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Conserved domains on  [gi|209862873|ref|NP_001129508|]
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zinc finger protein 692 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 295-413 3.79e-05

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


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 46.25  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862873 295 EALASTGSQaqSAPTPAWDEDTAQIGPKRIRKAAKRELMPCDFPGCGRIFSNRQYLNHHKKYQHIHQKSFSCPEPACGKS 374
Cdd:COG5189  314 RKLPCTNSS--SNGKLAHGGERNIDTPSRMLKVKDGKPYKCPVEGCNKKYKNQNGLKYHMLHGHQNQKLHENPSPEKMNI 391

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 209862873 375 FNFKKhlkehmklhsdtRDYICEFCARSFRTSSNLVIHR 413
Cdd:COG5189  392 FSAKD------------KPYRCEVCDKRYKNLNGLKYHR 418
COG5236 super family cl28715
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
363-490 1.37e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


The actual alignment was detected with superfamily member COG5236:

Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 41.16  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862873 363 SFSCPEPACGKSFNFKKHLKEHMKlhSDTRDYICEFCArsfrtssnlvihrrihTGEKPLQCEICGFTcrqKASLNWHQR 442
Cdd:COG5236  151 SFKCPKSKCHRRCGSLKELKKHYK--AQHGFVLCSECI----------------GNKKDFWNEIRLFR---SSTLRDHKN 209

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 209862873 443 KHAETVAALRFP-CEFCGKRFEKPDSVAAHRSKSHPALLLAPQESPSGP 490
Cdd:COG5236  210 GGLEEEGFKGHPlCIFCKIYFYDDDELRRHCRLRHEACHICDMVGPIRY 258
kgd super family cl39092
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 213-330 7.95e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


The actual alignment was detected with superfamily member PRK12270:

Pssm-ID: 476867 [Multi-domain]  Cd Length: 1228  Bit Score: 39.10  E-value: 7.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862873  213 DASLWTYSSSPDDSEPDAPrllPSPVTCTPKEGE-TPPAPAALSSPLAVPALSASSLSSRAPPPAevrvqpqlsrtPQAA 291
Cdd:PRK12270   26 DPSWREFFADYGPGSTAAP---TAAAAAAAAAASaPAAAPAAKAPAAPAPAPPAAAAPAAPPKPA-----------AAAA 91

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 209862873  292 QQTEALASTGSQAQSAPTPAWDEDTAQigpkRIRKAAKR 330
Cdd:PRK12270   92 AAAAPAAPPAAAAAAAPAAAAVEDEVT----PLRGAAAA 126
 
Name Accession Description Interval E-value
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 295-413 3.79e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 46.25  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862873 295 EALASTGSQaqSAPTPAWDEDTAQIGPKRIRKAAKRELMPCDFPGCGRIFSNRQYLNHHKKYQHIHQKSFSCPEPACGKS 374
Cdd:COG5189  314 RKLPCTNSS--SNGKLAHGGERNIDTPSRMLKVKDGKPYKCPVEGCNKKYKNQNGLKYHMLHGHQNQKLHENPSPEKMNI 391

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 209862873 375 FNFKKhlkehmklhsdtRDYICEFCARSFRTSSNLVIHR 413
Cdd:COG5189  392 FSAKD------------KPYRCEVCDKRYKNLNGLKYHR 418
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
363-490 1.37e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 41.16  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862873 363 SFSCPEPACGKSFNFKKHLKEHMKlhSDTRDYICEFCArsfrtssnlvihrrihTGEKPLQCEICGFTcrqKASLNWHQR 442
Cdd:COG5236  151 SFKCPKSKCHRRCGSLKELKKHYK--AQHGFVLCSECI----------------GNKKDFWNEIRLFR---SSTLRDHKN 209

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 209862873 443 KHAETVAALRFP-CEFCGKRFEKPDSVAAHRSKSHPALLLAPQESPSGP 490
Cdd:COG5236  210 GGLEEEGFKGHPlCIFCKIYFYDDDELRRHCRLRHEACHICDMVGPIRY 258
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 334-415 3.38e-03

C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 37.01  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862873  334 PCDFPGCGRIFSNRQYLNHHKKY-----QHIHQKSFSCPEPACGKSFNFKKHLKEHMKLHSDTRDYI-CEFCARSFRTSS 407
Cdd:pfam15909   1 PCSSPGCCLSFPSVRDLAQHLRThcpptQSLEGKLFRCSALSCTETFPSMQELVAHSKLHYKPNRYFkCENCLLRFRTHR 80


                  ....*...
gi 209862873  408 NLVIHRRI 415
Cdd:pfam15909  81 SLFKHLHV 88
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 340-393 5.35e-03

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: 36.00  E-value: 5.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 209862873 340 CGRIFSNRQYLNHHKKYQHihqksFSCPEpaCGKSFNFKKHLKEHMK-LHSDTRD 393
Cdd:cd20908    7 CDREFDDEKILIQHQKAKH-----FKCHI--CHKKLYTAGGLAVHCLqVHKETLT 54
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 423-444 7.63e-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: 7.63e-03
                          10        20
                  ....*....|....*....|..
gi 209862873  423 QCEICGFTCRQKASLNWHQRKH 444
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 213-330 7.95e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 39.10  E-value: 7.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862873  213 DASLWTYSSSPDDSEPDAPrllPSPVTCTPKEGE-TPPAPAALSSPLAVPALSASSLSSRAPPPAevrvqpqlsrtPQAA 291
Cdd:PRK12270   26 DPSWREFFADYGPGSTAAP---TAAAAAAAAAASaPAAAPAAKAPAAPAPAPPAAAAPAAPPKPA-----------AAAA 91

