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Conserved domains on  [gi|1524489517|gb|AZF36618|]
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hypothetical protein C4J88_1834 [Pseudomonas sp. R4-39-08]

Protein Classification

SRPBCC family protein( domain architecture ID 10172345)

uncharacterized SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may bind hydrophobic ligands

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like_5 cd08898
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 5-150 6.86e-68

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: 202.15  E-value: 6.86e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524489517   5 DRIERKVLLNASRKHVWEALTNAEQFGEWFGIALKgkTFVAGEPIEAPITYPGYEHVVWKARIERILPQTLFSFWWHPFA 84
Cdd:cd08898     1 DRIERTILIDAPRERVWRALTDPEHFGQWFGVKLG--PFVVGEGATGEITYPGYEHGVFPVTVVEVDPPRRFSFRWHPPA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524489517  85 VEKDVDYDQETPTLVEFTIEDRAPGILLRVVESGFDKVPQARRQKAFKMNSRGWDEQMGNIENYLD 150
Cdd:cd08898    79 IDPGEDYSAEPSTLVEFTLEPIAGGTLLTVTESGFDALPAERRAEAYRMNEGGWDEQLENLVAYVE 144
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like_5 cd08898
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 5-150 6.86e-68

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: 202.15  E-value: 6.86e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524489517   5 DRIERKVLLNASRKHVWEALTNAEQFGEWFGIALKgkTFVAGEPIEAPITYPGYEHVVWKARIERILPQTLFSFWWHPFA 84
Cdd:cd08898     1 DRIERTILIDAPRERVWRALTDPEHFGQWFGVKLG--PFVVGEGATGEITYPGYEHGVFPVTVVEVDPPRRFSFRWHPPA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524489517  85 VEKDVDYDQETPTLVEFTIEDRAPGILLRVVESGFDKVPQARRQKAFKMNSRGWDEQMGNIENYLD 150
Cdd:cd08898    79 IDPGEDYSAEPSTLVEFTLEPIAGGTLLTVTESGFDALPAERRAEAYRMNEGGWDEQLENLVAYVE 144
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 6-146 3.31e-16

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 70.45  E-value: 3.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524489517   6 RIERkvLLNASRKHVWEALTNAEQFGEWFGIALKGKT----FVAGEPIEAPITYPGYEHVVWKARIERILPQTLFSFWWH 81
Cdd:COG3832     9 TIER--EIDAPPERVWRAWTDPELLARWFGPKGWATVaefdLRVGGRFRFRMRGPDGEEFGFEGEVLEVEPPERLVFTWG 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524489517  82 pfavekdVDYDQETPTLVEFTIEDRAPGILLRVVESGFDkvPQARRQKAFKMNSRGWDEQMGNIE 146
Cdd:COG3832    87 -------FEDDPEGESTVTVTLEPEGGGTRLTLTHTGFS--AEDRDAVLAEGMEEGWTESLDRLK 142
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 14-150 3.27e-08

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: 49.24  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524489517  14 NASRKHVWEALTNAEQFGEWFGIALKGKTFVAGEPIEAPITYPGYEHvVWKARIERILPQTLFSFWWHPFavekdvDYDQ 93
Cdd:pfam08327   1 DAPPERVFRALTDPELLARWFTRTVAEMDLRPGGKFRFMRGPDGEEF-GGNGTYLELVPPKRIVYTWRLD------DWPE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524489517  94 ETPTLVEFTIEDRAPGILLRVVESGFDkvpqaRRQKAFKMNSRGWDEQMGNIENYLD 150
Cdd:pfam08327  74 GGYSTVTVELEEVGGGTRLTLTHTGEP-----AGEKEEMGMEEGWEQSLDQLKALLE 125
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like_5 cd08898
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 5-150 6.86e-68

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: 202.15  E-value: 6.86e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524489517   5 DRIERKVLLNASRKHVWEALTNAEQFGEWFGIALKgkTFVAGEPIEAPITYPGYEHVVWKARIERILPQTLFSFWWHPFA 84
Cdd:cd08898     1 DRIERTILIDAPRERVWRALTDPEHFGQWFGVKLG--PFVVGEGATGEITYPGYEHGVFPVTVVEVDPPRRFSFRWHPPA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524489517  85 VEKDVDYDQETPTLVEFTIEDRAPGILLRVVESGFDKVPQARRQKAFKMNSRGWDEQMGNIENYLD 150
Cdd:cd08898    79 IDPGEDYSAEPSTLVEFTLEPIAGGTLLTVTESGFDALPAERRAEAYRMNEGGWDEQLENLVAYVE 144
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 6-146 3.31e-16

