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Conserved domains on  [gi|489829235|ref|WP_003732990|]
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MULTISPECIES: SRPBCC family protein [Listeria]

Protein Classification

SRPBCC family protein( domain architecture ID 10172346)

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

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_CalC_Aha1-like_6 cd08899
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 2-154 4.72e-37

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: 124.71  E-value: 4.72e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829235   2 NEAIERRDDDMTiVSFEVEISAPIQEVFALLTTNTGLAKWFNeLEVGELGADGYLLFVMTPEE--KITMPIRAFEPNQKL 79
Cdd:cd08899    1 LGTVTRLDGGAT-LRFERLLPAPIEDVWAALTDPERLARWFA-PGTGDLRVGGRVEFVMDDEEgpNATGTILACEPPRLL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489829235  80 AFEWDQ----DEVAFELNKiTANKTRLTFTEQLTTITEHSPRDISGWHICLKKLQASAEGKIYDFNKTEFKTLFAKYQK 154
Cdd:cd08899   79 AFTWGEgggeSEVRFELAP-EGDGTRLTLTHRLLDERFGAGAVGAGWHLCLDVLEAALEGGPPAPFWDAFAQLEEEYRA 156
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like_6 cd08899
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 2-154 4.72e-37

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: 124.71  E-value: 4.72e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829235   2 NEAIERRDDDMTiVSFEVEISAPIQEVFALLTTNTGLAKWFNeLEVGELGADGYLLFVMTPEE--KITMPIRAFEPNQKL 79
Cdd:cd08899    1 LGTVTRLDGGAT-LRFERLLPAPIEDVWAALTDPERLARWFA-PGTGDLRVGGRVEFVMDDEEgpNATGTILACEPPRLL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489829235  80 AFEWDQ----DEVAFELNKiTANKTRLTFTEQLTTITEHSPRDISGWHICLKKLQASAEGKIYDFNKTEFKTLFAKYQK 154
Cdd:cd08899   79 AFTWGEgggeSEVRFELAP-EGDGTRLTLTHRLLDERFGAGAVGAGWHLCLDVLEAALEGGPPAPFWDAFAQLEEEYRA 156
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 8-130 3.01e-13

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 63.13  E-value: 3.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829235   8 RDDDMTIVSFEVEISAPIQEVFALLTTNTGLAKWF----------NELEVGelgadGYLLFVMTPEEKITMP----IRAF 73
Cdd:COG3832    1 ADAEDRTITIEREIDAPPERVWRAWTDPELLARWFgpkgwatvaeFDLRVG-----GRFRFRMRGPDGEEFGfegeVLEV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489829235  74 EPNQKLAFEWDQDE-------VAFELNKiTANKTRLTFTEQLTTITEHSPRDIS----GWHICLKKLQ 130
Cdd:COG3832   76 EPPERLVFTWGFEDdpegestVTVTLEP-EGGGTRLTLTHTGFSAEDRDAVLAEgmeeGWTESLDRLK 142
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 23-134 7.41e-06

Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic and archaeal proteins that bear similarity to a C-terminal region of human activator of 90 kDa heat shock protein ATPase homolog 1 (AHSA1/p38). This protein is known to interact with the middle domain of Hsp90, and stimulate its ATPase activity. It is probably a general upregulator of Hsp90 function, particularly contributing to its efficiency in conditions of increased stress. p38 is also known to interact with the cytoplasmic domain of the VSV G protein, and may thus be involved in protein transport. It has also been reported as being underexpressed in Down's syndrome. This region is found repeated in two members of this family (Swiss:Q8XY04 and Swiss:Q6MH87). The structure of YndB from Bacillus subtilis showed the helix-grip fold consisting of a beta-sheet with two small and one long alpha-helix which form a hydrophobic cavity that preferentially binds lipid-like molecules. This structure confirms its similarity with the eukaryote protein Aha1 and its classification as a member of the AHSA1 family).


Pssm-ID: 429921 [Multi-domain]  Cd Length: 125  Bit Score: 43.07  E-value: 7.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829235   23 APIQEVFALLTTNTGLAKWF------NELEVGelgadGYLLFVMTPEEK---ITMPIRAFEPNQKLAFEW---DQDEVAF 90
Cdd:pfam08327   2 APPERVFRALTDPELLARWFtrtvaeMDLRPG-----GKFRFMRGPDGEefgGNGTYLELVPPKRIVYTWrldDWPEGGY 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 489829235   91 ELNKIT----ANKTRLTFTEQLTTITEHSPRDIS-GWHICLKKLQASAE 134
Cdd:pfam08327  77 STVTVEleevGGGTRLTLTHTGEPAGEKEEMGMEeGWEQSLDQLKALLE 125
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like_6 cd08899
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 2-154 4.72e-37

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: 124.71  E-value: 4.72e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829235   2 NEAIERRDDDMTiVSFEVEISAPIQEVFALLTTNTGLAKWFNeLEVGELGADGYLLFVMTPEE--KITMPIRAFEPNQKL 79
Cdd:cd08899    1 LGTVTRLDGGAT-LRFERLLPAPIEDVWAALTDPERLARWFA-PGTGDLRVGGRVEFVMDDEEgpNATGTILACEPPRLL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489829235  80 AFEWDQ----DEVAFELNKiTANKTRLTFTEQLTTITEHSPRDISGWHICLKKLQASAEGKIYDFNKTEFKTLFAKYQK 154
Cdd:cd08899   79 AFTWGEgggeSEVRFELAP-EGDGTRLTLTHRLLDERFGAGAVGAGWHLCLDVLEAALEGGPPAPFWDAFAQLEEEYRA 156
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 8-130 3.01e-13

