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Conserved domains on  [gi|502189669|ref|WP_012728888|]
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iron-sulfur cluster assembly accessory protein [Tolumonas auensis]

Protein Classification

HesB/IscA family protein( domain architecture ID 10001059)

HesB/IscA family protein is a scaffold protein upon which 2Fe-2S clusters are assembled and subsequently transferred to acceptor proteins; similar to iron-sulfur assembly protein IscA that is involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway

Gene Ontology:  GO:0016226|GO:0051536
PubMed:  32108236

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IscA COG0316
Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein ...
 1-115 2.37e-12

Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440085 [Multi-domain]  Cd Length: 107  Bit Score: 58.24  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502189669   1 MIQIEESALTQLQRLQQQLVQECIGLRLIAKGDPCSGIKVDMGWTATQQPDDVLYRQSGLVFLADRRQWPLLKDCQISLA 80
Cdd:COG0316    1 PITLTDAAAKRIKRLLAKEGNPGLGLRVGVKGGGCSGFSYGLDFDDEPNEDDLVFEQDGVKVVVDPKSLPYLDGTEIDYV 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 502189669  81 ERQGQPGFNIQpqpaNcgscsPAAKST-NCPSTASV 115
Cdd:COG0316   81 EELLGSGFKFN----N-----PNAKSScGCGESFSV 107
 
Name Accession Description Interval E-value
IscA COG0316
Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein ...
 1-115 2.37e-12

Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440085 [Multi-domain]  Cd Length: 107  Bit Score: 58.24  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502189669   1 MIQIEESALTQLQRLQQQLVQECIGLRLIAKGDPCSGIKVDMGWTATQQPDDVLYRQSGLVFLADRRQWPLLKDCQISLA 80
Cdd:COG0316    1 PITLTDAAAKRIKRLLAKEGNPGLGLRVGVKGGGCSGFSYGLDFDDEPNEDDLVFEQDGVKVVVDPKSLPYLDGTEIDYV 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 502189669  81 ERQGQPGFNIQpqpaNcgscsPAAKST-NCPSTASV 115
Cdd:COG0316   81 EELLGSGFKFN----N-----PNAKSScGCGESFSV 107
TIGR00049 TIGR00049
Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be ...
 25-107 6.88e-04

Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be associated with the process of FeS-cluster assembly. The HesB proteins are associated with the nif gene cluster and the Rhizobium gene IscN has been shown to be required for nitrogen fixation. Nitrogenase includes multiple FeS clusters and many genes for their assembly. The E. coli SufA protein is associated with SufS, a NifS homolog and SufD which are involved in the FeS cluster assembly of the FhnF protein. The Azotobacter protein IscA (homologs of which are also found in E.coli) is associated which IscS, another NifS homolog and IscU, a nifU homolog as well as other factors consistent with a role in FeS cluster chemistry. A homolog from Geobacter contains a selenocysteine in place of an otherwise invariant cysteine, further suggesting a role in redox chemistry. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 272875 [Multi-domain]  Cd Length: 105  Bit Score: 36.40  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502189669   25 GLRLIAKGDPCSGIKVDMGWTATQQPDDVLYRQSGLVFLADRRQWPLLKDCQISLAERQGQPGFNIqpqpANcgscsPAA 104
Cdd:TIGR00049  23 GLRVGVKGGGCSGLQYGLEFDDEPNEDDEVFEQDGVKVVVDPKSLPYLDGSEIDYVEELLGSGFTF----TN-----PNA 93


                  ...
gi 502189669  105 KST 107
Cdd:TIGR00049  94 KGT 96
 
Name Accession Description Interval E-value
IscA COG0316
Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein ...
 1-115 2.37e-12

Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440085 [Multi-domain]  Cd Length: 107  Bit Score: 58.24  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502189669   1 MIQIEESALTQLQRLQQQLVQECIGLRLIAKGDPCSGIKVDMGWTATQQPDDVLYRQSGLVFLADRRQWPLLKDCQISLA 80
Cdd:COG0316    1 PITLTDAAAKRIKRLLAKEGNPGLGLRVGVKGGGCSGFSYGLDFDDEPNEDDLVFEQDGVKVVVDPKSLPYLDGTEIDYV 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 502189669  81 ERQGQPGFNIQpqpaNcgscsPAAKST-NCPSTASV 115
Cdd:COG0316   81 EELLGSGFKFN----N-----PNAKSScGCGESFSV 107
TIGR00049 TIGR00049
Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be ...
 25-107 6.88e-04

Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be associated with the process of FeS-cluster assembly. The HesB proteins are associated with the nif gene cluster and the Rhizobium gene IscN has been shown to be required for nitrogen fixation. Nitrogenase includes multiple FeS clusters and many genes for their assembly. The E. coli SufA protein is associated with SufS, a NifS homolog and SufD which are involved in the FeS cluster assembly of the FhnF protein. The Azotobacter protein IscA (homologs of which are also found in E.coli) is associated which IscS, another NifS homolog and IscU, a nifU homolog as well as other factors consistent with a role in FeS cluster chemistry. A homolog from Geobacter contains a selenocysteine in place of an otherwise invariant cysteine, further suggesting a role in redox chemistry. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 272875 [Multi-domain]  Cd Length: 105  Bit Score: 36.40  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502189669   25 GLRLIAKGDPCSGIKVDMGWTATQQPDDVLYRQSGLVFLADRRQWPLLKDCQISLAERQGQPGFNIqpqpANcgscsPAA 104
Cdd:TIGR00049  23 GLRVGVKGGGCSGLQYGLEFDDEPNEDDEVFEQDGVKVVVDPKSLPYLDGSEIDYVEELLGSGFTF----TN-----PNA 93


                  ...
gi 502189669  105 KST 107
Cdd:TIGR00049  94 KGT 96
 
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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