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Conserved domains on  [gi|528319456|gb|EPY54030|]
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hypothetical protein SPOG_02747 [Schizosaccharomyces cryophilus OY26]

Protein Classification

CHY zinc finger protein( domain architecture ID 10008518)

CHY zinc finger protein may bind zinc ions though conserved cysteine and histidine residues; similar to Saccharomyces cerevisiae helper of Tim protein 13, which is required for the assembly or recycling of the small Tim proteins in the mitochondrial intermembrane, thereby participating in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane

Gene Ontology:  GO:0008270
PubMed:  11179890|12665246

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4357 COG4357
Uncharacterized conserved protein, contains Zn-finger domain of CHY type [Function unknown];
1-104 6.09e-43

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


:

Pssm-ID: 443492  Cd Length: 107  Bit Score: 135.82  E-value: 6.09e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528319456   1 MSIPSTIYGLLVDDWSRCQHYHSELDIVALRCFACKRFYACFTCHNILESHRFEPWKETP-NLFPVLCGACKHNLTRDQY 79
Cdd:COG4357    1 MIHGIEVRGVVVDDETRCAHYHSELDVIAIKFACCGKYYPCYRCHEELADHEAEPWPRERfDEKAVLCGVCGTELTINEY 80

                         90       100
                 ....*....|....*....|....*
gi 528319456  80 QQTSNCPNCERPFNPNCRKHKSYYF 104
Cdd:COG4357   81 LEADSCPACGAAFNPGCALHYHLYF 105
 
Name Accession Description Interval E-value
COG4357 COG4357
Uncharacterized conserved protein, contains Zn-finger domain of CHY type [Function unknown];
1-104 6.09e-43

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


Pssm-ID: 443492  Cd Length: 107  Bit Score: 135.82  E-value: 6.09e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528319456   1 MSIPSTIYGLLVDDWSRCQHYHSELDIVALRCFACKRFYACFTCHNILESHRFEPWKETP-NLFPVLCGACKHNLTRDQY 79
Cdd:COG4357    1 MIHGIEVRGVVVDDETRCAHYHSELDVIAIKFACCGKYYPCYRCHEELADHEAEPWPRERfDEKAVLCGVCGTELTINEY 80

                         90       100
                 ....*....|....*....|....*
gi 528319456  80 QQTSNCPNCERPFNPNCRKHKSYYF 104
Cdd:COG4357   81 LEADSCPACGAAFNPGCALHYHLYF 105
zf-CHY pfam05495
CHY zinc finger; This family of domains are likely to bind to zinc ions. They contain many ...
 18-88 3.04e-07

CHY zinc finger; This family of domains are likely to bind to zinc ions. They contain many conserved cysteine and histidine residues. We have named this domain after the N-terminal motif CXHY. This domain can be found in isolation in some proteins, but is also often associated with pfam00097. One of the proteins in this family is a mitochondrial intermembrane space protein called Hot13. This protein is involved in the assembly of small TIM complexes.


Pssm-ID: 461665  Cd Length: 75  Bit Score: 43.88  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528319456   18 CQHYHSEldiVALRCFACKRFYACFTCHN-ILESHRFEPWKE---------TPNLFPVLCGACKHNLtrDQYQqtsnCPN 87
Cdd:pfam05495   1 CKHYHRN---CKLRCPCCGKWYPCRLCHDeVEDEHPLDRYAVtemlcmlcdTEQPVAVLCGNCGVTF--AEYF----CPI 71


                  .
gi 528319456   88 C 88
Cdd:pfam05495  72 C 72
 
Name Accession Description Interval E-value
COG4357 COG4357
Uncharacterized conserved protein, contains Zn-finger domain of CHY type [Function unknown];
1-104 6.09e-43

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


Pssm-ID: 443492  Cd Length: 107  Bit Score: 135.82  E-value: 6.09e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528319456   1 MSIPSTIYGLLVDDWSRCQHYHSELDIVALRCFACKRFYACFTCHNILESHRFEPWKETP-NLFPVLCGACKHNLTRDQY 79
Cdd:COG4357    1 MIHGIEVRGVVVDDETRCAHYHSELDVIAIKFACCGKYYPCYRCHEELADHEAEPWPRERfDEKAVLCGVCGTELTINEY 80

                         90       100
                 ....*....|....*....|....*
gi 528319456  80 QQTSNCPNCERPFNPNCRKHKSYYF 104
Cdd:COG4357   81 LEADSCPACGAAFNPGCALHYHLYF 105
zf-CHY pfam05495
CHY zinc finger; This family of domains are likely to bind to zinc ions. They contain many ...
 18-88 3.04e-07

CHY zinc finger; This family of domains are likely to bind to zinc ions. They contain many conserved cysteine and histidine residues. We have named this domain after the N-terminal motif CXHY. This domain can be found in isolation in some proteins, but is also often associated with pfam00097. One of the proteins in this family is a mitochondrial intermembrane space protein called Hot13. This protein is involved in the assembly of small TIM complexes.


Pssm-ID: 461665  Cd Length: 75  Bit Score: 43.88  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528319456   18 CQHYHSEldiVALRCFACKRFYACFTCHN-ILESHRFEPWKE---------TPNLFPVLCGACKHNLtrDQYQqtsnCPN 87
Cdd:pfam05495   1 CKHYHRN---CKLRCPCCGKWYPCRLCHDeVEDEHPLDRYAVtemlcmlcdTEQPVAVLCGNCGVTF--AEYF----CPI 71


                  .
gi 528319456   88 C 88
Cdd:pfam05495  72 C 72
 
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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