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Conserved domains on  [gi|556495888|ref|WP_023343575|]
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MULTISPECIES: SRPBCC family protein [Enterobacter]

Protein Classification

SRPBCC family protein( domain architecture ID 10172340)

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_3 cd08896
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 8-152 9.82e-82

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: 176905 [Multi-domain]  Cd Length: 146  Bit Score: 237.52  E-value: 9.82e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888   8 DLKLERVVDAPRDLLWLCWTTPEHIKNFFIPAPHKVTECDLDLRVGGRFNTVFEV-DGQRMDNRGVFLEIDPGKKLVFTD 86
Cdd:cd08896    1 DLVLSRTIDAPRELVWRAWTEPELLKQWFCPKPWTTEVAELDLRPGGAFRTVMRGpDGEEFPNPGCFLEVVPGERLVFTD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556495888  87 GYTEGWKPAEKPFMTAILLLEDVGEGkTRYTAIARHPTKEIREQHEQMGFHEGWGIVLDQLVGYVK 152
Cdd:cd08896   81 ALTPGWRPAEKPFMTAIITFEDEGGG-TRYTARARHWTEADRKQHEEMGFHDGWGTAADQLAALAE 145
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like_3 cd08896
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 8-152 9.82e-82

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: 176905 [Multi-domain]  Cd Length: 146  Bit Score: 237.52  E-value: 9.82e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888   8 DLKLERVVDAPRDLLWLCWTTPEHIKNFFIPAPHKVTECDLDLRVGGRFNTVFEV-DGQRMDNRGVFLEIDPGKKLVFTD 86
Cdd:cd08896    1 DLVLSRTIDAPRELVWRAWTEPELLKQWFCPKPWTTEVAELDLRPGGAFRTVMRGpDGEEFPNPGCFLEVVPGERLVFTD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556495888  87 GYTEGWKPAEKPFMTAILLLEDVGEGkTRYTAIARHPTKEIREQHEQMGFHEGWGIVLDQLVGYVK 152
Cdd:cd08896   81 ALTPGWRPAEKPFMTAIITFEDEGGG-TRYTARARHWTEADRKQHEEMGFHDGWGTAADQLAALAE 145
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 2-147 2.79e-38

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 127.08  E-value: 2.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888   2 TLDPETDLKLERVVDAPRDLLWLCWTTPEHIKNFFIPAPHkVTECDLDLRVGGRFNTVFEV-DGQRMDNRGVFLEIDPGK 80
Cdd:COG3832    1 ADAEDRTITIEREIDAPPERVWRAWTDPELLARWFGPKGW-ATVAEFDLRVGGRFRFRMRGpDGEEFGFEGEVLEVEPPE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556495888  81 KLVFTDgyteGWKPAEKPFMTAILLLEDVGEGkTRYTAIARHPTKEIREQHEQMGFHEGWGIVLDQL 147
Cdd:COG3832   80 RLVFTW----GFEDDPEGESTVTVTLEPEGGG-TRLTLTHTGFSAEDRDAVLAEGMEEGWTESLDRL 141
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 16-152 1.25e-33

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: 114.72  E-value: 1.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888   16 DAPRDLLWLCWTTPEHIKNFFipaphKVTECDLDLRVGGRFNTVFEVDGQRMDNRGVFLEIDPGKKLVFTDGYTEgwkPA 95
Cdd:pfam08327   1 DAPPERVFRALTDPELLARWF-----TRTVAEMDLRPGGKFRFMRGPDGEEFGGNGTYLELVPPKRIVYTWRLDD---WP 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 556495888   96 EKPFMTAILLLEDVGeGKTRYTAIArhpTKEIREQHEQMGFHEGWGIVLDQLVGYVK 152
Cdd:pfam08327  73 EGGYSTVTVELEEVG-GGTRLTLTH---TGEPAGEKEEMGMEEGWEQSLDQLKALLE 125
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like_3 cd08896
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 8-152 9.82e-82

