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Conserved domains on  [gi|338797801|ref|NP_001229750|]
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differentially expressed in FDCP 8 homolog isoform 2 [Homo sapiens]

Protein Classification

C1 domain-containing protein( domain architecture ID 3571)

C1 (protein kinase C conserved region 1) domain-containing protein similar to Homo sapiens differentially expressed in FDCP 8 homolog isoform 2

Gene Ontology:  GO:0035556
PubMed:  15817391

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
C1 super family cl00040
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
134-172 1.65e-15

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


The actual alignment was detected with superfamily member cd20819:

Pssm-ID: 412127  Cd Length: 62  Bit Score: 67.69  E-value: 1.65e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 338797801 134 RVLLEHRFYKEKSKS-VKQTCDKCNTIIWGLIQTWYTCTG 172
Cdd:cd20819    1 KVVLGHHFVLQKSKSsSKQYCDKCCGIIWGLLQTWYRCTD 40
 
Name Accession Description Interval E-value
C1_DEF8 cd20819
protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 ...
134-172 1.65e-15

protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 (DEF-8) and similar proteins; DEF-8 positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. It is involved in bone resorption. DEF-8 contains a protein kinase C conserved region 1 (C1) domain followed by a putative zinc-RING and/or ribbon. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410369  Cd Length: 62  Bit Score: 67.69  E-value: 1.65e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 338797801 134 RVLLEHRFYKEKSKS-VKQTCDKCNTIIWGLIQTWYTCTG 172
Cdd:cd20819    1 KVVLGHHFVLQKSKSsSKQYCDKCCGIIWGLLQTWYRCTD 40
 
Name Accession Description Interval E-value
C1_DEF8 cd20819
protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 ...
134-172 1.65e-15

protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 (DEF-8) and similar proteins; DEF-8 positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. It is involved in bone resorption. DEF-8 contains a protein kinase C conserved region 1 (C1) domain followed by a putative zinc-RING and/or ribbon. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410369  Cd Length: 62  Bit Score: 67.69  E-value: 1.65e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 338797801 134 RVLLEHRFYKEKSKS-VKQTCDKCNTIIWGLIQTWYTCTG 172
Cdd:cd20819    1 KVVLGHHFVLQKSKSsSKQYCDKCCGIIWGLLQTWYRCTD 40
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
139-171 4.15e-03

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 34.03  E-value: 4.15e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 338797801 139 HRFYKEKSKSVKqTCDKCNTIIWGLIQTWYTCT 171
Cdd:cd00029    1 HRFVPTTFSSPT-FCDVCGKLIWGLFKQGLKCS 32
 
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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