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Conserved domains on  [gi|1907070897|ref|XP_036010559|]
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E3 SUMO-protein ligase ZNF451 isoform X2 [Mus musculus]

Protein Classification

PIN_ZNF451-like domain-containing protein( domain architecture ID 13036800)

PIN_ZNF451-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PIN_ZNF451-like cd18721
LabA-like PIN domain of human zinc finger protein 451 and related proteins; Human ZNF451 (also ...
 556-672 6.97e-78

LabA-like PIN domain of human zinc finger protein 451 and related proteins; Human ZNF451 (also known as COASTER) functions as a transcriptional cofactor in promyelocytic leukemia bodies in the nucleus, it acts as a coactivator or corepressor, depending on the factors with which it interacts. ZNF451 interacts with p300 by the PIN-like domain and down regulates TGF-beta signaling in a p300-dependent and sumoylation-independent manner. This subfamily belongs to LabA-like PIN domain family which includes Synechococcus elongatus PCC 7942 LabA, human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_11.


:

Pssm-ID: 350288  Cd Length: 117  Bit Score: 244.95  E-value: 6.97e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070897 556 HIVFVDFDNWSNFFGHLPGHLNQGTFIWGFQGGNTNWKPPLSCKVYNYLSRIGCFFLHPRCSKRKDAADFAICMHAGRLD 635
Cdd:cd18721     1 HIVFVDLDNWSGFFKHLPGHLPQGTFVWGFQGGNTNWKPPKSCKIYNYLNRIGCFFLHPRCGKTKDAADFAICMHAGKLD 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907070897 636 EQLPKQIPFTILSGDQGFLELENQFKKTQRPAHILNP 672
Cdd:cd18721    81 ERLPKQIPFTILSGDKGFLELENQFKKTQRPAHILNP 117
 
Name Accession Description Interval E-value
PIN_ZNF451-like cd18721
LabA-like PIN domain of human zinc finger protein 451 and related proteins; Human ZNF451 (also ...
 556-672 6.97e-78

LabA-like PIN domain of human zinc finger protein 451 and related proteins; Human ZNF451 (also known as COASTER) functions as a transcriptional cofactor in promyelocytic leukemia bodies in the nucleus, it acts as a coactivator or corepressor, depending on the factors with which it interacts. ZNF451 interacts with p300 by the PIN-like domain and down regulates TGF-beta signaling in a p300-dependent and sumoylation-independent manner. This subfamily belongs to LabA-like PIN domain family which includes Synechococcus elongatus PCC 7942 LabA, human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_11.


Pssm-ID: 350288  Cd Length: 117  Bit Score: 244.95  E-value: 6.97e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070897 556 HIVFVDFDNWSNFFGHLPGHLNQGTFIWGFQGGNTNWKPPLSCKVYNYLSRIGCFFLHPRCSKRKDAADFAICMHAGRLD 635
Cdd:cd18721     1 HIVFVDLDNWSGFFKHLPGHLPQGTFVWGFQGGNTNWKPPKSCKIYNYLNRIGCFFLHPRCGKTKDAADFAICMHAGKLD 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907070897 636 EQLPKQIPFTILSGDQGFLELENQFKKTQRPAHILNP 672
Cdd:cd18721    81 ERLPKQIPFTILSGDKGFLELENQFKKTQRPAHILNP 117
PIN_11 pfam18479
PIN like domain; This is a eukaryotic/eumetazoan PIN like domain found in the C-terminal ...
 553-670 2.89e-76

PIN like domain; This is a eukaryotic/eumetazoan PIN like domain found in the C-terminal region of bilateral ZNF451 proteins such as isoform 1 of human ZNF451. ZNF451 was shown to interact with p300 by the PIN-like domain and to negatively regulate TGF-beta signalling in a p300-dependent and sumoylation-independent manner. This domain is suggested to posses a potential active nuclease due to the presence of at least four conserved Asp residues in the predicted active site. Furthermore, it contains several conserved Cys and His residues, which may suggest stabilization of the domain structure with an embedded short zinc-binding loop.


