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Conserved domains on  [gi|1510577648|gb|AYS80460|]
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RNA polymerase II largest subunit, partial [Liebermannia sp.]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNAP_largest_subunit_N super family cl19114
Largest subunit of RNA polymerase (RNAP), N-terminal domain; This region represents the ...
 1-166 1.70e-51

Largest subunit of RNA polymerase (RNAP), N-terminal domain; This region represents the N-terminal domain of the largest subunit of RNA polymerase (RNAP). RNAP is a large multi-protein complex responsible for the synthesis of RNA. It is the principle enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. At least three distinct RNAP complexes are found in eukaryotic nuclei; RNAP I transcribes the ribosomal RNA precursor, RNAP II the mRNA precursor, and RNAP III the 5S and tRNA genes. A single distinct RNAP complex is found in prokaryotes and archaea, respectively, which may be responsible for the synthesis of all RNAs. Structure studies reveal that prokaryotic and eukaryotic RNAPs share a conserved crab-claw-shaped structure. The largest and the second largest subunits each make up one clamp, one jaw, and part of the cleft. All RNAPs are metalloenzymes. At least one Mg2+ ion is bound in the catalytic center. In addition, all cellular RNAPs contain several tightly bound zinc ions to different subunits that vary between RNAPs from prokaryotic to eukaryotic lineages. This domain represents the N-terminal region of the largest subunit of RNAP, and includes part of the active site. In archaea and some of the photosynthetic organisms or cellular organelle, however, this domain exists as a separate subunit.


The actual alignment was detected with superfamily member cd02733:

Pssm-ID: 473139 [Multi-domain]  Cd Length: 751  Bit Score: 175.03  E-value: 1.70e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648   1 LADVSHQIVSPQGSKPVIGIVQDACVGSRLFTLKSSFFTRREAMSLLYSIDALPKQSDdisrymTPTILQPVELWTGKQI 80
Cdd:cd02733   398 LMMVPRQIVSPQSNKPVMGIVQDTLLGVRKLTKRDTFLEKDQVMNLLMWLPDWDGKIP------QPAILKPKPLWTGKQI 471

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648  81 FSAILPAPLFLSLPPPADVEESSeWFKRGalDGSVCVRSGILHCGVVDKRFVGAQAGGAIHAIFRDFGPSAARMFIDNVQ 160
Cdd:cd02733   472 FSLIIPKINNLIRSSSHHDGDKK-WISPG--DTKVIIENGELLSGILCKKTVGASSGGLIHVIWLEYGPEAARDFIGNIQ 548


                  ....*.
gi 1510577648 161 KLINHY 166
Cdd:cd02733   549 RVVNNW 554
 
Name Accession Description Interval E-value
RNAP_II_RPB1_N cd02733
Largest subunit (Rpb1) of eukaryotic RNA polymerase II (RNAP II), N-terminal domain; The two ...
 1-166 1.70e-51

Largest subunit (Rpb1) of eukaryotic RNA polymerase II (RNAP II), N-terminal domain; The two largest subunits of RNA polymerase II (RNAP II), Rpb1 and Rpb2, form the active site, DNA entry channel and RNA exit channel. RNAP II is a large multi-subunit complex responsible for the synthesis of mRNA in eukaryotes. RNAP II consists of a 10-subunit core enzyme and a peripheral heterodimer of two subunits. Structure studies suggest that RNAP complexes from different organisms share a crab-claw-shape structure. In yeast, Rpb1 and Rpb2, each makes up one clamp, one jaw, and part of the cleft. Rpb1_N contains part of the active site, forms the head and core of the one clamp, and makes up the pore and funnel regions of RNAP II.


Pssm-ID: 259848 [Multi-domain]  Cd Length: 751  Bit Score: 175.03  E-value: 1.70e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648   1 LADVSHQIVSPQGSKPVIGIVQDACVGSRLFTLKSSFFTRREAMSLLYSIDALPKQSDdisrymTPTILQPVELWTGKQI 80
Cdd:cd02733   398 LMMVPRQIVSPQSNKPVMGIVQDTLLGVRKLTKRDTFLEKDQVMNLLMWLPDWDGKIP------QPAILKPKPLWTGKQI 471

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648  81 FSAILPAPLFLSLPPPADVEESSeWFKRGalDGSVCVRSGILHCGVVDKRFVGAQAGGAIHAIFRDFGPSAARMFIDNVQ 160
Cdd:cd02733   472 FSLIIPKINNLIRSSSHHDGDKK-WISPG--DTKVIIENGELLSGILCKKTVGASSGGLIHVIWLEYGPEAARDFIGNIQ 548


                  ....*.
gi 1510577648 161 KLINHY 166
Cdd:cd02733   549 RVVNNW 554
RNA_pol_Rpb1_3 pfam04983
RNA polymerase Rpb1, domain 3; RNA polymerases catalyze the DNA dependent polymerization of ...
 7-166 7.77e-46

RNA polymerase Rpb1, domain 3; RNA polymerases catalyze the DNA dependent polymerization of RNA. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial. and chloroplast polymerases). This domain, domain 3, represents the pore domain. The 3' end of RNA is positioned close to this domain. The pore delimited by this domain is thought to act as a channel through which nucleotides enter the active site and/or where the 3' end of the RNA may be extruded during back-tracking.


Pssm-ID: 461507  Cd Length: 158  Bit Score: 147.39  E-value: 7.77e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648   7 QIVSPQGSKPVIGIVQDACVGSRLFTLKSSFFTRREAMSLLYSIDALPkqsddisrymTPTILQPV-ELWTGKQIFSAIL 85
Cdd:pfam04983   1 NILSPQNGKPIIGPSQDMVLGAYLLTREDTFFDREEVMQLLMYGIVLP----------HPAILKPIkPLWTGKQTFSRLL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648  86 PAPLFLSLPPPADVEESSEwfkrgaLDGSVCVRSGILHCGVVDKRFVGAQAGGAIHAIFRDFGPSAARMFIDNVQKLINH 165
Cdd:pfam04983  71 PNEINPKGKPKTNEEDLCE------NDSYVLINNGELISGVIDKKTVGKSLGSLIHIIYKEYGPEETAKFLDRLQKLGFR 144


                  .
gi 1510577648 166 Y 166
Cdd:pfam04983 145 Y 145
PRK08566 PRK08566
DNA-directed RNA polymerase subunit A'; Validated
 1-162 3.43e-32

DNA-directed RNA polymerase subunit A'; Validated


Pssm-ID: 236292 [Multi-domain]  Cd Length: 882  Bit Score: 120.73  E-value: 3.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648   1 LADVSHQIVSPQGSKPVIGIVQDACVGSRLFTLKSSFFTRREAMSLLYS--IDALPKQSddisrymtPTILQPVELWTGK 78
Cdd:PRK08566  480 LMLVQEHILSPRYGGPIIGGIQDHISGAYLLTRKSTLFTKEEALDLLRAagIDELPEPE--------PAIENGKPYWTGK 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648  79 QIFSAILPAPlfLSLPPPADVEESSEWFKRGAL--DGSVCVRSGILHCGVVDKRFVGAQAGGAIHAIFRDFGPSAARMFI 156
Cdd:PRK08566  552 QIFSLFLPKD--LNLEFKAKICSGCDECKKEDCehDAYVVIKNGKLLEGVIDKKAIGAEQGSILDRIVKEYGPERARRFL 629


                  ....*.
gi 1510577648 157 DNVQKL 162
Cdd:PRK08566  630 DSVTRL 635
 
Name Accession Description Interval E-value
RNAP_II_RPB1_N cd02733
Largest subunit (Rpb1) of eukaryotic RNA polymerase II (RNAP II), N-terminal domain; The two ...
 1-166 1.70e-51

Largest subunit (Rpb1) of eukaryotic RNA polymerase II (RNAP II), N-terminal domain; The two largest subunits of RNA polymerase II (RNAP II), Rpb1 and Rpb2, form the active site, DNA entry channel and RNA exit channel. RNAP II is a large multi-subunit complex responsible for the synthesis of mRNA in eukaryotes. RNAP II consists of a 10-subunit core enzyme and a peripheral heterodimer of two subunits. Structure studies suggest that RNAP complexes from different organisms share a crab-claw-shape structure. In yeast, Rpb1 and Rpb2, each makes up one clamp, one jaw, and part of the cleft. Rpb1_N contains part of the active site, forms the head and core of the one clamp, and makes up the pore and funnel regions of RNAP II.


