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Conserved domains on  [gi|1037266652|gb|ANL06740|]
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activator of Hsp90 ATPase 1 family protein (plasmid) [Rhizobium esperanzae]

Protein Classification

SRPBCC family protein( domain architecture ID 10167535)

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_9 cd07826
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
24-163 5.61e-58

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: 177.44  E-value: 5.61e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  24 ELVITRTFDAPPSTVYRAWSQPELFQRWWVPKSAPgisLVSCDMDVRTGGKYRLEFGAGGSDTVAFYGKYLEVVPNERIV 103
Cdd:cd07826     1 EIVITREFDAPRELVFRAHTDPELVKRWWGPRGLT---MTVCECDIRVGGSYRYVHRAPDGEEMGFHGVYHEVTPPERIV 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037266652 104 WTNDEGEEG---AITTVTFEDQGGRTLLVFHEIYPSKEALEEALQ-GSAVALPEQLEQLDQLLP 163
Cdd:cd07826    78 QTEEFEGLPdgvALETVTFTELGGRTRLTATSRYPSKEARDGVLAsGMEEGMEESYDRLDELLA 141
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like_9 cd07826
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
24-163 5.61e-58

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: 177.44  E-value: 5.61e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  24 ELVITRTFDAPPSTVYRAWSQPELFQRWWVPKSAPgisLVSCDMDVRTGGKYRLEFGAGGSDTVAFYGKYLEVVPNERIV 103
Cdd:cd07826     1 EIVITREFDAPRELVFRAHTDPELVKRWWGPRGLT---MTVCECDIRVGGSYRYVHRAPDGEEMGFHGVYHEVTPPERIV 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037266652 104 WTNDEGEEG---AITTVTFEDQGGRTLLVFHEIYPSKEALEEALQ-GSAVALPEQLEQLDQLLP 163
Cdd:cd07826    78 QTEEFEGLPdgvALETVTFTELGGRTRLTATSRYPSKEARDGVLAsGMEEGMEESYDRLDELLA 141
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
21-159 3.13e-38

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 127.46  E-value: 3.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  21 GDRELVITRTFDAPPSTVYRAWSQPELFQRWWVPKSapgiSLVSCDMDVRTGGKYRLEFGAGGSDTVAFYGKYLEVVPNE 100
Cdd:COG3832     4 EDRTITIEREIDAPPERVWRAWTDPELLARWFGPKG----WATVAEFDLRVGGRFRFRMRGPDGEEFGFEGEVLEVEPPE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037266652 101 RIVWTN---DEGEEGAITTVTFEDQGGRTLLVFHEIYPSKEALEEALQ-GSAVALPEQLEQLD 159
Cdd:COG3832    80 RLVFTWgfeDDPEGESTVTVTLEPEGGGTRLTLTHTGFSAEDRDAVLAeGMEEGWTESLDRLK 142
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
32-162 2.40e-27

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: 99.31  E-value: 2.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  32 DAPPSTVYRAWSQPELFQRWWvpksapgiSLVSCDMDVRTGGKYRLEFGAGGSDtVAFYGKYLEVVPNERIVWT---NDE 108
Cdd:pfam08327   1 DAPPERVFRALTDPELLARWF--------TRTVAEMDLRPGGKFRFMRGPDGEE-FGGNGTYLELVPPKRIVYTwrlDDW 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1037266652 109 GEEGAIT-TVTFEDQGGRTLLVF-HEIYPSKEALEEalqGSAVALPEQLEQLDQLL 162
Cdd:pfam08327  72 PEGGYSTvTVELEEVGGGTRLTLtHTGEPAGEKEEM---GMEEGWEQSLDQLKALL 124
PTZ00220 PTZ00220
Activator of HSP-90 ATPase; Provisional
31-120 8.99e-04

Activator of HSP-90 ATPase; Provisional


Pssm-ID: 173484  Cd Length: 132  Bit Score: 37.49  E-value: 8.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  31 FDAPPSTVYRAWSQPELFQRwwVPKSAPgislvsCDMDVRTGGKYRLEFGaggsdtvAFYGKYLEVVPNERIV--WTNDE 108
Cdd:PTZ00220    1 FYVPPEVLYNAFLDAYTLTR--LSLGSP------AEMDAKVGGKFSLFNG-------SVEGEFTELEKPKKIVqkWRFRD 65
                          90
                  ....*....|..
gi 1037266652 109 GEEGAITTVTFE 120
Cdd:PTZ00220   66 WEEDVYSKVTIE 77
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like_9 cd07826
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
24-163 5.61e-58