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 70.45  E-value: 3.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524489517   6 RIERkvLLNASRKHVWEALTNAEQFGEWFGIALKGKT----FVAGEPIEAPITYPGYEHVVWKARIERILPQTLFSFWWH 81
Cdd:COG3832     9 TIER--EIDAPPERVWRAWTDPELLARWFGPKGWATVaefdLRVGGRFRFRMRGPDGEEFGFEGEVLEVEPPERLVFTWG 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524489517  82 pfavekdVDYDQETPTLVEFTIEDRAPGILLRVVESGFDkvPQARRQKAFKMNSRGWDEQMGNIE 146
Cdd:COG3832    87 -------FEDDPEGESTVTVTLEPEGGGTRLTLTHTGFS--AEDRDAVLAEGMEEGWTESLDRLK 142
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 7-151 8.68e-14

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: 64.31  E-value: 8.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524489517   7 IERKVLLNASRKHVWEALTNAEQFGEWFGIALKGKTFVA-GEPIEAPITYPGYEHVVWKARIERILPQTLFSFWWHpfav 85
Cdd:cd07814     2 ITIEREFDAPPELVWRALTDPELLAQWFGPTTTAEMDLRvGGRWFFFMTGPDGEEGWVSGEVLEVEPPRRLVFTWA---- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524489517  86 ekDVDYDQETPTLVEFTIEDRAPGILLRVVESGFDkvPQARRQKAFKMNSRGWDEQMGNIENYLDK 151
Cdd:cd07814    78 --FSDETPGPETTVTVTLEETGGGTRLTLTHSGFP--EEDAEQEAREGMEEGWTGTLDRLKALLEK 139
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 14-150 3.27e-08

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: 49.24  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524489517  14 NASRKHVWEALTNAEQFGEWFGIALKGKTFVAGEPIEAPITYPGYEHvVWKARIERILPQTLFSFWWHPFavekdvDYDQ 93
Cdd:pfam08327   1 DAPPERVFRALTDPELLARWFTRTVAEMDLRPGGKFRFMRGPDGEEF-GGNGTYLELVPPKRIVYTWRLD------DWPE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1524489517  94 ETPTLVEFTIEDRAPGILLRVVESGFDkvpqaRRQKAFKMNSRGWDEQMGNIENYLD 150
Cdd:pfam08327  74 GGYSTVTVELEEVGGGTRLTLTHTGEP-----AGEKEEMGMEEGWEQSLDQLKALLE 125
SRPBCC_CalC_Aha1-like_GntR-HTH cd08893
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 20-149 1.17e-07

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: 48.01  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524489517  20 VWEALTNAEQFGEWFGIALKGKTFVAGEPIEAPITYPGYEHVVWKarIERILPQTLFSFWWHPFAvekDVDYDQETPTLV 99
Cdd:cd08893    15 VWQALTDPEFTRQYWGGTTVESDWKVGSAFEYRRGDDGTVDVEGE--VLESDPPRRLVHTWRAVW---DPEMAAEPPSRV 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1524489517 100 EFTIEDRAPGILLRVVESGFDKVPQARRQkafkmNSRGWDEQMGNIENYL 149
Cdd:cd08893    90 TFEIEPVGDVVKLTVTHDGFPPGSPTLEG-----VSGGWPAILSSLKTLL 134
SRPBCC_4 cd07822
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 7-115 8.91e-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: 176864  Cd Length: 141  Bit Score: 43.08  E-value: 8.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524489517   7 IERKVLLNASRKHVWEALTNAEQFGEW--FGIALKGKTFVAGEPIEAPITYPGYEHVVWKARIERILPQTLFSfwWH--- 81
Cdd:cd07822     2 ISTEIEINAPPEKVWEVLTDFPSYPEWnpFVRSATGLSLALGARLRFVVKLPGGPPRSFKPRVTEVEPPRRLA--WRggl 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1524489517  82 PFAVEKDVDYDQE----TPTLVEFTIEDRAPGILLRVV 115
Cdd:cd07822    80 PFPGLLDGEHSFEleplGDGGTRFVHRETFSGLLAPLV 117
COG4891 COG4891
Uncharacterized conserved protein [Function unknown];
14-77 5.69e-04

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443919  Cd Length: 138  Bit Score: 37.97  E-value: 5.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524489517  14 NASRKHVWEALTNAEQFGEW--FGIALKGkTFVAGEPIEAPITYPGYEHVVWKARIERILPQTLFS 77
Cdd:COG4891     6 DAPPERVWQVLTDFPSYPEWnpFIRSIEG-ELRVGARLTLRLRPPGGRPMTFRPRVTEVEPNRELR 70
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 7-132 9.85e-03

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: 34.61  E-value: 9.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524489517   7 IERKVLLNASRKHVWEALTNAEQFGEWFGIALKGKTFVAGEPIEA---PITYPGYEHVVWKARIERILPQTLFSFWW--H 81
Cdd:cd07812     1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGarfVGGRKGGRRLTLTSEVTEVDPPRPGRFRVtgG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1524489517  82 PFAVEKDVDY----DQETPTLVEFTIEDRAPGILLRVVESGFDKVPQARRQKAFK 132
Cdd:cd07812    81 GGGVDGTGEWrlepEGDGGTRVTYTVEYDPPGPLLKVFALLLAGALKRELAALLR 135
 
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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