Pssm-ID: 436532  Cd Length: 118  Bit Score: 240.92  E-value: 2.89e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070897 553 TMTHIVFVDFDNWSNFFGHLPGHLNQGTFIWGFQGGNTNWKPPLSCKVYNYLSRIGCFFLHPRCSKRKDAADFAICMHAG 632
Cdd:pfam18479   1 QMKHIVFVDLDNWTGIFKHLPHYFPQETFLWGFYGGNTKWFPPKSSDVYKKLVQDGCFFLHPKCSYTKDAADFALCLHAG 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907070897 633 RLDEQLPKQIPFTILSGDQGFLELENQFKKTQRPAHIL 670
Cdd:pfam18479  81 KLDERLPKHIPFTILSGDKGFYELSNQFENSKRHMHIV 118
 
Name Accession Description Interval E-value
PIN_ZNF451-like cd18721
LabA-like PIN domain of human zinc finger protein 451 and related proteins; Human ZNF451 (also ...
 556-672 6.97e-78

LabA-like PIN domain of human zinc finger protein 451 and related proteins; Human ZNF451 (also known as COASTER) functions as a transcriptional cofactor in promyelocytic leukemia bodies in the nucleus, it acts as a coactivator or corepressor, depending on the factors with which it interacts. ZNF451 interacts with p300 by the PIN-like domain and down regulates TGF-beta signaling in a p300-dependent and sumoylation-independent manner. This subfamily belongs to LabA-like PIN domain family which includes Synechococcus elongatus PCC 7942 LabA, human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Matelska et al. recently classified PIN-like domains into distinct groups; this subgroup includes some sequences belonging to one of these, PIN_11.


Pssm-ID: 350288  Cd Length: 117  Bit Score: 244.95  E-value: 6.97e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070897 556 HIVFVDFDNWSNFFGHLPGHLNQGTFIWGFQGGNTNWKPPLSCKVYNYLSRIGCFFLHPRCSKRKDAADFAICMHAGRLD 635
Cdd:cd18721     1 HIVFVDLDNWSGFFKHLPGHLPQGTFVWGFQGGNTNWKPPKSCKIYNYLNRIGCFFLHPRCGKTKDAADFAICMHAGKLD 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907070897 636 EQLPKQIPFTILSGDQGFLELENQFKKTQRPAHILNP 672
Cdd:cd18721    81 ERLPKQIPFTILSGDKGFLELENQFKKTQRPAHILNP 117
PIN_11 pfam18479
PIN like domain; This is a eukaryotic/eumetazoan PIN like domain found in the C-terminal ...
 553-670 2.89e-76

PIN like domain; This is a eukaryotic/eumetazoan PIN like domain found in the C-terminal region of bilateral ZNF451 proteins such as isoform 1 of human ZNF451. ZNF451 was shown to interact with p300 by the PIN-like domain and to negatively regulate TGF-beta signalling in a p300-dependent and sumoylation-independent manner. This domain is suggested to posses a potential active nuclease due to the presence of at least four conserved Asp residues in the predicted active site. Furthermore, it contains several conserved Cys and His residues, which may suggest stabilization of the domain structure with an embedded short zinc-binding loop.


Pssm-ID: 436532  Cd Length: 118  Bit Score: 240.92  E-value: 2.89e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070897 553 TMTHIVFVDFDNWSNFFGHLPGHLNQGTFIWGFQGGNTNWKPPLSCKVYNYLSRIGCFFLHPRCSKRKDAADFAICMHAG 632
Cdd:pfam18479   1 QMKHIVFVDLDNWTGIFKHLPHYFPQETFLWGFYGGNTKWFPPKSSDVYKKLVQDGCFFLHPKCSYTKDAADFALCLHAG 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907070897 633 RLDEQLPKQIPFTILSGDQGFLELENQFKKTQRPAHIL 670
Cdd:pfam18479  81 KLDERLPKHIPFTILSGDKGFYELSNQFENSKRHMHIV 118
PIN_LabA-like cd06167
PIN domain of Synechococcus elongatus LabA (low-amplitude and bright) and related proteins; ...
 557-672 1.32e-27

PIN domain of Synechococcus elongatus LabA (low-amplitude and bright) and related proteins; The LabA-like PIN domain family includes Synechococcus elongatus PCC 7942 LabA which participates in cyanobacterial circadian timing. It is required for negative feedback regulation of the autokinase/autophosphatase KaiC, a central component of the circadian clock system. In particular, LabA seems necessary for KaiC-dependent repression of gene expression. This family also includes the N-terminal domain of limkain b1, a human autoantigen associated with cytoplasmic vesicles. Other members are the LabA-like PIN domains of human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into this family.


Pssm-ID: 350201  Cd Length: 113  Bit Score: 107.50  E-value: 1.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070897 557 IVFVDFDNWSNFFGHLPGHLNQGTFI-WGFQG-GNTNWKPPLSCKVYNYlsrigCFFLHPRCSKRKDAADFAICMHAGRL 634
Cdd:cd06167     1 GVLVDADNCSNGFGALILRRYAGLFLqMGFEKyANINAQPLLVPPSNNR-----GFTVIRVAAKRKDAADVALVRQAGRL 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907070897 635 DEQlPKQIPFTILSGDQG-FLELENQFKKTQRPAHILNP 672
Cdd:cd06167    76 AYT-GAPDTVVLVSGDKLdFSDLIEKAKEAGLNVIVVGP 113
 
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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