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Conserved domains on  [gi|727180718|ref|WP_033643190|]
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MULTISPECIES: SRPBCC family protein [Serratia]

Protein Classification

SRPBCC family protein( domain architecture ID 10172346)

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_6 cd08899
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 8-176 6.42e-48

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: 152.83  E-value: 6.42e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718   8 IEPGTLRIQRLLPGPIERVWAYLTESDKRATWLAAGAMKLENGAPLELEFRNSdlagehEQPPAkykqhggcvsnRGHIT 87
Cdd:cd08899    8 DGGATLRFERLLPAPIEDVWAALTDPERLARWFAPGTGDLRVGGRVEFVMDDE------EGPNA-----------TGTIL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718  88 CLFPPRLLSFTWAEQeqGRPSEVTFELTEQGNAVLLTVTHRRLANRDEMLSVAGGWHTHLDILLDRLHDRAPQPFWSTHA 167
Cdd:cd08899   71 ACEPPRLLAFTWGEG--GGESEVRFELAPEGDGTRLTLTHRLLDERFGAGAVGAGWHLCLDVLEAALEGGPPAPFWDAFA 148


                 ....*....
gi 727180718 168 RLEEEYRAR 176
Cdd:cd08899  149 QLEEEYRAY 157
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like_6 cd08899
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 8-176 6.42e-48

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: 152.83  E-value: 6.42e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718   8 IEPGTLRIQRLLPGPIERVWAYLTESDKRATWLAAGAMKLENGAPLELEFRNSdlagehEQPPAkykqhggcvsnRGHIT 87
Cdd:cd08899    8 DGGATLRFERLLPAPIEDVWAALTDPERLARWFAPGTGDLRVGGRVEFVMDDE------EGPNA-----------TGTIL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718  88 CLFPPRLLSFTWAEQeqGRPSEVTFELTEQGNAVLLTVTHRRLANRDEMLSVAGGWHTHLDILLDRLHDRAPQPFWSTHA 167
Cdd:cd08899   71 ACEPPRLLAFTWGEG--GGESEVRFELAPEGDGTRLTLTHRLLDERFGAGAVGAGWHLCLDVLEAALEGGPPAPFWDAFA 148


                 ....*....
gi 727180718 168 RLEEEYRAR 176
Cdd:cd08899  149 QLEEEYRAY 157
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 6-150 1.27e-22

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 87.79  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718   6 MIIEPGTLRIQRLLPGPIERVWAYLTESDKRATWLAAGA------MKLENGAPLELEFRNSDlageheqppakykqhGGC 79
Cdd:COG3832    1 ADAEDRTITIEREIDAPPERVWRAWTDPELLARWFGPKGwatvaeFDLRVGGRFRFRMRGPD---------------GEE 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727180718  80 VSNRGHITCLFPPRLLSFTWA-EQEQGRPSEVTFELTEQGNAVLLTVTHRRLANRDE----MLSVAGGWHTHLDIL 150
Cdd:COG3832   66 FGFEGEVLEVEPPERLVFTWGfEDDPEGESTVTVTLEPEGGGTRLTLTHTGFSAEDRdavlAEGMEEGWTESLDRL 141
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 22-150 1.02e-14

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: 66.95  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718   22 PIERVWAYLTESDKRATW--LAAGAMKLENGAplELEFRNSDLAGEHeqppakykqhggcvSNRGHITCLFPPRLLSFTW 99
Cdd:pfam08327   3 PPERVFRALTDPELLARWftRTVAEMDLRPGG--KFRFMRGPDGEEF--------------GGNGTYLELVPPKRIVYTW 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 727180718  100 A--EQEQGRPSEVTFELTEQGNAVLLTVTHRRLANRDEMLS-VAGGWHTHLDIL 150
Cdd:pfam08327  67 RldDWPEGGYSTVTVELEEVGGGTRLTLTHTGEPAGEKEEMgMEEGWEQSLDQL 120
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like_6 cd08899
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 8-176 6.42e-48

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: 152.83  E-value: 6.42e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718   8 IEPGTLRIQRLLPGPIERVWAYLTESDKRATWLAAGAMKLENGAPLELEFRNSdlagehEQPPAkykqhggcvsnRGHIT 87
Cdd:cd08899    8 DGGATLRFERLLPAPIEDVWAALTDPERLARWFAPGTGDLRVGGRVEFVMDDE------EGPNA-----------TGTIL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718  88 CLFPPRLLSFTWAEQeqGRPSEVTFELTEQGNAVLLTVTHRRLANRDEMLSVAGGWHTHLDILLDRLHDRAPQPFWSTHA 167
Cdd:cd08899   71 ACEPPRLLAFTWGEG--GGESEVRFELAPEGDGTRLTLTHRLLDERFGAGAVGAGWHLCLDVLEAALEGGPPAPFWDAFA 148


                 ....*....
gi 727180718 168 RLEEEYRAR 176
Cdd:cd08899  149 QLEEEYRAY 157
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 6-150 1.27e-22

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 87.79  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718   6 MIIEPGTLRIQRLLPGPIERVWAYLTESDKRATWLAAGA------MKLENGAPLELEFRNSDlageheqppakykqhGGC 79
Cdd:COG3832    1 ADAEDRTITIEREIDAPPERVWRAWTDPELLARWFGPKGwatvaeFDLRVGGRFRFRMRGPD---------------GEE 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727180718  80 VSNRGHITCLFPPRLLSFTWA-EQEQGRPSEVTFELTEQGNAVLLTVTHRRLANRDE----MLSVAGGWHTHLDIL 150
Cdd:COG3832   66 FGFEGEVLEVEPPERLVFTWGfEDDPEGESTVTVTLEPEGGGTRLTLTHTGFSAEDRdavlAEGMEEGWTESLDRL 141
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 12-155 9.09e-15

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: 67.39  E-value: 9.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718  12 TLRIQRLLPGPIERVWAYLTESDKRATWLAAGAMKlengaplELEFRNSDLAGEHEQPPAKYKQHGgcvsnRGHITCLFP 91
Cdd:cd07814    1 TITIEREFDAPPELVWRALTDPELLAQWFGPTTTA-------EMDLRVGGRWFFFMTGPDGEEGWV-----SGEVLEVEP 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718  92 PRLLSFTWA--EQEQGRPSEVTFELTEQGNAVLLTVTHRRLANRDE----MLSVAGGWHTHLDILLDRLH 155
Cdd:cd07814   69 PRRLVFTWAfsDETPGPETTVTVTLEETGGGTRLTLTHSGFPEEDAeqeaREGMEEGWTGTLDRLKALLE 138
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 22-150 1.02e-14

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: 66.95  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718   22 PIERVWAYLTESDKRATW--LAAGAMKLENGAplELEFRNSDLAGEHeqppakykqhggcvSNRGHITCLFPPRLLSFTW 99
Cdd:pfam08327   3 PPERVFRALTDPELLARWftRTVAEMDLRPGG--KFRFMRGPDGEEF--------------GGNGTYLELVPPKRIVYTW 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 727180718  100 A--EQEQGRPSEVTFELTEQGNAVLLTVTHRRLANRDEMLS-VAGGWHTHLDIL 150
Cdd:pfam08327  67 RldDWPEGGYSTVTVELEEVGGGTRLTLTHTGEPAGEKEEMgMEEGWEQSLDQL 120
SRPBCC_CalC_Aha1-like_GntR-HTH cd08893
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 24-143 4.75e-12

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: 59.95  E-value: 4.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718  24 ERVWAYLTESDKRATWLAAGAM--KLENGAPLEleFRNSDLAGEHeqppakykqhggcvsNRGHITCLFPPRLLSFTW-- 99
Cdd:cd08893   13 EKVWQALTDPEFTRQYWGGTTVesDWKVGSAFE--YRRGDDGTVD---------------VEGEVLESDPPRRLVHTWra 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 727180718 100 ---AEQEQGRPSEVTFELTEQGNAVLLTVTHRRLANRDEML-SVAGGW 143
Cdd:cd08893   76 vwdPEMAAEPPSRVTFEIEPVGDVVKLTVTHDGFPPGSPTLeGVSGGW 123
SRPBCC_CalC_Aha1-like_5 cd08898
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 14-148 1.00e-08

Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins; SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands.


Pssm-ID: 176907 [Multi-domain]  Cd Length: 145  Bit Score: 51.54  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718  14 RIQR--LLPGPIERVWAYLTESDKRATWLaagamklengaPLELEFrnsDLAGEHEQPPAKYKQHGGcVSNRGHITCLFP 91
Cdd:cd08898    2 RIERtiLIDAPRERVWRALTDPEHFGQWF-----------GVKLGP---FVVGEGATGEITYPGYEH-GVFPVTVVEVDP 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727180718  92 PRLLSFTWA--------EQEQGRPSEVTFELTEQGNAVLLTVT---------HRRLANRdEMLSvaGGWHTHLD 148
Cdd:cd08898   67 PRRFSFRWHppaidpgeDYSAEPSTLVEFTLEPIAGGTLLTVTesgfdalpaERRAEAY-RMNE--GGWDEQLE 137
SRPBCC_Aha1 cd08892
Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related ...
 69-146 6.29e-05

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: 40.62  E-value: 6.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718  69 PPAKYKQHGGCVSnrGHITCLFPPRLLSFTW--AEQEQGRPSEVTFELTEQGNAVLLTVTHRRLANRDEMlSVAGGWHTH 146
Cdd:cd08892   39 VGGKFSLFGGNIT--GEFVELVPGKKIVQKWrfKSWPEGHYSTVTLTFTEKDDETELKLTQTGVPAGEEE-RTREGWERY 115
SRPBCC_CalC_Aha1-like_7 cd08900
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 12-154 1.71e-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: 176909  Cd Length: 143  Bit Score: 39.95  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180718  12 TLRIQRLLPGPIERVWAYLTESDKRATWLAAGAMklENGAPLELEFRnsdlAGEHEQppAKYKQHGGCVS-NRGHITCLF 90
Cdd:cd08900    1 TFTLERTYPAPPERVFAAWSDPAARARWFVPSPD--WTVLEDEFDFR----VGGREV--SRGGPKGGPEItVEARYHDIV 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727180718  91 PPRLLSFTWAEQEQGRP---SEVTFELTEQGNAVLLTVTHR--RLANRDEMLSVAGGWhthlDILLDRL 154
Cdd:cd08900   73 PDERIVYTYTMHIGGTLlsaSLATVEFAPEGGGTRLTLTEQgaFLDGDDDPAGREQGT----AALLDNL 137
 
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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