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Conserved domains on  [gi|1046893005|ref|XP_017449845|]
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activator of 90 kDa heat shock protein ATPase homolog 1 isoform X1 [Rattus norvegicus]

Protein Classification

SRPBCC family protein( domain architecture ID 10172333)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket; similar to Homo sapiens activator of 90 kDa heat shock protein ATPase homolog 1 isoform 2

Gene Ontology:  GO:0005488
PubMed:  18922149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC_Aha1 cd08892
Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related ...
 73-198 2.03e-71

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: 212.42  E-value: 2.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046893005  73 KITLKETFLTSPEELYRVFTTQELVQAFTHAPAALEADRGGKFHMVDGNVTGEFTDLVPEKHIAMKWRFKSWPEGHFATI 152
Cdd:cd08892     1 TISLTETFQVPAEELYEALTDEERVQAFTRSPAKVDAKVGGKFSLFGGNITGEFVELVPGKKIVQKWRFKSWPEGHYSTV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1046893005 153 TLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGY 198
Cdd:cd08892    81 TLTFTEKDDETELKLTQTGVPAGEEERTREGWERYYFESIKQTFGY 126
 
Name Accession Description Interval E-value
SRPBCC_Aha1 cd08892
Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related ...
 73-198 2.03e-71

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: 212.42  E-value: 2.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046893005  73 KITLKETFLTSPEELYRVFTTQELVQAFTHAPAALEADRGGKFHMVDGNVTGEFTDLVPEKHIAMKWRFKSWPEGHFATI 152
Cdd:cd08892     1 TISLTETFQVPAEELYEALTDEERVQAFTRSPAKVDAKVGGKFSLFGGNITGEFVELVPGKKIVQKWRFKSWPEGHYSTV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1046893005 153 TLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGY 198
Cdd:cd08892    81 TLTFTEKDDETELKLTQTGVPAGEEERTREGWERYYFESIKQTFGY 126
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 82-197 1.02e-29

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: 106.63  E-value: 1.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046893005  82 TSPEELYRVFTTQELVQA-FTHAPAALEADRGGKFHMVDGNV------TGEFTDLVPEKHIAMKWRFKSWPEGHFATITL 154
Cdd:pfam08327   2 APPERVFRALTDPELLARwFTRTVAEMDLRPGGKFRFMRGPDgeefggNGTYLELVPPKRIVYTWRLDDWPEGGYSTVTV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1046893005 155 TFIDKNGETELCMEGRGIPAPEEER--TRQGWQRYYfEGIKQTFG 197
Cdd:pfam08327  82 ELEEVGGGTRLTLTHTGEPAGEKEEmgMEEGWEQSL-DQLKALLE 125
COG5580 COG5580
Activator of HSP90 ATPase [Posttranslational modification, protein turnover, chaperones];
74-197 1.14e-22

Activator of HSP90 ATPase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444319  Cd Length: 129  Bit Score: 88.49  E-value: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046893005  74 ITLKETFLTSPEELYRVFTTQELVQAFTHAPAALEADRGGKFHMVDGNVTGEFTDLVPEKHIAMKWRFKSWPE-GHFATI 152
Cdd:COG5580     5 IKKYYTIPASPEEVYKALTDSQTHSAWTGGPAEMSPEVGGEFSAWDGYIVGRNLELEPGKKIVQSWRSSDFGDqEEDSIV 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1046893005 153 TLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFG 197
Cdd:COG5580    85 TIKLHPHGGGTSLELIHTNIPDGDGEDIVEGWDEYYFGPMKKYFE 129
PTZ00220 PTZ00220
Activator of HSP-90 ATPase; Provisional
 80-198 6.67e-22

Activator of HSP-90 ATPase; Provisional


Pssm-ID: 173484  Cd Length: 132  Bit Score: 86.41  E-value: 6.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046893005  80 FLTSPEELYRVFTTQ-ELVQAFTHAPAALEADRGGKFHMVDGNVTGEFTDLVPEKHIAMKWRFKSWPEGHFATITLTFID 158
Cdd:PTZ00220    1 FYVPPEVLYNAFLDAyTLTRLSLGSPAEMDAKVGGKFSLFNGSVEGEFTELEKPKKIVQKWRFRDWEEDVYSKVTIEFRA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1046893005 159 -KNGETELCMEGRGIPAPEE-------ERTRQGWQRYYFEGIKQTFGY 198
Cdd:PTZ00220   81 vEEDHTELKLTQTGIPSLDKfgnggclERCRNGWTQNFLDRFEKILGY 128
 
Name Accession Description Interval E-value
SRPBCC_Aha1 cd08892
Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related ...
 73-198 2.03e-71

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: 212.42  E-value: 2.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046893005  73 KITLKETFLTSPEELYRVFTTQELVQAFTHAPAALEADRGGKFHMVDGNVTGEFTDLVPEKHIAMKWRFKSWPEGHFATI 152
Cdd:cd08892     1 TISLTETFQVPAEELYEALTDEERVQAFTRSPAKVDAKVGGKFSLFGGNITGEFVELVPGKKIVQKWRFKSWPEGHYSTV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1046893005 153 TLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGY 198
Cdd:cd08892    81 TLTFTEKDDETELKLTQTGVPAGEEERTREGWERYYFESIKQTFGY 126
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 82-197 1.02e-29

