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Conserved domains on  [gi|927146440|ref|XP_013914713|]
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PREDICTED: methyltransferase-like protein 23 isoform X1 [Thamnophis sirtalis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 39-156 2.56e-19

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 82.62  E-value: 2.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927146440  39 LDPQYGMYVWPCAVVLAQYIWFHRRlVCGKRILEIGAGVSLPGIVAAKCGA-EVILSDNAEFseCLDNCRRSCQMNNLSg 117
Cdd:COG3897   44 APPPFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPE--ALAALRLNAALNGVA- 119

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 927146440 118 ICVIGLTWGHISPclltLAPVDIILGADVFFEPEDFEDV 156
Cdd:COG3897  120 ITTRLGDWRDPPA----AGGFDLILGGDVLYERDLAEPL 154
SAM_superfamily super family cl15755
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 166-215 3.16e-04

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


The actual alignment was detected with superfamily member cd08539:

Pssm-ID: 472832  Cd Length: 78  Bit Score: 38.47  E-value: 3.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 927146440 166 RNPHAQFWTTYQVrsanWS-IEGLLHKWEMKSTYVPLQSFEANKEQLAGSS 215
Cdd:cd08539    5 HEIHPQYWTKFQV----WEwLQHLLDTNQLDANCIPFQEFDINGEHLCSMS 51
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 39-156 2.56e-19

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 82.62  E-value: 2.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927146440  39 LDPQYGMYVWPCAVVLAQYIWFHRRlVCGKRILEIGAGVSLPGIVAAKCGA-EVILSDNAEFseCLDNCRRSCQMNNLSg 117
Cdd:COG3897   44 APPPFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPE--ALAALRLNAALNGVA- 119

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 927146440 118 ICVIGLTWGHISPclltLAPVDIILGADVFFEPEDFEDV 156
Cdd:COG3897  120 ITTRLGDWRDPPA----AGGFDLILGGDVLYERDLAEPL 154
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 44-169 1.39e-16

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 74.29  E-value: 1.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927146440   44 GMYVWPCAVVLAQYI------WFHRRLVCGKRILEIGAGVSLPGIVAAK--CGAEVILSDNAEFSECLdncRRSCQMNNL 115
Cdd:pfam10294  18 GGHVWDAAVVLSKYLemkifkELGANNLSGLNVLELGSGTGLVGIAVALllPGASVTITDLEEALELL---KKNIELNAL 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 927146440  116 SG-ICVIGLTWGH-ISPCLLTLAPVDIILGADVFFEPEDFEDVVSTVHFLMERNPH 169
Cdd:pfam10294  95 SSkVVVKVLDWGEnLPPDLFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESV 150
SAM_PNT-ESE-3-like cd08539
Sterile alpha motif (SAM)/Pointed domain of ESE-3 like ETS transcriptional regulators; SAM ...
 166-215 3.16e-04

Sterile alpha motif (SAM)/Pointed domain of ESE-3 like ETS transcriptional regulators; SAM Pointed domain of ESE-3-like (Epithelium-Specific ETS) subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. It can act as a major transactivator by providing a potential docking site for co-activators. The ESE-3 transcriptional activator is involved in regulation of glandular epithelium differentiation through the MAP kinase signaling cascade. It is found to be expressed in glandular epithelium of prostate, pancreas, salivary gland, and trachea. Additionally, ESE-3 is differentially expressed during monocyte-derived dendritic cells development. DNA binding consensus motif for ESE-3 consists of purine-rich GGAA/T core sequence. The expression profiles of these factors are altered in epithelial cancers. Members of this subfamily are potential targets for cancer therapy.


Pssm-ID: 188882  Cd Length: 78  Bit Score: 38.47  E-value: 3.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 927146440 166 RNPHAQFWTTYQVrsanWS-IEGLLHKWEMKSTYVPLQSFEANKEQLAGSS 215
Cdd:cd08539    5 HEIHPQYWTKFQV----WEwLQHLLDTNQLDANCIPFQEFDINGEHLCSMS 51
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 39-156 2.56e-19

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 82.62  E-value: 2.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927146440  39 LDPQYGMYVWPCAVVLAQYIWFHRRlVCGKRILEIGAGVSLPGIVAAKCGA-EVILSDNAEFseCLDNCRRSCQMNNLSg 117
Cdd:COG3897   44 APPPFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPE--ALAALRLNAALNGVA- 119

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 927146440 118 ICVIGLTWGHISPclltLAPVDIILGADVFFEPEDFEDV 156
Cdd:COG3897  120 ITTRLGDWRDPPA----AGGFDLILGGDVLYERDLAEPL 154
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 44-169 1.39e-16

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 74.29  E-value: 1.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927146440   44 GMYVWPCAVVLAQYI------WFHRRLVCGKRILEIGAGVSLPGIVAAK--CGAEVILSDNAEFSECLdncRRSCQMNNL 115
Cdd:pfam10294  18 GGHVWDAAVVLSKYLemkifkELGANNLSGLNVLELGSGTGLVGIAVALllPGASVTITDLEEALELL---KKNIELNAL 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 927146440  116 SG-ICVIGLTWGH-ISPCLLTLAPVDIILGADVFFEPEDFEDVVSTVHFLMERNPH 169
Cdd:pfam10294  95 SSkVVVKVLDWGEnLPPDLFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESV 150
SAM_PNT-ESE-3-like cd08539
Sterile alpha motif (SAM)/Pointed domain of ESE-3 like ETS transcriptional regulators; SAM ...
 166-215 3.16e-04

Sterile alpha motif (SAM)/Pointed domain of ESE-3 like ETS transcriptional regulators; SAM Pointed domain of ESE-3-like (Epithelium-Specific ETS) subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. It can act as a major transactivator by providing a potential docking site for co-activators. The ESE-3 transcriptional activator is involved in regulation of glandular epithelium differentiation through the MAP kinase signaling cascade. It is found to be expressed in glandular epithelium of prostate, pancreas, salivary gland, and trachea. Additionally, ESE-3 is differentially expressed during monocyte-derived dendritic cells development. DNA binding consensus motif for ESE-3 consists of purine-rich GGAA/T core sequence. The expression profiles of these factors are altered in epithelial cancers. Members of this subfamily are potential targets for cancer therapy.


Pssm-ID: 188882  Cd Length: 78  Bit Score: 38.47  E-value: 3.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 927146440 166 RNPHAQFWTTYQVrsanWS-IEGLLHKWEMKSTYVPLQSFEANKEQLAGSS 215
Cdd:cd08539    5 HEIHPQYWTKFQV----WEwLQHLLDTNQLDANCIPFQEFDINGEHLCSMS 51
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 59-161 9.56e-03

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 34.99  E-value: 9.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927146440  59 WFHRRLVCGKRILEIGAGvslPGIVA---AKCGAEVILSDNAEfsECLDNCRRSCQMNNLSGICvigltwGHISPCLLTL 135
Cdd:COG2227   17 LLARLLPAGGRVLDVGCG---TGRLAlalARRGADVTGVDISP--EALEIARERAAELNVDFVQ------GDLEDLPLED 85

                         90       100
                 ....*....|....*....|....*.
gi 927146440 136 APVDIILGADVFFEPEDFEDVVSTVH 161
Cdd:COG2227   86 GSFDLVICSEVLEHLPDPAALLRELA 111
 
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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