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 63.13  E-value: 3.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829235   8 RDDDMTIVSFEVEISAPIQEVFALLTTNTGLAKWF----------NELEVGelgadGYLLFVMTPEEKITMP----IRAF 73
Cdd:COG3832    1 ADAEDRTITIEREIDAPPERVWRAWTDPELLARWFgpkgwatvaeFDLRVG-----GRFRFRMRGPDGEEFGfegeVLEV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489829235  74 EPNQKLAFEWDQDE-------VAFELNKiTANKTRLTFTEQLTTITEHSPRDIS----GWHICLKKLQ 130
Cdd:COG3832   76 EPPERLVFTWGFEDdpegestVTVTLEP-EGGGTRLTLTHTGFSAEDRDAVLAEgmeeGWTESLDRLK 142
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 15-135 9.29e-11

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: 56.22  E-value: 9.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829235  15 VSFEVEISAPIQEVFALLTTNTGLAKWFNELEV--GELGADGYLLFVMTPEEKITMP----IRAFEPNQKLAFEWD---- 84
Cdd:cd07814    2 ITIEREFDAPPELVWRALTDPELLAQWFGPTTTaeMDLRVGGRWFFFMTGPDGEEGWvsgeVLEVEPPRRLVFTWAfsde 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489829235  85 ----QDEVAFELNKiTANKTRLTFTEqlTTITEHSPRDIS------GWHICLKKLQASAEG 135
Cdd:cd07814   82 tpgpETTVTVTLEE-TGGGTRLTLTH--SGFPEEDAEQEAregmeeGWTGTLDRLKALLEK 139
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 15-105 8.01e-07

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: 45.78  E-value: 8.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829235  15 VSFEVEISAPIQEVFALLTTNTGLAKWFNELEV--------GELGADGYLLFVMTPEEKITMPIRAFEPNQKLAFEW--- 83
Cdd:cd07812    1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERvevlgggeGGVGARFVGGRKGGRRLTLTSEVTEVDPPRPGRFRVtgg 80

                         90       100
                 ....*....|....*....|....*
gi 489829235  84 ---DQDEVAFELNKITANKTRLTFT 105
Cdd:cd07812   81 gggVDGTGEWRLEPEGDGGTRVTYT 105
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 23-134 7.41e-06

Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic and archaeal proteins that bear similarity to a C-terminal region of human activator of 90 kDa heat shock protein ATPase homolog 1 (AHSA1/p38). This protein is known to interact with the middle domain of Hsp90, and stimulate its ATPase activity. It is probably a general upregulator of Hsp90 function, particularly contributing to its efficiency in conditions of increased stress. p38 is also known to interact with the cytoplasmic domain of the VSV G protein, and may thus be involved in protein transport. It has also been reported as being underexpressed in Down's syndrome. This region is found repeated in two members of this family (Swiss:Q8XY04 and Swiss:Q6MH87). The structure of YndB from Bacillus subtilis showed the helix-grip fold consisting of a beta-sheet with two small and one long alpha-helix which form a hydrophobic cavity that preferentially binds lipid-like molecules. This structure confirms its similarity with the eukaryote protein Aha1 and its classification as a member of the AHSA1 family).


Pssm-ID: 429921 [Multi-domain]  Cd Length: 125  Bit Score: 43.07  E-value: 7.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829235   23 APIQEVFALLTTNTGLAKWF------NELEVGelgadGYLLFVMTPEEK---ITMPIRAFEPNQKLAFEW---DQDEVAF 90
Cdd:pfam08327   2 APPERVFRALTDPELLARWFtrtvaeMDLRPG-----GKFRFMRGPDGEefgGNGTYLELVPPKRIVYTWrldDWPEGGY 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 489829235   91 ELNKIT----ANKTRLTFTEQLTTITEHSPRDIS-GWHICLKKLQASAE 134
Cdd:pfam08327  77 STVTVEleevGGGTRLTLTHTGEPAGEKEEMGMEeGWEQSLDQLKALLE 125
SRPBCC_CalC_Aha1-like_5 cd08898
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 18-135 1.25e-05

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: 176907 [Multi-domain]  Cd Length: 145  Bit Score: 42.68  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829235  18 EVEISAPIQEVFALLTTNTGLAKWF----NELEVGElGADGYLLFvmTPEEKITMPIR--AFEPNQKLAFEW-----DQD 86
Cdd:cd08898    6 TILIDAPRERVWRALTDPEHFGQWFgvklGPFVVGE-GATGEITY--PGYEHGVFPVTvvEVDPPRRFSFRWhppaiDPG 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489829235  87 E---------VAFELNKItANKTRLTFTEQ-LTTITEHsPRDIS------GWHICLKKLQASAEG 135
Cdd:cd08898   83 EdysaepstlVEFTLEPI-AGGTLLTVTESgFDALPAE-RRAEAyrmnegGWDEQLENLVAYVEA 145
SRPBCC_4 cd07822
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 15-109 1.42e-03

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: 36.92  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829235  15 VSFEVEISAPIQEVFALLTTNTGLAKWF--------NELEVGElgadgYLLFVMTPEEKITMPIRA----FEPNQKLAFE 82
Cdd:cd07822    2 ISTEIEINAPPEKVWEVLTDFPSYPEWNpfvrsatgLSLALGA-----RLRFVVKLPGGPPRSFKPrvteVEPPRRLAWR 76

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489829235  83 -------WDQDEVAFELNKITANKTRLTFTEQLT 109
Cdd:cd07822   77 gglpfpgLLDGEHSFELEPLGDGGTRFVHRETFS 110
 
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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