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Conserved domains on  [gi|189409128|ref|NP_110378|]
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zinc finger E-box-binding homeobox 1 isoform b [Homo sapiens]

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;
946-971 4.59e-07

Zinc-finger double domain;


:

Pssm-ID: 404364 [Multi-domain]  Cd Length: 26  Bit Score: 46.96  E-value: 4.59e-07
                           10        20
                   ....*....|....*....|....*.
gi 189409128   946 HLIEHMRLHSGEKPYQCDKCGKRFSH 971
Cdd:pfam13465    1 NLKRHMRKHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
254-277 8.68e-07

Zinc-finger double domain;


:

Pssm-ID: 404364 [Multi-domain]  Cd Length: 26  Bit Score: 46.19  E-value: 8.68e-07
                           10        20
                   ....*....|....*....|....
gi 189409128   254 HLKEHLRIHSGEKPYECPNCKKRF 277
Cdd:pfam13465    1 NLKRHMRKHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
240-262 3.86e-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: 44.21  E-value: 3.86e-06
                           10        20
                   ....*....|....*....|...
gi 189409128   240 FKCTECGKAFKYKHHLKEHLRIH 262
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
932-954 3.26e-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: 41.52  E-value: 3.26e-05
                           10        20
                   ....*....|....*....|...
gi 189409128   932 HECGICKKAFKHKHHLIEHMRLH 954
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
918-943 6.92e-05

Zinc-finger double domain;


:

Pssm-ID: 404364 [Multi-domain]  Cd Length: 26  Bit Score: 40.80  E-value: 6.92e-05
                           10        20
                   ....*....|....*....|....*.
gi 189409128   918 SLLRHKYEHTGKRPHECGICKKAFKH 943
Cdd:pfam13465    1 NLKRHMRKHTGEKPYKCPECGKSFKS 26
MDN1 super family cl34967
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
27-197 5.64e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG5271:

Pssm-ID: 227596 [Multi-domain]  Cd Length: 4600  Bit Score: 44.22  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409128   27 VETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPgrSSEREGNAKNCWEDDRKEGQEilGPEAQADEAGCT 106
Cdd:COG5271  4002 VSKDSDLEDMDMEAADENKEEADAEKDEPMQDEDPLEENNTLD--EDIQQDDFSDLAEDDEKMNED--GFEENVQENEES 4077
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409128  107 VKDDeCESDAENEQNHDPNVEEF--LQQQDTAVIFPEApEEDQRQGTPEASGHDE----------NGTPD-AFSQL---L 170
Cdd:COG5271  4078 TEDG-VKSDEELEQGEVPEDQAIdnHPKMDAKSTFASA-EADEENTDKGIVGENEelgeedgvrgNGTADgEFEQVqedT 4155
                         170       180       190
                  ....*....|....*....|....*....|..
gi 189409128  171 TCPY-----CDRGYKrftSLKEHIKYRHEKNE 197
Cdd:COG5271  4156 STPKeamseADRQYQ---SLGDHLREWQQANR 4184
homeodomain super family cl00084
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
581-629 6.94e-04

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


The actual alignment was detected with superfamily member pfam00046:

Pssm-ID: 412151  Cd Length: 55  Bit Score: 38.63  E-value: 6.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 189409128   581 NLSPSQpplknlLSLLKAYYALNAQPSAEELSKIADSVNLPLDVVKKWF 629
Cdd:pfam00046    4 TFTPEQ------LEELEKEFQKNPYPSREEREELAAQLGLTERQVKVWF 46
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
200-222 4.52e-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: 4.52e-03
                           10        20
                   ....*....|....*....|...
gi 189409128   200 FSCSLCSYTFAYRTQLERHMTSH 222
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
946-971 4.59e-07

Zinc-finger double domain;


Pssm-ID: 404364 [Multi-domain]  Cd Length: 26  Bit Score: 46.96  E-value: 4.59e-07
                           10        20
                   ....*....|....*....|....*.
gi 189409128   946 HLIEHMRLHSGEKPYQCDKCGKRFSH 971
Cdd:pfam13465    1 NLKRHMRKHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
254-277 8.68e-07

Zinc-finger double domain;


Pssm-ID: 404364 [Multi-domain]  Cd Length: 26  Bit Score: 46.19  E-value: 8.68e-07
                           10        20
                   ....*....|....*....|....
gi 189409128   254 HLKEHLRIHSGEKPYECPNCKKRF 277
Cdd:pfam13465    1 NLKRHMRKHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
240-262 3.86e-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: 44.21  E-value: 3.86e-06
                           10        20
                   ....*....|....*....|...
gi 189409128   240 FKCTECGKAFKYKHHLKEHLRIH 262
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
932-954 3.26e-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: 41.52  E-value: 3.26e-05
                           10        20
                   ....*....|....*....|...
gi 189409128   932 HECGICKKAFKHKHHLIEHMRLH 954
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
918-943 6.92e-05

