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Conserved domains on  [gi|30425138|ref|NP_780633|]
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proline-rich protein 9 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cornifin super family cl25524
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
4-108 3.76e-03

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


The actual alignment was detected with superfamily member pfam02389:

Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 34.64  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425138     4 NDQQCKQPCVPPP---CLQKTQEKCQAQAEDVCVSSCQDPCQDKCPQQAQEVCVSQCQELSQGNCPQQGQDPCLPPSQDQ 80
Cdd:pfam02389   1 HQQQVKQPCQPPPqepCVPTTKEPCHSKVPEPCNPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEP 80
                          90       100
                  ....*....|....*....|....*...
gi 30425138    81 CLPQCAEPCQELAQTKCVEEFPQKVQEK 108
Cdd:pfam02389  81 CSPKVPEPCHPKAPEPCHPKVPEPCYPK 108
 
Name Accession Description Interval E-value
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
4-108 3.76e-03

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 34.64  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425138     4 NDQQCKQPCVPPP---CLQKTQEKCQAQAEDVCVSSCQDPCQDKCPQQAQEVCVSQCQELSQGNCPQQGQDPCLPPSQDQ 80
Cdd:pfam02389   1 HQQQVKQPCQPPPqepCVPTTKEPCHSKVPEPCNPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEP 80
                          90       100
                  ....*....|....*....|....*...
gi 30425138    81 CLPQCAEPCQELAQTKCVEEFPQKVQEK 108
Cdd:pfam02389  81 CSPKVPEPCHPKAPEPCHPKVPEPCYPK 108
 
Name Accession Description Interval E-value
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
4-108 3.76e-03

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 34.64  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425138     4 NDQQCKQPCVPPP---CLQKTQEKCQAQAEDVCVSSCQDPCQDKCPQQAQEVCVSQCQELSQGNCPQQGQDPCLPPSQDQ 80
Cdd:pfam02389   1 HQQQVKQPCQPPPqepCVPTTKEPCHSKVPEPCNPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEP 80
                          90       100
                  ....*....|....*....|....*...
gi 30425138    81 CLPQCAEPCQELAQTKCVEEFPQKVQEK 108
Cdd:pfam02389  81 CSPKVPEPCHPKAPEPCHPKVPEPCYPK 108
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
11-97 9.61e-03

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 33.49  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425138    11 PCVPPPCLQKTQEKCQAQAEDVCVSSCQDPCQDKCPQQAQEVCVSQCQELSQGNCPQQGQDPCLPPSQDQCLPQCAEPCQ 90
Cdd:pfam02389  35 PKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEPCSPKVPEPCHPKAPEPCHPKVPEPCYPKAPEPCQ 114

                  ....*..
gi 30425138    91 ELAQTKC 97
Cdd:pfam02389 115 PKVPEPC 121
 
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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