Pssm-ID: 259848 [Multi-domain]  Cd Length: 751  Bit Score: 175.03  E-value: 1.70e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648   1 LADVSHQIVSPQGSKPVIGIVQDACVGSRLFTLKSSFFTRREAMSLLYSIDALPKQSDdisrymTPTILQPVELWTGKQI 80
Cdd:cd02733   398 LMMVPRQIVSPQSNKPVMGIVQDTLLGVRKLTKRDTFLEKDQVMNLLMWLPDWDGKIP------QPAILKPKPLWTGKQI 471

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648  81 FSAILPAPLFLSLPPPADVEESSeWFKRGalDGSVCVRSGILHCGVVDKRFVGAQAGGAIHAIFRDFGPSAARMFIDNVQ 160
Cdd:cd02733   472 FSLIIPKINNLIRSSSHHDGDKK-WISPG--DTKVIIENGELLSGILCKKTVGASSGGLIHVIWLEYGPEAARDFIGNIQ 548


                  ....*.
gi 1510577648 161 KLINHY 166
Cdd:cd02733   549 RVVNNW 554
RNA_pol_Rpb1_3 pfam04983
RNA polymerase Rpb1, domain 3; RNA polymerases catalyze the DNA dependent polymerization of ...
 7-166 7.77e-46

RNA polymerase Rpb1, domain 3; RNA polymerases catalyze the DNA dependent polymerization of RNA. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial. and chloroplast polymerases). This domain, domain 3, represents the pore domain. The 3' end of RNA is positioned close to this domain. The pore delimited by this domain is thought to act as a channel through which nucleotides enter the active site and/or where the 3' end of the RNA may be extruded during back-tracking.


Pssm-ID: 461507  Cd Length: 158  Bit Score: 147.39  E-value: 7.77e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648   7 QIVSPQGSKPVIGIVQDACVGSRLFTLKSSFFTRREAMSLLYSIDALPkqsddisrymTPTILQPV-ELWTGKQIFSAIL 85
Cdd:pfam04983   1 NILSPQNGKPIIGPSQDMVLGAYLLTREDTFFDREEVMQLLMYGIVLP----------HPAILKPIkPLWTGKQTFSRLL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648  86 PAPLFLSLPPPADVEESSEwfkrgaLDGSVCVRSGILHCGVVDKRFVGAQAGGAIHAIFRDFGPSAARMFIDNVQKLINH 165
Cdd:pfam04983  71 PNEINPKGKPKTNEEDLCE------NDSYVLINNGELISGVIDKKTVGKSLGSLIHIIYKEYGPEETAKFLDRLQKLGFR 144


                  .
gi 1510577648 166 Y 166
Cdd:pfam04983 145 Y 145
PRK08566 PRK08566
DNA-directed RNA polymerase subunit A'; Validated
 1-162 3.43e-32

DNA-directed RNA polymerase subunit A'; Validated


Pssm-ID: 236292 [Multi-domain]  Cd Length: 882  Bit Score: 120.73  E-value: 3.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648   1 LADVSHQIVSPQGSKPVIGIVQDACVGSRLFTLKSSFFTRREAMSLLYS--IDALPKQSddisrymtPTILQPVELWTGK 78
Cdd:PRK08566  480 LMLVQEHILSPRYGGPIIGGIQDHISGAYLLTRKSTLFTKEEALDLLRAagIDELPEPE--------PAIENGKPYWTGK 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648  79 QIFSAILPAPlfLSLPPPADVEESSEWFKRGAL--DGSVCVRSGILHCGVVDKRFVGAQAGGAIHAIFRDFGPSAARMFI 156
Cdd:PRK08566  552 QIFSLFLPKD--LNLEFKAKICSGCDECKKEDCehDAYVVIKNGKLLEGVIDKKAIGAEQGSILDRIVKEYGPERARRFL 629


                  ....*.
gi 1510577648 157 DNVQKL 162
Cdd:PRK08566  630 DSVTRL 635
RNAP_I_RPA1_N cd01435
Largest subunit (RPA1) of eukaryotic RNA polymerase I (RNAP I), N-terminal domain; RPA1 is the ...
 1-166 4.63e-31

Largest subunit (RPA1) of eukaryotic RNA polymerase I (RNAP I), N-terminal domain; RPA1 is the largest subunit of the eukaryotic RNA polymerase I (RNAP I). RNAP I is a multi-subunit protein complex responsible for the synthesis of rRNA precursors. RNAP I consists of at least 14 different subunits, the largest being homologous to subunit Rpb1 of yeast RNAP II and subunit beta' of bacterial RNAP. The yeast member of this family is known as Rpb190. Structure studies suggest that different RNA polymerase complexes share a similar crab-claw-shaped structure. The N-terminal domain of Rpb1, the largest subunit of RNAP II in yeast, forms part of the active site. It makes up the head and core of one clamp, as well as the pore and funnel structures of RNAP II. The strong homology between RPA1 and Rpb1 suggests a similar functional and structural role.