Zinc-finger double domain;


Pssm-ID: 404364 [Multi-domain]  Cd Length: 26  Bit Score: 40.80  E-value: 6.92e-05
                           10        20
                   ....*....|....*....|....*.
gi 189409128   918 SLLRHKYEHTGKRPHECGICKKAFKH 943
Cdd:pfam13465    1 NLKRHMRKHTGEKPYKCPECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
240-262 4.18e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 38.60  E-value: 4.18e-04
                            10        20
                    ....*....|....*....|...
gi 189409128    240 FKCTECGKAFKYKHHLKEHLRIH 262
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
27-197 5.64e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227596 [Multi-domain]  Cd Length: 4600  Bit Score: 44.22  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409128   27 VETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPgrSSEREGNAKNCWEDDRKEGQEilGPEAQADEAGCT 106
Cdd:COG5271  4002 VSKDSDLEDMDMEAADENKEEADAEKDEPMQDEDPLEENNTLD--EDIQQDDFSDLAEDDEKMNED--GFEENVQENEES 4077
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409128  107 VKDDeCESDAENEQNHDPNVEEF--LQQQDTAVIFPEApEEDQRQGTPEASGHDE----------NGTPD-AFSQL---L 170
Cdd:COG5271  4078 TEDG-VKSDEELEQGEVPEDQAIdnHPKMDAKSTFASA-EADEENTDKGIVGENEelgeedgvrgNGTADgEFEQVqedT 4155
                         170       180       190
                  ....*....|....*....|....*....|..
gi 189409128  171 TCPY-----CDRGYKrftSLKEHIKYRHEKNE 197
Cdd:COG5271  4156 STPKeamseADRQYQ---SLGDHLREWQQANR 4184
Homeobox pfam00046
Homeobox domain;
581-629 6.94e-04

Homeobox domain;


Pssm-ID: 395001  Cd Length: 55  Bit Score: 38.63  E-value: 6.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 189409128   581 NLSPSQpplknlLSLLKAYYALNAQPSAEELSKIADSVNLPLDVVKKWF 629
Cdd:pfam00046    4 TFTPEQ------LEELEKEFQKNPYPSREEREELAAQLGLTERQVKVWF 46
GET2 pfam08690
GET complex subunit GET2; This family corresponds to the GET complex subunit GET2. The GET ...
60-170 2.28e-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.


Pssm-ID: 400847  Cd Length: 308  Bit Score: 41.23  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409128    60 DLPTDQTVLPgrSSEREGNAKNCWEDDRKEGQEILGPEAQADEAGCTVKDDECESDAENEqnhDPNVEEFLQQQDTAvif 139
Cdd:pfam08690   45 DEPAAPSTTP--ASTTASSSPSADEHDDPEIVDISEIASQPKKTASVPKKPPSSEESDPE---NPQLDQMFKQLLGQ--- 116
                           90       100       110
                   ....*....|....*....|....*....|.
gi 189409128   140 peapeedQRQGTPEASGHDENGTPDAFSQLL 170
Cdd:pfam08690  117 -------QQQGGGENGQPAGSSTPDLFSQMM 140
ZnF_C2H2 smart00355
zinc finger;
932-954 2.54e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 2.54e-03
                            10        20
                    ....*....|....*....|...
gi 189409128    932 HECGICKKAFKHKHHLIEHMRLH 954
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
200-222 4.52e-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: 4.52e-03
                           10        20
                   ....*....|....*....|...
gi 189409128   200 FSCSLCSYTFAYRTQLERHMTSH 222
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
200-222 5.58e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 5.58e-03
                            10        20
                    ....*....|....*....|...
gi 189409128    200 FSCSLCSYTFAYRTQLERHMTSH 222
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
946-971 4.59e-07

Zinc-finger double domain;


Pssm-ID: 404364 [Multi-domain]  Cd Length: 26  Bit Score: 46.96  E-value: 4.59e-07
                           10        20
                   ....*....|....*....|....*.
gi 189409128   946 HLIEHMRLHSGEKPYQCDKCGKRFSH 971
Cdd:pfam13465    1 NLKRHMRKHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
254-277 8.68e-07

Zinc-finger double domain;


