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Conserved domains on  [gi|83759158|gb|AAI10349|]
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Zinc finger protein 276 [Homo sapiens]

Protein Classification

zinc-finger associated domain-containing protein( domain architecture ID 10544311)

zinc-finger associated domain (ZAD)-containing protein similar to Drosophila melanogaster zinc finger protein hangover, zinc finger protein kipf and protein phyllopod

CATH:  3.40.1800.20
Gene Ontology:  GO:0008270
SCOP:  4001830

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 3-80 7.64e-07

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


:

Pssm-ID: 462262  Cd Length: 75  Bit Score: 46.68  E-value: 7.64e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83759158     3 HCRLCHgkFSSRSLRSISErapgasmerPSAEERVLVRDFQRLLGVAVRQDPTLSPFVCKSCHAQFYQCHSLLKSFLQ 80
Cdd:pfam07776   1 VCRLCL--DESDELIPIFD---------PSDSEKTLAEILEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLE 67
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 359-444 5.40e-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: 45.86  E-value: 5.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83759158 359 YKCPYQGCTAVYRGADGMKKHIKEHHEEVRERPCPHPGCNKVFMIdrylqrhvklihtEVRNYICDECGQTFKQRKHLLV 438
Cdd:COG5189 350 YKCPVEGCNKKYKNQNGLKYHMLHGHQNQKLHENPSPEKMNIFSA-------------KDKPYRCEVCDKRYKNLNGLKY 416


                ....*.
gi 83759158 439 HQmRHS 444
Cdd:COG5189 417 HR-KHS 421
 
Name Accession Description Interval E-value
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 3-80 7.64e-07

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 462262  Cd Length: 75  Bit Score: 46.68  E-value: 7.64e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83759158     3 HCRLCHgkFSSRSLRSISErapgasmerPSAEERVLVRDFQRLLGVAVRQDPTLSPFVCKSCHAQFYQCHSLLKSFLQ 80
Cdd:pfam07776   1 VCRLCL--DESDELIPIFD---------PSDSEKTLAEILEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLE 67
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 359-444 5.40e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.86  E-value: 5.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83759158 359 YKCPYQGCTAVYRGADGMKKHIKEHHEEVRERPCPHPGCNKVFMIdrylqrhvklihtEVRNYICDECGQTFKQRKHLLV 438
Cdd:COG5189 350 YKCPVEGCNKKYKNQNGLKYHMLHGHQNQKLHENPSPEKMNIFSA-------------KDKPYRCEVCDKRYKNLNGLKY 416


                ....*.
gi 83759158 439 HQmRHS 444
Cdd:COG5189 417 HR-KHS 421
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 4-80 2.36e-04

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 214871  Cd Length: 73  Bit Score: 39.81  E-value: 2.36e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83759158      4 CRLCHGkfSSRSLRSISERAPGASmerpsaeervLVRDFQRLLGVAVRQDPTLSPFVCKSCHAQFYQCHSLLKSFLQ 80
Cdd:smart00868   2 CRLCLS--ESENLVSIFDESSEAS----------LAEKIEECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRE 66
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 421-443 1.93e-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: 1.93e-03
                          10        20
                  ....*....|....*....|...
gi 83759158   421 YICDECGQTFKQRKHLLVHQMRH 443
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 392-475 2.48e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 40.63  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83759158  392 CPHPGCNKVFMIDrylqrhvklihtEVRNYI-CDECGQTFKQR---KHLLVHQmrhsgaKPLQCEvCGFQCRqraslKYH 467
Cdd:PLN03086 436 CPHDGCGIVLRVE------------EAKNHVhCEKCGQAFQQGemeKHMKVFH------EPLQCP-CGVVLE-----KEQ 491


                 ....*...
gi 83759158  468 MTKHKAET 475
Cdd:PLN03086 492 MVQHQAST 499
 
Name Accession Description Interval E-value
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 3-80 7.64e-07

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 462262  Cd Length: 75  Bit Score: 46.68  E-value: 7.64e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83759158     3 HCRLCHgkFSSRSLRSISErapgasmerPSAEERVLVRDFQRLLGVAVRQDPTLSPFVCKSCHAQFYQCHSLLKSFLQ 80
Cdd:pfam07776   1 VCRLCL--DESDELIPIFD---------PSDSEKTLAEILEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLE 67
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 359-444 5.40e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.86  E-value: 5.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83759158 359 YKCPYQGCTAVYRGADGMKKHIKEHHEEVRERPCPHPGCNKVFMIdrylqrhvklihtEVRNYICDECGQTFKQRKHLLV 438
Cdd:COG5189 350 YKCPVEGCNKKYKNQNGLKYHMLHGHQNQKLHENPSPEKMNIFSA-------------KDKPYRCEVCDKRYKNLNGLKY 416


                ....*.
gi 83759158 439 HQmRHS 444
Cdd:COG5189 417 HR-KHS 421
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 4-80 2.36e-04

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 214871  Cd Length: 73  Bit Score: 39.81  E-value: 2.36e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83759158      4 CRLCHGkfSSRSLRSISERAPGASmerpsaeervLVRDFQRLLGVAVRQDPTLSPFVCKSCHAQFYQCHSLLKSFLQ 80
Cdd:smart00868   2 CRLCLS--ESENLVSIFDESSEAS----------LAEKIEECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRE 66
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 421-443 1.93e-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: 1.93e-03
                          10        20
                  ....*....|....*....|...
gi 83759158   421 YICDECGQTFKQRKHLLVHQMRH 443
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 392-475 2.48e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 40.63  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83759158  392 CPHPGCNKVFMIDrylqrhvklihtEVRNYI-CDECGQTFKQR---KHLLVHQmrhsgaKPLQCEvCGFQCRqraslKYH 467
Cdd:PLN03086 436 CPHDGCGIVLRVE------------EAKNHVhCEKCGQAFQQGemeKHMKVFH------EPLQCP-CGVVLE-----KEQ 491


                 ....*...
gi 83759158  468 MTKHKAET 475
Cdd:PLN03086 492 MVQHQAST 499
 
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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