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Conserved domains on  [gi|1907138973|ref|XP_036017398|]
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zinc finger protein 341 isoform X1 [Mus musculus]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
313-718 6.57e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.78  E-value: 6.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 313 KCSYCDKSfTKNFDLQQH----IRSHTGEKPFQCIACGRAFAQK--SNVKKHMQTHkvwppgrSGGTVSRNSvtvqvmal 386
Cdd:COG5048    32 RPDSCPNC-TDSFSRLEHltrhIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTH-------HNNPSDLNS-------- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 387 NPNRQEEEDTGLGQSLSSTTQPQaLPTAGEDEGDKPEAKQVVLIDSSYLCQFCPSKFSTYFQLKSHMIQHKKEQVykcvv 466
Cdd:COG5048    96 KSLPLSNSKASSSSLSSSSSNSN-DNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHP----- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 467 kSCAQMFPKLDTFLEHIRSHQEELS--YRCHLCSKDfpslydlGVHQYS-HSLLPQHSPKKDSTVYKCVKCVNKYStPEA 543
Cdd:COG5048   170 -PLPANSLSKDPSSNLSLLISSNVStsIPSSSENSP-------LSSSYSiPSSSSDQNLENSSSSLPLTTNSQLSP-KSL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 544 LEHHVQTATHSFPCPHCQKVFPCERYLRRH----------LPTHGSGGRFRCQICKKFFRKEHYLKLH--AHIHSGE--K 609
Cdd:COG5048   241 LSQSPSSLSSSDSSSSASESPRSSLPTASSqssspnesdsSSEKGFSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 610 PYKC--SVCESAFNRKDKLKRHMLIHEPFKKYKCPFSM----HTGCSKEFNRQDKLKAHILSHAGLKLHKCGLCSKSFSR 683
Cdd:COG5048   321 PFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNssskFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKR 400

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1907138973 684 RAHLAEHQRAHT--GNYKFRCAGCAKGFSRHKYLKDH 718
Cdd:COG5048   401 DSNLSLHIITHLsfRPYNCKNPPCSKSFNRHYNLIPH 437
KREPA super family cl49620
Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, ...
 227-364 5.91e-05

Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, respectively) proteins are components of the RNA editing complex of parasitic protozoans such as Trypanosoma and Leishmania species. These parasites have a uniquely organized mitochondrial genome, the kinetoplast. Most kinetoplast-transcribed mRNAs are cryptic and encode multiple subunits for the electron transport chain following maturation through a uridine insertion/deletion process called RNA editing. KREPAs participate in the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. The editosome, a high molecular mass enzyme complex, carries out the reaction with the help of critical enzymes and structural proteins. Five related editosome proteins KREPA1 (TbMP81), KREPA2 (TbMP63), KREPA3 (TbMP42), KREPA4 (TbMP24), KREPA5 (TbMP19), and KREPA6 (TbMP18) play critical roles in the structure and auxiliary functions of the editing process without any predicted catalytic function. The KREPA1, KREPA2, and KREPA3 proteins contain C2H2 zinc finger motifs and KREPA4 and KREPA6, contain RNA-binding domains but all have a conserved C-terminal sequences that resemble an oligonucleotide-binding (OB)-fold domain. Thus, this group of five proteins is likely to be involved in protein-protein and/or protein-RNA interactions. RNA editing is crucial for the parasite's survival in both its bloodstream and procyclic form life cycle stages which allows the parasite to adapt to its environment and maintain its viability.


The actual alignment was detected with superfamily member cd23959:

Pssm-ID: 483960 [Multi-domain]  Cd Length: 424  Bit Score: 46.40  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 227 ALGMQPYPPLEVPSQCveAPVYPTPPVYSPGKqefkPKGPSSTAPMTNATG-STVATFDSPPTlktrrakGASGLPEAAG 305
Cdd:cd23959   171 AAQQSSASPGEVASPF--ASGTVSASPFATAT----DTAPSSGAPDGFPAEaSAPSPFAAPAS-------AASFPAAPVA 237

