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Conserved domains on  [gi|624384295|gb|KBT43180|]
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hypothetical protein Z548_02284 [Mycobacterium tuberculosis 2233BH]

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 cl44048
Ligand-binding SRPBCC domain [General function prediction only];
10-159 7.48e-16

Ligand-binding SRPBCC domain [General function prediction only];


The actual alignment was detected with superfamily member COG4276:

Pssm-ID: 443417  Cd Length: 153  Bit Score: 69.89  E-value: 7.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384295  10 IERQSVVAAPAEQVWQRVVTPEGINDELRPWMTMSVPRGA-----KGMTVDtvpigapigraW-LRLFGVlpfdydRLS- 82
Cdd:COG4276    4 FERETRIPAPLEEVFDFHSRPDNLERLTPPWMGERILSGVpggleLGDRVT-----------YrLRHFGI------PQRw 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384295  83 ---IAELEPGRRFREDSTMLSMRQWQHERTVTPEGDtKTIVRDRITFQTRAGL---RFAAPLIAAGLRALFGHRHRRLQR 156
Cdd:COG4276   67 tseITEVEPPHYFVDEQVKGPFKSWRHEHRFEEVGG-GTLMTDRVEYELPLGLlgrLAHGLFVKKYLERIFAYRHRVLKE 145


                 ...
gi 624384295 157 HFA 159
Cdd:COG4276  146 LLE 148
 
Name Accession Description Interval E-value
SRPBCC COG4276
Ligand-binding SRPBCC domain [General function prediction only];
10-159 7.48e-16

Ligand-binding SRPBCC domain [General function prediction only];


Pssm-ID: 443417  Cd Length: 153  Bit Score: 69.89  E-value: 7.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384295  10 IERQSVVAAPAEQVWQRVVTPEGINDELRPWMTMSVPRGA-----KGMTVDtvpigapigraW-LRLFGVlpfdydRLS- 82
Cdd:COG4276    4 FERETRIPAPLEEVFDFHSRPDNLERLTPPWMGERILSGVpggleLGDRVT-----------YrLRHFGI------PQRw 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384295  83 ---IAELEPGRRFREDSTMLSMRQWQHERTVTPEGDtKTIVRDRITFQTRAGL---RFAAPLIAAGLRALFGHRHRRLQR 156
Cdd:COG4276   67 tseITEVEPPHYFVDEQVKGPFKSWRHEHRFEEVGG-GTLMTDRVEYELPLGLlgrLAHGLFVKKYLERIFAYRHRVLKE 145


                 ...
gi 624384295 157 HFA 159
Cdd:COG4276  146 LLE 148
SRPBCC_3 cd07820
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 10-151 3.03e-07

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: 176862  Cd Length: 137  Bit Score: 46.83  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384295  10 IERQSVVAAPAEQVWQ--------RVVTPegindelrPWMTMSV-----PRGAKGMTVDTVPIGAPIGRAWLRLfgvlpf 76
Cdd:cd07820    1 LERSTVIPAPIEEVFDfhsrpdnlERLTP--------PWLEFAVlgrtpGLIYGGARVTYRLRHFGIPQRWTTE------ 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384295  77 dydrlsIAELEPGRRFREdsTMLS--MRQWQHERTVTPEGDtKTIVRDRITFQTRAGL--RFAAPLIAAG-LRALFGHRH 151
Cdd:cd07820   67 ------ITEVEPPRRFVD--EQVSgpFRSWRHTHRFEAIGG-GTLMTDRVEYRLPLGPlgRLAAPLVVRRyLERFFAYRH 137
 
Name Accession Description Interval E-value
SRPBCC COG4276
Ligand-binding SRPBCC domain [General function prediction only];
10-159 7.48e-16

Ligand-binding SRPBCC domain [General function prediction only];


Pssm-ID: 443417  Cd Length: 153  Bit Score: 69.89  E-value: 7.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384295  10 IERQSVVAAPAEQVWQRVVTPEGINDELRPWMTMSVPRGA-----KGMTVDtvpigapigraW-LRLFGVlpfdydRLS- 82
Cdd:COG4276    4 FERETRIPAPLEEVFDFHSRPDNLERLTPPWMGERILSGVpggleLGDRVT-----------YrLRHFGI------PQRw 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384295  83 ---IAELEPGRRFREDSTMLSMRQWQHERTVTPEGDtKTIVRDRITFQTRAGL---RFAAPLIAAGLRALFGHRHRRLQR 156
Cdd:COG4276   67 tseITEVEPPHYFVDEQVKGPFKSWRHEHRFEEVGG-GTLMTDRVEYELPLGLlgrLAHGLFVKKYLERIFAYRHRVLKE 145


                 ...
gi 624384295 157 HFA 159
Cdd:COG4276  146 LLE 148
SRPBCC_3 cd07820
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 10-151 3.03e-07

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: 176862  Cd Length: 137  Bit Score: 46.83  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384295  10 IERQSVVAAPAEQVWQ--------RVVTPegindelrPWMTMSV-----PRGAKGMTVDTVPIGAPIGRAWLRLfgvlpf 76
Cdd:cd07820    1 LERSTVIPAPIEEVFDfhsrpdnlERLTP--------PWLEFAVlgrtpGLIYGGARVTYRLRHFGIPQRWTTE------ 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384295  77 dydrlsIAELEPGRRFREdsTMLS--MRQWQHERTVTPEGDtKTIVRDRITFQTRAGL--RFAAPLIAAG-LRALFGHRH 151
Cdd:cd07820   67 ------ITEVEPPRRFVD--EQVSgpFRSWRHTHRFEAIGG-GTLMTDRVEYRLPLGPlgRLAAPLVVRRyLERFFAYRH 137
SRPBCC_4 cd07822
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 10-154 4.25e-04

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: 176864  Cd Length: 141  Bit Score: 38.46  E-value: 4.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384295  10 IERQSVVAAPAEQVWQRVVTPEGINdELRPWMTmsvprgakGMTVDTVPIGAPIgRAWLRLFGVLPFDYDrLSIAELEPG 89
Cdd:cd07822    2 ISTEIEINAPPEKVWEVLTDFPSYP-EWNPFVR--------SATGLSLALGARL-RFVVKLPGGPPRSFK-PRVTEVEPP 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 624384295  90 RRFREDSTMLSMRQWQHER--TVTPEGDTKTIVRDRITFQtraGLrfAAPLIAAGLRALFGHRHRRL 154
Cdd:cd07822   71 RRLAWRGGLPFPGLLDGEHsfELEPLGDGGTRFVHRETFS---GL--LAPLVLLGLGRDLRAGFEAM 132
 
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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