NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|166796499|gb|AAI59420|]
View 

CDGSH iron sulfur domain 1 [Rattus norvegicus]

Protein Classification

CDGSH iron-sulfur domain-containing protein( domain architecture ID 10301506)

CDGSH iron-sulfur domain (CISD)-containing protein similar to Homo sapiens CISD1, also called mitoNEET, which contains only a single CDGSH motif and is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity

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;
55-93 1.77e-15

CDGSH-type zinc finger. Function unknown;


:

Pssm-ID: 197836  Cd Length: 38  Bit Score: 64.29  E-value: 1.77e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 166796499    55 KVVHAFDMEDlGDKAVYCRCWRSKKFPFCDGAHIKHNEE 93
Cdd:smart00704   1 KRPDEVEVEK-RKKYALCRCGRSKNFPYCDGSHKKHNEQ 38
MitoNEET_N super family cl11265
Iron-containing outer mitochondrial membrane protein N-terminus; MitoNEET_N is the N-terminal ...
12-41 1.43e-11

Iron-containing outer mitochondrial membrane protein N-terminus; MitoNEET_N is the N-terminal region of the MitoNEET and Miner-type proteins that carry a zf-CDGSH, pfam09360, redox-active 2Fe-2S cluster. The whole protein regulates oxidative capacity. The domain is an anchor sequence that tethers the protein to the outer membrane.


The actual alignment was detected with superfamily member pfam10660:

Pssm-ID: 313801  Cd Length: 64  Bit Score: 55.00  E-value: 1.43e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 166796499   12 EWIAAVTFAAGTAALGYLAYKKFYAKESRT 41
Cdd:pfam10660  35 DWLALVPFAAVTAALGYLAYKAFMPKKRRR 64
 
Name Accession Description Interval E-value
ZnF_CDGSH smart00704
CDGSH-type zinc finger. Function unknown;
55-93 1.77e-15

CDGSH-type zinc finger. Function unknown;


Pssm-ID: 197836  Cd Length: 38  Bit Score: 64.29  E-value: 1.77e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 166796499    55 KVVHAFDMEDlGDKAVYCRCWRSKKFPFCDGAHIKHNEE 93
Cdd:smart00704   1 KRPDEVEVEK-RKKYALCRCGRSKNFPYCDGSHKKHNEQ 38
MitoNEET_N pfam10660
Iron-containing outer mitochondrial membrane protein N-terminus; MitoNEET_N is the N-terminal ...
12-41 1.43e-11

Iron-containing outer mitochondrial membrane protein N-terminus; MitoNEET_N is the N-terminal region of the MitoNEET and Miner-type proteins that carry a zf-CDGSH, pfam09360, redox-active 2Fe-2S cluster. The whole protein regulates oxidative capacity. The domain is an anchor sequence that tethers the protein to the outer membrane.


Pssm-ID: 313801  Cd Length: 64  Bit Score: 55.00  E-value: 1.43e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 166796499   12 EWIAAVTFAAGTAALGYLAYKKFYAKESRT 41
Cdd:pfam10660  35 DWLALVPFAAVTAALGYLAYKAFMPKKRRR 64
zf-CDGSH pfam09360
Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than ...
54-87 3.47e-09

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: 48.45  E-value: 3.47e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 166796499   54 PKVVHAFDMEDL-----GDKAVYCRCWRSKKFPFCDGAH 87
Cdd:pfam09360   2 PLLVEDADGETVesregRFVVALCRCGRSKNKPFCDGSH 40
COG3369 COG3369
Uncharacterized conserved protein, contains Zn-finger domain of CDGSH type [Function unknown];
45-98 1.26e-07

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


Pssm-ID: 442596  Cd Length: 68  Bit Score: 45.08  E-value: 1.26e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166796499  45 VNLQIQKDNPKVVHA------FDMEDLGDKAVY--CRCWRSKKFPFCDGAHIKHNEETGDNV 98
Cdd:COG3369    4 VKITVAKNGPLLVEGdveivdADGNEYEEGKRYalCRCGLSKNKPFCDGSHKGTGFEPEGEA 65
 
Name Accession Description Interval E-value
ZnF_CDGSH smart00704
CDGSH-type zinc finger. Function unknown;
55-93 1.77e-15

CDGSH-type zinc finger. Function unknown;


Pssm-ID: 197836  Cd Length: 38  Bit Score: 64.29  E-value: 1.77e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 166796499    55 KVVHAFDMEDlGDKAVYCRCWRSKKFPFCDGAHIKHNEE 93
Cdd:smart00704   1 KRPDEVEVEK-RKKYALCRCGRSKNFPYCDGSHKKHNEQ 38
MitoNEET_N pfam10660
Iron-containing outer mitochondrial membrane protein N-terminus; MitoNEET_N is the N-terminal ...
12-41 1.43e-11

Iron-containing outer mitochondrial membrane protein N-terminus; MitoNEET_N is the N-terminal region of the MitoNEET and Miner-type proteins that carry a zf-CDGSH, pfam09360, redox-active 2Fe-2S cluster. The whole protein regulates oxidative capacity. The domain is an anchor sequence that tethers the protein to the outer membrane.


Pssm-ID: 313801  Cd Length: 64  Bit Score: 55.00  E-value: 1.43e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 166796499   12 EWIAAVTFAAGTAALGYLAYKKFYAKESRT 41
Cdd:pfam10660  35 DWLALVPFAAVTAALGYLAYKAFMPKKRRR 64
zf-CDGSH pfam09360
Iron-binding zinc finger CDGSH type; The CDGSH-type zinc finger domain binds iron rather than ...
54-87 3.47e-09

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: 48.45  E-value: 3.47e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 166796499   54 PKVVHAFDMEDL-----GDKAVYCRCWRSKKFPFCDGAH 87
Cdd:pfam09360   2 PLLVEDADGETVesregRFVVALCRCGRSKNKPFCDGSH 40
COG3369 COG3369
Uncharacterized conserved protein, contains Zn-finger domain of CDGSH type [Function unknown];
45-98 1.26e-07

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


Pssm-ID: 442596  Cd Length: 68  Bit Score: 45.08  E-value: 1.26e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166796499  45 VNLQIQKDNPKVVHA------FDMEDLGDKAVY--CRCWRSKKFPFCDGAHIKHNEETGDNV 98
Cdd:COG3369    4 VKITVAKNGPLLVEGdveivdADGNEYEEGKRYalCRCGLSKNKPFCDGSHKGTGFEPEGEA 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