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907138973 306 KPKAQKL--KCSYCDKSFTKNFDLQQHIRSHTGEKPfqciacgrafaQKSNVKKHMQTHKV 364
Cdd:cd23959   238 NGEAATPthACTICGKAFSTHEGLRMHSKAKHGVEL-----------EKAKTAKRKKRRSV 287
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
313-718 6.57e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.78  E-value: 6.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 313 KCSYCDKSfTKNFDLQQH----IRSHTGEKPFQCIACGRAFAQK--SNVKKHMQTHkvwppgrSGGTVSRNSvtvqvmal 386
Cdd:COG5048    32 RPDSCPNC-TDSFSRLEHltrhIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTH-------HNNPSDLNS-------- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 387 NPNRQEEEDTGLGQSLSSTTQPQaLPTAGEDEGDKPEAKQVVLIDSSYLCQFCPSKFSTYFQLKSHMIQHKKEQVykcvv 466
Cdd:COG5048    96 KSLPLSNSKASSSSLSSSSSNSN-DNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHP----- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 467 kSCAQMFPKLDTFLEHIRSHQEELS--YRCHLCSKDfpslydlGVHQYS-HSLLPQHSPKKDSTVYKCVKCVNKYStPEA 543
Cdd:COG5048   170 -PLPANSLSKDPSSNLSLLISSNVStsIPSSSENSP-------LSSSYSiPSSSSDQNLENSSSSLPLTTNSQLSP-KSL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 544 LEHHVQTATHSFPCPHCQKVFPCERYLRRH----------LPTHGSGGRFRCQICKKFFRKEHYLKLH--AHIHSGE--K 609
Cdd:COG5048   241 LSQSPSSLSSSDSSSSASESPRSSLPTASSqssspnesdsSSEKGFSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 610 PYKC--SVCESAFNRKDKLKRHMLIHEPFKKYKCPFSM----HTGCSKEFNRQDKLKAHILSHAGLKLHKCGLCSKSFSR 683
Cdd:COG5048   321 PFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNssskFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKR 400

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1907138973 684 RAHLAEHQRAHT--GNYKFRCAGCAKGFSRHKYLKDH 718
Cdd:COG5048   401 DSNLSLHIITHLsfRPYNCKNPPCSKSFNRHYNLIPH 437
zf-H2C2_2 pfam13465
Zinc-finger double domain;
326-351 7.52e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.13  E-value: 7.52e-06
                          10        20
                  ....*....|....*....|....*.
gi 1907138973 326 DLQQHIRSHTGEKPFQCIACGRAFAQ 351
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 311-363 3.60e-05

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 42.93  E-value: 3.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907138973 311 KLKCSYCDKSFTKNFDLQQHIRSHTgekpFQCIACGRAFAQKSNVKKHMQT-HK 363
Cdd:cd20908     1 KPWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQvHK 50
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 227-364 5.91e-05

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 46.40  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 227 ALGMQPYPPLEVPSQCveAPVYPTPPVYSPGKqefkPKGPSSTAPMTNATG-STVATFDSPPTlktrrakGASGLPEAAG 305
Cdd:cd23959   171 AAQQSSASPGEVASPF--ASGTVSASPFATAT----DTAPSSGAPDGFPAEaSAPSPFAAPAS-------AASFPAAPVA 237

