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Conserved domains on  [gi|503919091|ref|WP_014153085|]
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MULTISPECIES: SRPBCC family protein [Streptomyces]

Protein Classification

SRPBCC family protein( domain architecture ID 10167397)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket; similar to Penicillium simplicissimum penitrem biosynthesis cluster 1 protein I

CATH:  3.30.530.20
Gene Ontology:  GO:0005488
PubMed:  18922149
SCOP:  3000738

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 4-140 6.86e-09

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.


:

Pssm-ID: 176854  Cd Length: 141  Bit Score: 51.56  E-value: 6.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091   4 RHRLIRRTPEDVWRVLSDAERYGDWVVGTARAEPDEGRWPDVGAAlRYEIRLGPLTLHNRTVVRRSEPASVLELEADSGR 83
Cdd:cd07812    3 ASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGAR-FVGGRKGGRRLTLTSEVTEVDPPRPGRFRVTGGG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091  84 LG-TARIAMELRPWGGN-TLLIFD-EHPLRGAGGALHNGLLEVAQQVRHRAMLGRLAHVC 140
Cdd:cd07812   82 GGvDGTGEWRLEPEGDGgTRVTYTvEYDPPGPLLKVFALLLAGALKRELAALLRALKARL 141
 
Name Accession Description Interval E-value
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 4-140 6.86e-09

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.


Pssm-ID: 176854  Cd Length: 141  Bit Score: 51.56  E-value: 6.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091   4 RHRLIRRTPEDVWRVLSDAERYGDWVVGTARAEPDEGRWPDVGAAlRYEIRLGPLTLHNRTVVRRSEPASVLELEADSGR 83
Cdd:cd07812    3 ASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGAR-FVGGRKGGRRLTLTSEVTEVDPPRPGRFRVTGGG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091  84 LG-TARIAMELRPWGGN-TLLIFD-EHPLRGAGGALHNGLLEVAQQVRHRAMLGRLAHVC 140
Cdd:cd07812   82 GGvDGTGEWRLEPEGDGgTRVTYTvEYDPPGPLLKVFALLLAGALKRELAALLRALKARL 141
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 3-117 2.06e-06

Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and metabolism];


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 44.64  E-value: 2.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091   3 VRHRLIRRTPEDVWRVLSDAERYGDWVVGTARAEPDEGRWpDVGAALRYEIRLGPLTLH-NRTVVRRSEPASVLEL--EA 79
Cdd:COG3832    9 TIEREIDAPPERVWRAWTDPELLARWFGPKGWATVAEFDL-RVGGRFRFRMRGPDGEEFgFEGEVLEVEPPERLVFtwGF 87

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503919091  80 DSGRLGTARIAMELRPWGGNTLLIFDEHPLRGAGGALH 117
Cdd:COG3832   88 EDDPEGESTVTVTLEPEGGGTRLTLTHTGFSAEDRDAV 125
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 6-141 7.72e-05

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. It also includes other proteins of the START superfamily.


Pssm-ID: 431388  Cd Length: 139  Bit Score: 40.55  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091    6 RLIRRTPEDVWRVLSDAERYGDWVVGTARAEPDEGRWPDVGAALRYEIRLGPLTLHNrTVVRRSEPASVLELEADSGRLG 85
Cdd:pfam10604   3 IEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGGGGPLRGVVGTLRVGGRRGTVRE-ELVEYDPAPRLLAYRIVEPLGV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 503919091   86 TARIA-MELRPWGGNTLLIFDEHP-LRGAGGALHNGLLEVAQQVRHRAMLGRLAHVCE 141
Cdd:pfam10604  82 ANYVGtWTVTPAGGGTRVTWTGEFdGPPLGGPFRDPAAARAVKGDYRAGLDRLKAVLE 139
 
Name Accession Description Interval E-value
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 4-140 6.86e-09

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.


Pssm-ID: 176854  Cd Length: 141  Bit Score: 51.56  E-value: 6.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091   4 RHRLIRRTPEDVWRVLSDAERYGDWVVGTARAEPDEGRWPDVGAAlRYEIRLGPLTLHNRTVVRRSEPASVLELEADSGR 83
Cdd:cd07812    3 ASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGAR-FVGGRKGGRRLTLTSEVTEVDPPRPGRFRVTGGG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091  84 LG-TARIAMELRPWGGN-TLLIFD-EHPLRGAGGALHNGLLEVAQQVRHRAMLGRLAHVC 140
Cdd:cd07812   82 GGvDGTGEWRLEPEGDGgTRVTYTvEYDPPGPLLKVFALLLAGALKRELAALLRALKARL 141
SRPBCC_6 cd07824
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 11-107 1.79e-06

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: 176866  Cd Length: 146  Bit Score: 45.00  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091  11 TPEDVWRVLSDAERYGDWVVGTAR-AEPDEGRWPDVGAALRYEIR-LGPLTLHNRTVVRRSEPASVLELEAdSGRL-GTA 87
Cdd:cd07824   12 PPEAVWDVLVDAESWPDWWPGVERvVELEPGDEAGIGARRRYTWRgLLPYRLRFELRVTRIEPLSLLEVRA-SGDLeGVG 90

                         90       100
                 ....*....|....*....|
gi 503919091  88 RiaMELRPWGGNTLLIFDEH 107
Cdd:cd07824   91 R--WTLAPDGSGTVVRYDWE 108
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 3-117 2.06e-06

Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and metabolism];


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 44.64  E-value: 2.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091   3 VRHRLIRRTPEDVWRVLSDAERYGDWVVGTARAEPDEGRWpDVGAALRYEIRLGPLTLH-NRTVVRRSEPASVLEL--EA 79
Cdd:COG3832    9 TIEREIDAPPERVWRAWTDPELLARWFGPKGWATVAEFDL-RVGGRFRFRMRGPDGEEFgFEGEVLEVEPPERLVFtwGF 87

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503919091  80 DSGRLGTARIAMELRPWGGNTLLIFDEHPLRGAGGALH 117
Cdd:COG3832   88 EDDPEGESTVTVTLEPEGGGTRLTLTHTGFSAEDRDAV 125
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 6-141 7.72e-05

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. It also includes other proteins of the START superfamily.


Pssm-ID: 431388  Cd Length: 139  Bit Score: 40.55  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091    6 RLIRRTPEDVWRVLSDAERYGDWVVGTARAEPDEGRWPDVGAALRYEIRLGPLTLHNrTVVRRSEPASVLELEADSGRLG 85
Cdd:pfam10604   3 IEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGGGGPLRGVVGTLRVGGRRGTVRE-ELVEYDPAPRLLAYRIVEPLGV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 503919091   86 TARIA-MELRPWGGNTLLIFDEHP-LRGAGGALHNGLLEVAQQVRHRAMLGRLAHVCE 141
Cdd:pfam10604  82 ANYVGtWTVTPAGGGTRVTWTGEFdGPPLGGPFRDPAAARAVKGDYRAGLDRLKAVLE 139
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 6-141 4.93e-04

Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human Aha1, and related proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Micromonospora echinospora CalC, human Aha1, and related proteins. Proteins in this group belong to the SRPBCC domain superfamily of proteins, which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM), by a self sacrificing mechanism which results in inactivation of both CalC and the highly reactive diradical enediyne species. MeCalC can also inactivate two other enediynes, shishijimicin and namenamicin. A crucial Gly of the MeCalC CLM resistance mechanism is not conserved in this subgroup. This family also includes the C-terminal, Bet v1-like domain of Aha1, one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity, and may regulate the dwell time of Hsp90 with client proteins. Aha1 can act as either a positive or negative regulator of chaperone-dependent activation, depending on the client protein, but the mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases.


Pssm-ID: 176856 [Multi-domain]  Cd Length: 139  Bit Score: 38.11  E-value: 4.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091   6 RLIRRTPEDVWRVLSDAERYGDWVVGTARAEPDegrWPDVGAALRYEIRLGPLTLHNRTVVRRSEPASVLELE---ADSG 82
Cdd:cd07814    6 REFDAPPELVWRALTDPELLAQWFGPTTTAEMD---LRVGGRWFFFMTGPDGEEGWVSGEVLEVEPPRRLVFTwafSDET 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503919091  83 RLGTARIAMELRPWGGNTLLIFDEHPLRGAGGAlhnglLEVAQQVRH--RAMLGRLAHVCE 141
Cdd:cd07814   83 PGPETTVTVTLEETGGGTRLTLTHSGFPEEDAE-----QEAREGMEEgwTGTLDRLKALLE 138
SRPBCC_CalC_Aha1-like_6 cd08899
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 6-119 5.57e-04

Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins; SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands.


Pssm-ID: 176908 [Multi-domain]  Cd Length: 157  Bit Score: 38.04  E-value: 5.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091   6 RLIRRTPEDVWRVLSDAERYGDWvvgTARAEPDegrwPDVGAalRYEIRLGPLTLHNRTV-VRRSEPASVLELEADSGRl 84
Cdd:cd08899   17 RLLPAPIEDVWAALTDPERLARW---FAPGTGD----LRVGG--RVEFVMDDEEGPNATGtILACEPPRLLAFTWGEGG- 86

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 503919091  85 GTARIAMELRPWGGNTLLIFDEHPLRGAGGALHNG 119
Cdd:cd08899   87 GESEVRFELAPEGDGTRLTLTHRLLDERFGAGAVG 121
SRPBCC_CalC_Aha1-like_GntR-HTH cd08893
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 8-102 4.04e-03

Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins; some contain an N-terminal GntR family winged HTH DNA-binding domain; SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. Some proteins in this subgroup contain an N-terminal winged helix-turn-helix DNA-binding domain found in the GntR family of proteins which include bacterial transcriptional regulators and their putative homologs from eukaryota and archaea.


Pssm-ID: 176902 [Multi-domain]  Cd Length: 136  Bit Score: 35.68  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503919091   8 IRRTPEDVWRVLSDAERYGDWVVGTaRAEPDegrwPDVGAALRYeIRLGPLTLHNRTVVRRSEPASVL------ELEADS 81
Cdd:cd08893    8 IRATPEKVWQALTDPEFTRQYWGGT-TVESD----WKVGSAFEY-RRGDDGTVDVEGEVLESDPPRRLvhtwraVWDPEM 81

                         90       100
                 ....*....|....*....|.
gi 503919091  82 GRLGTARIAMELRPWGGNTLL 102
Cdd:cd08893   82 AAEPPSRVTFEIEPVGDVVKL 102
 
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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