprotein complex ...
16-174 3.86e-18

Elongator subcomplex subunit Elp5; 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: 410904  Cd Length: 143  Bit Score: 79.21  E-value: 3.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007537679  16 DSVEWEGRSLLKALVKKSALCGEQVHILGCEVSEEEfregfdsdinnrlVYHDFFRDPLnwskteeafpGGPLGALRAMC 95
Cdd:cd19496     5 DSLEQSSRPLLNEFVRRALSRSTNVVYVSFETLNKP-------------SYADHFIDAT----------SKSLQELIKEI 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007537679  96 KRTDPVP------VTIALDSLSWLLLRlPCTTLCQVLHAVSHQDScpgdsssvgkVSVLGLLHEELH--------GPGPV 161
Cdd:cd19496    62 KSYLPSPsqtkkkVLVIIDSLNYILLH-SNSSLAQFLSSLASPGH----------VSVLGTYHSDLPessdsnayYPSPL 130
                         170
                  ....*....|...
gi 2007537679 162 GALSSLAQTEVTL 174
Cdd:cd19496   131 KLLQFMATTILTV 143
 
Name Accession Description Interval E-value
Elp5 cd19496
Elongator subcomplex subunit Elp5; Elongator is a highly conserved multiprotein complex ...
16-174 3.86e-18

Elongator subcomplex subunit Elp5; 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: 410904  Cd Length: 143  Bit Score: 79.21  E-value: 3.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007537679  16 DSVEWEGRSLLKALVKKSALCGEQVHILGCEVSEEEfregfdsdinnrlVYHDFFRDPLnwskteeafpGGPLGALRAMC 95
Cdd:cd19496     5 DSLEQSSRPLLNEFVRRALSRSTNVVYVSFETLNKP-------------SYADHFIDAT----------SKSLQELIKEI 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007537679  96 KRTDPVP------VTIALDSLSWLLLRlPCTTLCQVLHAVSHQDScpgdsssvgkVSVLGLLHEELH--------GPGPV 161
Cdd:cd19496    62 KSYLPSPsqtkkkVLVIIDSLNYILLH-SNSSLAQFLSSLASPGH----------VSVLGTYHSDLPessdsnayYPSPL 130
                         170
                  ....*....|...
gi 2007537679 162 GALSSLAQTEVTL 174
Cdd:cd19496   131 KLLQFMATTILTV 143
Elong_Iki1 pfam10483
Elongator subunit Iki1; This family is a component of the RNA polymerase II elongator complex. ...
16-282 5.49e-03

Elongator subunit Iki1; This family is a component of the RNA polymerase II elongator complex. This complex is involved in elongation of RNA polymerase II transcription and in modification of wobble nucleosides in tRNA.


Pssm-ID: 431307  Cd Length: 282  Bit Score: 37.57  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007537679  16 DSVEWEGRSLLKALVKKSALCGEQVHILGCEVSeeefregfdsdinNRLVYHDFFRDPLNWSKteeafpggPLGALRA-- 93
Cdd:pfam10483  19 DSLEQSARPLLREFIRRAKSSKTKVIYVSFETL-------------NKPSYADVFIDATARGK--------DLKELRKei 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007537679  94 ----MCKRTDPVPVTIALDSLSWLLLrlPCTTLCQVLhavshqdscpgdSSSVGK-VSVLGLLH-------EELHGPGPV 161
Cdd:pfam10483  78 sshlPPPPSETKKTLVIIDSLNPLYI--PNESLAQFL------------SSLISPsVSLVAVYHtdvplpnQNPYYPSPL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007537679 162 GALSSLAQTEVTLggtmgQASAHILCR-----RPRQRPT--------------------------DQTQWFSILPDFSLD 210
Cdd:pfam10483 144 TLLSYLATTILTV-----HSLSHELARkaardRSLSEPVfglleglngvlfgivlelenrrksgrAVSEWFVLDPATHTY 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2007537679 211 LQEGPSVESQPYSDPHIPPVDPTTHLTFNLHLSKKEREARDSLILPFqFssEKQQALlrprpGQATSHIFYE 282
Cdd:pfam10483 219 EVIKEAETEAPPEDEVMLLDDHPLTSTFNLGLTEKQKRAREGVVLPY-F--DAQKSL-----GGEGGAILYE 282
 
Name Accession Description Interval E-value
Elp5 cd19496
Elongator subcomplex subunit Elp5; Elongator is a highly conserved multiprotein complex ...
16-174 3.86e-18

Elongator subcomplex subunit Elp5; 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: 410904  Cd Length: 143  Bit Score: 79.21  E-value: 3.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007537679  16 DSVEWEGRSLLKALVKKSALCGEQVHILGCEVSEEEfregfdsdinnrlVYHDFFRDPLnwskteeafpGGPLGALRAMC 95
Cdd:cd19496     5 DSLEQSSRPLLNEFVRRALSRSTNVVYVSFETLNKP-------------SYADHFIDAT----------SKSLQELIKEI 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007537679  96 KRTDPVP------VTIALDSLSWLLLRlPCTTLCQVLHAVSHQDScpgdsssvgkVSVLGLLHEELH--------GPGPV 161
Cdd:cd19496    62 KSYLPSPsqtkkkVLVIIDSLNYILLH-SNSSLAQFLSSLASPGH----------VSVLGTYHSDLPessdsnayYPSPL 130
                         170
                  ....*....|...
gi 2007537679 162 GALSSLAQTEVTL 174
Cdd:cd19496   131 KLLQFMATTILTV 143
Elong_Iki1 pfam10483
Elongator subunit Iki1; This family is a component of the RNA polymerase II elongator complex. ...
16-282 5.49e-03

Elongator subunit Iki1; This family is a component of the RNA polymerase II elongator complex. This complex is involved in elongation of RNA polymerase II transcription and in modification of wobble nucleosides in tRNA.


Pssm-ID: 431307  Cd Length: 282  Bit Score: 37.57  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007537679  16 DSVEWEGRSLLKALVKKSALCGEQVHILGCEVSeeefregfdsdinNRLVYHDFFRDPLNWSKteeafpggPLGALRA-- 93
Cdd:pfam10483  19 DSLEQSARPLLREFIRRAKSSKTKVIYVSFETL-------------NKPSYADVFIDATARGK--------DLKELRKei 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007537679  94 ----MCKRTDPVPVTIALDSLSWLLLrlPCTTLCQVLhavshqdscpgdSSSVGK-VSVLGLLH-------EELHGPGPV 161
Cdd:pfam10483  78 sshlPPPPSETKKTLVIIDSLNPLYI--PNESLAQFL------------SSLISPsVSLVAVYHtdvplpnQNPYYPSPL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007537679 162 GALSSLAQTEVTLggtmgQASAHILCR-----RPRQRPT--------------------------DQTQWFSILPDFSLD 210
Cdd:pfam10483 144 TLLSYLATTILTV-----HSLSHELARkaardRSLSEPVfglleglngvlfgivlelenrrksgrAVSEWFVLDPATHTY 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2007537679 211 LQEGPSVESQPYSDPHIPPVDPTTHLTFNLHLSKKEREARDSLILPFqFssEKQQALlrprpGQATSHIFYE 282
Cdd:pfam10483 219 EVIKEAETEAPPEDEVMLLDDHPLTSTFNLGLTEKQKRAREGVVLPY-F--DAQKSL-----GGEGGAILYE 282
 
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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