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: 176905 [Multi-domain]  Cd Length: 146  Bit Score: 237.52  E-value: 9.82e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888   8 DLKLERVVDAPRDLLWLCWTTPEHIKNFFIPAPHKVTECDLDLRVGGRFNTVFEV-DGQRMDNRGVFLEIDPGKKLVFTD 86
Cdd:cd08896    1 DLVLSRTIDAPRELVWRAWTEPELLKQWFCPKPWTTEVAELDLRPGGAFRTVMRGpDGEEFPNPGCFLEVVPGERLVFTD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556495888  87 GYTEGWKPAEKPFMTAILLLEDVGEGkTRYTAIARHPTKEIREQHEQMGFHEGWGIVLDQLVGYVK 152
Cdd:cd08896   81 ALTPGWRPAEKPFMTAIITFEDEGGG-TRYTARARHWTEADRKQHEEMGFHDGWGTAADQLAALAE 145
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 2-147 2.79e-38

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 127.08  E-value: 2.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888   2 TLDPETDLKLERVVDAPRDLLWLCWTTPEHIKNFFIPAPHkVTECDLDLRVGGRFNTVFEV-DGQRMDNRGVFLEIDPGK 80
Cdd:COG3832    1 ADAEDRTITIEREIDAPPERVWRAWTDPELLARWFGPKGW-ATVAEFDLRVGGRFRFRMRGpDGEEFGFEGEVLEVEPPE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556495888  81 KLVFTDgyteGWKPAEKPFMTAILLLEDVGEGkTRYTAIARHPTKEIREQHEQMGFHEGWGIVLDQL 147
Cdd:COG3832   80 RLVFTW----GFEDDPEGESTVTVTLEPEGGG-TRLTLTHTGFSAEDRDAVLAEGMEEGWTESLDRL 141
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 16-152 1.25e-33

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: 114.72  E-value: 1.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888   16 DAPRDLLWLCWTTPEHIKNFFipaphKVTECDLDLRVGGRFNTVFEVDGQRMDNRGVFLEIDPGKKLVFTDGYTEgwkPA 95
Cdd:pfam08327   1 DAPPERVFRALTDPELLARWF-----TRTVAEMDLRPGGKFRFMRGPDGEEFGGNGTYLELVPPKRIVYTWRLDD---WP 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 556495888   96 EKPFMTAILLLEDVGeGKTRYTAIArhpTKEIREQHEQMGFHEGWGIVLDQLVGYVK 152
Cdd:pfam08327  73 EGGYSTVTVELEEVG-GGTRLTLTH---TGEPAGEKEEMGMEEGWEQSLDQLKALLE 125
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 8-153 1.77e-28

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: 102.06  E-value: 1.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888   8 DLKLERVVDAPRDLLWLCWTTPEHIKNFFipapHKVTECDLDLRVGGRFNTVF-EVDGQRMDNRGVFLEIDPGKKLVFTD 86
Cdd:cd07814    1 TITIEREFDAPPELVWRALTDPELLAQWF----GPTTTAEMDLRVGGRWFFFMtGPDGEEGWVSGEVLEVEPPRRLVFTW 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556495888  87 GYTEGWKPAEkpfMTAILLLEDVGeGKTRYTAIARHPTKEIREQHEQMGFHEGWGIVLDQLVGYVKG 153
Cdd:cd07814   77 AFSDETPGPE---TTVTVTLEETG-GGTRLTLTHSGFPEEDAEQEAREGMEEGWTGTLDRLKALLEK 139
SRPBCC_CalC_Aha1-like_9 cd07826
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 8-147 9.19e-23

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: 176868  Cd Length: 142  Bit Score: 87.69  E-value: 9.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888   8 DLKLERVVDAPRDLLWLCWTTPEHIKNFFIPAPHKVTECDLDLRVGGRFNTVFEV-DGQRMDNRGVFLEIDPGKKLVFTD 86
Cdd:cd07826    1 EIVITREFDAPRELVFRAHTDPELVKRWWGPRGLTMTVCECDIRVGGSYRYVHRApDGEEMGFHGVYHEVTPPERIVQTE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556495888  87 GYTEGWKPAEKPFMTaillLEDVGeGKTRYTAIARHPTKEIREQHEQMGFHEGWGIVLDQL 147
Cdd:cd07826   81 EFEGLPDGVALETVT----FTELG-GRTRLTATSRYPSKEARDGVLASGMEEGMEESYDRL 136
SRPBCC_CalC_Aha1-like_1 cd08894
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 9-152 7.11e-19

