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Conserved domains on  [gi|1958645352|ref|XP_038967312|]
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zinc finger protein 574 isoform X2 [Rattus norvegicus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 11472214)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  11361095|22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
496-850 4.58e-07

FOG: Zn-finger [General function prediction only];


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.55  E-value: 4.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 496 HKCSICGKMFKKKSHVRNHLRTHTGERPFPCPD--CSKPFNSPANLARHRLTHTGERPYRCgdCGKAFTQSSTLRQHRLV 573
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLN--SKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 574 HAQHFPYR---CQECGVRFHRPYRLLMHRYHHTGEYPYKCRECPRSFLLR--RLLEVHQLVVHAGRQPhrcPSCGAAFPS 648
Cdd:COG5048   112 SSSSNSNDnnlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqSNSLHPPLPANSLSKD---PSSNLSLLI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 649 SLRLRehrcaaaaaQAPRRFECGTCGKKVGSAARLQAHEAAHAAAGPgevlakEPPAPRAARATRTPVAPSPTALGGTTS 728
Cdd:COG5048   189 SSNVS---------TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSS------LPLTTNSQLSPKSLLSQSPSSLSSSDS 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 729 AAPAAPARRRGLECSECKKLFSTETSLQVHRRIHTgerPYPCPDCGKAFRQSTHLKDHRR--LHTGE--RPFAC--EVCG 802
Cdd:COG5048   254 SSSASESPRSSLPTASSQSSSPNESDSSSEKGFSL---PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCG 330

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958645352 803 KAFAISMRLAEHRRIHTGERPYSCP--DCGKSYRSFSNLWKHRKTHQQQH 850
Cdd:COG5048   331 KLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
lambda-1 super family cl17035
inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays ...
 458-492 7.45e-03

inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays nucleoside triphosphate phosphohydrolase (NTPase), RNA-5'-triphosphatase (RTPase), and RNA helicase activity and may play a role in the transcription of the virus genome, the unwinding or reannealing of double-stranded RNA during RNA synthesis. The RTPase activity constitutes the first step in the capping of RNA, resulting in a 5'-diphosphorylated RNA plus-strand. lambda1 is an Orthoreovirus core protein, VP3 is the homologous core protein in Aquareoviruses.


The actual alignment was detected with superfamily member cd11674:

Pssm-ID: 212564  Cd Length: 1166  Bit Score: 40.14  E-value: 7.45e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958645352  458 SAEPAAPGTYRCLLCSREFSKALQLTRHQRFVHRL 492
Cdd:cd11674     65 KATPINPSSYVCNVCMAEFSSMDQLAEHQRTTHSI 99
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
496-850 4.58e-07

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.55  E-value: 4.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 496 HKCSICGKMFKKKSHVRNHLRTHTGERPFPCPD--CSKPFNSPANLARHRLTHTGERPYRCgdCGKAFTQSSTLRQHRLV 573
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLN--SKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 574 HAQHFPYR---CQECGVRFHRPYRLLMHRYHHTGEYPYKCRECPRSFLLR--RLLEVHQLVVHAGRQPhrcPSCGAAFPS 648
Cdd:COG5048   112 SSSSNSNDnnlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqSNSLHPPLPANSLSKD---PSSNLSLLI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 649 SLRLRehrcaaaaaQAPRRFECGTCGKKVGSAARLQAHEAAHAAAGPgevlakEPPAPRAARATRTPVAPSPTALGGTTS 728
Cdd:COG5048   189 SSNVS---------TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSS------LPLTTNSQLSPKSLLSQSPSSLSSSDS 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 729 AAPAAPARRRGLECSECKKLFSTETSLQVHRRIHTgerPYPCPDCGKAFRQSTHLKDHRR--LHTGE--RPFAC--EVCG 802
Cdd:COG5048   254 SSSASESPRSSLPTASSQSSSPNESDSSSEKGFSL---PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCG 330

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958645352 803 KAFAISMRLAEHRRIHTGERPYSCP--DCGKSYRSFSNLWKHRKTHQQQH 850
Cdd:COG5048   331 KLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
zf-H2C2_2 pfam13465
Zinc-finger double domain;
754-779 3.68e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 3.68e-05
                          10        20
                  ....*....|....*....|....*.
gi 1958645352 754 SLQVHRRIHTGERPYPCPDCGKAFRQ 779
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
lambda-1 cd11674
inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays ...
 458-492 7.45e-03

inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays nucleoside triphosphate phosphohydrolase (NTPase), RNA-5'-triphosphatase (RTPase), and RNA helicase activity and may play a role in the transcription of the virus genome, the unwinding or reannealing of double-stranded RNA during RNA synthesis. The RTPase activity constitutes the first step in the capping of RNA, resulting in a 5'-diphosphorylated RNA plus-strand. lambda1 is an Orthoreovirus core protein, VP3 is the homologous core protein in Aquareoviruses.


