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Conserved domains on  [gi|24582151|ref|NP_723159|]
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uncharacterized protein Dmel_CG31642 [Drosophila melanogaster]

Protein Classification

ZZ-type zinc finger protein( domain architecture ID 10115782)

ZZ-type zinc finger protein may function as a molecular serve as scaffold in various cell signaling pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 15-65 2.20e-19

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


:

Pssm-ID: 239078  Cd Length: 49  Bit Score: 81.62  E-value: 2.20e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 24582151  15 HRCENCKISDFQGRRYTCRFCAEYTLCGKCFDANHlpASPQHRYYHPMSVY 65
Cdd:cd02338   1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGV--TTERHLFDHPMQCI 49
 
Name Accession Description Interval E-value
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 15-65 2.20e-19

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 81.62  E-value: 2.20e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 24582151  15 HRCENCKISDFQGRRYTCRFCAEYTLCGKCFDANHlpASPQHRYYHPMSVY 65
Cdd:cd02338   1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGV--TTERHLFDHPMQCI 49
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 12-45 5.24e-04

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 37.85  E-value: 5.24e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 24582151    12 HFGHRCENCKISDFQGRRYTCRFCAEYTLCGKCF 45
Cdd:pfam00569   2 HKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF 35
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 11-57 2.18e-03

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 36.26  E-value: 2.18e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 24582151     11 RHFGHRCENCKiSDFQGRRYTCRFCAEYTLCGKCFDANHlpASPQHR 57
Cdd:smart00291   1 VHHSYSCDTCG-KPIVGVRYHCLVCPDYDLCQSCFAKGS--AGGEHS 44
 
Name Accession Description Interval E-value
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 15-65 2.20e-19

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 81.62  E-value: 2.20e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 24582151  15 HRCENCKISDFQGRRYTCRFCAEYTLCGKCFDANHlpASPQHRYYHPMSVY 65
Cdd:cd02338   1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGV--TTERHLFDHPMQCI 49
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 16-58 2.51e-06

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 44.35  E-value: 2.51e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24582151  16 RCENCKiSDFQGRRYTCRFCAEYTLCGKCFDANHLPASPQHRY 58
Cdd:cd02249   2 SCDGCL-KPIVGVRYHCLVCEDFDLCSSCYAKGKKGHPPDHSF 43
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 16-65 1.03e-05

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 42.73  E-value: 1.03e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24582151  16 RCENCKISDFQGRRYTCRFCAEYTLCGKCFDANHlpASPQHRYYHPMSVY 65
Cdd:cd02334   2 KCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGR--TSKSHKNSHPMKEY 49
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 17-58 7.37e-05

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 40.13  E-value: 7.37e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24582151  17 CENCKISDFQGRRYTCRFCAEYTLCGKCFDAN-HLPASPQHRY 58
Cdd:cd02339   3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDkHDLEHRFYRY 45
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 16-62 3.20e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 38.39  E-value: 3.20e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 24582151  16 RCENCKiSDFQGRRYTCRFCAEYTLCGKCfdanhlPASPQHrYYHPM 62
Cdd:cd02340   2 ICDGCQ-GPIVGVRYKCLVCPDYDLCESC------EAKGVH-PEHAM 40
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 12-45 5.24e-04

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 37.85  E-value: 5.24e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 24582151    12 HFGHRCENCKISDFQGRRYTCRFCAEYTLCGKCF 45
Cdd:pfam00569   2 HKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCF 35
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 16-45 6.62e-04

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 37.56  E-value: 6.62e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 24582151  16 RCENCKISDFQGRRYTCRFCAEYTLCGKCF 45
Cdd:cd02344   2 TCDGCQMFPINGPRFKCRNCDDFDFCENCF 31
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 11-57 2.18e-03

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 36.26  E-value: 2.18e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 24582151     11 RHFGHRCENCKiSDFQGRRYTCRFCAEYTLCGKCFDANHlpASPQHR 57
Cdd:smart00291   1 VHHSYSCDTCG-KPIVGVRYHCLVCPDYDLCQSCFAKGS--AGGEHS 44
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
 17-53 3.74e-03

Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of the RSC complex, which is closely related to the SWI/SNF complex and is involved in remodeling chromatin structure. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239076  Cd Length: 45  Bit Score: 35.37  E-value: 3.74e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 24582151  17 CENCKIsDFQGRRYTCRFCAEYTLCGKCFDANHLPAS 53
Cdd:cd02336   3 CFTCGN-DCTRVRYHNLKAKKYDLCPSCYQEGRFPSN 38
 
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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