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Conserved domains on  [gi|38636478|emb|CAC83812|]
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secreted phosphoprotein 24 precursor [Mus musculus]

Protein Classification

Spp-24 domain-containing protein( domain architecture ID 10538481)

Spp-24 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Spp-24 pfam07448
Secreted phosphoprotein 24 (Spp-24) cystatin-like domain; This family represents a conserved ...
 63-125 1.15e-37

Secreted phosphoprotein 24 (Spp-24) cystatin-like domain; This family represents a conserved region approximately 60 residues long within secreted phosphoprotein 24 (Spp-24), which seems to be restricted to vertebrates. This is a non-collagenous protein found in bone that is related in sequence to the cystatin family of thiol protease inhibitors. This suggests that Spp-24 could function to modulate the thiol protease activities known to be involved in bone turnover. It is also possible that the intact form of Spp-24 found in bone could be a precursor to a biologically active peptide that coordinates an aspect of bone turnover.


:

Pssm-ID: 429466  Cd Length: 64  Bit Score: 124.92  E-value: 1.15e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38636478    63 VLDEDTLVMNLEFSVQETTCLRDSG-DPSTCAFQRGYSVPTAACRSTVQMSKGQVKDVWAHCRW 125
Cdd:pfam07448   1 VLDEDSLSMDLEFSIRETTCRRDSGeDPSTCDFQRGYYVPAAVCRSTVQMSAEQVQDVWVRCRW 64
 
Name Accession Description Interval E-value
Spp-24 pfam07448
Secreted phosphoprotein 24 (Spp-24) cystatin-like domain; This family represents a conserved ...
 63-125 1.15e-37

Secreted phosphoprotein 24 (Spp-24) cystatin-like domain; This family represents a conserved region approximately 60 residues long within secreted phosphoprotein 24 (Spp-24), which seems to be restricted to vertebrates. This is a non-collagenous protein found in bone that is related in sequence to the cystatin family of thiol protease inhibitors. This suggests that Spp-24 could function to modulate the thiol protease activities known to be involved in bone turnover. It is also possible that the intact form of Spp-24 found in bone could be a precursor to a biologically active peptide that coordinates an aspect of bone turnover.


Pssm-ID: 429466  Cd Length: 64  Bit Score: 124.92  E-value: 1.15e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38636478    63 VLDEDTLVMNLEFSVQETTCLRDSG-DPSTCAFQRGYSVPTAACRSTVQMSKGQVKDVWAHCRW 125
Cdd:pfam07448   1 VLDEDSLSMDLEFSIRETTCRRDSGeDPSTCDFQRGYYVPAAVCRSTVQMSAEQVQDVWVRCRW 64
CY smart00043
Cystatin-like domain; Cystatins are a family of cysteine protease inhibitors that occur mainly ...
 30-109 6.64e-03

Cystatin-like domain; Cystatins are a family of cysteine protease inhibitors that occur mainly as single domain proteins. However some extracellular proteins such as kininogen, His-rich glycoprotein and fetuin also contain these domains.


Pssm-ID: 214484  Cd Length: 107  Bit Score: 35.10  E-value: 6.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38636478     30 LQEALSASVAKVNSQSLSPYLFRAtrssLKRVNVLDEDTLVMN--LEFSVQETTCLRDSGDPSTCAFQRGysvPTAACRS 107
Cdd:smart00043  16 VQEAADFAVAEYNKKSNDKYELRV----IKVVSAKSQVVAGTNyyLKVEVGETNCKKLSVDLENCPFLDQ---GEKFCTA 88


                   ..
gi 38636478    108 TV 109
Cdd:smart00043  89 KV 90
 
Name Accession Description Interval E-value
Spp-24 pfam07448
Secreted phosphoprotein 24 (Spp-24) cystatin-like domain; This family represents a conserved ...
 63-125 1.15e-37

Secreted phosphoprotein 24 (Spp-24) cystatin-like domain; This family represents a conserved region approximately 60 residues long within secreted phosphoprotein 24 (Spp-24), which seems to be restricted to vertebrates. This is a non-collagenous protein found in bone that is related in sequence to the cystatin family of thiol protease inhibitors. This suggests that Spp-24 could function to modulate the thiol protease activities known to be involved in bone turnover. It is also possible that the intact form of Spp-24 found in bone could be a precursor to a biologically active peptide that coordinates an aspect of bone turnover.


Pssm-ID: 429466  Cd Length: 64  Bit Score: 124.92  E-value: 1.15e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38636478    63 VLDEDTLVMNLEFSVQETTCLRDSG-DPSTCAFQRGYSVPTAACRSTVQMSKGQVKDVWAHCRW 125
Cdd:pfam07448   1 VLDEDSLSMDLEFSIRETTCRRDSGeDPSTCDFQRGYYVPAAVCRSTVQMSAEQVQDVWVRCRW 64
CY smart00043
Cystatin-like domain; Cystatins are a family of cysteine protease inhibitors that occur mainly ...
 30-109 6.64e-03

Cystatin-like domain; Cystatins are a family of cysteine protease inhibitors that occur mainly as single domain proteins. However some extracellular proteins such as kininogen, His-rich glycoprotein and fetuin also contain these domains.


Pssm-ID: 214484  Cd Length: 107  Bit Score: 35.10  E-value: 6.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38636478     30 LQEALSASVAKVNSQSLSPYLFRAtrssLKRVNVLDEDTLVMN--LEFSVQETTCLRDSGDPSTCAFQRGysvPTAACRS 107
Cdd:smart00043  16 VQEAADFAVAEYNKKSNDKYELRV----IKVVSAKSQVVAGTNyyLKVEVGETNCKKLSVDLENCPFLDQ---GEKFCTA 88


                   ..
gi 38636478    108 TV 109
Cdd:smart00043  89 KV 90
 
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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