Pssm-ID: 212564  Cd Length: 1166  Bit Score: 40.14  E-value: 7.45e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958645352  458 SAEPAAPGTYRCLLCSREFSKALQLTRHQRFVHRL 492
Cdd:cd11674     65 KATPINPSSYVCNVCMAEFSSMDQLAEHQRTTHSI 99
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
496-850 4.58e-07

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.55  E-value: 4.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 496 HKCSICGKMFKKKSHVRNHLRTHTGERPFPCPD--CSKPFNSPANLARHRLTHTGERPYRCgdCGKAFTQSSTLRQHRLV 573
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLN--SKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 574 HAQHFPYR---CQECGVRFHRPYRLLMHRYHHTGEYPYKCRECPRSFLLR--RLLEVHQLVVHAGRQPhrcPSCGAAFPS 648
Cdd:COG5048   112 SSSSNSNDnnlLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqSNSLHPPLPANSLSKD---PSSNLSLLI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 649 SLRLRehrcaaaaaQAPRRFECGTCGKKVGSAARLQAHEAAHAAAGPgevlakEPPAPRAARATRTPVAPSPTALGGTTS 728
Cdd:COG5048   189 SSNVS---------TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSS------LPLTTNSQLSPKSLLSQSPSSLSSSDS 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 729 AAPAAPARRRGLECSECKKLFSTETSLQVHRRIHTgerPYPCPDCGKAFRQSTHLKDHRR--LHTGE--RPFAC--EVCG 802
Cdd:COG5048   254 SSSASESPRSSLPTASSQSSSPNESDSSSEKGFSL---PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCG 330

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958645352 803 KAFAISMRLAEHRRIHTGERPYSCP--DCGKSYRSFSNLWKHRKTHQQQH 850
Cdd:COG5048   331 KLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
467-586 5.33e-06

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.08  E-value: 5.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 467 YRCLLCSREFSKALQLTRHQRFV-HRLE--RRHKC--SICGKMFKKKSHVRNHLRTHTGERPFPC--------------- 526
Cdd:COG5048   290 IKSKQCNISFSRSSPLTRHLRSVnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEkllnssskfspllnn 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 527 ----------------------PDCSKPFNSPANLARHRLTHTGERP--YRCGDCGKAFTQSSTLRQHRLVHAQHFPYRC 582
Cdd:COG5048   370 eppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLC 449


                  ....
gi 1958645352 583 QECG 586
Cdd:COG5048   450 SILK 453
zf-H2C2_2 pfam13465
Zinc-finger double domain;
754-779 3.68e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 3.68e-05
                          10        20
                  ....*....|....*....|....*.
gi 1958645352 754 SLQVHRRIHTGERPYPCPDCGKAFRQ 779
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
766-838 4.57e-05

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 4.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958645352 766 RPYPCPDCGKAFRQSTHLKDHRRLHTGERPFACEVCGKAFAISMRLA--EHRRIHTGERPYSCPDCGKSYRSFSN 838
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLElsRHLRTHHNNPSDLNSKSLPLSNSKAS 106
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 759-844 4.64e-05

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 47.02  E-value: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 759 RRIHT-GERPYPCP--DCGKAFRQSTHLKDHRrLHTGERPFACEVCGKAfaismrlaEHRRIHTGERPYSCPDCGKSYRS 835
Cdd:COG5189   340 RMLKVkDGKPYKCPveGCNKKYKNQNGLKYHM-LHGHQNQKLHENPSPE--------KMNIFSAKDKPYRCEVCDKRYKN 410


                  ....*....
gi 1958645352 836 FSNLWKHRK 844
Cdd:COG5189   411 LNGLKYHRK 419
zf-H2C2_2 pfam13465
Zinc-finger double domain;
538-563 1.89e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.89e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958645352 538 NLARHRLTHTGERPYRCGDCGKAFTQ 563
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
782-806 2.61e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.61e-04
                          10        20
                  ....*....|....*....|....*
gi 1958645352 782 HLKDHRRLHTGERPFACEVCGKAFA 806
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 520-603 3.57e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.94  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 520 GERPFPCP--DCSKPFNSPANLARHRLThtgerpyrcGDCGKAFTQSSTLRQHRLVHAQHFPYRCQECGVRFHRPYRLLM 597
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYHMLH---------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 1958645352 598 HRYHHT 603
Cdd:COG5189   417 HRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
810-835 6.70e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 6.70e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958645352 810 RLAEHRRIHTGERPYSCPDCGKSYRS 835
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 496-518 7.44e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.66  E-value: 7.44e-04
                          10        20
                  ....*....|....*....|...
gi 1958645352 496 HKCSICGKMFKKKSHVRNHLRTH 518
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 824-846 8.87e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.28  E-value: 8.87e-04
                          10        20
                  ....*....|....*....|...
gi 1958645352 824 YSCPDCGKSYRSFSNLWKHRKTH 846
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 768-790 1.15e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.89  E-value: 1.15e-03
                          10        20
                  ....*....|....*....|...
gi 1958645352 768 YPCPDCGKAFRQSTHLKDHRRLH 790
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
510-535 1.24e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|....*.
gi 1958645352 510 HVRNHLRTHTGERPFPCPDCSKPFNS 535
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 552-574 2.85e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 2.85e-03
                          10        20
                  ....*....|....*....|...
gi 1958645352 552 YRCGDCGKAFTQSSTLRQHRLVH 574
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
794-851 4.79e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 4.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645352 794 RPFACEVCGKAFAISMRLAEHRRIHTGERPYSCPD--CGKSYRSFSNLWKHRKTHQQQHQ 851
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPS 91
lambda-1 cd11674
inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays ...
 458-492 7.45e-03

inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays nucleoside triphosphate phosphohydrolase (NTPase), RNA-5'-triphosphatase (RTPase), and RNA helicase activity and may play a role in the transcription of the virus genome, the unwinding or reannealing of double-stranded RNA during RNA synthesis. The RTPase activity constitutes the first step in the capping of RNA, resulting in a 5'-diphosphorylated RNA plus-strand. lambda1 is an Orthoreovirus core protein, VP3 is the homologous core protein in Aquareoviruses.


Pssm-ID: 212564  Cd Length: 1166  Bit Score: 40.14  E-value: 7.45e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958645352  458 SAEPAAPGTYRCLLCSREFSKALQLTRHQRFVHRL 492
Cdd:cd11674     65 KATPINPSSYVCNVCMAEFSSMDQLAEHQRTTHSI 99
 
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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