NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489056191|ref|WP_002966331|]
View 

MULTISPECIES: metal-sulfur cluster assembly factor [Brucella]

Protein Classification

metal-sulfur cluster assembly factor( domain architecture ID 10005417)

metal-sulfur cluster assembly factor similar to Bacillus subtilis Fe-S protein maturation auxiliary factor YitW, which may function as a Fe-S cluster carrier

CATH:  3.30.300.130
SCOP:  4003743

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PaaD COG2151
Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, ...
 7-98 3.61e-36

Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441754  Cd Length: 102  Bit Score: 118.29  E-value: 3.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056191   7 ERIKACVREALRAVQDPELAVNLVDLGMIYAVEISDDGMVHVKMTTTTRGCPAAGFLTQAVQACIEEIEGVTGARVELTY 86
Cdd:COG2151    6 EPLEEEVWEALKTVYDPEIPVNIVDLGLIYDVEVDDDGRVKVTMTLTTPGCPAADVIPDDVEEALEEVPGVEDVEVELVW 85

                         90
                 ....*....|..
gi 489056191  87 EPEWKPEMAIPE 98
Cdd:COG2151   86 DPPWTPDRMSEE 97
 
Name Accession Description Interval E-value
PaaD COG2151
Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, ...
 7-98 3.61e-36

Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441754  Cd Length: 102  Bit Score: 118.29  E-value: 3.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056191   7 ERIKACVREALRAVQDPELAVNLVDLGMIYAVEISDDGMVHVKMTTTTRGCPAAGFLTQAVQACIEEIEGVTGARVELTY 86
Cdd:COG2151    6 EPLEEEVWEALKTVYDPEIPVNIVDLGLIYDVEVDDDGRVKVTMTLTTPGCPAADVIPDDVEEALEEVPGVEDVEVELVW 85

                         90
                 ....*....|..
gi 489056191  87 EPEWKPEMAIPE 98
Cdd:COG2151   86 DPPWTPDRMSEE 97
SUF_assoc TIGR02945
FeS assembly SUF system protein; Members of this family belong to the broader pfam01883, or ...
 8-94 2.22e-30

FeS assembly SUF system protein; Members of this family belong to the broader pfam01883, or Domain of Unknown Function DUF59. Many members of DUF59 are candidate ring hydroxylating complex subunits. However, members of the narrower family defined here all are found in genomes that carry the FeS assembly SUF system. For 70 % of these species, the member of this protein family is found as part of the SUF locus, usually immediately downstream of the sufS gene. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 131990  Cd Length: 99  Bit Score: 103.92  E-value: 2.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056191    8 RIKACVREALRAVQDPELAVNLVDLGMIYAVEISDDGMVHVKMTTTTRGCPAAGFLTQAVQACIEEIEGVTGARVELTYE 87
Cdd:TIGR02945   1 RLKDAVIEALKTVYDPEIPVNIYELGLIYDIDVDDDGHVDIQMTLTAPNCPVAGSMPGEVENAVRAVPGVGSVTVELVWD 80


                  ....*..
gi 489056191   88 PEWKPEM 94
Cdd:TIGR02945  81 PPWTPER 87
FeS_assembly_P pfam01883
Iron-sulfur cluster assembly protein; This family has an alpha/beta topology, with 13 ...
 10-82 7.39e-15

Iron-sulfur cluster assembly protein; This family has an alpha/beta topology, with 13 conserved hydrophobic residues at its core and a putative active site containing a highly conserved cysteine. Members of this family are involved in a range of physiological functions. The family includes PaaJ (PhaH) from Pseudomonas putida. PaaJ forms a complex with PaaG (PhaF), PaaI (PhaG) and PaaK (PhaI), which hydroxylates phenylacetic acid to 2-hydroxyphenylacetic acid. It also includes PaaD from Escherichia coli, a member of a multicomponent oxygenase involved in phenylacetyl-CoA hydroxylation. Furthermore, several members of this family are shown to be involved in iron-sulfur (FeS) cluster assembly. Iron-sulfur (FeS) clusters are inorganic co-factors that are are able to transfer electrons and act as catalysts. They are involved in diverse cellular processes including cellular respiration, DNA replication and repair, antibiotic resistance, and dinitrogen fixation. The biogenesis of such clusters from elemental iron and sulfur is an enzymatic process that requires a set of specialized proteins. Proteins containing this domain include the chloroplast protein HCF101 (high chlorophyll fluorescence 101), which has been described as an essential and specific factor for assembly of [4Fe-4S]-cluster-containing protein complexes such as the membrane complex Photosystem I (PSI) and the heterodimeric FTR (ferredoxin-thioredoxin reductase) complex and is involved in the assembly of [4Fe-4S] clusters and their transfer to apoproteins. The mature HCF101 protein contains this domain at the N-terminal as well as eight cysteine residues along the sequence. All cysteine residues are conserved among higher plants, but of the two cysteine residues located in this domain only Cys128 is highly conserved and is present in the highly conserved P-loop domain of the plant HCF101 (CKGGVGKS). SufT protein from Staphylococcus aureus is composed of this domain solely and is shown to be involved in the maturation of FeS proteins. Given all this data, it is hypothesized that this domain might play a role in FeS cluster assembly.