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: 177.44  E-value: 5.61e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  24 ELVITRTFDAPPSTVYRAWSQPELFQRWWVPKSAPgisLVSCDMDVRTGGKYRLEFGAGGSDTVAFYGKYLEVVPNERIV 103
Cdd:cd07826     1 EIVITREFDAPRELVFRAHTDPELVKRWWGPRGLT---MTVCECDIRVGGSYRYVHRAPDGEEMGFHGVYHEVTPPERIV 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037266652 104 WTNDEGEEG---AITTVTFEDQGGRTLLVFHEIYPSKEALEEALQ-GSAVALPEQLEQLDQLLP 163
Cdd:cd07826    78 QTEEFEGLPdgvALETVTFTELGGRTRLTATSRYPSKEARDGVLAsGMEEGMEESYDRLDELLA 141
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
21-159 3.13e-38

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 127.46  E-value: 3.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  21 GDRELVITRTFDAPPSTVYRAWSQPELFQRWWVPKSapgiSLVSCDMDVRTGGKYRLEFGAGGSDTVAFYGKYLEVVPNE 100
Cdd:COG3832     4 EDRTITIEREIDAPPERVWRAWTDPELLARWFGPKG----WATVAEFDLRVGGRFRFRMRGPDGEEFGFEGEVLEVEPPE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037266652 101 RIVWTN---DEGEEGAITTVTFEDQGGRTLLVFHEIYPSKEALEEALQ-GSAVALPEQLEQLD 159
Cdd:COG3832    80 RLVFTWgfeDDPEGESTVTVTLEPEGGGTRLTLTHTGFSAEDRDAVLAeGMEEGWTESLDRLK 142
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
24-162 1.62e-32

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: 112.84  E-value: 1.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  24 ELVITRTFDAPPSTVYRAWSQPELFQRWWVPksapgisLVSCDMDVRTGGKYRLEFGAGGSDTVAFYGKYLEVVPNERIV 103
Cdd:cd07814     1 TITIEREFDAPPELVWRALTDPELLAQWFGP-------TTTAEMDLRVGGRWFFFMTGPDGEEGWVSGEVLEVEPPRRLV 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037266652 104 WT----NDEGEEGAITTVTFEDQGGRTLLVF-HEIYPSKEALEEALQGSAVALPEQLEQLDQLL 162
Cdd:cd07814    74 FTwafsDETPGPETTVTVTLEETGGGTRLTLtHSGFPEEDAEQEAREGMEEGWTGTLDRLKALL 137
SRPBCC_CalC_Aha1-like_1 cd08894
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
24-162 2.47e-29

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: 104.66  E-value: 2.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  24 ELVITRTFDAPPSTVYRAWSQPELFQRWWVPKsapGISLVSCDMDVRTGGKYRleFGAGGSDTVAFYGK--YLEVVPNER 101
Cdd:cd08894     1 EIVTTRVIDAPRDLVFAAWTDPEHLAQWWGPE---GFTNTTHEFDLRPGGRWR--FVMHGPDGTDYPNRivFLEIEPPER 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037266652 102 IVWTNDEGEEGAITTVTFEDQGGRTLLVFHEIYPSKEALEEALQGSAVALPEQ-LEQLDQLL 162
Cdd:cd08894    76 IVYDHGSGPPRFRLTVTFEEQGGKTRLTWRQVFPTAAERCEKIKFGAVEGNEQtLDRLAAYL 137
SRPBCC_CalC_Aha1-like_3 cd08896
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
24-158 2.63e-28

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: 102.31  E-value: 2.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  24 ELVITRTFDAPPSTVYRAWSQPELFQRWWVPKsaPGiSLVSCDMDVRTGGKYRLEFGAGGSDTVAFYGKYLEVVPNERIV 103
Cdd:cd08896     1 DLVLSRTIDAPRELVWRAWTEPELLKQWFCPK--PW-TTEVAELDLRPGGAFRTVMRGPDGEEFPNPGCFLEVVPGERLV 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037266652 104 WTN--DEG----EEGAITTV-TFEDQGGRTLLVFHEIYPSKEALE--EAL---QGSAVALpEQLEQL 158
Cdd:cd08896    78 FTDalTPGwrpaEKPFMTAIiTFEDEGGGTRYTARARHWTEADRKqhEEMgfhDGWGTAA-DQLAAL 143
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
32-162 2.40e-27

