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Conserved domains on  [gi|156416026|ref|NP_001095924|]
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zinc finger protein 219 [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10443135)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
512-537 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 156416026  512 HLKVHLRVHTGERPYKCPHCDYAGTQ 537
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 500-520 1.93e-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: 38.82  E-value: 1.93e-04
                          10        20
                  ....*....|....*....|.
gi 156416026  500 CPFCGKSFRSAHHLKVHLRVH 520
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 274-296 1.62e-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: 36.12  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|...
gi 156416026  274 FRCQVCGQSFTQSWFLKGHMRKH 296
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
RPC10 COG1996
DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; ...
 53-93 2.32e-03

DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger is part of the Pathway/BioSystem: RNA polymerase


:

Pssm-ID: 441599  Cd Length: 48  Bit Score: 36.60  E-value: 2.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 156416026  53 GERRFPCPVCGKRFRFNsilalhlrahPGAQAFQCPHCGHR 93
Cdd:COG1996    2 AMVEYKCPRCGAEVELD----------EGTPAIRCPYCGSR 32
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 302-324 4.36e-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: 4.36e-03
                          10        20
                  ....*....|....*....|...
gi 156416026  302 HACPVCGRCFKEPWFLKNHMKVH 324
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 85-107 8.41e-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: 8.41e-03
                          10        20
                  ....*....|....*....|...
gi 156416026   85 FQCPHCGHRAAQRALLRSHLRTH 107
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 453-612 9.21e-03

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 39.29  E-value: 9.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156416026 453 HPRPGEGPGHSASAAGAQARSTATQEENGLLVGGTRP-EGGRGATGKDCPFCGKSFRSAHHlkvhlrvhtgeRPYKCPhc 531
Cdd:PTZ00449 507 HDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPkEGGKPGETKEGEVGKKPGPAKEH-----------KPSKIP-- 573

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156416026 532 DYAGTQSGSLKYHLQRHHREQRSgagpgppPEPPPPSQRGSAPQSGAKPS----PQPATWVEGASSPRPPSSGAGPGSRR 607
Cdd:PTZ00449 574 TLSKKPEFPKDPKHPKDPEEPKK-------PKRPRSAQRPTRPKSPKLPElldiPKSPKRPESPKSPKRPPPPQRPSSPE 646


                 ....*
gi 156416026 608 KPASP 612
Cdd:PTZ00449 647 RPEGP 651
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
512-537 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 156416026  512 HLKVHLRVHTGERPYKCPHCDYAGTQ 537
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 500-520 1.93e-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: 38.82  E-value: 1.93e-04
                          10        20
                  ....*....|....*....|.
gi 156416026  500 CPFCGKSFRSAHHLKVHLRVH 520
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 274-296 1.62e-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: 36.12  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|...
gi 156416026  274 FRCQVCGQSFTQSWFLKGHMRKH 296
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
RPC10 COG1996
DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; ...
 53-93 2.32e-03

DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger is part of the Pathway/BioSystem: RNA polymerase


Pssm-ID: 441599  Cd Length: 48  Bit Score: 36.60  E-value: 2.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 156416026  53 GERRFPCPVCGKRFRFNsilalhlrahPGAQAFQCPHCGHR 93
Cdd:COG1996    2 AMVEYKCPRCGAEVELD----------EGTPAIRCPYCGSR 32
ZnF_C2H2 smart00355
zinc finger;
500-520 2.73e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.73e-03
                           10        20
                   ....*....|....*....|.
gi 156416026   500 CPFCGKSFRSAHHLKVHLRVH 520
Cdd:smart00355   3 CPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 302-324 4.36e-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: 4.36e-03
                          10        20
                  ....*....|....*....|...
gi 156416026  302 HACPVCGRCFKEPWFLKNHMKVH 324
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 85-107 8.41e-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: 8.41e-03
                          10        20
                  ....*....|....*....|...
gi 156416026   85 FQCPHCGHRAAQRALLRSHLRTH 107
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 453-612 9.21e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 39.29  E-value: 9.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156416026 453 HPRPGEGPGHSASAAGAQARSTATQEENGLLVGGTRP-EGGRGATGKDCPFCGKSFRSAHHlkvhlrvhtgeRPYKCPhc 531
Cdd:PTZ00449 507 HDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPkEGGKPGETKEGEVGKKPGPAKEH-----------KPSKIP-- 573