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: 176903  Cd Length: 139  Bit Score: 77.32  E-value: 7.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888   9 LKLERVVDAPRDLLWLCWTTPEHIKNFFIPAPHKVTECDLDLRVGGRFNTVFE-VDGQRMDNRGVFLEIDPGKKLVftdg 87
Cdd:cd08894    2 IVTTRVIDAPRDLVFAAWTDPEHLAQWWGPEGFTNTTHEFDLRPGGRWRFVMHgPDGTDYPNRIVFLEIEPPERIV---- 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556495888  88 YTEGWKPaekPFMTAILLLEDVGeGKTRYTAIARHPTKEIREQHEQMGFHEGWGIVLDQLVGYVK 152
Cdd:cd08894   78 YDHGSGP---PRFRLTVTFEEQG-GKTRLTWRQVFPTAAERCEKIKFGAVEGNEQTLDRLAAYLA 138
SRPBCC_CalC_Aha1-like_4 cd08897
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 11-85 4.64e-12

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: 176906 [Multi-domain]  Cd Length: 133  Bit Score: 59.61  E-value: 4.64e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556495888  11 LERVVDAPRDLLWLCWTTPEHIK--NFFIPAPHkVTECDLDLRVGGRFNTVFEVDGQRM--DNRGVFLEIDPGKKLVFT 85
Cdd:cd08897    4 VETTVDAPIEKVWEAWTTPEHITkwNFASDDWH-CPSAENDLRVGGKFSYRMEAKDGSMgfDFEGTYTEVEPHKLIEYT 81
SRPBCC_CalC_Aha1-like_7 cd08900
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 11-152 1.95e-08

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: 176909  Cd Length: 143  Bit Score: 49.97  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888  11 LERVVDAPRDLLWLCWTTPEHIKNFFIPAP-HKVTECDLDLRVGGRFNTVFEVDGQ-RMDNRGVFLEIDPGKKLVFTDGY 88
Cdd:cd08900    4 LERTYPAPPERVFAAWSDPAARARWFVPSPdWTVLEDEFDFRVGGREVSRGGPKGGpEITVEARYHDIVPDERIVYTYTM 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888  89 TEGWKpaekpFMTAILL---LEDVGEGkTRYT---AIARHPTKEIREQHEQmgfheGWGIVLDQLVGYVK 152
Cdd:cd08900   84 HIGGT-----LLSASLAtveFAPEGGG-TRLTlteQGAFLDGDDDPAGREQ-----GTAALLDNLAAELE 142
SRPBCC_CalC_Aha1-like_6 cd08899
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 3-153 1.98e-06

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: 44.98  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888   3 LDPETDLKLERVVDAPRDLLWLCWTTPEHIKNFFIPAphkvtecDLDLRVGGRFNTVFeVDGQRMDNRGVFLEIDPGKKL 82
Cdd:cd08899    7 LDGGATLRFERLLPAPIEDVWAALTDPERLARWFAPG-------TGDLRVGGRVEFVM-DDEEGPNATGTILACEPPRLL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556495888  83 VFT--DGYTEGWKPAEkpfmtaillLEDVGEGkTRYTAIARHPTkeirEQHEQMGFHEGWGIVLDQLVGYVKG 153
Cdd:cd08899   79 AFTwgEGGGESEVRFE---------LAPEGDG-TRLTLTHRLLD----ERFGAGAVGAGWHLCLDVLEAALEG 137
SRPBCC_CalC_Aha1-like_2 cd08895
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 10-153 2.10e-06

