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Conserved domains on  [gi|1034639643|ref|XP_016863618|]
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rRNA N6-adenosine-methyltransferase ZCCHC4 isoform X2 [Homo sapiens]

Protein Classification

ERI1 exoribonuclease 2( domain architecture ID 12072592)

ERI1 exoribonuclease 2 is a 3'-5' exonuclease family protein containing a GRF zinc finger; and may catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
N6-adenineMlase pfam10237
Probable N6-adenine methyltransferase; This is a protein of approximately 200 residues which ...
 169-256 2.04e-22

Probable N6-adenine methyltransferase; This is a protein of approximately 200 residues which is conserved from plants to humans. It contains a highly conserved QFW motif close to the N-terminus and a DPPF motif in the centre. The DPPF motif is characteriztic of N-6 adenine-specific DNA methylases, and this family is found in eukaryotes.


:

Pssm-ID: 463014  Cd Length: 118  Bit Score: 91.84  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639643 169 TNAQYLFADRSCQFLVDLL--SALGFRRVLCVGTPRLHELIKLtasgDKKSNIKSLLLDIDFRYsQFYMEDsFCHYNMFN 246
Cdd:pfam10237   1 QLSQFWYSDETAETLAKELldGADKDTRIACLSAPSLYEALKK----LLPPRINSLLLEYDKRF-AVYGPD-FVFYDYNN 74

                          90
                  ....*....|....
gi 1034639643 247 HH----FFDGKVDY 256
Cdd:pfam10237  75 PLdlpeFLKGSFDR 88
zf-GRF super family cl46396
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
 38-82 1.80e-09

GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396.


The actual alignment was detected with superfamily member pfam06839:

Pssm-ID: 480736  Cd Length: 45  Bit Score: 53.18  E-value: 1.80e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1034639643  38 PLCPHGpTLLFVKV--TQGKEETRRFYACSACRDrKDCNFFQWEDEK 82
Cdd:pfam06839   1 PLCPCG-QRAVLLTvrKTGPNPGRQFYKCPVGRE-KQCGFFQWADEV 45
DHHC super family cl19890
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 325-354 8.46e-03

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


The actual alignment was detected with superfamily member pfam01529:

Pssm-ID: 418707  Cd Length: 132  Bit Score: 36.58  E-value: 8.46e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034639643 325 NHCFLCKKCVKPSWIHCSICNHC-AVPDHSC 354
Cdd:pfam01529   6 KYCSTCNIYKPPRSKHCRVCNRCvLRFDHHC 36
 
Name Accession Description Interval E-value
N6-adenineMlase pfam10237
Probable N6-adenine methyltransferase; This is a protein of approximately 200 residues which ...
 169-256 2.04e-22

Probable N6-adenine methyltransferase; This is a protein of approximately 200 residues which is conserved from plants to humans. It contains a highly conserved QFW motif close to the N-terminus and a DPPF motif in the centre. The DPPF motif is characteriztic of N-6 adenine-specific DNA methylases, and this family is found in eukaryotes.


Pssm-ID: 463014  Cd Length: 118  Bit Score: 91.84  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639643 169 TNAQYLFADRSCQFLVDLL--SALGFRRVLCVGTPRLHELIKLtasgDKKSNIKSLLLDIDFRYsQFYMEDsFCHYNMFN 246
Cdd:pfam10237   1 QLSQFWYSDETAETLAKELldGADKDTRIACLSAPSLYEALKK----LLPPRINSLLLEYDKRF-AVYGPD-FVFYDYNN 74

                          90
                  ....*....|....
gi 1034639643 247 HH----FFDGKVDY 256
Cdd:pfam10237  75 PLdlpeFLKGSFDR 88
zf-GRF pfam06839
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
 38-82 1.80e-09

GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396.


Pssm-ID: 462017  Cd Length: 45  Bit Score: 53.18  E-value: 1.80e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1034639643  38 PLCPHGpTLLFVKV--TQGKEETRRFYACSACRDrKDCNFFQWEDEK 82
Cdd:pfam06839   1 PLCPCG-QRAVLLTvrKTGPNPGRQFYKCPVGRE-KQCGFFQWADEV 45
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 325-354 8.46e-03

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


Pssm-ID: 396215  Cd Length: 132  Bit Score: 36.58  E-value: 8.46e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034639643 325 NHCFLCKKCVKPSWIHCSICNHC-AVPDHSC 354
Cdd:pfam01529   6 KYCSTCNIYKPPRSKHCRVCNRCvLRFDHHC 36
 
Name Accession Description Interval E-value
N6-adenineMlase pfam10237
Probable N6-adenine methyltransferase; This is a protein of approximately 200 residues which ...
 169-256 2.04e-22

Probable N6-adenine methyltransferase; This is a protein of approximately 200 residues which is conserved from plants to humans. It contains a highly conserved QFW motif close to the N-terminus and a DPPF motif in the centre. The DPPF motif is characteriztic of N-6 adenine-specific DNA methylases, and this family is found in eukaryotes.


Pssm-ID: 463014  Cd Length: 118  Bit Score: 91.84  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639643 169 TNAQYLFADRSCQFLVDLL--SALGFRRVLCVGTPRLHELIKLtasgDKKSNIKSLLLDIDFRYsQFYMEDsFCHYNMFN 246
Cdd:pfam10237   1 QLSQFWYSDETAETLAKELldGADKDTRIACLSAPSLYEALKK----LLPPRINSLLLEYDKRF-AVYGPD-FVFYDYNN 74

                          90
                  ....*....|....
gi 1034639643 247 HH----FFDGKVDY 256
Cdd:pfam10237  75 PLdlpeFLKGSFDR 88
zf-GRF pfam06839
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
 38-82 1.80e-09

GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396.


Pssm-ID: 462017  Cd Length: 45  Bit Score: 53.18  E-value: 1.80e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1034639643  38 PLCPHGpTLLFVKV--TQGKEETRRFYACSACRDrKDCNFFQWEDEK 82
Cdd:pfam06839   1 PLCPCG-QRAVLLTvrKTGPNPGRQFYKCPVGRE-KQCGFFQWADEV 45
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 325-354 8.46e-03

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


Pssm-ID: 396215  Cd Length: 132  Bit Score: 36.58  E-value: 8.46e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034639643 325 NHCFLCKKCVKPSWIHCSICNHC-AVPDHSC 354
Cdd:pfam01529   6 KYCSTCNIYKPPRSKHCRVCNRCvLRFDHHC 36
 
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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