Pssm-ID: 460370  Cd Length: 73  Bit Score: 63.42  E-value: 7.39e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489056191   10 KACVREALRAVQDPELAVNLVDLGMIYAVEIsDDGMVHVKMTTTTRGCPAAGFLTQAVQACIEEIEG-VTGARV 82
Cdd:pfam01883   1 KAAVLAALRTVIDPETGVDLVSLGLVRNIDI-EGGKVSVDITLTYPACPAAEAIRADAEAALRALPGeVVEVSV 73
 
Name Accession Description Interval E-value
PaaD COG2151
Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, ...
 7-98 3.61e-36

Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441754  Cd Length: 102  Bit Score: 118.29  E-value: 3.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056191   7 ERIKACVREALRAVQDPELAVNLVDLGMIYAVEISDDGMVHVKMTTTTRGCPAAGFLTQAVQACIEEIEGVTGARVELTY 86
Cdd:COG2151    6 EPLEEEVWEALKTVYDPEIPVNIVDLGLIYDVEVDDDGRVKVTMTLTTPGCPAADVIPDDVEEALEEVPGVEDVEVELVW 85

                         90
                 ....*....|..
gi 489056191  87 EPEWKPEMAIPE 98
Cdd:COG2151   86 DPPWTPDRMSEE 97
SUF_assoc TIGR02945
FeS assembly SUF system protein; Members of this family belong to the broader pfam01883, or ...
 8-94 2.22e-30

FeS assembly SUF system protein; Members of this family belong to the broader pfam01883, or Domain of Unknown Function DUF59. Many members of DUF59 are candidate ring hydroxylating complex subunits. However, members of the narrower family defined here all are found in genomes that carry the FeS assembly SUF system. For 70 % of these species, the member of this protein family is found as part of the SUF locus, usually immediately downstream of the sufS gene. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 131990  Cd Length: 99  Bit Score: 103.92  E-value: 2.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056191    8 RIKACVREALRAVQDPELAVNLVDLGMIYAVEISDDGMVHVKMTTTTRGCPAAGFLTQAVQACIEEIEGVTGARVELTYE 87
Cdd:TIGR02945   1 RLKDAVIEALKTVYDPEIPVNIYELGLIYDIDVDDDGHVDIQMTLTAPNCPVAGSMPGEVENAVRAVPGVGSVTVELVWD 80


                  ....*..
gi 489056191   88 PEWKPEM 94
Cdd:TIGR02945  81 PPWTPER 87
FeS_assembly_P pfam01883
Iron-sulfur cluster assembly protein; This family has an alpha/beta topology, with 13 ...
 10-82 7.39e-15

Iron-sulfur cluster assembly protein; This family has an alpha/beta topology, with 13 conserved hydrophobic residues at its core and a putative active site containing a highly conserved cysteine. Members of this family are involved in a range of physiological functions. The family includes PaaJ (PhaH) from Pseudomonas putida. PaaJ forms a complex with PaaG (PhaF), PaaI (PhaG) and PaaK (PhaI), which hydroxylates phenylacetic acid to 2-hydroxyphenylacetic acid. It also includes PaaD from Escherichia coli, a member of a multicomponent oxygenase involved in phenylacetyl-CoA hydroxylation. Furthermore, several members of this family are shown to be involved in iron-sulfur (FeS) cluster assembly. Iron-sulfur (FeS) clusters are inorganic co-factors that are are able to transfer electrons and act as catalysts. They are involved in diverse cellular processes including cellular respiration, DNA replication and repair, antibiotic resistance, and dinitrogen fixation. The biogenesis of such clusters from elemental iron and sulfur is an enzymatic process that requires a set of specialized proteins. Proteins containing this domain include the chloroplast protein HCF101 (high chlorophyll fluorescence 101), which has been described as an essential and specific factor for assembly of [4Fe-4S]-cluster-containing protein complexes such as the membrane complex Photosystem I (PSI) and the heterodimeric FTR (ferredoxin-thioredoxin reductase) complex and is involved in the assembly of [4Fe-4S] clusters and their transfer to apoproteins. The mature HCF101 protein contains this domain at the N-terminal as well as eight cysteine residues along the sequence. All cysteine residues are conserved among higher plants, but of the two cysteine residues located in this domain only Cys128 is highly conserved and is present in the highly conserved P-loop domain of the plant HCF101 (CKGGVGKS). SufT protein from Staphylococcus aureus is composed of this domain solely and is shown to be involved in the maturation of FeS proteins. Given all this data, it is hypothesized that this domain might play a role in FeS cluster assembly.


Pssm-ID: 460370  Cd Length: 73  Bit Score: 63.42  E-value: 7.39e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489056191   10 KACVREALRAVQDPELAVNLVDLGMIYAVEIsDDGMVHVKMTTTTRGCPAAGFLTQAVQACIEEIEG-VTGARV 82
Cdd:pfam01883   1 KAAVLAALRTVIDPETGVDLVSLGLVRNIDI-EGGKVSVDITLTYPACPAAEAIRADAEAALRALPGeVVEVSV 73
PA_CoA_Oxy4 TIGR02159
phenylacetate-CoA oxygenase, PaaJ subunit; Phenylacetate-CoA oxygenase is comprised of a five ...
 20-90 5.31e-10

phenylacetate-CoA oxygenase, PaaJ subunit; Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA. [Energy metabolism, Other]


Pssm-ID: 131214  Cd Length: 146  Bit Score: 52.87  E-value: 5.31e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489056191   20 VQDPEL-AVNLVDLGMIYAVEISDDGmVHVKMTTTTRGCPAAGFLTQAVQACIEEIeGVTGARVELTYEPEW 90
Cdd:TIGR02159   1 VPDPEIpVVSVTDLGMVREVDVDGGG-VVVKFTPTYSGCPALEVIRQDIRDAVRAL-GVEVVEVSTSLDPPW 70
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH