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Conserved domains on  [gi|2571039672|ref|WP_307766347|]
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SRPBCC domain-containing protein [Aeromonas rivipollensis]

Protein Classification

SRPBCC family protein( domain architecture ID 10172343)

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_4 cd08897
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 2-134 2.43e-77

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: 224.86  E-value: 2.43e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672   2 KISVSVRVERPLVLVWEGWNTPASIMAWNAASPEWHCPSSRVDLRVGGLFCHRMAARDGSMEFDFEGTFTEVVPPTSLGY 81
Cdd:cd08897     1 KITVETTVDAPIEKVWEAWTTPEHITKWNFASDDWHCPSAENDLRVGGKFSYRMEAKDGSMGFDFEGTYTEVEPHKLIEY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2571039672  82 VMDDGRAVRVTFVEEQGGTRVHEEFDAESEHSGEQQRAGWQSILDNFKRYMES 134
Cdd:cd08897    81 TMEDGREVEVEFTEEGDGTKVVETFDAENENPVEMQRQGWQAILDNFKKYVES 133
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like_4 cd08897
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 2-134 2.43e-77

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: 224.86  E-value: 2.43e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672   2 KISVSVRVERPLVLVWEGWNTPASIMAWNAASPEWHCPSSRVDLRVGGLFCHRMAARDGSMEFDFEGTFTEVVPPTSLGY 81
Cdd:cd08897     1 KITVETTVDAPIEKVWEAWTTPEHITKWNFASDDWHCPSAENDLRVGGKFSYRMEAKDGSMGFDFEGTYTEVEPHKLIEY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2571039672  82 VMDDGRAVRVTFVEEQGGTRVHEEFDAESEHSGEQQRAGWQSILDNFKRYMES 134
Cdd:cd08897    81 TMEDGREVEVEFTEEGDGTKVVETFDAENENPVEMQRQGWQAILDNFKKYVES 133
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 2-129 4.85e-22

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 85.09  E-value: 4.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672   2 KISVSVRVERPLVLVWEGWNTPASIMAWNAasPEWHCPSSRVDLRVGGLFCHRMAARDGSmEFDFEGTFTEVVPPTSLGY 81
Cdd:COG3832     7 TITIEREIDAPPERVWRAWTDPELLARWFG--PKGWATVAEFDLRVGGRFRFRMRGPDGE-EFGFEGEVLEVEPPERLVF 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2571039672  82 VMDDGRA------VRVTFVEEQGGTRV---HEEFDAESE--HSGEQQRAGWQSILDNFK 129
Cdd:COG3832    84 TWGFEDDpegestVTVTLEPEGGGTRLtltHTGFSAEDRdaVLAEGMEEGWTESLDRLK 142
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 15-133 2.70e-20

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: 80.05  E-value: 2.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672  15 LVWEGWNTPASIMAWnaaspeWHCPSSRVDLRVGGLFchRMAARDGSMEFDFEGTFTEVVPPTSLGY--VMDDGRA---- 88
Cdd:pfam08327   6 RVFRALTDPELLARW------FTRTVAEMDLRPGGKF--RFMRGPDGEEFGGNGTYLELVPPKRIVYtwRLDDWPEggys 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2571039672  89 -VRVTFVEEQGGTRVHEEFDAESEHSGEQ--QRAGWQSILDNFKRYME 133
Cdd:pfam08327  78 tVTVELEEVGGGTRLTLTHTGEPAGEKEEmgMEEGWEQSLDQLKALLE 125
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like_4 cd08897
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 2-134 2.43e-77

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: 224.86  E-value: 2.43e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672   2 KISVSVRVERPLVLVWEGWNTPASIMAWNAASPEWHCPSSRVDLRVGGLFCHRMAARDGSMEFDFEGTFTEVVPPTSLGY 81
Cdd:cd08897     1 KITVETTVDAPIEKVWEAWTTPEHITKWNFASDDWHCPSAENDLRVGGKFSYRMEAKDGSMGFDFEGTYTEVEPHKLIEY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2571039672  82 VMDDGRAVRVTFVEEQGGTRVHEEFDAESEHSGEQQRAGWQSILDNFKRYMES 134
Cdd:cd08897    81 TMEDGREVEVEFTEEGDGTKVVETFDAENENPVEMQRQGWQAILDNFKKYVES 133
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 2-129 4.85e-22