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907138973 306 KPKAQKL--KCSYCDKSFTKNFDLQQHIRSHTGEKPfqciacgrafaQKSNVKKHMQTHKV 364
Cdd:cd23959   238 NGEAATPthACTICGKAFSTHEGLRMHSKAKHGVEL-----------EKAKTAKRKKRRSV 287
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
313-718 6.57e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.78  E-value: 6.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 313 KCSYCDKSfTKNFDLQQH----IRSHTGEKPFQCIACGRAFAQK--SNVKKHMQTHkvwppgrSGGTVSRNSvtvqvmal 386
Cdd:COG5048    32 RPDSCPNC-TDSFSRLEHltrhIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTH-------HNNPSDLNS-------- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 387 NPNRQEEEDTGLGQSLSSTTQPQaLPTAGEDEGDKPEAKQVVLIDSSYLCQFCPSKFSTYFQLKSHMIQHKKEQVykcvv 466
Cdd:COG5048    96 KSLPLSNSKASSSSLSSSSSNSN-DNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHP----- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 467 kSCAQMFPKLDTFLEHIRSHQEELS--YRCHLCSKDfpslydlGVHQYS-HSLLPQHSPKKDSTVYKCVKCVNKYStPEA 543
Cdd:COG5048   170 -PLPANSLSKDPSSNLSLLISSNVStsIPSSSENSP-------LSSSYSiPSSSSDQNLENSSSSLPLTTNSQLSP-KSL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 544 LEHHVQTATHSFPCPHCQKVFPCERYLRRH----------LPTHGSGGRFRCQICKKFFRKEHYLKLH--AHIHSGE--K 609
Cdd:COG5048   241 LSQSPSSLSSSDSSSSASESPRSSLPTASSqssspnesdsSSEKGFSLPIKSKQCNISFSRSSPLTRHlrSVNHSGEslK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 610 PYKC--SVCESAFNRKDKLKRHMLIHEPFKKYKCPFSM----HTGCSKEFNRQDKLKAHILSHAGLKLHKCGLCSKSFSR 683
Cdd:COG5048   321 PFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNssskFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKR 400

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1907138973 684 RAHLAEHQRAHT--GNYKFRCAGCAKGFSRHKYLKDH 718
Cdd:COG5048   401 DSNLSLHIITHLsfRPYNCKNPPCSKSFNRHYNLIPH 437
zf-H2C2_2 pfam13465
Zinc-finger double domain;
326-351 7.52e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.13  E-value: 7.52e-06
                          10        20
                  ....*....|....*....|....*.
gi 1907138973 326 DLQQHIRSHTGEKPFQCIACGRAFAQ 351
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 311-363 3.60e-05

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 42.93  E-value: 3.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907138973 311 KLKCSYCDKSFTKNFDLQQHIRSHTgekpFQCIACGRAFAQKSNVKKHMQT-HK 363
Cdd:cd20908     1 KPWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQvHK 50
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 227-364 5.91e-05

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 46.40  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 227 ALGMQPYPPLEVPSQCveAPVYPTPPVYSPGKqefkPKGPSSTAPMTNATG-STVATFDSPPTlktrrakGASGLPEAAG 305
Cdd:cd23959   171 AAQQSSASPGEVASPF--ASGTVSASPFATAT----DTAPSSGAPDGFPAEaSAPSPFAAPAS-------AASFPAAPVA 237

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907138973 306 KPKAQKL--KCSYCDKSFTKNFDLQQHIRSHTGEKPfqciacgrafaQKSNVKKHMQTHKV 364
Cdd:cd23959   238 NGEAATPthACTICGKAFSTHEGLRMHSKAKHGVEL-----------EKAKTAKRKKRRSV 287
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
430-593 8.22e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 8.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 430 IDSSYLCQFCPSKFSTYFQLKSHM------IQHKKEQVykCVVKSCAQMFPKLDTFLEHIRSHQEELSYRCHL--CSKDF 501
Cdd:COG5048   286 FSLPIKSKQCNISFSRSSPLTRHLrsvnhsGESLKPFS--CPYSLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKF 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907138973 502 PSLYDLGVHQY-SHSLLPQHSPKKDSTVYKCVK-CVNKYSTPEALEHHVQTATHSFPCPHCQKVFPCERYLRRHLPTHGS 579
Cdd:COG5048   364 SPLLNNEPPQSlQQYKDLKNDKKSETLSNSCIRnFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTN 443

                         170
                  ....*....|....
gi 1907138973 580 GGRFRCQICKKFFR 593
Cdd:COG5048   444 HAPLLCSILKSFRR 457
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 313-334 1.25e-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: 1.25e-03
                          10        20
                  ....*....|....*....|..
gi 1907138973 313 KCSYCDKSFTKNFDLQQHIRSH 334
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 672-694 6.20e-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: 34.97  E-value: 6.20e-03
                          10        20
                  ....*....|....*....|...
gi 1907138973 672 HKCGLCSKSFSRRAHLAEHQRAH 694
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 611-633 9.73e-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: 34.20  E-value: 9.73e-03
                          10        20
                  ....*....|....*....|...
gi 1907138973 611 YKCSVCESAFNRKDKLKRHMLIH 633
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
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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