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 209862873  292 QQTEALASTGSQAQSAPTPAWDEDTAQigpkRIRKAAKR 330
Cdd:PRK12270   92 AAAAPAAPPAAAAAAAPAAAAVEDEVT----PLRGAAAA 126
 
Name Accession Description Interval E-value
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 295-413 3.79e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 46.25  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862873 295 EALASTGSQaqSAPTPAWDEDTAQIGPKRIRKAAKRELMPCDFPGCGRIFSNRQYLNHHKKYQHIHQKSFSCPEPACGKS 374
Cdd:COG5189  314 RKLPCTNSS--SNGKLAHGGERNIDTPSRMLKVKDGKPYKCPVEGCNKKYKNQNGLKYHMLHGHQNQKLHENPSPEKMNI 391

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 209862873 375 FNFKKhlkehmklhsdtRDYICEFCARSFRTSSNLVIHR 413
Cdd:COG5189  392 FSAKD------------KPYRCEVCDKRYKNLNGLKYHR 418
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
363-490 1.37e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 41.16  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862873 363 SFSCPEPACGKSFNFKKHLKEHMKlhSDTRDYICEFCArsfrtssnlvihrrihTGEKPLQCEICGFTcrqKASLNWHQR 442
Cdd:COG5236  151 SFKCPKSKCHRRCGSLKELKKHYK--AQHGFVLCSECI----------------GNKKDFWNEIRLFR---SSTLRDHKN 209

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 209862873 443 KHAETVAALRFP-CEFCGKRFEKPDSVAAHRSKSHPALLLAPQESPSGP 490
Cdd:COG5236  210 GGLEEEGFKGHPlCIFCKIYFYDDDELRRHCRLRHEACHICDMVGPIRY 258
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 334-415 3.38e-03

C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 37.01  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862873  334 PCDFPGCGRIFSNRQYLNHHKKY-----QHIHQKSFSCPEPACGKSFNFKKHLKEHMKLHSDTRDYI-CEFCARSFRTSS 407
Cdd:pfam15909   1 PCSSPGCCLSFPSVRDLAQHLRThcpptQSLEGKLFRCSALSCTETFPSMQELVAHSKLHYKPNRYFkCENCLLRFRTHR 80


                  ....*...
gi 209862873  408 NLVIHRRI 415
Cdd:pfam15909  81 SLFKHLHV 88
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 394-416 3.95e-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: 3.95e-03
                          10        20
                  ....*....|....*....|...
gi 209862873  394 YICEFCARSFRTSSNLVIHRRIH 416
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
389-490 4.00e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862873 389 SDTRDYICEFCARSFRTSSNLVIHRRIHTGEKPLQCEICGFTCRQKASLNWHQRKHAETVAALRFPCEFCGKRFEKPDSV 468
Cdd:COG5048   29 NAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSS 108

                         90       100
                 ....*....|....*....|..
gi 209862873 469 AAHRSKSHPALLLAPQESPSGP 490
Cdd:COG5048  109 SLSSSSSNSNDNNLLSSHSLPP 130
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 364-388 4.86e-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: 34.58  E-value: 4.86e-03
                          10        20
                  ....*....|....*....|....*
gi 209862873  364 FSCPEpaCGKSFNFKKHLKEHMKLH 388
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 340-393 5.35e-03

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: 36.00  E-value: 5.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 209862873 340 CGRIFSNRQYLNHHKKYQHihqksFSCPEpaCGKSFNFKKHLKEHMK-LHSDTRD 393
Cdd:cd20908    7 CDREFDDEKILIQHQKAKH-----FKCHI--CHKKLYTAGGLAVHCLqVHKETLT 54
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 423-444 7.63e-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: 7.63e-03
                          10        20
                  ....*....|....*....|..
gi 209862873  423 QCEICGFTCRQKASLNWHQRKH 444
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 213-330 7.95e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 39.10  E-value: 7.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862873  213 DASLWTYSSSPDDSEPDAPrllPSPVTCTPKEGE-TPPAPAALSSPLAVPALSASSLSSRAPPPAevrvqpqlsrtPQAA 291
Cdd:PRK12270   26 DPSWREFFADYGPGSTAAP---TAAAAAAAAAASaPAAAPAAKAPAAPAPAPPAAAAPAAPPKPA-----------AAAA 91

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 209862873  292 QQTEALASTGSQAQSAPTPAWDEDTAQigpkRIRKAAKR 330
Cdd:PRK12270   92 AAAAPAAPPAAAAAAAPAAAAVEDEVT----PLRGAAAA 126
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 220-318 8.46e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 38.94  E-value: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862873 220 SSSPDDSEPDaPRLLPSPVTCTPKEGETPPAPAALSSPlaVPALSASSLSSRAPPPAevrVQPQL--SRTPQ-------A 290
Cdd:PHA03269  46 PHQAASRAPD-PAVAPTSAASRKPDLAQAPTPAASEKF--DPAPAPHQAASRAPDPA---VAPQLaaAPKPDaaeaftsA 119

                         90       100
                 ....*....|....*....|....*....
gi 209862873 291 AQQTEALASTG-SQAQSAPTPAWDEDTAQ 318
Cdd:PHA03269 120 AQAHEAPADAGtSAASKKPDPAAHTQHSP 148
 
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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