Pssm-ID: 259844 [Multi-domain]  Cd Length: 779  Bit Score: 117.67  E-value: 4.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648   1 LADVSHQIVSPQGSKPVIGIVQDACVGSRLFTLKSSFFTRREAMSLLYSIDALPKQSDDISRYMT--PTILQPVELWTGK 78
Cdd:cd01435   424 IASTDNQYLVPTDGKPLRGLIQDHVVSGVLLTSRDTFFTREEYQQLVYAALRPLFTSDKDGRIKLlpPAILKPKPLWTGK 503

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648  79 QIFSAIL-------PAPLFLSLPPPADVEESSEWFKRGALDGSVCVRSGILHCGVVDKRFVGAQAGGAIHAIFRDFGPSA 151
Cdd:cd01435   504 QVISTILknlipgnAPLLNLSGKKKTKKKVGGGKWGGGSEESQVIIRNGELLTGVLDKSQFGASAYGLVHAVYELYGGET 583

                         170
                  ....*....|....*
gi 1510577648 152 ARMFIDNVQKLINHY 166
Cdd:cd01435   584 AGKLLSALGRLFTAY 598
RNAP_archeal_A' cd02582
A' subunit of archaeal RNA polymerase (RNAP); A' is the largest subunit of the archaeal RNA ...
 1-167 4.94e-31

A' subunit of archaeal RNA polymerase (RNAP); A' is the largest subunit of the archaeal RNA polymerase (RNAP). Archaeal RNAP is closely related to RNA polymerases in eukaryotes based on the subunit compositions. Archaeal RNAP is a large multi-protein complex, made up of 11 to 13 subunits, depending on the species, that are responsible for the synthesis of RNA. Structure studies suggest that RNAP complexes from different organisms share a crab-claw-shaped structure. The largest eukaryotic RNAP subunit is encoded by two separate archaeal subunits (A' and A'') which correspond to the N- and C-terminal domains of eukaryotic RNAP II Rpb1, respectively. The N-terminal domain of Rpb1 forms part of the active site and includes the head and the core of one clamp as well as the pore and funnel structures of RNAP II. Based on a structural comparison among the archaeal, bacterial and eukaryotic RNAPs the DNA binding channel and the active site are part of A' subunit which is conserved. The strong similarity between subunit A' and the N-terminal domain of Rpb1 suggests a similar functional and structural role for these two proteins.


Pssm-ID: 259846 [Multi-domain]  Cd Length: 861  Bit Score: 117.35  E-value: 4.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648   1 LADVSHQIVSPQGSKPVIGIVQDACVGSRLFTLKSSFFTRREAMSLLYSID---ALPKqsddisrymtPTILQPVELWTG 77
Cdd:cd02582   476 LMLVQEHILSPRYGGPIIGGIQDYISGAYLLTRKTTLFTKEEALQLLSAAGydgLLPE----------PAILEPKPLWTG 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648  78 KQIFSAILPAPLFLSLPPPADVEESSEWFKRGALDGSVCVRSGILHCGVVDKRFVGAQAGGAI-HAIFRDFGPSAARMFI 156
Cdd:cd02582   546 KQLFSLFLPKDLNFEGKAKVCSGCSECKDEDCPNDGYVVIKNGKLLEGVIDKKAIGAEQPGSLlHRIAKEYGNEVARRFL 625

                         170
                  ....*....|.
gi 1510577648 157 DNVQKLINHYV 167
Cdd:cd02582   626 DSVTRLAIRFI 636
RNAP_III_RPC1_N cd02583
Largest subunit (RPC1) of eukaryotic RNA polymerase III (RNAP III), N-terminal domain; Rpc1 ...
 1-162 6.22e-23

Largest subunit (RPC1) of eukaryotic RNA polymerase III (RNAP III), N-terminal domain; Rpc1 (C160) subunit forms part of the active site region of RNAP III. RNAP III is one of the three distinct classes of nuclear RNAP in eukaryotes that is responsible for the synthesis of tRNAs, 5SrRNA, Alu-RNA, U6 snRNA genes, and some others. RNAP III is the largest nuclear RNA polymerase with 17 subunits. Structure studies suggest that different RNA polymerase complexes share a similar crab-claw-shaped structure. The N-terminal domain of Rpb1, the largest subunit of RNAP II in yeast, forms part of the active site, making up the head and core of the one clamp, as well as the pore and funnel structures of RNAP II. The strong homology between Rpc1 and Rpb1 suggests a similar functional and structural role.


