NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|54261779|ref|NP_998204|]
View 

AN1-type zinc finger protein 5a [Danio rerio]

Protein Classification

zinc finger A20 and AN1 domain-containing stress-associated protein( domain architecture ID 10484704)

zinc finger A20 and AN1 domain-containing stress-associated protein similar to Homo sapiens AN1-type zinc finger protein that is involved in protein degradation via the ubiquitin-proteasome system

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ZnF_AN1 smart00154
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ...
 154-191 1.92e-14

AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis.


:

Pssm-ID: 197545  Cd Length: 39  Bit Score: 64.72  E-value: 1.92e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 54261779    154 CFTCRKRVGLTGFDCR-CGNLFCGIHRYSDKHNCTYDYK 191
Cdd:smart00154   1 CHFCRKKVGLTGFKCRhCGNLFCGEHRLPEDHDCPGDYK 39
zf-A20 pfam01754
A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding ...
 12-35 1.55e-09

A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding Domain. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappa B activation.


:

Pssm-ID: 460313  Cd Length: 24  Bit Score: 51.35  E-value: 1.55e-09
                          10        20
                  ....*....|....*....|....
gi 54261779    12 ILCTTGCGFYGNPRTNGMCSVCYK 35
Cdd:pfam01754   1 LLCRNGCGFYGSPATNGLCSKCYK 24
 
Name Accession Description Interval E-value
ZnF_AN1 smart00154
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ...
 154-191 1.92e-14

AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis.


Pssm-ID: 197545  Cd Length: 39  Bit Score: 64.72  E-value: 1.92e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 54261779    154 CFTCRKRVGLTGFDCR-CGNLFCGIHRYSDKHNCTYDYK 191
Cdd:smart00154   1 CHFCRKKVGLTGFKCRhCGNLFCGEHRLPEDHDCPGDYK 39
zf-A20 pfam01754
A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding ...
 12-35 1.55e-09

A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding Domain. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappa B activation.


Pssm-ID: 460313  Cd Length: 24  Bit Score: 51.35  E-value: 1.55e-09
                          10        20
                  ....*....|....*....|....
gi 54261779    12 ILCTTGCGFYGNPRTNGMCSVCYK 35
Cdd:pfam01754   1 LLCRNGCGFYGSPATNGLCSKCYK 24
zf-AN1 pfam01428
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ...
 156-188 1.97e-06

AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis. The following pattern describes the zinc finger. C-X2-C-X(9-12)-C-X(1-2)-C-X4-C-X2-H-X5-H-X-C Where X can be any amino acid, and numbers in brackets indicate the number of residues.


Pssm-ID: 460208  Cd Length: 37  Bit Score: 43.06  E-value: 1.97e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 54261779   156 TCRKRVGLTgFDCR-CGNLFCGIHRYSDKHNCTY 188
Cdd:pfam01428   5 GCKKKDFLP-FKCRfCGKNFCLKHRLPEDHDCSG 37
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 11-35 7.92e-06

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 41.42  E-value: 7.92e-06
                           10        20
                   ....*....|....*....|....*.
gi 54261779     11 PILC-TTGCGFYGNPRTNGMCSVCYK 35
Cdd:smart00259   1 PIKCrRPGCGFFGNPATEGLCSKCFK 26
FYVE1_Vac1p_like cd15761
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ...
 150-178 3.96e-03

FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277300  Cd Length: 76  Bit Score: 34.94  E-value: 3.96e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 54261779 150 KKNRCFTCRKRVG-LTGF-DCR-CGNLFCGIH 178
Cdd:cd15761   9 GKSRCSECGKTLNkKNGIvNCRkCGELFCNEH 40
 
Name Accession Description Interval E-value
ZnF_AN1 smart00154
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ...
 154-191 1.92e-14

AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis.


Pssm-ID: 197545  Cd Length: 39  Bit Score: 64.72  E-value: 1.92e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 54261779    154 CFTCRKRVGLTGFDCR-CGNLFCGIHRYSDKHNCTYDYK 191
Cdd:smart00154   1 CHFCRKKVGLTGFKCRhCGNLFCGEHRLPEDHDCPGDYK 39
zf-A20 pfam01754
A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding ...
 12-35 1.55e-09

A20-like zinc finger; The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding Domain. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappa B activation.


Pssm-ID: 460313  Cd Length: 24  Bit Score: 51.35  E-value: 1.55e-09
                          10        20
                  ....*....|....*....|....
gi 54261779    12 ILCTTGCGFYGNPRTNGMCSVCYK 35
Cdd:pfam01754   1 LLCRNGCGFYGSPATNGLCSKCYK 24
zf-AN1 pfam01428
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ...
 156-188 1.97e-06

AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis. The following pattern describes the zinc finger. C-X2-C-X(9-12)-C-X(1-2)-C-X4-C-X2-H-X5-H-X-C Where X can be any amino acid, and numbers in brackets indicate the number of residues.


Pssm-ID: 460208  Cd Length: 37  Bit Score: 43.06  E-value: 1.97e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 54261779   156 TCRKRVGLTgFDCR-CGNLFCGIHRYSDKHNCTY 188
Cdd:pfam01428   5 GCKKKDFLP-FKCRfCGKNFCLKHRLPEDHDCSG 37
ZnF_A20 smart00259
A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger ...
 11-35 7.92e-06

A20-like zinc fingers; A20- (an inhibitor of cell death)-like zinc fingers. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappaB activation.


Pssm-ID: 128555  Cd Length: 26  Bit Score: 41.42  E-value: 7.92e-06
                           10        20
                   ....*....|....*....|....*.
gi 54261779     11 PILC-TTGCGFYGNPRTNGMCSVCYK 35
Cdd:smart00259   1 PIKCrRPGCGFFGNPATEGLCSKCFK 26
FYVE1_Vac1p_like cd15761
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ...
 150-178 3.96e-03

FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277300  Cd Length: 76  Bit Score: 34.94  E-value: 3.96e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 54261779 150 KKNRCFTCRKRVG-LTGF-DCR-CGNLFCGIH 178
Cdd:cd15761   9 GKSRCSECGKTLNkKNGIvNCRkCGELFCNEH 40
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH