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Conserved domains on  [gi|21105468|gb|AAM34677|]
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KIAA1323-like protein [Danio rerio]

Protein Classification

ZZ-type zinc finger protein( domain architecture ID 10535423)

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
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 154-218 4.69e-29

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


:

Pssm-ID: 461991  Cd Length: 66  Bit Score: 103.83  E-value: 4.69e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21105468   154 GGRVVRGVDWQWEDQDGGNGRRGKVTEIQDWSAASPHSAAYVLWDNGAKNLYRVGFEGMSDLKCV 218
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 83-127 4.21e-27

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: 98.30  E-value: 4.21e-27
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 21105468  83 TMCDTCRQQPIIGIRWKCAECTNYDLCTTCYHGDKHHLRHRFYRI 127
Cdd:cd02339   1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 15-72 6.51e-19

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


:

Pssm-ID: 461991  Cd Length: 66  Bit Score: 77.64  E-value: 6.51e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21105468    15 GARVIRGPDWKWGKQDGGEGHVGTVR-----SFESPEEVVVV-WDNGTAANYR--CSGAYDVRILD 72
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVqWDNGSTNVYRvgYEGKYDLKVVD 66
 
Name Accession Description Interval E-value
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 154-218 4.69e-29

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 103.83  E-value: 4.69e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21105468   154 GGRVVRGVDWQWEDQDGGNGRRGKVTEIQDWSAASPHSAAYVLWDNGAKNLYRVGFEGMSDLKCV 218
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 83-127 4.21e-27

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: 98.30  E-value: 4.21e-27
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 21105468  83 TMCDTCRQQPIIGIRWKCAECTNYDLCTTCYHGDKHHLRHRFYRI 127
Cdd:cd02339   1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 15-72 6.51e-19

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 77.64  E-value: 6.51e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21105468    15 GARVIRGPDWKWGKQDGGEGHVGTVR-----SFESPEEVVVV-WDNGTAANYR--CSGAYDVRILD 72
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVqWDNGSTNVYRvgYEGKYDLKVVD 66
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 85-123 1.12e-10

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: 55.14  E-value: 1.12e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 21105468     85 CDTCrQQPIIGIRWKCAECTNYDLCTTCYHGDKHHLRHR 123
Cdd:smart00291   7 CDTC-GKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 79-119 1.08e-09

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: 52.49  E-value: 1.08e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 21105468    79 KHDGTMCDTCRQQPIIGIRWKCAECTNYDLCTTCYHGDKHH 119
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGG 41
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
85-138 1.77e-04

Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 41.98  E-value: 1.77e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21105468  85 CDTCRQQPIIGIRWKCAECTNYDLCTTCY----HGDKHHLRHRfYRITTPGSERVLLE 138
Cdd:COG5114   8 CDVCFLDMTDLTFIKCNECPAVDLCLPCFvngiETGVHSPYHG-YRIIETNSYPIGEE 64
 
Name Accession Description Interval E-value
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 154-218 4.69e-29

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 103.83  E-value: 4.69e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21105468   154 GGRVVRGVDWQWEDQDGGNGRRGKVTEIQDWSAASPHSAAYVLWDNGAKNLYRVGFEGMSDLKCV 218
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 83-127 4.21e-27

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: 98.30  E-value: 4.21e-27
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 21105468  83 TMCDTCRQQPIIGIRWKCAECTNYDLCTTCYHGDKHHLRHRFYRI 127
Cdd:cd02339   1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
 15-72 6.51e-19

Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain (either Ring or Hect).


