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Conserved domains on  [gi|446075489|ref|WP_000153344|]
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MULTISPECIES: SRPBCC domain-containing protein [Staphylococcus]

Protein Classification

SRPBCC family protein( domain architecture ID 10167422)

DUF3074 domain-containing 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 cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 10-155 9.38e-24

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: 90.12  E-value: 9.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446075489  10 IIFSRTIEAPIEKVFDAYTTKALFEKWFHPkdasTKVFRFNAVSGGDAFYAIKTPTMTSYTL-AEYKTVKRPYLIEYIDS 88
Cdd:cd07814    2 ITIEREFDAPPELVWRALTDPELLAQWFGP----TTTAEMDLRVGGRWFFFMTGPDGEEGWVsGEVLEVEPPRRLVFTWA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446075489  89 FATpqgakDTKMPSMKITLSFSKSNTTKTTVTSTSVFPTkEAAQQVINMGVEQGMNQTLDQLDALLK 155
Cdd:cd07814   78 FSD-----ETPGPETTVTVTLEETGGGTRLTLTHSGFPE-EDAEQEAREGMEEGWTGTLDRLKALLE 138
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 10-155 9.38e-24

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: 90.12  E-value: 9.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446075489  10 IIFSRTIEAPIEKVFDAYTTKALFEKWFHPkdasTKVFRFNAVSGGDAFYAIKTPTMTSYTL-AEYKTVKRPYLIEYIDS 88
Cdd:cd07814    2 ITIEREFDAPPELVWRALTDPELLAQWFGP----TTTAEMDLRVGGRWFFFMTGPDGEEGWVsGEVLEVEPPRRLVFTWA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446075489  89 FATpqgakDTKMPSMKITLSFSKSNTTKTTVTSTSVFPTkEAAQQVINMGVEQGMNQTLDQLDALLK 155
Cdd:cd07814   78 FSD-----ETPGPETTVTVTLEETGGGTRLTLTHSGFPE-EDAEQEAREGMEEGWTGTLDRLKALLE 138
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 5-151 1.40e-17

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 74.30  E-value: 1.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446075489   5 VEDNKIIFSRTIEAPIEKVFDAYTTKALFEKWFHPKDASTKVfRFNAVSGGDAFYAIKTPTMTSYTL-AEYKTVKRPYLI 83
Cdd:COG3832    3 AEDRTITIEREIDAPPERVWRAWTDPELLARWFGPKGWATVA-EFDLRVGGRFRFRMRGPDGEEFGFeGEVLEVEPPERL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446075489  84 EYIDSFA-------------TPQGAKdTKMpsmkiTLSFSksnttkttvtstsvFPTKEAAQQVINMGVEQGMNQTLDQL 150
Cdd:COG3832   82 VFTWGFEddpegestvtvtlEPEGGG-TRL-----TLTHT--------------GFSAEDRDAVLAEGMEEGWTESLDRL 141


                 .
gi 446075489 151 D 151
Cdd:COG3832  142 K 142
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 18-155 5.46e-17

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: 71.96  E-value: 5.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446075489   18 APIEKVFDAYTTKALFEKWFHPKDASTKVFRfnavsGGdAFYAIKTPTMTSYTLA-EYKTVKRPYLIEYIDSFatpqgAK 96
Cdd:pfam08327   2 APPERVFRALTDPELLARWFTRTVAEMDLRP-----GG-KFRFMRGPDGEEFGGNgTYLELVPPKRIVYTWRL-----DD 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446075489   97 DTKMPSMKITLSFSKSNTTKTTVTSTsvfpTKEAAQQVINMGVEQGMNQTLDQLDALLK 155
Cdd:pfam08327  71 WPEGGYSTVTVELEEVGGGTRLTLTH----TGEPAGEKEEMGMEEGWEQSLDQLKALLE 125
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 10-155 9.38e-24

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: 90.12  E-value: 9.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446075489  10 IIFSRTIEAPIEKVFDAYTTKALFEKWFHPkdasTKVFRFNAVSGGDAFYAIKTPTMTSYTL-AEYKTVKRPYLIEYIDS 88
Cdd:cd07814    2 ITIEREFDAPPELVWRALTDPELLAQWFGP----TTTAEMDLRVGGRWFFFMTGPDGEEGWVsGEVLEVEPPRRLVFTWA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446075489  89 FATpqgakDTKMPSMKITLSFSKSNTTKTTVTSTSVFPTkEAAQQVINMGVEQGMNQTLDQLDALLK 155
Cdd:cd07814   78 FSD-----ETPGPETTVTVTLEETGGGTRLTLTHSGFPE-EDAEQEAREGMEEGWTGTLDRLKALLE 138
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 5-151 1.40e-17

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 74.30  E-value: 1.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446075489   5 VEDNKIIFSRTIEAPIEKVFDAYTTKALFEKWFHPKDASTKVfRFNAVSGGDAFYAIKTPTMTSYTL-AEYKTVKRPYLI 83
Cdd:COG3832    3 AEDRTITIEREIDAPPERVWRAWTDPELLARWFGPKGWATVA-EFDLRVGGRFRFRMRGPDGEEFGFeGEVLEVEPPERL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446075489  84 EYIDSFA-------------TPQGAKdTKMpsmkiTLSFSksnttkttvtstsvFPTKEAAQQVINMGVEQGMNQTLDQL 150
Cdd:COG3832   82 VFTWGFEddpegestvtvtlEPEGGG-TRL-----TLTHT--------------GFSAEDRDAVLAEGMEEGWTESLDRL 141