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: 176904  Cd Length: 146  Bit Score: 44.58  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888  10 KLERVVDAPRDLLWLCWTTPEHIKNFFIPAPHKVTECDLDLRVGGRFNTVF----EVDGQRMDN----RGVFLEIDPGKK 81
Cdd:cd08895    3 RLHRVIAAPPERVYRAFLDPDALAKWLPPDGMTGTVHEFDAREGGGFRMSLtyfdPSVGKTTGNtdvfGGRFLELVPNER 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556495888  82 LVFTDGYTEGWKPAEkpfMTAILLLEDVGEGkTRYTAIARH-PTKEIREQHEqmgfhEGWGIVLDQLVGYVKG 153
Cdd:cd08895   83 IVYTDVFDDPSLSGE---MTMTWTLSPVSGG-TDVTIVQSGiPDGIPPEDCE-----LGWQESLANLAALVEA 146
SRPBCC_CalC_Aha1-like_GntR-HTH cd08893
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 22-117 1.06e-05

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: 42.61  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888  22 LWLCWTTPEHIKNFFIpaphkVTECDLDLRVGGRFnTVFEVDGQRMDNRGVFLEIDPGKKLVFTdgytegWKPAEKPFMT 101
Cdd:cd08893   15 VWQALTDPEFTRQYWG-----GTTVESDWKVGSAF-EYRRGDDGTVDVEGEVLESDPPRRLVHT------WRAVWDPEMA 82

                         90
                 ....*....|....*.
gi 556495888 102 AillledvgEGKTRYT 117
Cdd:cd08893   83 A--------EPPSRVT 90
SRPBCC_CalC_Aha1-like_5 cd08898
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 14-153 1.58e-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: 176907 [Multi-domain]  Cd Length: 145  Bit Score: 39.60  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888  14 VVDAPRDLLWLCWTTPEHIKNFFipaPHKVTECDLDLRVGGRFnTVFEVDGQRMDNRGVflEIDPGKKLVFT---DGYTE 90
Cdd:cd08898    8 LIDAPRERVWRALTDPEHFGQWF---GVKLGPFVVGEGATGEI-TYPGYEHGVFPVTVV--EVDPPRRFSFRwhpPAIDP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888  91 GWKPAEKPFMTAILLLEDVGEGkTRYT-------AIARHPTKEIREQHEQmgfheGWGIVLDQLVGYVKG 153
Cdd:cd08898   82 GEDYSAEPSTLVEFTLEPIAGG-TLLTvtesgfdALPAERRAEAYRMNEG-----GWDEQLENLVAYVEA 145
SRPBCC_Aha1 cd08892
Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related ...
 8-85 1.37e-03

Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related proteins; This subfamily includes the C-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Aha1, and related domains. 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. Aha1 is one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Hsp90, Aha1, and other accessory proteins interact in a chaperone cycle driven by ATP binding and hydrolysis. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity. One Aha1 molecule binds per Hsp90 dimer. The N- and C- terminal domains of Aha1 cooperatively bind across the dimer interface of Hsp90. The C-terminal domain of Aha1 binds the N-terminal Hsp90 ATPase domain. Aha1 may regulate the dwell time of Hsp90 with client proteins. Aha1 may act as either a negative or positive regulator of chaperone-dependent activation, depending on the client protein; for example, it acts as a negative regulator in the case of Saccharomyces cerevisiae MAL63 MAL-activator, and acts as a positive regulator in the case of glucocorticoid receptor and v-Src kinase. 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: 176901 [Multi-domain]  Cd Length: 126  Bit Score: 36.77  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556495888   8 DLKLERVVDAPRDLLWLCWTTPEHIKNFfipaphkvT--ECDLDLRVGGRFnTVFevDGqrmdN-RGVFLEIDPGKKLVF 84
Cdd:cd08892    1 TISLTETFQVPAEELYEALTDEERVQAF--------TrsPAKVDAKVGGKF-SLF--GG----NiTGEFVELVPGKKIVQ 65


                 .
gi 556495888  85 T 85
Cdd:cd08892   66 K 66
 
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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