Pssm-ID: 259847 [Multi-domain]  Cd Length: 816  Bit Score: 94.15  E-value: 6.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648   1 LADVSHQIVSPQGSKPVIGIVQDACVGSRLFTLKSSFFTRREAMSLL-YSIDA-----LPkqsddisrymTPTILQPVEL 74
Cdd:cd02583   450 LMGVKNNLVTPRNGEPLIAATQDFLTASYLLTSKDVFFDRAQFCQLCsYMLDGeikidLP----------PPAILKPVEL 519

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648  75 WTGKQIFSAIL-PAPlflSLPPPADVEESSEWFKRGAL-----DGSVCVRSGILHCGVVDKRFVGAQA-GGAIHAIFRDF 147
Cdd:cd02583   520 WTGKQIFSLLLrPNK---KSPVLVNLEAKEKSYTKKSPdmcpnDGYVVIRNSELLCGRLDKSTLGSGSkNSLFYVLLRDY 596

                         170
                  ....*....|....*
gi 1510577648 148 GPSAARMFIDNVQKL 162
Cdd:cd02583   597 GPEAAAAAMNRLAKL 611
PRK14977 PRK14977
bifunctional DNA-directed RNA polymerase A'/A'' subunit; Provisional
 1-167 1.16e-18

bifunctional DNA-directed RNA polymerase A'/A'' subunit; Provisional


Pssm-ID: 184940 [Multi-domain]  Cd Length: 1321  Bit Score: 82.00  E-value: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648    1 LADVSHQIVSPQGSKPVIGIVQDACVGSRLFTLKSSFFTRREAMSLLYS---IDALPKQSddisrymtpTILQPVELWTG 77
Cdd:PRK14977   496 LMGVKDNLISPRTGGPIIGALQDFITAAYLITKDDALFDKNEASNIAMLagiTDPLPEPA---------IKTKDGPAWTG 566

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648   78 KQIFSAILPAPL-FLSLPPPADVEESSEWFKRGALDGSVCVRSGILHCGVVDKRFVGAQAGG---AIHAIFRDFGPSAAR 153
Cdd:PRK14977   567 KQLFSLFLPKDFnFEGIAKWSAGKAGEAKDPSCLGDGYVLIKEGELISGVIDDNIIGALVEEpesLIDRIAKDYGEAVAI 646

                          170
                   ....*....|....
gi 1510577648  154 MFIDNVQKLINHYV 167
Cdd:PRK14977   647 EFLNKILIIAKKEI 660
RNAP_IV_RPD1_N cd10506
Largest subunit (NRPD1) of higher plant RNA polymerase IV, N-terminal domain; NRPD1 and NRPE1 ...
 1-162 5.06e-08

Largest subunit (NRPD1) of higher plant RNA polymerase IV, N-terminal domain; NRPD1 and NRPE1 are the largest subunits of plant DNA-dependent RNA polymerase IV and V that, together with second largest subunits (NRPD2 and NRPE2), form the active site region of the DNA entry and RNA exit channel. Higher plants have five multi-subunit nuclear RNA polymerases; RNAP I, RNAP II and RNAP III, which are essential for viability, plus the two isoforms of the non-essential polymerase RNAP IV and V, which specialize in small RNA-mediated gene silencing pathways. RNAP IV and/or V might be involved in RNA-directed DNA methylation of endogenous repetitive elements, silencing of transgenes, regulation of flowering-time genes, inducible regulation of adjacent gene pairs, and spreading of mobile silencing signals. The subunit compositions of RNAP IV and V reveal that they evolved from RNAP II.


Pssm-ID: 259849 [Multi-domain]  Cd Length: 744  Bit Score: 51.25  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648   1 LADVSHQIVSPQGSKPVIGIVQDACVGSRLFTLKSSFFTRREAMSL-LYSidalPKQSDDISRYMTPTILQPveLWTGKQ 79
Cdd:cd10506   368 LVALPKQLISSQSGQNLLSLTQDSLLAAHLMTERGVFLDKAQMQQLqMLC----PSQLPPPAIIKSPPSNGP--LWTGKQ 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510577648  80 IFSAILPAPLFLSLPppadveessewfkrgalDGSVCVRSG-ILHCGvvDKRFVGAQAGGAIHAIFRDFGPSAARMFIDN 158
Cdd:cd10506   442 LFQMLLPTDLDYSFP-----------------SNLVFISDGeLISSS--GGSSWLRDSEGNLFSILVKHGPGKALDFLDS 502


                  ....
gi 1510577648 159 VQKL 162
Cdd:cd10506   503 AQGL 506
 
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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