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Conserved domains on  [gi|446556284|ref|WP_000633630|]
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MULTISPECIES: LIC13081 family protein [Leptospira]

Protein Classification

SRPBCC family protein( domain architecture ID 51693)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 5-137 2.76e-12

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


The actual alignment was detected with superfamily member cd08865:

Pssm-ID: 472699  Cd Length: 140  Bit Score: 60.38  E-value: 2.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556284   5 TVTFLVSYSLDDTFRFVADFRNLIYWGDKISNVspilsKNGNSFPI-----YELLYSFGPFKLKANYSAKEWIPNSRMIM 79
Cdd:cd08865    2 EESIVIERPVEEVFAYLADFENAPEWDPGVVEV-----EKITDGPVgvgtrYHQVRKFLGRRIELTYEITEYEPGRRVVF 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446556284  80 EIQSSLIDQRDIYTFQITDRGTKITFTNHSKLKLPYHFIEKIFASGIRGRIYKEMRQL 137
Cdd:cd08865   77 RGSSGPFPYEDTYTFEPVGGGTRVRYTAELEPGGFARLLDPLMAPAFRRRARAALENL 134
 
Name Accession Description Interval E-value
SRPBCC_10 cd08865
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 5-137 2.76e-12

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176874  Cd Length: 140  Bit Score: 60.38  E-value: 2.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556284   5 TVTFLVSYSLDDTFRFVADFRNLIYWGDKISNVspilsKNGNSFPI-----YELLYSFGPFKLKANYSAKEWIPNSRMIM 79
Cdd:cd08865    2 EESIVIERPVEEVFAYLADFENAPEWDPGVVEV-----EKITDGPVgvgtrYHQVRKFLGRRIELTYEITEYEPGRRVVF 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446556284  80 EIQSSLIDQRDIYTFQITDRGTKITFTNHSKLKLPYHFIEKIFASGIRGRIYKEMRQL 137
Cdd:cd08865   77 RGSSGPFPYEDTYTFEPVGGGTRVRYTAELEPGGFARLLDPLMAPAFRRRARAALENL 134
 
Name Accession Description Interval E-value
SRPBCC_10 cd08865
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 5-137 2.76e-12

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176874  Cd Length: 140  Bit Score: 60.38  E-value: 2.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556284   5 TVTFLVSYSLDDTFRFVADFRNLIYWGDKISNVspilsKNGNSFPI-----YELLYSFGPFKLKANYSAKEWIPNSRMIM 79
Cdd:cd08865    2 EESIVIERPVEEVFAYLADFENAPEWDPGVVEV-----EKITDGPVgvgtrYHQVRKFLGRRIELTYEITEYEPGRRVVF 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446556284  80 EIQSSLIDQRDIYTFQITDRGTKITFTNHSKLKLPYHFIEKIFASGIRGRIYKEMRQL 137
Cdd:cd08865   77 RGSSGPFPYEDTYTFEPVGGGTRVRYTAELEPGGFARLLDPLMAPAFRRRARAALENL 134
 
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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