Pssm-ID: 461991  Cd Length: 66  Bit Score: 77.64  E-value: 6.51e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21105468    15 GARVIRGPDWKWGKQDGGEGHVGTVR-----SFESPEEVVVV-WDNGTAANYR--CSGAYDVRILD 72
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVeirdwDSESPRSTVRVqWDNGSTNVYRvgYEGKYDLKVVD 66
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 85-127 1.22e-12

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: 60.53  E-value: 1.22e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 21105468  85 CDTCrQQPIIGIRWKCAECTNYDLCTTCYHG--DKHHLRHRFYRI 127
Cdd:cd02249   3 CDGC-LKPIVGVRYHCLVCEDFDLCSSCYAKgkKGHPPDHSFTEI 46
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 85-127 9.30e-11

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: 55.34  E-value: 9.30e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 21105468  85 CDTCrQQPIIGIRWKCAECTNYDLCTTCyHGDKHHLRHRFYRI 127
Cdd:cd02340   3 CDGC-QGPIVGVRYKCLVCPDYDLCESC-EAKGVHPEHAMLKI 43
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 85-123 1.12e-10

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: 55.14  E-value: 1.12e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 21105468     85 CDTCrQQPIIGIRWKCAECTNYDLCTTCYHGDKHHLRHR 123
Cdd:smart00291   7 CDTC-GKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 85-127 1.65e-10

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: 54.90  E-value: 1.65e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 21105468  85 CDTCRQQPIIGIRWKCAECTNYDLCTTCYHGDKHHLRHRFYRI 127
Cdd:cd02344   3 CDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGRI 45
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 79-119 1.08e-09

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: 52.49  E-value: 1.08e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 21105468    79 KHDGTMCDTCRQQPIIGIRWKCAECTNYDLCTTCYHGDKHH 119
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGG 41
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 83-122 8.01e-09

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: 50.43  E-value: 8.01e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 21105468  83 TMCDTCRQQPIIGIRWKCAECTNYDLCTTCY----HGDKHHLRH 122
Cdd:cd02334   1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFfsgrTSKSHKNSH 44
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 85-125 2.79e-07

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: 46.19  E-value: 2.79e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 21105468  85 CDTCRQQPIIGIRWKCAECTNYDLCTTCYHGDKHHLRHRFY 125
Cdd:cd02338   3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFD 43
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 85-127 1.58e-06

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 43.96  E-value: 1.58e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 21105468  85 CDTCRQQPIIGIRWKCAECTN--YDLCTTCYH-GDKHHLRHRFYRI 127
Cdd:cd02341   3 CDSCGIEPIPGTRYHCSECDDgdFDLCQDCVVkGESHQEDHWLVKI 48
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 85-127 4.47e-06

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 42.58  E-value: 4.47e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 21105468  85 CDTCRQQPIIGIRWKCAECTNYDLCTTCY----HGDKHHLRHRFYRI 127
Cdd:cd02345   3 CSACRKQDISGIRFPCQVCRDYSLCLGCYtkgrETKRHNSLHIMYEL 49
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 85-123 5.71e-06

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 42.28  E-value: 5.71e-06
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 21105468  85 CDTCRQQPIIGIRWKCAECTNYDLCTTCYHGDKHHLRHR 123
Cdd:cd02335   3 CDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHR 41
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
 85-114 7.81e-05

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: 39.10  E-value: 7.81e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 21105468  85 CDTCRQQPIIGIRWKCAECTNYDLCTTCYH 114
Cdd:cd02342   3 CDGCGVLPITGPRYKSKVKEDYDLCTICFS 32
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
85-138 1.77e-04

Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 41.98  E-value: 1.77e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21105468  85 CDTCRQQPIIGIRWKCAECTNYDLCTTCY----HGDKHHLRHRfYRITTPGSERVLLE 138
Cdd:COG5114   8 CDVCFLDMTDLTFIKCNECPAVDLCLPCFvngiETGVHSPYHG-YRIIETNSYPIGEE 64
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 83-119 1.18e-03

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 35.62  E-value: 1.18e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 21105468  83 TMCDTCRQqpIIGIRWKCAECTNYDLCTTCYHGDKHH 119
Cdd:cd02337   1 YTCNECKH--HVETRWHCTVCEDYDLCITCYNTKNHP 35
 
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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