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Conserved domains on  [gi|1034598860|ref|XP_016879862|]
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G patch domain-containing protein 8 isoform X2 [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10573383)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
58-85 4.06e-05

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


:

Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 41.77  E-value: 4.06e-05
                           10        20
                   ....*....|....*....|....*...
gi 1034598860   58 FYCELCDKQYQKHQEFDNHINSydHAHK 85
Cdd:pfam12171    2 FYCVLCDKYFKSENALQNHLKS--KKHK 27
 
Name Accession Description Interval E-value
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
58-85 4.06e-05

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 41.77  E-value: 4.06e-05
                           10        20
                   ....*....|....*....|....*...
gi 1034598860   58 FYCELCDKQYQKHQEFDNHINSydHAHK 85
Cdd:pfam12171    2 FYCVLCDKYFKSENALQNHLKS--KKHK 27
 
Name Accession Description Interval E-value
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
58-85 4.06e-05

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 41.77  E-value: 4.06e-05
                           10        20
                   ....*....|....*....|....*...
gi 1034598860   58 FYCELCDKQYQKHQEFDNHINSydHAHK 85
Cdd:pfam12171    2 FYCVLCDKYFKSENALQNHLKS--KKHK 27
 
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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