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Conserved domains on  [gi|119586982|gb|EAW66578|]
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hCG14941, isoform CRA_a [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10443076)

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|30718982
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
48-73 1.02e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.83  E-value: 1.02e-06
                           10        20
                   ....*....|....*....|....*.
gi 119586982    48 SLSQHMRKHTGEKPYKCPYCDHRASQ 73
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 34-56 2.02e-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: 39.59  E-value: 2.02e-04
                           10        20
                   ....*....|....*....|...
gi 119586982    34 HTCCICGKSFPFQSSLSQHMRKH 56
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
915-1037 5.71e-04

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14951:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 618  Bit Score: 43.93  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586982  915 KPVPAPGGGGFSRSATPTPTVIARAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPDSlkAKFSAQPQGPPPAKGEGGA 994
Cdd:PRK14951  365 KPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPP--APVAAPAAAAPAAAPAAAP 442

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 119586982  995 PPLPPREPPSKAAQElRTLATCAAGSRGDAALQAQPGVAGAPP 1037
Cdd:PRK14951  443 AAVALAPAPPAQAAP-ETVAIPVRVAPEPAVASAAPAPAAAPA 484
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1098-1120 3.54e-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: 3.54e-03
                           10        20
                   ....*....|....*....|...
gi 119586982  1098 FVCIECGKSFHQPGHLRAHMRAH 1120
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 248-270 6.19e-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: 35.35  E-value: 6.19e-03
                           10        20
                   ....*....|....*....|...
gi 119586982   248 FPCEVCGQAFSQTWFLKAHMKKH 270
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
48-73 1.02e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.83  E-value: 1.02e-06
                           10        20
                   ....*....|....*....|....*.
gi 119586982    48 SLSQHMRKHTGEKPYKCPYCDHRASQ 73
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 34-56 2.02e-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: 39.59  E-value: 2.02e-04
                           10        20
                   ....*....|....*....|...
gi 119586982    34 HTCCICGKSFPFQSSLSQHMRKH 56
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 915-1037 5.71e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.93  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586982  915 KPVPAPGGGGFSRSATPTPTVIARAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPDSlkAKFSAQPQGPPPAKGEGGA 994
Cdd:PRK14951  365 KPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPP--APVAAPAAAAPAAAPAAAP 442

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 119586982  995 PPLPPREPPSKAAQElRTLATCAAGSRGDAALQAQPGVAGAPP 1037
Cdd:PRK14951  443 AAVALAPAPPAQAAP-ETVAIPVRVAPEPAVASAAPAPAAAPA 484
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1098-1120 3.54e-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: 3.54e-03
                           10        20
                   ....*....|....*....|...
gi 119586982  1098 FVCIECGKSFHQPGHLRAHMRAH 1120
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 248-270 6.19e-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: 35.35  E-value: 6.19e-03
                           10        20
                   ....*....|....*....|...
gi 119586982   248 FPCEVCGQAFSQTWFLKAHMKKH 270
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
1098-1120 6.85e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 6.85e-03
                            10        20
                    ....*....|....*....|...
gi 119586982   1098 FVCIECGKSFHQPGHLRAHMRAH 1120
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
34-56 9.20e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.75  E-value: 9.20e-03
                            10        20
                    ....*....|....*....|...
gi 119586982     34 HTCCICGKSFPFQSSLSQHMRKH 56
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
48-73 1.02e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.83  E-value: 1.02e-06
                           10        20
                   ....*....|....*....|....*.
gi 119586982    48 SLSQHMRKHTGEKPYKCPYCDHRASQ 73
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
62-84 6.26e-05

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 41.00  E-value: 6.26e-05
                           10        20
                   ....*....|....*....|...
gi 119586982    62 YKCPYCDHRASQKGNLKIHIRSH 84
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 34-56 2.02e-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: 39.59  E-value: 2.02e-04
                           10        20
                   ....*....|....*....|...
gi 119586982    34 HTCCICGKSFPFQSSLSQHMRKH 56
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 915-1037 5.71e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.93  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586982  915 KPVPAPGGGGFSRSATPTPTVIARAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPDSlkAKFSAQPQGPPPAKGEGGA 994
Cdd:PRK14951  365 KPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPP--APVAAPAAAAPAAAPAAAP 442

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 119586982  995 PPLPPREPPSKAAQElRTLATCAAGSRGDAALQAQPGVAGAPP 1037
Cdd:PRK14951  443 AAVALAPAPPAQAAP-ETVAIPVRVAPEPAVASAAPAPAAAPA 484
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 62-84 1.08e-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: 37.28  E-value: 1.08e-03
                           10        20
                   ....*....|....*....|...
gi 119586982    62 YKCPYCDHRASQKGNLKIHIRSH 84
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
 906-1037 1.29e-03

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 42.63  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586982  906 AKPRQEASSKPVPAPGGGGFSRSATPTPTVIA--RAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPdslkAKFSAQPQ 983
Cdd:PTZ00436  197 AAAKQKAAAKKAAAPSGKKSAKAAAPAKAAAApaKAAAPPAKAAAAPAKAAAAPAKAAAPPAKAAAPP----AKAAAPPA 272

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119586982  984 GPPPAKGEGGAPPLPPREPPSKAAQE-LRTLATCAAGSRGDAALQAQPGVAGAPP 1037
Cdd:PTZ00436  273 KAAAPPAKAAAPPAKAAAPPAKAAAApAKAAAAPAKAAAAPAKAAAPPAKAAAPP 327
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
875-990 3.22e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 41.68  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586982  875 CALWAPGPDGyrqTKPCHGQEPHGAATQGPLAKPRQEASSKPVPAPGGGGFSRSATPTPTVIARAGAQPSANSKPVEKFG 954
Cdd:PRK14971  360 AQLTQKGDDA---SGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVP 436

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 119586982  955 VPPAGAGFAPTNKHSAPDSLKAKFSAQPQGPPPAKG 990
Cdd:PRK14971  437 VNPPSTAPQAVRPAQFKEEKKIPVSKVSSLGPSTLR 472
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 918-1048 3.48e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586982  918 PAPGGGGFSRSATPTPTVIARAGAQPSANSKPVEKfgVPPAGAGFAPTNKHSAPDSLKAKFSAQPQGPPPAKGEGGAPPL 997
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAP--AAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 119586982  998 PPREPPSKAAQELRTLATCAAGSRGDAalqaqpGVAGAPPVLHSIKQEPVA 1048
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAAPAAPA------GAAPAQPAPAPAATPPAG 712
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1098-1120 3.54e-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: 3.54e-03
                           10        20
                   ....*....|....*....|...
gi 119586982  1098 FVCIECGKSFHQPGHLRAHMRAH 1120
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
918-1037 4.08e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.37  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586982  918 PAPGGG----GFSRSATPTPTVIARAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPdSLKAKFSAQPQGPPPAKGEGG 993
Cdd:PRK07003  360 PAVTGGgapgGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAA-AAATRAEAPPAAPAPPATADR 438

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 119586982  994 APPLPPREPPSKAAQELRTLATCAAGSRgDAALQAQPGVAGAPP 1037
Cdd:PRK07003  439 GDDAADGDAPVPAKANARASADSRCDER-DAQPPADSGSASAPA 481
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
898-1056 4.56e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.37  E-value: 4.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586982  898 GAATQGPLAKPRQEASSKPVPAPGGGGFSRSATPTPTVIARAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPDSLKAK 977
Cdd:PRK07003  367 APGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGD 446

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119586982  978 FSAQPQGPPPAKGEGGAPPLPPREPPSKAAQelrtlATCAAGSRGDAALQAQPGVAGAPPVLHSIKQEPVAEGHEKRLD 1056
Cdd:PRK07003  447 APVPAKANARASADSRCDERDAQPPADSGSA-----SAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASRED 520
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
842-1058 5.74e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.99  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586982  842 GGMPGSKSGSSPLGVVtkaasmPKNKESHSGGPCALWAPgpdgyrqtkpchgqePHGAATQGPLAKPRQEASskpVPAPG 921
Cdd:PRK07003  365 GGAPGGGVPARVAGAV------PAPGARAAAAVGASAVP---------------AVTAVTGAAGAALAPKAA---AAAAA 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586982  922 GGGFSRSATPTPTVIARAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPDSLKA-KFSAQPQGPPPAKGEGGAPPLPPR 1000
Cdd:PRK07003  421 TRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGsASAPASDAPPDAAFEPAPRAAAPS 500

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119586982 1001 EPPSKAAQELRTLatcAAGSRGD-AALQAQPGVAGAPPVLHSIKQEPVAEGHEKRLDIL 1058
Cdd:PRK07003  501 AATPAAVPDARAP---AAASREDaPAAAAPPAPEARPPTPAAAAPAARAGGAAAALDVL 556
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 248-270 6.19e-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: 35.35  E-value: 6.19e-03
                           10        20
                   ....*....|....*....|...
gi 119586982   248 FPCEVCGQAFSQTWFLKAHMKKH 270
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 34-56 6.56e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 35.31  E-value: 6.56e-03
                           10        20
                   ....*....|....*....|...
gi 119586982    34 HTCCICGKSFPFQSSLSQHMRKH 56
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23
ZnF_C2H2 smart00355
zinc finger;
1098-1120 6.85e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 6.85e-03
                            10        20
                    ....*....|....*....|...
gi 119586982   1098 FVCIECGKSFHQPGHLRAHMRAH 1120
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
34-56 9.20e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 34.75  E-value: 9.20e-03
                            10        20
                    ....*....|....*....|...
gi 119586982     34 HTCCICGKSFPFQSSLSQHMRKH 56
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 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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