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: 106.63  E-value: 1.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046893005  82 TSPEELYRVFTTQELVQA-FTHAPAALEADRGGKFHMVDGNV------TGEFTDLVPEKHIAMKWRFKSWPEGHFATITL 154
Cdd:pfam08327   2 APPERVFRALTDPELLARwFTRTVAEMDLRPGGKFRFMRGPDgeefggNGTYLELVPPKRIVYTWRLDDWPEGGYSTVTV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1046893005 155 TFIDKNGETELCMEGRGIPAPEEER--TRQGWQRYYfEGIKQTFG 197
Cdd:pfam08327  82 ELEEVGGGTRLTLTHTGEPAGEKEEmgMEEGWEQSL-DQLKALLE 125
COG5580 COG5580
Activator of HSP90 ATPase [Posttranslational modification, protein turnover, chaperones];
74-197 1.14e-22

Activator of HSP90 ATPase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444319  Cd Length: 129  Bit Score: 88.49  E-value: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046893005  74 ITLKETFLTSPEELYRVFTTQELVQAFTHAPAALEADRGGKFHMVDGNVTGEFTDLVPEKHIAMKWRFKSWPE-GHFATI 152
Cdd:COG5580     5 IKKYYTIPASPEEVYKALTDSQTHSAWTGGPAEMSPEVGGEFSAWDGYIVGRNLELEPGKKIVQSWRSSDFGDqEEDSIV 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1046893005 153 TLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFG 197
Cdd:COG5580    85 TIKLHPHGGGTSLELIHTNIPDGDGEDIVEGWDEYYFGPMKKYFE 129
PTZ00220 PTZ00220
Activator of HSP-90 ATPase; Provisional
 80-198 6.67e-22

Activator of HSP-90 ATPase; Provisional


Pssm-ID: 173484  Cd Length: 132  Bit Score: 86.41  E-value: 6.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046893005  80 FLTSPEELYRVFTTQ-ELVQAFTHAPAALEADRGGKFHMVDGNVTGEFTDLVPEKHIAMKWRFKSWPEGHFATITLTFID 158
Cdd:PTZ00220    1 FYVPPEVLYNAFLDAyTLTRLSLGSPAEMDAKVGGKFSLFNGSVEGEFTELEKPKKIVQKWRFRDWEEDVYSKVTIEFRA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1046893005 159 -KNGETELCMEGRGIPAPEE-------ERTRQGWQRYYFEGIKQTFGY 198
Cdd:PTZ00220   81 vEEDHTELKLTQTGIPSLDKfgnggclERCRNGWTQNFLDRFEKILGY 128
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 74-194 8.50e-16

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: 70.86  E-value: 8.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046893005  74 ITLKETFLTSPEELYRVFTTQELVQA--FTHAPAALEADRGGKFHMVDGN-------VTGEFTDLVPEKHIAMKWRFKSW 144
Cdd:cd07814     2 ITIEREFDAPPELVWRALTDPELLAQwfGPTTTAEMDLRVGGRWFFFMTGpdgeegwVSGEVLEVEPPRRLVFTWAFSDE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046893005 145 PEGHFATITLTFIDKNGETELCMEGRGIPAPEE-----ERTRQGWQRyYFEGIKQ 194
Cdd:cd07814    82 TPGPETTVTVTLEETGGGTRLTLTHSGFPEEDAeqearEGMEEGWTG-TLDRLKA 135
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 73-185 2.16e-12

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 61.98  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046893005  73 KITLKETFLTSPEELYRVFTTQELVQA-FTHAPAALEAD----RGGKFHMV----DGN---VTGEFTDLVPEKHIAMKWR 140
Cdd:COG3832     7 TITIEREIDAPPERVWRAWTDPELLARwFGPKGWATVAEfdlrVGGRFRFRmrgpDGEefgFEGEVLEVEPPERLVFTWG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1046893005 141 FKSWPEGHFaTITLTFIDKNGETELCMEGRGIPAPEEERT-----RQGWQ 185
Cdd:COG3832    87 FEDDPEGES-TVTVTLEPEGGGTRLTLTHTGFSAEDRDAVlaegmEEGWT 135
SRPBCC_CalC_Aha1-like_9 cd07826
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 79-165 9.06e-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: 176868  Cd Length: 142  Bit Score: 38.00  E-value: 9.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046893005  79 TFLTSPEELYRVFTTQELVQAFTHAPA------ALEADRGGKFHMV----DGN---VTGEFTDLVPEKHIAMKWRFKSWP 145
Cdd:cd07826     7 EFDAPRELVFRAHTDPELVKRWWGPRGltmtvcECDIRVGGSYRYVhrapDGEemgFHGVYHEVTPPERIVQTEEFEGLP 86

                          90       100
                  ....*....|....*....|
gi 1046893005 146 eGHFATITLTFIDKNGETEL 165
Cdd:cd07826    87 -DGVALETVTFTELGGRTRL 105
SRPBCC_CalC_Aha1-like_2 cd08895
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 74-185 9.84e-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: 176904  Cd Length: 146  Bit Score: 38.03  E-value: 9.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046893005  74 ITLKETFLTSPEELYRVFTTQE-LVQ-----AFTHAPAALEADRGGKFHMV-----------DGN---VTGEFTDLVPEK 133
Cdd:cd08895     2 DRLHRVIAAPPERVYRAFLDPDaLAKwlppdGMTGTVHEFDAREGGGFRMSltyfdpsvgktTGNtdvFGGRFLELVPNE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046893005 134 HIAMKWRFK--SWPEGHFATITLTfiDKNGETELCMEGRGIPA--PEEErTRQGWQ 185
Cdd:cd08895    82 RIVYTDVFDdpSLSGEMTMTWTLS--PVSGGTDVTIVQSGIPDgiPPED-CELGWQ 134
 
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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