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Conserved domains on  [gi|544956254|ref|WP_021361484|]
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Rossmann-like domain-containing protein [Clostridioides difficile]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2014 super family cl34391
Uncharacterized conserved protein, contains DUF4213 and DUF364 domains [Function unknown];
78-218 7.61e-11

Uncharacterized conserved protein, contains DUF4213 and DUF364 domains [Function unknown];


The actual alignment was detected with superfamily member COG2014:

Pssm-ID: 441617 [Multi-domain]  Cd Length: 249  Bit Score: 60.27  E-value: 7.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956254  78 SLKDILSLDLHDNPHDRSLFIASLNAVMKylgktdrtiHCKNNEPEICAKKFPEFIKMEFGNPKVAIIGYQPAIIDNIKD 157
Cdd:COG2014   64 PARELAELLLSWNPLERSLGLAAINALSN---------SPLDAEPKGLEDGDAFDLLPIKKGKKVAVVGYFPPLLEKLRK 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544956254 158 -FFETRVLDLNPEFvdtiqynvkiEDGIRD--YEDVISWADLVICTGSTLCNNSIINFLSLNKP 218
Cdd:COG2014  135 kGAELTVLERNPRR----------PGDLPDpaAEELLPEADVVIITGTTLVNKTLDRLLELAKN 188
 
Name Accession Description Interval E-value
COG2014 COG2014
Uncharacterized conserved protein, contains DUF4213 and DUF364 domains [Function unknown];
78-218 7.61e-11

Uncharacterized conserved protein, contains DUF4213 and DUF364 domains [Function unknown];


Pssm-ID: 441617 [Multi-domain]  Cd Length: 249  Bit Score: 60.27  E-value: 7.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956254  78 SLKDILSLDLHDNPHDRSLFIASLNAVMKylgktdrtiHCKNNEPEICAKKFPEFIKMEFGNPKVAIIGYQPAIIDNIKD 157
Cdd:COG2014   64 PARELAELLLSWNPLERSLGLAAINALSN---------SPLDAEPKGLEDGDAFDLLPIKKGKKVAVVGYFPPLLEKLRK 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544956254 158 -FFETRVLDLNPEFvdtiqynvkiEDGIRD--YEDVISWADLVICTGSTLCNNSIINFLSLNKP 218
Cdd:COG2014  135 kGAELTVLERNPRR----------PGDLPDpaAEELLPEADVVIITGTTLVNKTLDRLLELAKN 188
DUF364 pfam04016
Putative heavy-metal chelation; This domain of unknown function has a PLP-dependent ...
 141-209 1.44e-06

Putative heavy-metal chelation; This domain of unknown function has a PLP-dependent transferase-like fold. Its genomic context suggests that it may have a role in anaerobic vitamin B12 biosynthesis. This domain is often found at the C-terminus of proteins containing DUF4213, pfam13938. The structure of UnioProtKB:B8FUJ5, PDB:3l5o, suggests that the protein has an enolase N-terminal-like fold and this Rossmann-like C-terminal domain. Structural and bioinformatic analyses reveal partial similarities to Rossmann-like methyltransferases, with residues from the enolase-like fold combining to form a unique active site that is likely to be involved in the condensation or hydrolysis of molecules implicated in the synthesis of flavins, pterins or other siderophores. The protein may be playing a role in heavy-metal chelation.


Pssm-ID: 397911  Cd Length: 147  Bit Score: 46.44  E-value: 1.44e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956254  141 KVAIIGYQPAIIDNIKD-FFETRVLDLNPefvdTIQYNVKIEDGIRDYEDVISWADLVICTGSTLCNNSI 209
Cdd:pfam04016  13 KVAVVGYFAPVLKRLRErGAELTVLERNP----NLLDGEEGDYPDEAAEELLPEADVVIITGTTLVNGTL 78
 
Name Accession Description Interval E-value
COG2014 COG2014
Uncharacterized conserved protein, contains DUF4213 and DUF364 domains [Function unknown];
78-218 7.61e-11

Uncharacterized conserved protein, contains DUF4213 and DUF364 domains [Function unknown];


Pssm-ID: 441617 [Multi-domain]  Cd Length: 249  Bit Score: 60.27  E-value: 7.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956254  78 SLKDILSLDLHDNPHDRSLFIASLNAVMKylgktdrtiHCKNNEPEICAKKFPEFIKMEFGNPKVAIIGYQPAIIDNIKD 157
Cdd:COG2014   64 PARELAELLLSWNPLERSLGLAAINALSN---------SPLDAEPKGLEDGDAFDLLPIKKGKKVAVVGYFPPLLEKLRK 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544956254 158 -FFETRVLDLNPEFvdtiqynvkiEDGIRD--YEDVISWADLVICTGSTLCNNSIINFLSLNKP 218
Cdd:COG2014  135 kGAELTVLERNPRR----------PGDLPDpaAEELLPEADVVIITGTTLVNKTLDRLLELAKN 188
DUF364 pfam04016
Putative heavy-metal chelation; This domain of unknown function has a PLP-dependent ...
 141-209 1.44e-06

Putative heavy-metal chelation; This domain of unknown function has a PLP-dependent transferase-like fold. Its genomic context suggests that it may have a role in anaerobic vitamin B12 biosynthesis. This domain is often found at the C-terminus of proteins containing DUF4213, pfam13938. The structure of UnioProtKB:B8FUJ5, PDB:3l5o, suggests that the protein has an enolase N-terminal-like fold and this Rossmann-like C-terminal domain. Structural and bioinformatic analyses reveal partial similarities to Rossmann-like methyltransferases, with residues from the enolase-like fold combining to form a unique active site that is likely to be involved in the condensation or hydrolysis of molecules implicated in the synthesis of flavins, pterins or other siderophores. The protein may be playing a role in heavy-metal chelation.


Pssm-ID: 397911  Cd Length: 147  Bit Score: 46.44  E-value: 1.44e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544956254  141 KVAIIGYQPAIIDNIKD-FFETRVLDLNPefvdTIQYNVKIEDGIRDYEDVISWADLVICTGSTLCNNSI 209
Cdd:pfam04016  13 KVAVVGYFAPVLKRLRErGAELTVLERNP----NLLDGEEGDYPDEAAEELLPEADVVIITGTTLVNGTL 78
 
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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