Pssm-ID: 404364 [Multi-domain]  Cd Length: 26  Bit Score: 46.19  E-value: 8.68e-07
                           10        20
                   ....*....|....*....|....
gi 189409128   254 HLKEHLRIHSGEKPYECPNCKKRF 277
Cdd:pfam13465    1 NLKRHMRKHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
240-262 3.86e-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: 44.21  E-value: 3.86e-06
                           10        20
                   ....*....|....*....|...
gi 189409128   240 FKCTECGKAFKYKHHLKEHLRIH 262
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
932-954 3.26e-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: 41.52  E-value: 3.26e-05
                           10        20
                   ....*....|....*....|...
gi 189409128   932 HECGICKKAFKHKHHLIEHMRLH 954
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
918-943 6.92e-05

Zinc-finger double domain;


Pssm-ID: 404364 [Multi-domain]  Cd Length: 26  Bit Score: 40.80  E-value: 6.92e-05
                           10        20
                   ....*....|....*....|....*.
gi 189409128   918 SLLRHKYEHTGKRPHECGICKKAFKH 943
Cdd:pfam13465    1 NLKRHMRKHTGEKPYKCPECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
240-262 4.18e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 38.60  E-value: 4.18e-04
                            10        20
                    ....*....|....*....|...
gi 189409128    240 FKCTECGKAFKYKHHLKEHLRIH 262
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
27-197 5.64e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227596 [Multi-domain]  Cd Length: 4600  Bit Score: 44.22  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409128   27 VETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPgrSSEREGNAKNCWEDDRKEGQEilGPEAQADEAGCT 106
Cdd:COG5271  4002 VSKDSDLEDMDMEAADENKEEADAEKDEPMQDEDPLEENNTLD--EDIQQDDFSDLAEDDEKMNED--GFEENVQENEES 4077
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409128  107 VKDDeCESDAENEQNHDPNVEEF--LQQQDTAVIFPEApEEDQRQGTPEASGHDE----------NGTPD-AFSQL---L 170
Cdd:COG5271  4078 TEDG-VKSDEELEQGEVPEDQAIdnHPKMDAKSTFASA-EADEENTDKGIVGENEelgeedgvrgNGTADgEFEQVqedT 4155
                         170       180       190
                  ....*....|....*....|....*....|..
gi 189409128  171 TCPY-----CDRGYKrftSLKEHIKYRHEKNE 197
Cdd:COG5271  4156 STPKeamseADRQYQ---SLGDHLREWQQANR 4184
Homeobox pfam00046
Homeobox domain;
581-629 6.94e-04

Homeobox domain;


Pssm-ID: 395001  Cd Length: 55  Bit Score: 38.63  E-value: 6.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 189409128   581 NLSPSQpplknlLSLLKAYYALNAQPSAEELSKIADSVNLPLDVVKKWF 629
Cdd:pfam00046    4 TFTPEQ------LEELEKEFQKNPYPSREEREELAAQLGLTERQVKVWF 46
GET2 pfam08690
GET complex subunit GET2; This family corresponds to the GET complex subunit GET2. The GET ...
60-170 2.28e-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.


Pssm-ID: 400847  Cd Length: 308  Bit Score: 41.23  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409128    60 DLPTDQTVLPgrSSEREGNAKNCWEDDRKEGQEILGPEAQADEAGCTVKDDECESDAENEqnhDPNVEEFLQQQDTAvif 139
Cdd:pfam08690   45 DEPAAPSTTP--ASTTASSSPSADEHDDPEIVDISEIASQPKKTASVPKKPPSSEESDPE---NPQLDQMFKQLLGQ--- 116
                           90       100       110
                   ....*....|....*....|....*....|.
gi 189409128   140 peapeedQRQGTPEASGHDENGTPDAFSQLL 170
Cdd:pfam08690  117 -------QQQGGGENGQPAGSSTPDLFSQMM 140
ZnF_C2H2 smart00355
zinc finger;
932-954 2.54e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 2.54e-03
                            10        20
                    ....*....|....*....|...
gi 189409128    932 HECGICKKAFKHKHHLIEHMRLH 954
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
240-262 4.30e-03

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


Pssm-ID: 404733  Cd Length: 24  Bit Score: 35.70  E-value: 4.30e-03
                           10        20
                   ....*....|....*....|...
gi 189409128   240 FKCTECGKAFKYKHHLKEHLRIH 262
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
960-980 4.35e-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: 4.35e-03
                           10        20
                   ....*....|....*....|.
gi 189409128   960 YQCDKCGKRFSHSGSYSQHMN 980
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR 21
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
200-222 4.52e-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: 4.52e-03
                           10        20
                   ....*....|....*....|...
gi 189409128   200 FSCSLCSYTFAYRTQLERHMTSH 222
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
200-222 5.58e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 5.58e-03
                            10        20
                    ....*....|....*....|...
gi 189409128    200 FSCSLCSYTFAYRTQLERHMTSH 222
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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