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Conserved domains on  [gi|2217313591|ref|XP_047292620|]
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vascular endothelial zinc finger 1 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 189-246 1.16e-05

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 47.79  E-value: 1.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217313591 189 DEKPFECPI--CNQRFKRKDRMTYH-VRSHEGGIT----------------KPYTCSVCGKGFSRPDHLSCHVKHVH 246
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYHmLHGHQNQKLhenpspekmnifsakdKPYRCEVCDKRYKNLNGLKYHRKHSH 422
motB super family cl32828
flagellar motor protein MotB; Reviewed
 377-494 3.22e-03

flagellar motor protein MotB; Reviewed


The actual alignment was detected with superfamily member PRK12799:

Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 40.08  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217313591 377 EAANLCQTSTAATTPVTLTTPFSITSSVSSGTMSNPVTVAAAmSMRSPVNVSSAVNITSPmnighpvTITSPLSMTSPLT 456
Cdd:PRK12799  286 KATGLKQIDTHGTVPVAAVTPSSAVTQSSAITPSSAAIPSPA-VIPSSVTTQSATTTQAS-------AVALSSAGVLPSD 357

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217313591 457 LTTPVNLPTPVTAPVNIAHPV------------TITSPMNLPTPMTLAAP 494
Cdd:PRK12799  358 VTLPGTVALPAAEPVNMQPQPmsttetqqsstgNITSTANGPTTSLPAAP 407
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 165-187 8.40e-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: 33.81  E-value: 8.40e-03
                          10        20
                  ....*....|....*....|...
gi 2217313591 165 HACEMCGKAFRDVYHLNRHKLSH 187
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 189-246 1.16e-05

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 47.79  E-value: 1.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217313591 189 DEKPFECPI--CNQRFKRKDRMTYH-VRSHEGGIT----------------KPYTCSVCGKGFSRPDHLSCHVKHVH 246
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYHmLHGHQNQKLhenpspekmnifsakdKPYRCEVCDKRYKNLNGLKYHRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
179-204 3.09e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.09e-04
                          10        20
                  ....*....|....*....|....*.
gi 2217313591 179 HLNRHKLSHSDEKPFECPICNQRFKR 204
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
motB PRK12799
flagellar motor protein MotB; Reviewed
 377-494 3.22e-03

flagellar motor protein MotB; Reviewed


Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 40.08  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217313591 377 EAANLCQTSTAATTPVTLTTPFSITSSVSSGTMSNPVTVAAAmSMRSPVNVSSAVNITSPmnighpvTITSPLSMTSPLT 456
Cdd:PRK12799  286 KATGLKQIDTHGTVPVAAVTPSSAVTQSSAITPSSAAIPSPA-VIPSSVTTQSATTTQAS-------AVALSSAGVLPSD 357

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217313591 457 LTTPVNLPTPVTAPVNIAHPV------------TITSPMNLPTPMTLAAP 494
Cdd:PRK12799  358 VTLPGTVALPAAEPVNMQPQPmsttetqqsstgNITSTANGPTTSLPAAP 407
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 165-187 8.40e-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: 33.81  E-value: 8.40e-03
                          10        20
                  ....*....|....*....|...
gi 2217313591 165 HACEMCGKAFRDVYHLNRHKLSH 187
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 189-246 1.16e-05

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 47.79  E-value: 1.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217313591 189 DEKPFECPI--CNQRFKRKDRMTYH-VRSHEGGIT----------------KPYTCSVCGKGFSRPDHLSCHVKHVH 246
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYHmLHGHQNQKLhenpspekmnifsakdKPYRCEVCDKRYKNLNGLKYHRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
179-204 3.09e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.09e-04
                          10        20
                  ....*....|....*....|....*.
gi 2217313591 179 HLNRHKLSHSDEKPFECPICNQRFKR 204
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
motB PRK12799
flagellar motor protein MotB; Reviewed
 377-494 3.22e-03

flagellar motor protein MotB; Reviewed


Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 40.08  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217313591 377 EAANLCQTSTAATTPVTLTTPFSITSSVSSGTMSNPVTVAAAmSMRSPVNVSSAVNITSPmnighpvTITSPLSMTSPLT 456
Cdd:PRK12799  286 KATGLKQIDTHGTVPVAAVTPSSAVTQSSAITPSSAAIPSPA-VIPSSVTTQSATTTQAS-------AVALSSAGVLPSD 357

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217313591 457 LTTPVNLPTPVTAPVNIAHPV------------TITSPMNLPTPMTLAAP 494
Cdd:PRK12799  358 VTLPGTVALPAAEPVNMQPQPmsttetqqsstgNITSTANGPTTSLPAAP 407
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 165-187 8.40e-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: 33.81  E-value: 8.40e-03
                          10        20
                  ....*....|....*....|...
gi 2217313591 165 HACEMCGKAFRDVYHLNRHKLSH 187
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 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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