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Conserved domains on  [gi|815891121|ref|NP_001295194|]
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zinc finger E-box-binding homeobox 1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
923-948 4.15e-07

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.98  E-value: 4.15e-07
                           10        20
                   ....*....|....*....|....*.
gi 815891121   923 HLIEHMRLHSGEKPYQCDKCGKRFSH 948
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
234-257 5.25e-07

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.60  E-value: 5.25e-07
                           10        20
                   ....*....|....*....|....
gi 815891121   234 HLKEHLRIHSGEKPYECPNCKKRF 257
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 220-242 4.75e-06

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: 43.83  E-value: 4.75e-06
                           10        20
                   ....*....|....*....|...
gi 815891121   220 FKCTECGKAFKYKHHLKEHLRIH 242
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
895-920 5.35e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 5.35e-05
                           10        20
                   ....*....|....*....|....*.
gi 815891121   895 SLLRHKYEHTGKRPHECGICRKAFKH 920
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
Homeodomain super family cl47488
Homeodomain;
560-607 2.07e-03

Homeodomain;


The actual alignment was detected with superfamily member pfam00046:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 37.48  E-value: 2.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 815891121   560 LSPSQpplknlLSLLKAYYALNAQPSTEELTKIADSVNLPLDVVKKWF 607
Cdd:pfam00046    7 FTPEQ------LEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWF 48
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 180-202 5.36e-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: 35.35  E-value: 5.36e-03
                           10        20
                   ....*....|....*....|...
gi 815891121   180 FSCSLCSYTFAYRTQLERHMTSH 202
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
GET2 super family cl07347
GET complex subunit GET2; This family corresponds to the GET complex subunit GET2. The GET ...
 9-150 6.07e-03

GET complex subunit GET2; This family corresponds to the GET complex subunit GET2. The GET complex is involved in the retrieval of ER resident proteins from the Golgi. It forms a complex with GET1 and constitutes the ER membrane receptor for GET3. It facilitates the release of tail- anchored (TA) proteins from GET3 and mediates the subsequent entry into the ER membrane.


The actual alignment was detected with superfamily member pfam08690:

Pssm-ID: 400847  Cd Length: 308  Bit Score: 40.08  E-value: 6.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891121     9 RRKQ------ANPRRNNVTNYNtvveANSDSDDEDKLHIVEEESVTDAADCEGGVPDDELPTDqtvlPGGSDRAGSAKNC 82
Cdd:pfam08690   12 RRQAkmanggASSRLNKITGQG----SSVKLSTTSVLDEPAAPSTTPASTTASSSPSADEHDD----PEIVDISEIASQP 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815891121    83 WQDDVKDDECDSdAENEQNHDPNVEEFLQQQDTAviypeapeedQRQGTPEASGHDDNGTPDAFSQLL 150
Cdd:pfam08690   84 KKTASVPKKPPS-SEESDPENPQLDQMFKQLLGQ----------QQQGGGENGQPAGSSTPDLFSQMM 140
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
923-948 4.15e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.98  E-value: 4.15e-07
                           10        20
                   ....*....|....*....|....*.
gi 815891121   923 HLIEHMRLHSGEKPYQCDKCGKRFSH 948
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
234-257 5.25e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.60  E-value: 5.25e-07
                           10        20
                   ....*....|....*....|....
gi 815891121   234 HLKEHLRIHSGEKPYECPNCKKRF 257
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 220-242 4.75e-06

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: 43.83  E-value: 4.75e-06
                           10        20
                   ....*....|....*....|...
gi 815891121   220 FKCTECGKAFKYKHHLKEHLRIH 242
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
895-920 5.35e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 5.35e-05
                           10        20
                   ....*....|....*....|....*.
gi 815891121   895 SLLRHKYEHTGKRPHECGICRKAFKH 920
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
220-242 5.15e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 38.22  E-value: 5.15e-04
                            10        20
                    ....*....|....*....|...
gi 815891121    220 FKCTECGKAFKYKHHLKEHLRIH 242
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
Homeodomain pfam00046
Homeodomain;
560-607 2.07e-03

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 37.48  E-value: 2.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 815891121   560 LSPSQpplknlLSLLKAYYALNAQPSTEELTKIADSVNLPLDVVKKWF 607
Cdd:pfam00046    7 FTPEQ------LEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWF 48
ZnF_C2H2 smart00355
zinc finger;
909-931 4.68e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 4.68e-03
                            10        20
                    ....*....|....*....|...
gi 815891121    909 HECGICRKAFKHKHHLIEHMRLH 931
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 180-202 5.36e-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: 35.35  E-value: 5.36e-03
                           10        20
                   ....*....|....*....|...
gi 815891121   180 FSCSLCSYTFAYRTQLERHMTSH 202
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
GET2 pfam08690
GET complex subunit GET2; This family corresponds to the GET complex subunit GET2. The GET ...
 9-150 6.07e-03

GET complex subunit GET2; This family corresponds to the GET complex subunit GET2. The GET complex is involved in the retrieval of ER resident proteins from the Golgi. It forms a complex with GET1 and constitutes the ER membrane receptor for GET3. It facilitates the release of tail- anchored (TA) proteins from GET3 and mediates the subsequent entry into the ER membrane.


