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Conserved domains on  [gi|564396176|ref|XP_006255820|]
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zinc finger CCCH domain-containing protein 18 isoform X1 [Rattus norvegicus]

Protein Classification

zinc finger CCCH domain-containing protein( domain architecture ID 16058599)

zinc finger CCCH domain-containing protein similar to mammalian Zinc finger CCCH domain-containing protein 18 (ZC3H18) that interacts with ZFC3H1 in a RNase-insensitive manner

CATH:  4.10.1000.10
Gene Ontology:  GO:0046872|GO:0003676
PubMed:  12665246|27990022
SCOP:  3001741

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
zf-CCCH_4 pfam18044
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ...
253-298 1.26e-03

CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and one histidine to coordinate the zinc ion. This domain is found in a wide variety of proteins such as E3 ligases.


:

Pssm-ID: 465626  Cd Length: 22  Bit Score: 37.18  E-value: 1.26e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 564396176   253 PTCRFFMKdvvtplstllppipnsiplrgqvkGNCTWGMNCRFIHP 298
Cdd:pfam18044    1 RLCRYFQK------------------------GGCRYGDNCRFSHD 22
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
26-164 6.51e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 40.66  E-value: 6.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396176   26 LPEQPTDLWVLMDVAESPELEPHSPDEEQPALSDDDilRESGSEQDLDGAGERASDLE---EEENATRVQSQEEIHSDEE 102
Cdd:NF033609  544 VPEQPDEPGEIEPIPEDSDSDPGSDSGSDSSNSDSG--SDSGSDSTSDSGSDSASDSDsasDSDSASDSDSASDSDSASD 621
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564396176  103 DQASEPKSQDQDSEAHELSRGPAGSPCEEGDDAEEDGTSDLRDEASSVTRELDEHELDYDEE 164
Cdd:NF033609  622 SDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 683
 
Name Accession Description Interval E-value
zf-CCCH_4 pfam18044
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ...
253-298 1.26e-03

CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and one histidine to coordinate the zinc ion. This domain is found in a wide variety of proteins such as E3 ligases.


Pssm-ID: 465626  Cd Length: 22  Bit Score: 37.18  E-value: 1.26e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 564396176   253 PTCRFFMKdvvtplstllppipnsiplrgqvkGNCTWGMNCRFIHP 298
Cdd:pfam18044    1 RLCRYFQK------------------------GGCRYGDNCRFSHD 22
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
26-164 6.51e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 40.66  E-value: 6.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396176   26 LPEQPTDLWVLMDVAESPELEPHSPDEEQPALSDDDilRESGSEQDLDGAGERASDLE---EEENATRVQSQEEIHSDEE 102
Cdd:NF033609  544 VPEQPDEPGEIEPIPEDSDSDPGSDSGSDSSNSDSG--SDSGSDSTSDSGSDSASDSDsasDSDSASDSDSASDSDSASD 621
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564396176  103 DQASEPKSQDQDSEAHELSRGPAGSPCEEGDDAEEDGTSDLRDEASSVTRELDEHELDYDEE 164
Cdd:NF033609  622 SDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 683
 
Name Accession Description Interval E-value
zf-CCCH_4 pfam18044
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ...
253-298 1.26e-03

CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and one histidine to coordinate the zinc ion. This domain is found in a wide variety of proteins such as E3 ligases.


Pssm-ID: 465626  Cd Length: 22  Bit Score: 37.18  E-value: 1.26e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 564396176   253 PTCRFFMKdvvtplstllppipnsiplrgqvkGNCTWGMNCRFIHP 298
Cdd:pfam18044    1 RLCRYFQK------------------------GGCRYGDNCRFSHD 22
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
26-164 6.51e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 40.66  E-value: 6.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564396176   26 LPEQPTDLWVLMDVAESPELEPHSPDEEQPALSDDDilRESGSEQDLDGAGERASDLE---EEENATRVQSQEEIHSDEE 102
Cdd:NF033609  544 VPEQPDEPGEIEPIPEDSDSDPGSDSGSDSSNSDSG--SDSGSDSTSDSGSDSASDSDsasDSDSASDSDSASDSDSASD 621
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564396176  103 DQASEPKSQDQDSEAHELSRGPAGSPCEEGDDAEEDGTSDLRDEASSVTRELDEHELDYDEE 164
Cdd:NF033609  622 SDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 683
 
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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