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: 99.31  E-value: 2.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  32 DAPPSTVYRAWSQPELFQRWWvpksapgiSLVSCDMDVRTGGKYRLEFGAGGSDtVAFYGKYLEVVPNERIVWT---NDE 108
Cdd:pfam08327   1 DAPPERVFRALTDPELLARWF--------TRTVAEMDLRPGGKFRFMRGPDGEE-FGGNGTYLELVPPKRIVYTwrlDDW 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1037266652 109 GEEGAIT-TVTFEDQGGRTLLVF-HEIYPSKEALEEalqGSAVALPEQLEQLDQLL 162
Cdd:pfam08327  72 PEGGYSTvTVELEEVGGGTRLTLtHTGEPAGEKEEM---GMEEGWEQSLDQLKALL 124
SRPBCC_CalC_Aha1-like_7 cd08900
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
25-157 1.63e-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: 176909  Cd Length: 143  Bit Score: 79.63  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  25 LVITRTFDAPPSTVYRAWSQPELFQRWWVPKSAPGISLVScdMDVRTGGKYRLEFGAGGSDTVAFYGKYLEVVPNERIVW 104
Cdd:cd08900     2 FTLERTYPAPPERVFAAWSDPAARARWFVPSPDWTVLEDE--FDFRVGGREVSRGGPKGGPEITVEARYHDIVPDERIVY 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037266652 105 TNDEGEEG-----AITTVTFEDQGGRTLLVFHE---IYPSKEALEEALQGSAVALpEQLEQ 157
Cdd:cd08900    80 TYTMHIGGtllsaSLATVEFAPEGGGTRLTLTEqgaFLDGDDDPAGREQGTAALL-DNLAA 139
SRPBCC_CalC_Aha1-like_2 cd08895
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
29-162 5.10e-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: 176904  Cd Length: 146  Bit Score: 78.48  E-value: 5.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  29 RTFDAPPSTVYRAWSQPELFQRWWVPKSAPGISLvscDMDVRTGGKYRLEF-------GAGGSDTVAFYGKYLEVVPNER 101
Cdd:cd08895     6 RVIAAPPERVYRAFLDPDALAKWLPPDGMTGTVH---EFDAREGGGFRMSLtyfdpsvGKTTGNTDVFGGRFLELVPNER 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037266652 102 IVWT---NDEGEEGAIT-TVTFEDQGGRTLL-VFHEIYP---SKEALEEALQGSavalpeqLEQLDQLL 162
Cdd:cd08895    83 IVYTdvfDDPSLSGEMTmTWTLSPVSGGTDVtIVQSGIPdgiPPEDCELGWQES-------LANLAALV 144
SRPBCC_CalC_Aha1-like_6 cd08899
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
17-130 1.73e-13

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: 64.24  E-value: 1.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  17 VERRGDRELVITRTFDAPPSTVYRAWSQPELFQRWWvpksAPGislvscDMDVRTGGKYRLEFGAGGSDTVAfyGKYLEV 96
Cdd:cd08899     5 TRLDGGATLRFERLLPAPIEDVWAALTDPERLARWF----APG------TGDLRVGGRVEFVMDDEEGPNAT--GTILAC 72
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1037266652  97 VPNERIVWTNDEGEEGAITTVTFEDQGGRTLLVF 130
Cdd:cd08899    73 EPPRLLAFTWGEGGGESEVRFELAPEGDGTRLTL 106
SRPBCC_Aha1 cd08892
Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related ...
24-130 1.12e-09

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: 53.33  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  24 ELVITRTFDAPPSTVYRAWSQPELFQRWwvpksapgiSLVSCDMDVRTGGKYRLeFgaGGSDTvafyGKYLEVVPNERIV 103
Cdd:cd08892     1 TISLTETFQVPAEELYEALTDEERVQAF---------TRSPAKVDAKVGGKFSL-F--GGNIT----GEFVELVPGKKIV 64
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1037266652 104 --WTNDEGEEG--AITTVTFEDQGGRTLLVF 130
Cdd:cd08892    65 qkWRFKSWPEGhySTVTLTFTEKDDETELKL 95
SRPBCC_CalC_Aha1-like_4 cd08897
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
26-129 2.41e-09

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: 52.68  E-value: 2.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  26 VITRTFDAPPSTVYRAWSQPELFQRW------W-VPKSapgislvscDMDVRTGGK--YRLEF--GAGGSDtvaFYGKYL 94
Cdd:cd08897     3 TVETTVDAPIEKVWEAWTTPEHITKWnfasddWhCPSA---------ENDLRVGGKfsYRMEAkdGSMGFD---FEGTYT 70
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1037266652  95 EVVPNERIVWTNDEGEEGaitTVTFEDQGGRTLLV 129
Cdd:cd08897    71 EVEPHKLIEYTMEDGREV---EVEFTEEGDGTKVV 102
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
30-126 1.76e-07

Uncharacterized protein, contains SRPBCC domain [Function unknown];