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 85.09  E-value: 4.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672   2 KISVSVRVERPLVLVWEGWNTPASIMAWNAasPEWHCPSSRVDLRVGGLFCHRMAARDGSmEFDFEGTFTEVVPPTSLGY 81
Cdd:COG3832     7 TITIEREIDAPPERVWRAWTDPELLARWFG--PKGWATVAEFDLRVGGRFRFRMRGPDGE-EFGFEGEVLEVEPPERLVF 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2571039672  82 VMDDGRA------VRVTFVEEQGGTRV---HEEFDAESE--HSGEQQRAGWQSILDNFK 129
Cdd:COG3832    84 TWGFEDDpegestVTVTLEPEGGGTRLtltHTGFSAEDRdaVLAEGMEEGWTESLDRLK 142
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 15-133 2.70e-20

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: 80.05  E-value: 2.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672  15 LVWEGWNTPASIMAWnaaspeWHCPSSRVDLRVGGLFchRMAARDGSMEFDFEGTFTEVVPPTSLGY--VMDDGRA---- 88
Cdd:pfam08327   6 RVFRALTDPELLARW------FTRTVAEMDLRPGGKF--RFMRGPDGEEFGGNGTYLELVPPKRIVYtwRLDDWPEggys 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2571039672  89 -VRVTFVEEQGGTRVHEEFDAESEHSGEQ--QRAGWQSILDNFKRYME 133
Cdd:pfam08327  78 tVTVELEEVGGGTRLTLTHTGEPAGEKEEmgMEEGWEQSLDQLKALLE 125
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 3-133 5.97e-17

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: 71.63  E-value: 5.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672   3 ISVSVRVERPLVLVWEGWNTPASIMAWnaaspeWH-CPSSRVDLRVGGLFCHRMAARDGsMEFDFEGTFTEVVPPTSLGY 81
Cdd:cd07814     2 ITIEREFDAPPELVWRALTDPELLAQW------FGpTTTAEMDLRVGGRWFFFMTGPDG-EEGWVSGEVLEVEPPRRLVF 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2571039672  82 VMDDGRA-------VRVTFVEEQGGTRV---HEEFDAESEHSGEQQ--RAGWQSILDNFKRYME 133
Cdd:cd07814    75 TWAFSDEtpgpettVTVTLEETGGGTRLtltHSGFPEEDAEQEAREgmEEGWTGTLDRLKALLE 138
SRPBCC_CalC_Aha1-like_3 cd08896
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 15-134 7.28e-11

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: 56.09  E-value: 7.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672  15 LVWEGWNTPASIMAWNAASPeWHCPSSRVDLRVGGLFCHRMAARDGSmEFDFEGTFTEVVPPTSL--------GYVMDDG 86
Cdd:cd08896    14 LVWRAWTEPELLKQWFCPKP-WTTEVAELDLRPGGAFRTVMRGPDGE-EFPNPGCFLEVVPGERLvftdaltpGWRPAEK 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672  87 R---AVrVTFVEEQGGTRvheeFDAESEHSGEQQRA---------GWQSILDNFKRYMES 134
Cdd:cd08896    92 PfmtAI-ITFEDEGGGTR----YTARARHWTEADRKqheemgfhdGWGTAADQLAALAES 146
SRPBCC_CalC_Aha1-like_9 cd07826
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 7-102 2.63e-10

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: 54.56  E-value: 2.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672   7 VRVER----PLVLVWEGWNTPASIMAWNAAsPEWHCPSSRVDLRVGGLFCHRMAARDGSmEFDFEGTFTEVVPP-----T 77
Cdd:cd07826     2 IVITRefdaPRELVFRAHTDPELVKRWWGP-RGLTMTVCECDIRVGGSYRYVHRAPDGE-EMGFHGVYHEVTPPerivqT 79

