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Conserved domains on  [gi|17565338|ref|NP_507173|]
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ZZ-type domain-containing protein [Caenorhabditis elegans]

Protein Classification

ZZ-type zinc finger protein( domain architecture ID 10115811)

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

Gene Ontology:  GO:0008270
PubMed:  30691308|8848831

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 133-175 1.49e-16

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: 69.21  E-value: 1.49e-16
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 17565338 133 VRCDSCYTTITGHRFKCTICTDYDICSSCEARNAHAQHTMLRI 175
Cdd:cd02340   1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGVHPEHAMLKI 43
 
Name Accession Description Interval E-value
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 133-175 1.49e-16

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: 69.21  E-value: 1.49e-16
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 17565338 133 VRCDSCYTTITGHRFKCTICTDYDICSSCEARNAHAQHTMLRI 175
Cdd:cd02340   1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGVHPEHAMLKI 43
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 130-168 6.72e-08

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: 46.66  E-value: 6.72e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 17565338    130 HPIVRCDSCYTTITGHRFKCTICTDYDICSSCEARNAHA 168
Cdd:smart00291   2 HHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAG 40
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 129-172 2.93e-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: 37.08  E-value: 2.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 17565338   129 THPIVRCDSC-YTTITGHRFKCTICTDYDICSSCEARNAHAQHTM 172
Cdd:pfam00569   1 IHKVYTCNGCsNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGNHQM 45
 
Name Accession Description Interval E-value
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 133-175 1.49e-16

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: 69.21  E-value: 1.49e-16
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 17565338 133 VRCDSCYTTITGHRFKCTICTDYDICSSCEARNAHAQHTMLRI 175
Cdd:cd02340   1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGVHPEHAMLKI 43
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 130-168 6.72e-08

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: 46.66  E-value: 6.72e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 17565338    130 HPIVRCDSCYTTITGHRFKCTICTDYDICSSCEARNAHA 168
Cdd:smart00291   2 HHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAG 40
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 133-175 2.40e-07

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: 45.50  E-value: 2.40e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 17565338 133 VRCDSCYTTITGHRFKCTICTDYDICSSCEARNAHA---QHTMLRI 175
Cdd:cd02249   1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGKKGhppDHSFTEI 46
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 133-172 2.16e-05

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: 40.02  E-value: 2.16e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 17565338 133 VRCDSC-YTTITGHRFKCTICTDYDICSSC-EARNAHAQHTM 172
Cdd:cd02338   1 VSCDGCgKSNFTGRRYKCLICYDYDLCADCyDSGVTTERHLF 42
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 133-175 3.78e-05

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: 39.49  E-value: 3.78e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 17565338 133 VRCDSCYT-TITGHRFKCTICTDYDICSSC-EARNAHAQHTMLRI 175
Cdd:cd02344   1 VTCDGCQMfPINGPRFKCRNCDDFDFCENCfKTRKHNTRHTFGRI 45
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 135-167 8.60e-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: 38.59  E-value: 8.60e-05
                        10        20        30
                ....*....|....*....|....*....|....
gi 17565338 135 CDSCYTT-ITGHRFKCTICTDYDICSSCEARNAH 167
Cdd:cd02339   3 CDTCRKQgIIGIRWKCAECPNYDLCTTCYHGDKH 36
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 129-172 2.93e-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: 37.08  E-value: 2.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 17565338   129 THPIVRCDSC-YTTITGHRFKCTICTDYDICSSCEARNAHAQHTM 172
Cdd:pfam00569   1 IHKVYTCNGCsNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGNHQM 45
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
 133-164 3.67e-04

Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239082  Cd Length: 43  Bit Score: 36.79  E-value: 3.67e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 17565338 133 VRCDSC-YTTITGHRFKCTICTDYDICSSCEAR 164
Cdd:cd02342   1 IQCDGCgVLPITGPRYKSKVKEDYDLCTICFSR 33
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 133-161 4.46e-03

Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239083  Cd Length: 48  Bit Score: 33.83  E-value: 4.46e-03
                        10        20
                ....*....|....*....|....*....
gi 17565338 133 VRCDSCYTTITGHRFKCTICTDYDICSSC 161
Cdd:cd02343   1 ISCDGCDEIAPWHRYRCLQCTDMDLCKTC 29
 
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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