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Conserved domains on  [gi|18423312|ref|NP_568764|]
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2 iron, 2 sulfur cluster binding protein [Arabidopsis thaliana]

Protein Classification

CDGSH iron-sulfur domain-containing protein( domain architecture ID 1710)

CDGSH iron-sulfur domain-containing protein binds a redox-active pH-labile 2Fe-2S cluster; similar to Arabidopsis thaliana CDGSH iron-sulfur domain-containing protein NEET that plays an important role in plant development, senescence, reactive oxygen homeostasis, and iron metabolism

CATH:  3.40.5.90
Gene Ontology:  GO:0051537|GO:0106034|GO:0046872
PubMed:  29556009
SCOP:  3002112

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-CDGSH super family cl02748
Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than ...
 73-94 8.59e-10

Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than zinc as a redox-active pH-labile 2Fe-2S cluster. The conserved sequence C-X-C-X2-(S/T)-X3-P-X-C-D-G-(S/A/T)-H is a defining feature of this family. The domain is oriented towards the cytoplasm and is tethered to the mitochondrial membrane by a more N-terminal domain found in higher vertebrates, MitoNEET_N, pfam10660. The domain forms a uniquely folded homo-dimer and spans the outer mitochondrial membrane, orienting the iron-binding residues towards the cytoplasm.


The actual alignment was detected with superfamily member smart00704:

Pssm-ID: 470664  Cd Length: 38  Bit Score: 49.65  E-value: 8.59e-10
                           10        20
                   ....*....|....*....|..
gi 18423312     73 YCRCWRSGTFPLCDGSHVKHNK 94
Cdd:smart00704  16 LCRCGRSKNFPYCDGSHKKHNE 37
 
Name Accession Description Interval E-value
ZnF_CDGSH smart00704
CDGSH-type zinc finger. Function unknown;
73-94 8.59e-10

CDGSH-type zinc finger. Function unknown;


Pssm-ID: 197836  Cd Length: 38  Bit Score: 49.65  E-value: 8.59e-10
                           10        20
                   ....*....|....*....|..
gi 18423312     73 YCRCWRSGTFPLCDGSHVKHNK 94
Cdd:smart00704  16 LCRCGRSKNFPYCDGSHKKHNE 37
zf-CDGSH pfam09360
Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than ...
 60-89 8.62e-08

Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than zinc as a redox-active pH-labile 2Fe-2S cluster. The conserved sequence C-X-C-X2-(S/T)-X3-P-X-C-D-G-(S/A/T)-H is a defining feature of this family. The domain is oriented towards the cytoplasm and is tethered to the mitochondrial membrane by a more N-terminal domain found in higher vertebrates, MitoNEET_N, pfam10660. The domain forms a uniquely folded homo-dimer and spans the outer mitochondrial membrane, orienting the iron-binding residues towards the cytoplasm.


Pssm-ID: 462769  Cd Length: 41  Bit Score: 44.60  E-value: 8.62e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 18423312    60 SVVVTELSKNITPYCRCWRSGTFPLCDGSH 89
Cdd:pfam09360  11 ETVESREGRFVVALCRCGRSKNKPFCDGSH 40
COG3369 COG3369
Uncharacterized conserved protein, contains Zn-finger domain of CDGSH type [Function unknown];
48-93 7.82e-06

Uncharacterized conserved protein, contains Zn-finger domain of CDGSH type [Function unknown];


Pssm-ID: 442596  Cd Length: 68  Bit Score: 40.46  E-value: 7.82e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 18423312  48 PEIRKN-------EDKVVDSVVVTELSKNITPYCRCWRSGTFPLCDGSHVKHN 93
Cdd:COG3369   6 ITVAKNgpllvegDVEIVDADGNEYEEGKRYALCRCGLSKNKPFCDGSHKGTG 58
 
Name Accession Description Interval E-value
ZnF_CDGSH smart00704
CDGSH-type zinc finger. Function unknown;
73-94 8.59e-10

CDGSH-type zinc finger. Function unknown;


Pssm-ID: 197836  Cd Length: 38  Bit Score: 49.65  E-value: 8.59e-10
                           10        20
                   ....*....|....*....|..
gi 18423312     73 YCRCWRSGTFPLCDGSHVKHNK 94
Cdd:smart00704  16 LCRCGRSKNFPYCDGSHKKHNE 37
zf-CDGSH pfam09360
Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than ...
 60-89 8.62e-08

Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than zinc as a redox-active pH-labile 2Fe-2S cluster. The conserved sequence C-X-C-X2-(S/T)-X3-P-X-C-D-G-(S/A/T)-H is a defining feature of this family. The domain is oriented towards the cytoplasm and is tethered to the mitochondrial membrane by a more N-terminal domain found in higher vertebrates, MitoNEET_N, pfam10660. The domain forms a uniquely folded homo-dimer and spans the outer mitochondrial membrane, orienting the iron-binding residues towards the cytoplasm.


Pssm-ID: 462769  Cd Length: 41  Bit Score: 44.60  E-value: 8.62e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 18423312    60 SVVVTELSKNITPYCRCWRSGTFPLCDGSH 89
Cdd:pfam09360  11 ETVESREGRFVVALCRCGRSKNKPFCDGSH 40
COG3369 COG3369
Uncharacterized conserved protein, contains Zn-finger domain of CDGSH type [Function unknown];
48-93 7.82e-06

Uncharacterized conserved protein, contains Zn-finger domain of CDGSH type [Function unknown];


Pssm-ID: 442596  Cd Length: 68  Bit Score: 40.46  E-value: 7.82e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 18423312  48 PEIRKN-------EDKVVDSVVVTELSKNITPYCRCWRSGTFPLCDGSHVKHN 93
Cdd:COG3369   6 ITVAKNgpllvegDVEIVDADGNEYEEGKRYALCRCGLSKNKPFCDGSHKGTG 58
 
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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