Pssm-ID: 444363  Cd Length: 154  Bit Score: 47.98  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  30 TFDAPPSTVYRAWSQPELFQRWwvpksAPGISlvscDMDVRTGGKYRLEFGAGGSDTVAFYGKYLEVVPNERIVWTNDEG 109
Cdd:COG5637     9 TINAPVEEVYAYWRDFENLPRF-----MKGVE----SVTVLDDTRSHWVAKGPLGVTVEWDAEITEQVPGERIAWRSVEG 79
                          90
                  ....*....|....*..
gi 1037266652 110 EEGAITTVTFEDQGGRT 126
Cdd:COG5637    80 DIPNAGVVRFEPAGGRG 96
SRPBCC_8 cd07817
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
32-125 4.91e-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: 176859  Cd Length: 139  Bit Score: 43.75  E-value: 4.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  32 DAPPSTVYRAWSQPELFQRWwvpksAPGISLVSCDMDVRTggKYRLEFGAGGsdTVAFYGKYLEVVPNERIVWTNDEGEE 111
Cdd:cd07817     9 NVPVEEVYDFWRDFENLPRF-----MSHVESVEQLDDTRS--HWKAKGPAGL--SVEWDAEITEQVPNERIAWRSVEGAD 79
                          90
                  ....*....|....
gi 1037266652 112 GAITTVTFEDQGGR 125
Cdd:cd07817    80 PNAGSVRFRPAPGR 93
SRPBCC_CalC_Aha1-like_8 cd08901
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
34-128 4.89e-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: 176910 [Multi-domain]  Cd Length: 136  Bit Score: 38.41  E-value: 4.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  34 PPSTVYRAWSQPELFQRWWVPKSAPGISlvscdmdvrTGGKYRLEFG-AGGSDTVafygKYLEVVPNERIV--WtndeGE 110
Cdd:cd08901    11 PVAEVFEAFVDPEITTKFWFTGSSGRLE---------EGKTVTWDWEmYGASVPV----NVLEIEPNKRIVieW----GD 73
                          90       100
                  ....*....|....*....|.
gi 1037266652 111 EGAITTVTF---EDQGGRTLL 128
Cdd:cd08901    74 PGEPTTVEWtfeELDDGRTFV 94
PTZ00220 PTZ00220
Activator of HSP-90 ATPase; Provisional
31-120 8.99e-04

Activator of HSP-90 ATPase; Provisional


Pssm-ID: 173484  Cd Length: 132  Bit Score: 37.49  E-value: 8.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  31 FDAPPSTVYRAWSQPELFQRwwVPKSAPgislvsCDMDVRTGGKYRLEFGaggsdtvAFYGKYLEVVPNERIV--WTNDE 108
Cdd:PTZ00220    1 FYVPPEVLYNAFLDAYTLTR--LSLGSP------AEMDAKVGGKFSLFNG-------SVEGEFTELEKPKKIVqkWRFRD 65
                          90
                  ....*....|..
gi 1037266652 109 GEEGAITTVTFE 120
Cdd:PTZ00220   66 WEEDVYSKVTIE 77
SRPBCC_4 cd07822
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
32-132 2.52e-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: 36.15  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  32 DAPPSTVYRAWSQPELFQRW--WVPKSAPGislvscdmDVRTGGKYRLEFGAGGSDTVAFYGKYLEVVPNERIVWTNDEG 109
Cdd:cd07822     9 NAPPEKVWEVLTDFPSYPEWnpFVRSATGL--------SLALGARLRFVVKLPGGPPRSFKPRVTEVEPPRRLAWRGGLP 80
                          90       100
                  ....*....|....*....|....*..
gi 1037266652 110 EEGAIT---TVTFEDQG-GRTLLVFHE 132
Cdd:cd07822    81 FPGLLDgehSFELEPLGdGGTRFVHRE 107
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
28-134 8.08e-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: 34.99  E-value: 8.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  28 TRTFDAPPSTVYRAWSQPELFQRWWVPksapgisLVSCDMDVRTGGKYRLEFGAGGSDTVAFYGKY--LEVVPNERIVWT 105
Cdd:cd07812     4 SIEIPAPPEAVWDLLSDPERWPEWSPG-------LERVEVLGGGEGGVGARFVGGRKGGRRLTLTSevTEVDPPRPGRFR 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1037266652 106 NDEGEEGAITTVTFE---DQGGRTLLVFHEIY 134
Cdd:cd07812    77 VTGGGGGVDGTGEWRlepEGDGGTRVTYTVEY 108
SRPBCC_CalC_Aha1-like_GntR-HTH cd08893
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
32-135 8.55e-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: 34.91  E-value: 8.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037266652  32 DAPPSTVYRAWSQPELFQRWWVpksapGISLVScdmDVRTGGKYrlEFGAGGSDTVAFYGKYLEVVPNERIVWT-----N 106
Cdd:cd08893     9 RATPEKVWQALTDPEFTRQYWG-----GTTVES---DWKVGSAF--EYRRGDDGTVDVEGEVLESDPPRRLVHTwravwD 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1037266652 107 DEGEEGAITTVTF--EDQGGRT-LLVFHEIYP 135
Cdd:cd08893    79 PEMAAEPPSRVTFeiEPVGDVVkLTVTHDGFP 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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