Pssm-ID: 400847  Cd Length: 308  Bit Score: 40.08  E-value: 6.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891121     9 RRKQ------ANPRRNNVTNYNtvveANSDSDDEDKLHIVEEESVTDAADCEGGVPDDELPTDqtvlPGGSDRAGSAKNC 82
Cdd:pfam08690   12 RRQAkmanggASSRLNKITGQG----SSVKLSTTSVLDEPAAPSTTPASTTASSSPSADEHDD----PEIVDISEIASQP 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815891121    83 WQDDVKDDECDSdAENEQNHDPNVEEFLQQQDTAviypeapeedQRQGTPEASGHDDNGTPDAFSQLL 150
Cdd:pfam08690   84 KKTASVPKKPPS-SEESDPENPQLDQMFKQLLGQ----------QQQGGGENGQPAGSSTPDLFSQMM 140
ZnF_C2H2 smart00355
zinc finger;
180-202 6.67e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 6.67e-03
                            10        20
                    ....*....|....*....|...
gi 815891121    180 FSCSLCSYTFAYRTQLERHMTSH 202
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
923-948 4.15e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.98  E-value: 4.15e-07
                           10        20
                   ....*....|....*....|....*.
gi 815891121   923 HLIEHMRLHSGEKPYQCDKCGKRFSH 948
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
234-257 5.25e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 46.60  E-value: 5.25e-07
                           10        20
                   ....*....|....*....|....
gi 815891121   234 HLKEHLRIHSGEKPYECPNCKKRF 257
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 220-242 4.75e-06

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: 43.83  E-value: 4.75e-06
                           10        20
                   ....*....|....*....|...
gi 815891121   220 FKCTECGKAFKYKHHLKEHLRIH 242
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
895-920 5.35e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 5.35e-05
                           10        20
                   ....*....|....*....|....*.
gi 815891121   895 SLLRHKYEHTGKRPHECGICRKAFKH 920
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 909-931 8.71e-05

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: 40.36  E-value: 8.71e-05
                           10        20
                   ....*....|....*....|...
gi 815891121   909 HECGICRKAFKHKHHLIEHMRLH 931
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
220-242 5.15e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 38.22  E-value: 5.15e-04
                            10        20
                    ....*....|....*....|...
gi 815891121    220 FKCTECGKAFKYKHHLKEHLRIH 242
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
Homeodomain pfam00046
Homeodomain;
560-607 2.07e-03

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 37.48  E-value: 2.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 815891121   560 LSPSQpplknlLSLLKAYYALNAQPSTEELTKIADSVNLPLDVVKKWF 607
Cdd:pfam00046    7 FTPEQ------LEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWF 48
ZnF_C2H2 smart00355
zinc finger;
909-931 4.68e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 4.68e-03
                            10        20
                    ....*....|....*....|...
gi 815891121    909 HECGICRKAFKHKHHLIEHMRLH 931
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 937-957 5.20e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 5.20e-03
                           10        20
                   ....*....|....*....|.
gi 815891121   937 YQCDKCGKRFSHSGSYSQHMN 957
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR 21
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 180-202 5.36e-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: 35.35  E-value: 5.36e-03
                           10        20
                   ....*....|....*....|...
gi 815891121   180 FSCSLCSYTFAYRTQLERHMTSH 202
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 220-242 5.90e-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: 5.90e-03
                           10        20
                   ....*....|....*....|...
gi 815891121   220 FKCTECGKAFKYKHHLKEHLRIH 242
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23
GET2 pfam08690
GET complex subunit GET2; This family corresponds to the GET complex subunit GET2. The GET ...
 9-150 6.07e-03

GET complex subunit GET2; This family corresponds to the GET complex subunit GET2. The GET complex is involved in the retrieval of ER resident proteins from the Golgi. It forms a complex with GET1 and constitutes the ER membrane receptor for GET3. It facilitates the release of tail- anchored (TA) proteins from GET3 and mediates the subsequent entry into the ER membrane.


Pssm-ID: 400847  Cd Length: 308  Bit Score: 40.08  E-value: 6.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891121     9 RRKQ------ANPRRNNVTNYNtvveANSDSDDEDKLHIVEEESVTDAADCEGGVPDDELPTDqtvlPGGSDRAGSAKNC 82
Cdd:pfam08690   12 RRQAkmanggASSRLNKITGQG----SSVKLSTTSVLDEPAAPSTTPASTTASSSPSADEHDD----PEIVDISEIASQP 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815891121    83 WQDDVKDDECDSdAENEQNHDPNVEEFLQQQDTAviypeapeedQRQGTPEASGHDDNGTPDAFSQLL 150
Cdd:pfam08690   84 KKTASVPKKPPS-SEESDPENPQLDQMFKQLLGQ----------QQQGGGENGQPAGSSTPDLFSQMM 140
zf-H2C2_2 pfam13465
Zinc-finger double domain;
195-231 6.18e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 6.18e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 815891121   195 LERHMTSHKsgreqrhvtqsgGNRKFKCTECGKAFKY 231
Cdd:pfam13465    2 LKRHMRTHT------------GEKPYKCPECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
180-202 6.67e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 6.67e-03
                            10        20
                    ....*....|....*....|...
gi 815891121    180 FSCSLCSYTFAYRTQLERHMTSH 202
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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