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Conserved domains on  [gi|506356775|ref|WP_015876494|]
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SRPBCC family protein [Burkholderia glumae]

Protein Classification

SRPBCC family protein( domain architecture ID 10172260)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket; similar to Aspergillus terreus acetylaranotin biosynthesis cluster protein L (AtaL) which is a non-ribosomal peptide synthetase and is required for the biosynthesis of the toxin acetylaranotin

Gene Ontology:  GO:0005488
PubMed:  18922149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC_DUF1857 cd08863
DUF1857, an uncharacterized ligand-binding domain of the SRPBCC domain superfamily; ...
 2-149 4.71e-60

DUF1857, an uncharacterized ligand-binding domain of the SRPBCC domain superfamily; Uncharacterized family 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: 176872  Cd Length: 141  Bit Score: 182.53  E-value: 4.71e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506356775   2 NFEHLIQINatDDPTLPTLTRDQLWEGLVLRAEQPQLFVIGLDRCEIRERTETTLERELHFGQARIRDRVTFTTNHQVRY 81
Cdd:cd08863    1 NFEHTVPIN--DPGNIPTLTRAQLWRGLVLRAREPQLFVPGLDRCEVLSESGTVLERELTFGPAKIRETVTLEPPSRVHF 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506356775  82 DIHAAdgeiGGSLTMTIEERADAELFLRFEYHTTLPEtADSEDARQTQGIVKEAYRTSDIDTVRLIRE 149
Cdd:cd08863   79 LQADA----GGTLTNTIEEPEDGALYLRFVYETTLPE-VAEEEAKAYQEIVKQAYKEADIDTVRTIRE 141
 
Name Accession Description Interval E-value
SRPBCC_DUF1857 cd08863
DUF1857, an uncharacterized ligand-binding domain of the SRPBCC domain superfamily; ...
 2-149 4.71e-60

DUF1857, an uncharacterized ligand-binding domain of the SRPBCC domain superfamily; Uncharacterized family 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: 176872  Cd Length: 141  Bit Score: 182.53  E-value: 4.71e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506356775   2 NFEHLIQINatDDPTLPTLTRDQLWEGLVLRAEQPQLFVIGLDRCEIRERTETTLERELHFGQARIRDRVTFTTNHQVRY 81
Cdd:cd08863    1 NFEHTVPIN--DPGNIPTLTRAQLWRGLVLRAREPQLFVPGLDRCEVLSESGTVLERELTFGPAKIRETVTLEPPSRVHF 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506356775  82 DIHAAdgeiGGSLTMTIEERADAELFLRFEYHTTLPEtADSEDARQTQGIVKEAYRTSDIDTVRLIRE 149
Cdd:cd08863   79 LQADA----GGTLTNTIEEPEDGALYLRFVYETTLPE-VAEEEAKAYQEIVKQAYKEADIDTVRTIRE 141
AtaL pfam08982
Acetylaranotin biosynthesis cluster protein L; This entry includes acetylaranotin biosynthesis ...
 7-151 1.49e-47

Acetylaranotin biosynthesis cluster protein L; This entry includes acetylaranotin biosynthesis cluster protein L (AtaL) from Aspergillus terreus, which is a non-ribosomal peptide synthetase. It is required for the biosynthesis of the toxin acetylaranotin, which is a disulfide bridged cyclic dipeptide. There are a number of steps in the biosyntheis of this epipolythiodioxopiperazine toxin from two phenylananines, but the specific function of AtaL has yet to be determined. homologs are also known from bacteria.


Pssm-ID: 430354  Cd Length: 146  Bit Score: 151.20  E-value: 1.49e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506356775    7 IQINATDDP--TLPTLTRDQLWEGLVLRAEQPQLFVIGLDRCEIRERTETTLERELHFGQA---RIRDRVTFTTNHQVRY 81
Cdd:pfam08982   1 IAYTAPINPpgASPVLTRAQLWAGLQRKARSPQEFVPAITSCEVLSEEGDVVTREVTFGAGaggVVREVVTLYPPTRVDF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506356775   82 DIHAadgeiGGSLTMTIEERADAELFLRFEYHTTLPE-TADSEDARQTQGIVKEAYRTSDIDTVRLIREYA 151
Cdd:pfam08982  81 EQPD-----GSSITNTISEGAPGDLYLTFTFEWRHPEvEPGSEEAKKLEEKYKKAAKEAVEDTIEVIRELV 146
 
Name Accession Description Interval E-value
SRPBCC_DUF1857 cd08863
DUF1857, an uncharacterized ligand-binding domain of the SRPBCC domain superfamily; ...
 2-149 4.71e-60

DUF1857, an uncharacterized ligand-binding domain of the SRPBCC domain superfamily; Uncharacterized family 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: 176872  Cd Length: 141  Bit Score: 182.53  E-value: 4.71e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506356775   2 NFEHLIQINatDDPTLPTLTRDQLWEGLVLRAEQPQLFVIGLDRCEIRERTETTLERELHFGQARIRDRVTFTTNHQVRY 81
Cdd:cd08863    1 NFEHTVPIN--DPGNIPTLTRAQLWRGLVLRAREPQLFVPGLDRCEVLSESGTVLERELTFGPAKIRETVTLEPPSRVHF 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506356775  82 DIHAAdgeiGGSLTMTIEERADAELFLRFEYHTTLPEtADSEDARQTQGIVKEAYRTSDIDTVRLIRE 149
Cdd:cd08863   79 LQADA----GGTLTNTIEEPEDGALYLRFVYETTLPE-VAEEEAKAYQEIVKQAYKEADIDTVRTIRE 141
AtaL pfam08982
Acetylaranotin biosynthesis cluster protein L; This entry includes acetylaranotin biosynthesis ...
 7-151 1.49e-47

Acetylaranotin biosynthesis cluster protein L; This entry includes acetylaranotin biosynthesis cluster protein L (AtaL) from Aspergillus terreus, which is a non-ribosomal peptide synthetase. It is required for the biosynthesis of the toxin acetylaranotin, which is a disulfide bridged cyclic dipeptide. There are a number of steps in the biosyntheis of this epipolythiodioxopiperazine toxin from two phenylananines, but the specific function of AtaL has yet to be determined. homologs are also known from bacteria.


Pssm-ID: 430354  Cd Length: 146  Bit Score: 151.20  E-value: 1.49e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506356775    7 IQINATDDP--TLPTLTRDQLWEGLVLRAEQPQLFVIGLDRCEIRERTETTLERELHFGQA---RIRDRVTFTTNHQVRY 81
Cdd:pfam08982   1 IAYTAPINPpgASPVLTRAQLWAGLQRKARSPQEFVPAITSCEVLSEEGDVVTREVTFGAGaggVVREVVTLYPPTRVDF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506356775   82 DIHAadgeiGGSLTMTIEERADAELFLRFEYHTTLPE-TADSEDARQTQGIVKEAYRTSDIDTVRLIREYA 151
Cdd:pfam08982  81 EQPD-----GSSITNTISEGAPGDLYLTFTFEWRHPEvEPGSEEAKKLEEKYKKAAKEAVEDTIEVIRELV 146
 
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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