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156416026 532 DYAGTQSGSLKYHLQRHHREQRSgagpgppPEPPPPSQRGSAPQSGAKPS----PQPATWVEGASSPRPPSSGAGPGSRR 607
Cdd:PTZ00449 574 TLSKKPEFPKDPKHPKDPEEPKK-------PKRPRSAQRPTRPKSPKLPElldiPKSPKRPESPKSPKRPPPPQRPSSPE 646


                 ....*
gi 156416026 608 KPASP 612
Cdd:PTZ00449 647 RPEGP 651
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
512-537 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 156416026  512 HLKVHLRVHTGERPYKCPHCDYAGTQ 537
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
526-549 9.19e-05

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 39.84  E-value: 9.19e-05
                          10        20
                  ....*....|....*....|....
gi 156416026  526 YKCPHCDYAGTQSGSLKYHLQRHH 549
Cdd:pfam13909   1 YKCSQCDYSTAWKSNLKRHLRKHT 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 500-520 1.93e-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: 38.82  E-value: 1.93e-04
                          10        20
                  ....*....|....*....|.
gi 156416026  500 CPFCGKSFRSAHHLKVHLRVH 520
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 274-296 1.62e-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: 36.12  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|...
gi 156416026  274 FRCQVCGQSFTQSWFLKGHMRKH 296
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
RPC10 COG1996
DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; ...
 53-93 2.32e-03

DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger is part of the Pathway/BioSystem: RNA polymerase


Pssm-ID: 441599  Cd Length: 48  Bit Score: 36.60  E-value: 2.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 156416026  53 GERRFPCPVCGKRFRFNsilalhlrahPGAQAFQCPHCGHR 93
Cdd:COG1996    2 AMVEYKCPRCGAEVELD----------EGTPAIRCPYCGSR 32
ZnF_C2H2 smart00355
zinc finger;
500-520 2.73e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 2.73e-03
                           10        20
                   ....*....|....*....|.
gi 156416026   500 CPFCGKSFRSAHHLKVHLRVH 520
Cdd:smart00355   3 CPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 302-324 4.36e-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: 4.36e-03
                          10        20
                  ....*....|....*....|...
gi 156416026  302 HACPVCGRCFKEPWFLKNHMKVH 324
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 85-107 8.41e-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: 8.41e-03
                          10        20
                  ....*....|....*....|...
gi 156416026   85 FQCPHCGHRAAQRALLRSHLRTH 107
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 453-612 9.21e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 39.29  E-value: 9.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156416026 453 HPRPGEGPGHSASAAGAQARSTATQEENGLLVGGTRP-EGGRGATGKDCPFCGKSFRSAHHlkvhlrvhtgeRPYKCPhc 531
Cdd:PTZ00449 507 HDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPkEGGKPGETKEGEVGKKPGPAKEH-----------KPSKIP-- 573

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156416026 532 DYAGTQSGSLKYHLQRHHREQRSgagpgppPEPPPPSQRGSAPQSGAKPS----PQPATWVEGASSPRPPSSGAGPGSRR 607
Cdd:PTZ00449 574 TLSKKPEFPKDPKHPKDPEEPKK-------PKRPRSAQRPTRPKSPKLPElldiPKSPKRPESPKSPKRPPPPQRPSSPE 646


                 ....*
gi 156416026 608 KPASP 612
Cdd:PTZ00449 647 RPEGP 651
 
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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