                 .
gi 446075489 151 D 151
Cdd:COG3832  142 K 142
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 18-155 5.46e-17

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: 71.96  E-value: 5.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446075489   18 APIEKVFDAYTTKALFEKWFHPKDASTKVFRfnavsGGdAFYAIKTPTMTSYTLA-EYKTVKRPYLIEYIDSFatpqgAK 96
Cdd:pfam08327   2 APPERVFRALTDPELLARWFTRTVAEMDLRP-----GG-KFRFMRGPDGEEFGGNgTYLELVPPKRIVYTWRL-----DD 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446075489   97 DTKMPSMKITLSFSKSNTTKTTVTSTsvfpTKEAAQQVINMGVEQGMNQTLDQLDALLK 155
Cdd:pfam08327  71 WPEGGYSTVTVELEEVGGGTRLTLTH----TGEPAGEKEEMGMEEGWEQSLDQLKALLE 125
SRPBCC_CalC_Aha1-like_9 cd07826
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 10-154 6.52e-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: 176868  Cd Length: 142  Bit Score: 61.88  E-value: 6.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446075489  10 IIFSRTIEAPIEKVFDAYTTKALFEKWFHPKDASTKVFRFNAVSGGDAFYAIKTPTMTSYTL-AEYKTVKRPYLIEYIDS 88
Cdd:cd07826    2 IVITREFDAPRELVFRAHTDPELVKRWWGPRGLTMTVCECDIRVGGSYRYVHRAPDGEEMGFhGVYHEVTPPERIVQTEE 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446075489  89 FAtpqgakdtKMPSMK--ITLSFSKSNTTKTTVTSTSvFPTKEAAQQVINMGVEQGMNQTLDQLDALL 154
Cdd:cd07826   82 FE--------GLPDGValETVTFTELGGRTRLTATSR-YPSKEARDGVLASGMEEGMEESYDRLDELL 140
SRPBCC_CalC_Aha1-like_1 cd08894
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 9-155 1.18e-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: 176903  Cd Length: 139  Bit Score: 56.13  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446075489   9 KIIFSRTIEAPIEKVFDAYTTKALFEKWFHPKDASTKVFRFNAVSGGDAFYAIKTPTMTSY-TLAEYKTVKRPYLIEY-- 85
Cdd:cd08894    1 EIVTTRVIDAPRDLVFAAWTDPEHLAQWWGPEGFTNTTHEFDLRPGGRWRFVMHGPDGTDYpNRIVFLEIEPPERIVYdh 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446075489  86 ------IDSFAT--PQGAKdTKMpSMKITlsfsksnttkttvtstsvFPTKEAAQQVINMGVEQGMNQTLDQLDALLK 155
Cdd:cd08894   81 gsgpprFRLTVTfeEQGGK-TRL-TWRQV------------------FPTAAERCEKIKFGAVEGNEQTLDRLAAYLA 138
SRPBCC_CalC_Aha1-like_3 cd08896
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 10-59 4.87e-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: 176905 [Multi-domain]  Cd Length: 146  Bit Score: 51.85  E-value: 4.87e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446075489  10 IIFSRTIEAPIEKVFDAYTTKALFEKWFHPKDASTKVFRFNAVSGGdAFY 59
Cdd:cd08896    2 LVLSRTIDAPRELVWRAWTEPELLKQWFCPKPWTTEVAELDLRPGG-AFR 50
SRPBCC_CalC_Aha1-like_2 cd08895
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 10-92 9.17e-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: 176904  Cd Length: 146  Bit Score: 40.35  E-value: 9.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446075489  10 IIFSRTIEAPIEKVFDAYTTKALFEKWFHPKDASTKVFRFNAVSGG--------DAFYAIKTPTMTSYTLAEYKTVKRPY 81
Cdd:cd08895    2 DRLHRVIAAPPERVYRAFLDPDALAKWLPPDGMTGTVHEFDAREGGgfrmsltyFDPSVGKTTGNTDVFGGRFLELVPNE 81

                         90
                 ....*....|.
gi 446075489  82 LIEYIDSFATP 92
Cdd:cd08895   82 RIVYTDVFDDP 92
SRPBCC_CalC_Aha1-like_7 cd08900
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 10-55 1.66e-03

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: 36.49  E-value: 1.66e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446075489  10 IIFSRTIEAPIEKVFDAYTTKALFEKWFHPKDAST-KVFRFNAVSGG 55
Cdd:cd08900    2 FTLERTYPAPPERVFAAWSDPAARARWFVPSPDWTvLEDEFDFRVGG 48
SRPBCC_CalC_Aha1-like_6 cd08899
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 2-39 2.50e-03

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: 36.12  E-value: 2.50e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446075489   2 TIKVEDNKIIFSRTIEAPIEKVFDAYTTKALFEKWFHP 39
Cdd:cd08899    5 TRLDGGATLRFERLLPAPIEDVWAALTDPERLARWFAP 42
 
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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