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Conserved domains on  [gi|115534146|ref|NP_497920|]
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Iron-binding zinc finger CDGSH type domain-containing protein [Caenorhabditis elegans]

Protein Classification

CDGSH iron-sulfur domain-containing protein( domain architecture ID 10653775)

CDGSH iron-sulfur domain-containing protein binds a redox-active pH-labile 2Fe-2S cluster

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
ZnF_CDGSH smart00704
CDGSH-type zinc finger. Function unknown;
74-111 5.30e-13

CDGSH-type zinc finger. Function unknown;


:

Pssm-ID: 197836  Cd Length: 38  Bit Score: 59.66  E-value: 5.30e-13
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 115534146    74 KLPTKVHMKKDKVYAWCSCGYSGSQPLCDGSHNSIRIP 111
Cdd:smart00704   1 KRPDEVEVEKRKKYALCRCGRSKNFPYCDGSHKKHNEQ 38
zf-CDGSH super family cl02748
Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than ...
 127-156 2.38e-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.


The actual alignment was detected with superfamily member COG3369:

Pssm-ID: 470664  Cd Length: 68  Bit Score: 48.16  E-value: 2.38e-08
                         10        20        30
                 ....*....|....*....|....*....|
gi 115534146 127 TVWLCNCKQTNNRPFCDGSHKTVTDEDKKA 156
Cdd:COG3369   35 RYALCRCGLSKNKPFCDGSHKGTGFEPEGE 64
 
Name Accession Description Interval E-value
ZnF_CDGSH smart00704
CDGSH-type zinc finger. Function unknown;
74-111 5.30e-13

CDGSH-type zinc finger. Function unknown;


Pssm-ID: 197836  Cd Length: 38  Bit Score: 59.66  E-value: 5.30e-13
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 115534146    74 KLPTKVHMKKDKVYAWCSCGYSGSQPLCDGSHNSIRIP 111
Cdd:smart00704   1 KRPDEVEVEKRKKYALCRCGRSKNFPYCDGSHKKHNEQ 38
COG3369 COG3369
Uncharacterized conserved protein, contains Zn-finger domain of CDGSH type [Function unknown];
68-108 1.50e-09

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


Pssm-ID: 442596  Cd Length: 68  Bit Score: 51.24  E-value: 1.50e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 115534146  68 TGKVHSKLPTKVHMKKDKVYAWCSCGYSGSQPLCDGSHNSI 108
Cdd:COG3369   17 EGDVEIVDADGNEYEEGKRYALCRCGLSKNKPFCDGSHKGT 57
COG3369 COG3369
Uncharacterized conserved protein, contains Zn-finger domain of CDGSH type [Function unknown];
127-156 2.38e-08

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


Pssm-ID: 442596  Cd Length: 68  Bit Score: 48.16  E-value: 2.38e-08
                         10        20        30
                 ....*....|....*....|....*....|
gi 115534146 127 TVWLCNCKQTNNRPFCDGSHKTVTDEDKKA 156
Cdd:COG3369   35 RYALCRCGLSKNKPFCDGSHKGTGFEPEGE 64
ZnF_CDGSH smart00704
CDGSH-type zinc finger. Function unknown;
117-147 8.72e-08

CDGSH-type zinc finger. Function unknown;


Pssm-ID: 197836  Cd Length: 38  Bit Score: 46.18  E-value: 8.72e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 115534146   117 PVRFIPDKDMTVWLCNCKQTNNRPFCDGSHK 147
Cdd:smart00704   3 PDEVEVEKRKKYALCRCGRSKNFPYCDGSHK 33
zf-CDGSH pfam09360
Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than ...
 108-147 8.60e-07

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: 43.44  E-value: 8.60e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 115534146  108 IRIPDLKLKPVRFIPDKDMtVWLCNCKQTNNRPFCDGSHK 147
Cdd:pfam09360   3 LLVEDADGETVESREGRFV-VALCRCGRSKNKPFCDGSHK 41
zf-CDGSH pfam09360
Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than ...
 82-105 2.06e-05

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: 39.59  E-value: 2.06e-05
                          10        20
                  ....*....|....*....|....
gi 115534146   82 KKDKVYAWCSCGYSGSQPLCDGSH 105
Cdd:pfam09360  17 EGRFVVALCRCGRSKNKPFCDGSH 40
 
Name Accession Description Interval E-value
ZnF_CDGSH smart00704
CDGSH-type zinc finger. Function unknown;
74-111 5.30e-13

CDGSH-type zinc finger. Function unknown;


Pssm-ID: 197836  Cd Length: 38  Bit Score: 59.66  E-value: 5.30e-13
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 115534146    74 KLPTKVHMKKDKVYAWCSCGYSGSQPLCDGSHNSIRIP 111
Cdd:smart00704   1 KRPDEVEVEKRKKYALCRCGRSKNFPYCDGSHKKHNEQ 38
COG3369 COG3369
Uncharacterized conserved protein, contains Zn-finger domain of CDGSH type [Function unknown];
68-108 1.50e-09

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


Pssm-ID: 442596  Cd Length: 68  Bit Score: 51.24  E-value: 1.50e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 115534146  68 TGKVHSKLPTKVHMKKDKVYAWCSCGYSGSQPLCDGSHNSI 108
Cdd:COG3369   17 EGDVEIVDADGNEYEEGKRYALCRCGLSKNKPFCDGSHKGT 57
COG3369 COG3369
Uncharacterized conserved protein, contains Zn-finger domain of CDGSH type [Function unknown];
127-156 2.38e-08

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


Pssm-ID: 442596  Cd Length: 68  Bit Score: 48.16  E-value: 2.38e-08
                         10        20        30
                 ....*....|....*....|....*....|
gi 115534146 127 TVWLCNCKQTNNRPFCDGSHKTVTDEDKKA 156
Cdd:COG3369   35 RYALCRCGLSKNKPFCDGSHKGTGFEPEGE 64
ZnF_CDGSH smart00704
CDGSH-type zinc finger. Function unknown;
117-147 8.72e-08

CDGSH-type zinc finger. Function unknown;


Pssm-ID: 197836  Cd Length: 38  Bit Score: 46.18  E-value: 8.72e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 115534146   117 PVRFIPDKDMTVWLCNCKQTNNRPFCDGSHK 147
Cdd:smart00704   3 PDEVEVEKRKKYALCRCGRSKNFPYCDGSHK 33
zf-CDGSH pfam09360
Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than ...
 108-147 8.60e-07

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: 43.44  E-value: 8.60e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 115534146  108 IRIPDLKLKPVRFIPDKDMtVWLCNCKQTNNRPFCDGSHK 147
Cdd:pfam09360   3 LLVEDADGETVESREGRFV-VALCRCGRSKNKPFCDGSHK 41
zf-CDGSH pfam09360
Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than ...
 82-105 2.06e-05

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: 39.59  E-value: 2.06e-05
                          10        20
                  ....*....|....*....|....
gi 115534146   82 KKDKVYAWCSCGYSGSQPLCDGSH 105
Cdd:pfam09360  17 EGRFVVALCRCGRSKNKPFCDGSH 40
 
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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