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Conserved domains on  [gi|1034605068|ref|XP_016881586|]
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zinc finger protein 516 isoform X1 [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 1034605068   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 1034605068   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 1034605068  915 KPVPAPGGGGFSRSATPTPTVIARAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPDSlkAKFSAQPQGPPPAKGEGGA 994
Cdd:PRK14951   365 KPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPP--APVAAPAAAAPAAAPAAAP 442

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1034605068  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 1034605068 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 1034605068  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 1034605068   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 1034605068   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 1034605068  915 KPVPAPGGGGFSRSATPTPTVIARAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPDSlkAKFSAQPQGPPPAKGEGGA 994
Cdd:PRK14951   365 KPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPP--APVAAPAAAAPAAAPAAAP 442

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1034605068  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 1034605068 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 1034605068  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 1034605068  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 1034605068    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 1034605068   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 1034605068   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 1034605068   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 1034605068  915 KPVPAPGGGGFSRSATPTPTVIARAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPDSlkAKFSAQPQGPPPAKGEGGA 994
Cdd:PRK14951   365 KPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPP--APVAAPAAAAPAAAPAAAP 442

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1034605068  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 1034605068   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 1034605068  906 AKPRQEASSKPVPAPGGGGFSRSATPTPTVIA--RAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPdslkAKFSAQPQ 983
Cdd:PTZ00436   197 AAAKQKAAAKKAAAPSGKKSAKAAAPAKAAAApaKAAAPPAKAAAAPAKAAAAPAKAAAPPAKAAAPP----AKAAAPPA 272

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034605068  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 1034605068  875 CALWAPGPDGyrqTKPCHGQEPHGAATQGPLAKPRQEASSKPVPAPGGGGFSRSATPTPTVIARAGAQPSANSKPVEKFG 954
Cdd:PRK14971   360 AQLTQKGDDA---SGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVP 436

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1034605068  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 1034605068  918 PAPGGGGFSRSATPTPTVIARAGAQPSANSKPVEKfgVPPAGAGFAPTNKHSAPDSLKAKFSAQPQGPPPAKGEGGAPPL 997
Cdd:PRK07764   590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAP--AAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034605068  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 1034605068 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 1034605068  918 PAPGGG----GFSRSATPTPTVIARAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPdSLKAKFSAQPQGPPPAKGEGG 993
Cdd:PRK07003   360 PAVTGGgapgGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAA-AAATRAEAPPAAPAPPATADR 438

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1034605068  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 1034605068  898 GAATQGPLAKPRQEASSKPVPAPGGGGFSRSATPTPTVIARAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPDSLKAK 977
Cdd:PRK07003   367 APGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGD 446

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034605068  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 1034605068  842 GGMPGSKSGSSPLGVVtkaasmPKNKESHSGGPCALWAPgpdgyrqtkpchgqePHGAATQGPLAKPRQEASskpVPAPG 921
Cdd:PRK07003   365 GGAPGGGVPARVAGAV------PAPGARAAAAVGASAVP---------------AVTAVTGAAGAALAPKAA---AAAAA 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605068  922 GGGFSRSATPTPTVIARAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPDSLKA-KFSAQPQGPPPAKGEGGAPPLPPR 1000
Cdd:PRK07003   421 TRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGsASAPASDAPPDAAFEPAPRAAAPS 500

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034605068 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 1034605068  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 1034605068   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 1034605068  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 1034605068    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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