NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|193205053|ref|NP_001122648|]
View 

CDGSH iron-sulfur domain-containing protein 2 homologue [Caenorhabditis elegans]

Protein Classification

CDGSH iron-sulfur domain-containing protein( domain architecture ID 10653773)

CDGSH iron-sulfur domain-containing protein binds a redox-active pH-labile 2Fe-2S cluster; similar to Homo sapiens zinc finger CDGSH domain-containing protein 1

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ZnF_CDGSH smart00704
CDGSH-type zinc finger. Function unknown;
81-119 6.96e-14

CDGSH-type zinc finger. Function unknown;


:

Pssm-ID: 197836  Cd Length: 38  Bit Score: 61.20  E-value: 6.96e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 193205053    81 KIVDTVDIEDiGEKKAFCRCWKSEKWPYCDGSHGKHNKE 119
Cdd:smart00704   1 KRPDEVEVEK-RKKYALCRCGRSKNFPYCDGSHKKHNEQ 38
 
Name Accession Description Interval E-value
ZnF_CDGSH smart00704
CDGSH-type zinc finger. Function unknown;
81-119 6.96e-14

CDGSH-type zinc finger. Function unknown;


Pssm-ID: 197836  Cd Length: 38  Bit Score: 61.20  E-value: 6.96e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 193205053    81 KIVDTVDIEDiGEKKAFCRCWKSEKWPYCDGSHGKHNKE 119
Cdd:smart00704   1 KRPDEVEVEK-RKKYALCRCGRSKNFPYCDGSHKKHNEQ 38
zf-CDGSH pfam09360
Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than ...
 85-113 5.74e-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: 5.74e-07
                          10        20
                  ....*....|....*....|....*....
gi 193205053   85 TVDIEDIGEKKAFCRCWKSEKWPYCDGSH 113
Cdd:pfam09360  12 TVESREGRFVVALCRCGRSKNKPFCDGSH 40
COG3369 COG3369
Uncharacterized conserved protein, contains Zn-finger domain of CDGSH type [Function unknown];
73-124 9.62e-07

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


Pssm-ID: 442596  Cd Length: 68  Bit Score: 43.54  E-value: 9.62e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193205053  73 YKIQLDSNKIVDTVDIEDIGEKKAFCRCWKSEKWPYCDGSHGKHNKETGDNV 124
Cdd:COG3369   14 LLVEGDVEIVDADGNEYEEGKRYALCRCGLSKNKPFCDGSHKGTGFEPEGEA 65
 
Name Accession Description Interval E-value
ZnF_CDGSH smart00704
CDGSH-type zinc finger. Function unknown;
81-119 6.96e-14

CDGSH-type zinc finger. Function unknown;


Pssm-ID: 197836  Cd Length: 38  Bit Score: 61.20  E-value: 6.96e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 193205053    81 KIVDTVDIEDiGEKKAFCRCWKSEKWPYCDGSHGKHNKE 119
Cdd:smart00704   1 KRPDEVEVEK-RKKYALCRCGRSKNFPYCDGSHKKHNEQ 38
zf-CDGSH pfam09360
Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than ...
 85-113 5.74e-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: 5.74e-07
                          10        20
                  ....*....|....*....|....*....
gi 193205053   85 TVDIEDIGEKKAFCRCWKSEKWPYCDGSH 113
Cdd:pfam09360  12 TVESREGRFVVALCRCGRSKNKPFCDGSH 40
COG3369 COG3369
Uncharacterized conserved protein, contains Zn-finger domain of CDGSH type [Function unknown];
73-124 9.62e-07

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


Pssm-ID: 442596  Cd Length: 68  Bit Score: 43.54  E-value: 9.62e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193205053  73 YKIQLDSNKIVDTVDIEDIGEKKAFCRCWKSEKWPYCDGSHGKHNKETGDNV 124
Cdd:COG3369   14 LLVEGDVEIVDADGNEYEEGKRYALCRCGLSKNKPFCDGSHKGTGFEPEGEA 65
 
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