                          90       100
                  ....*....|....*....|....*.
gi 2571039672  78 SLGYVMDDGRAV-RVTFVEEQGGTRV 102
Cdd:cd07826    80 EEFEGLPDGVALeTVTFTELGGRTRL 105
SRPBCC_CalC_Aha1-like_GntR-HTH cd08893
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 36-133 6.23e-10

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: 53.40  E-value: 6.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672  36 WHCPSSRVDLRVGGLFCHRmaaRDGSMEFDFEGTFTEVVPPTSL--------GYVMDDGRAVRVTF-VEEQGG----TRV 102
Cdd:cd08893    29 WGGTTVESDWKVGSAFEYR---RGDDGTVDVEGEVLESDPPRRLvhtwravwDPEMAAEPPSRVTFeIEPVGDvvklTVT 105

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2571039672 103 HEEFDAESEHSgEQQRAGWQSILDNFKRYME 133
Cdd:cd08893   106 HDGFPPGSPTL-EGVSGGWPAILSSLKTLLE 135
SRPBCC_CalC_Aha1-like_7 cd08900
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 16-134 9.78e-07

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: 44.96  E-value: 9.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672  16 VWEGWNTPASIMAWNAASPEWHCPSSRVDLRVGGLFCHRMAArDGSMEFDFEGTFTEVVPPTSL--GYVMD-DGRA---- 88
Cdd:cd08900    15 VFAAWSDPAARARWFVPSPDWTVLEDEFDFRVGGREVSRGGP-KGGPEITVEARYHDIVPDERIvyTYTMHiGGTLlsas 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2571039672  89 -VRVTFVEEQGGTR----VHEEFDAESEHSgEQQRAGWQSILDNFKRYMES 134
Cdd:cd08900    94 lATVEFAPEGGGTRltltEQGAFLDGDDDP-AGREQGTAALLDNLAAELER 143
SRPBCC_CalC_Aha1-like_2 cd08895
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 6-134 4.64e-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: 43.43  E-value: 4.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672   6 SVRVER----PLVLVWEGWNTPASIMAWNAasPE-WHCPSSRVDLRVGGLFchRM-----AARDGSMEFD---FEGTFTE 72
Cdd:cd08895     1 TDRLHRviaaPPERVYRAFLDPDALAKWLP--PDgMTGTVHEFDAREGGGF--RMsltyfDPSVGKTTGNtdvFGGRFLE 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2571039672  73 VVPPTSLGY--VMDDGR-----AVRVTFVEEQGGTRVHEEF----DAESEHSGEqqrAGWQSILDNFKRYMES 134
Cdd:cd08895    77 LVPNERIVYtdVFDDPSlsgemTMTWTLSPVSGGTDVTIVQsgipDGIPPEDCE---LGWQESLANLAALVEA 146
SRPBCC_CalC_Aha1-like_1 cd08894
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 5-133 9.39e-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: 176903  Cd Length: 139  Bit Score: 39.57  E-value: 9.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2571039672   5 VSVRV-ERPLVLVWEGWNTPASIMAWnaaspeW-----HCPSSRVDLRVGGLFCHRMAARDGSmEFDFEGTFTEVVPPTS 78
Cdd:cd08894     3 VTTRViDAPRDLVFAAWTDPEHLAQW------WgpegfTNTTHEFDLRPGGRWRFVMHGPDGT-DYPNRIVFLEIEPPER 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2571039672  79 LGY--VMDDGRA-VRVTFVEEQGGTRV--HEEFDaESEHSGEQQR----AGWQSILDNFKRYME 133
Cdd:cd08894    76 IVYdhGSGPPRFrLTVTFEEQGGKTRLtwRQVFP-TAAERCEKIKfgavEGNEQTLDRLAAYLA 138
 
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.
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