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Conserved domains on  [gi|578813965|ref|XP_006715932|]
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zinc finger protein 800 isoform X2 [Homo sapiens]

Protein Classification

zf-C2H2_11 and zf-C2H2_assoc2 domain-containing protein( domain architecture ID 11244373)

protein containing domains zf-C2H2_11, zf-C2H2_assoc2, and zf-C2H2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
zf-C2H2_assoc2 pfam16624
Unstructured region upstream of a zinc-finger; zf-C2H2_assoc2 is a short region of natively ...
359-453 1.06e-47

Unstructured region upstream of a zinc-finger; zf-C2H2_assoc2 is a short region of natively unstructured sequence immediately upstream of a C2H2-type zinc-finger on eukaryotic Zinc-finger proteins 592 and 800. The function is not known.


:

Pssm-ID: 465207 [Multi-domain]  Cd Length: 95  Bit Score: 163.23  E-value: 1.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813965  359 SKREKGPNNTANSSEIKVKVEPADSVESSPPSITHSPQNELKGTNHSNEKKNTPAAQKNKVKQDSESPKSTSPSAAGGQQ 438
Cdd:pfam16624   1 SKSENGPANEASGTEIKVKEEPSDEVESSSPPISHSPQNELKGTNQGPEKKSTPTAQKNKVKQESESPKSSSPLATAGQQ 80
                          90
                  ....*....|....*
gi 578813965  439 KTRKPKLSAGFDFKQ 453
Cdd:pfam16624  81 KPRKPKLSVGFDFKQ 95
zf-C2H2_11 pfam16622
zinc-finger C2H2-type; Zinc-finger of C2H2 type found in higher eukaryotes.
325-351 8.30e-09

zinc-finger C2H2-type; Zinc-finger of C2H2 type found in higher eukaryotes.


:

Pssm-ID: 465205  Cd Length: 27  Bit Score: 51.28  E-value: 8.30e-09
                          10        20
                  ....*....|....*....|....*..
gi 578813965  325 TACKCLLCKRKYSSQIMLKRHMQIVHK 351
Cdd:pfam16622   1 STCQCLLCGLCFTSQGSLSRHLFIVHK 27
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
586-608 2.59e-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: 2.59e-03
                          10        20
                  ....*....|....*....|...
gi 578813965  586 HRCNKCGKAFAKKTYLEHHKKTH 608
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-C2H2_assoc2 pfam16624
Unstructured region upstream of a zinc-finger; zf-C2H2_assoc2 is a short region of natively ...
359-453 1.06e-47

Unstructured region upstream of a zinc-finger; zf-C2H2_assoc2 is a short region of natively unstructured sequence immediately upstream of a C2H2-type zinc-finger on eukaryotic Zinc-finger proteins 592 and 800. The function is not known.


Pssm-ID: 465207 [Multi-domain]  Cd Length: 95  Bit Score: 163.23  E-value: 1.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813965  359 SKREKGPNNTANSSEIKVKVEPADSVESSPPSITHSPQNELKGTNHSNEKKNTPAAQKNKVKQDSESPKSTSPSAAGGQQ 438
Cdd:pfam16624   1 SKSENGPANEASGTEIKVKEEPSDEVESSSPPISHSPQNELKGTNQGPEKKSTPTAQKNKVKQESESPKSSSPLATAGQQ 80
                          90
                  ....*....|....*
gi 578813965  439 KTRKPKLSAGFDFKQ 453
Cdd:pfam16624  81 KPRKPKLSVGFDFKQ 95
zf-C2H2_11 pfam16622
zinc-finger C2H2-type; Zinc-finger of C2H2 type found in higher eukaryotes.
325-351 8.30e-09

zinc-finger C2H2-type; Zinc-finger of C2H2 type found in higher eukaryotes.


Pssm-ID: 465205  Cd Length: 27  Bit Score: 51.28  E-value: 8.30e-09
                          10        20
                  ....*....|....*....|....*..
gi 578813965  325 TACKCLLCKRKYSSQIMLKRHMQIVHK 351
Cdd:pfam16622   1 STCQCLLCGLCFTSQGSLSRHLFIVHK 27
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
586-608 2.59e-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: 2.59e-03
                          10        20
                  ....*....|....*....|...
gi 578813965  586 HRCNKCGKAFAKKTYLEHHKKTH 608
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-C2H2_assoc2 pfam16624
Unstructured region upstream of a zinc-finger; zf-C2H2_assoc2 is a short region of natively ...
359-453 1.06e-47

Unstructured region upstream of a zinc-finger; zf-C2H2_assoc2 is a short region of natively unstructured sequence immediately upstream of a C2H2-type zinc-finger on eukaryotic Zinc-finger proteins 592 and 800. The function is not known.


Pssm-ID: 465207 [Multi-domain]  Cd Length: 95  Bit Score: 163.23  E-value: 1.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813965  359 SKREKGPNNTANSSEIKVKVEPADSVESSPPSITHSPQNELKGTNHSNEKKNTPAAQKNKVKQDSESPKSTSPSAAGGQQ 438
Cdd:pfam16624   1 SKSENGPANEASGTEIKVKEEPSDEVESSSPPISHSPQNELKGTNQGPEKKSTPTAQKNKVKQESESPKSSSPLATAGQQ 80
                          90
                  ....*....|....*
gi 578813965  439 KTRKPKLSAGFDFKQ 453
Cdd:pfam16624  81 KPRKPKLSVGFDFKQ 95
zf-C2H2_11 pfam16622
zinc-finger C2H2-type; Zinc-finger of C2H2 type found in higher eukaryotes.
325-351 8.30e-09

zinc-finger C2H2-type; Zinc-finger of C2H2 type found in higher eukaryotes.


Pssm-ID: 465205  Cd Length: 27  Bit Score: 51.28  E-value: 8.30e-09
                          10        20
                  ....*....|....*....|....*..
gi 578813965  325 TACKCLLCKRKYSSQIMLKRHMQIVHK 351
Cdd:pfam16622   1 STCQCLLCGLCFTSQGSLSRHLFIVHK 27
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
586-608 2.59e-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: 2.59e-03
                          10        20
                  ....*....|....*....|...
gi 578813965  586 HRCNKCGKAFAKKTYLEHHKKTH 608
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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