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Conserved domains on  [gi|491202538|ref|WP_005060880|]
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SRPBCC domain-containing protein [Mycobacteroides abscessus]

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 ...
 9-144 9.48e-18

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: 74.32  E-value: 9.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491202538   9 SITHSEYYPYPVDKVWDVLVSRELTAS---QVKEVSDAPVEVGSTRVIVTHPQpavGFDGVVRTTYTSVEPYEHIEQVLT 85
Cdd:cd07814    1 TITIEREFDAPPELVWRALTDPELLAQwfgPTTTAEMDLRVGGRWFFFMTGPD---GEEGWVSGEVLEVEPPRRLVFTWA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491202538  86 ----APGIEVTSRWNLLPEPGGTRLRVTYSRFDPSiPLHRQWRTMLFSGAGPILNSLREMLDK 144
Cdd:cd07814   78 fsdeTPGPETTVTVTLEETGGGTRLTLTHSGFPEE-DAEQEAREGMEEGWTGTLDRLKALLEK 139
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 9-144 9.48e-18

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: 74.32  E-value: 9.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491202538   9 SITHSEYYPYPVDKVWDVLVSRELTAS---QVKEVSDAPVEVGSTRVIVTHPQpavGFDGVVRTTYTSVEPYEHIEQVLT 85
Cdd:cd07814    1 TITIEREFDAPPELVWRALTDPELLAQwfgPTTTAEMDLRVGGRWFFFMTGPD---GEEGWVSGEVLEVEPPRRLVFTWA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491202538  86 ----APGIEVTSRWNLLPEPGGTRLRVTYSRFDPSiPLHRQWRTMLFSGAGPILNSLREMLDK 144
Cdd:cd07814   78 fsdeTPGPETTVTVTLEETGGGTRLTLTHSGFPEE-DAEQEAREGMEEGWTGTLDRLKALLEK 139
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 6-138 2.40e-11

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 57.74  E-value: 2.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491202538   6 DPTSITHSEYYPYPVDKVWDVLVSRELTAS-----QVKEVSDAPVEVGSTRVIVTHPQPavGFDGVVRTTYTSVEPYEHI 80
Cdd:COG3832    4 EDRTITIEREIDAPPERVWRAWTDPELLARwfgpkGWATVAEFDLRVGGRFRFRMRGPD--GEEFGFEGEVLEVEPPERL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491202538  81 EQ---VLTAPGIEVTSRWNLLPEPGGTRLRVTYSRFDPSiPLHRQWRTMLFSGAGPILNSL 138
Cdd:COG3832   82 VFtwgFEDDPEGESTVTVTLEPEGGGTRLTLTHTGFSAE-DRDAVLAEGMEEGWTESLDRL 141
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 17-114 2.80e-05

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: 41.15  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491202538   17 PYPVDKVWDVLVSRELTAsQVKEVSDAPVE--VGSTRVIVTHPQPaVGFDGVVrtTYTSVEPYEHIEQ--VLTAPGIEVT 92
Cdd:pfam08327   1 DAPPERVFRALTDPELLA-RWFTRTVAEMDlrPGGKFRFMRGPDG-EEFGGNG--TYLELVPPKRIVYtwRLDDWPEGGY 76

                          90       100
                  ....*....|....*....|....
gi 491202538   93 S--RWNLLPEPGGTRLRVTYSRFD 114
Cdd:pfam08327  77 StvTVELEEVGGGTRLTLTHTGEP 100
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 9-144 9.48e-18

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: 74.32  E-value: 9.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491202538   9 SITHSEYYPYPVDKVWDVLVSRELTAS---QVKEVSDAPVEVGSTRVIVTHPQpavGFDGVVRTTYTSVEPYEHIEQVLT 85
Cdd:cd07814    1 TITIEREFDAPPELVWRALTDPELLAQwfgPTTTAEMDLRVGGRWFFFMTGPD---GEEGWVSGEVLEVEPPRRLVFTWA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491202538  86 ----APGIEVTSRWNLLPEPGGTRLRVTYSRFDPSiPLHRQWRTMLFSGAGPILNSLREMLDK 144
Cdd:cd07814   78 fsdeTPGPETTVTVTLEETGGGTRLTLTHSGFPEE-DAEQEAREGMEEGWTGTLDRLKALLEK 139
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 6-138 2.40e-11

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 57.74  E-value: 2.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491202538   6 DPTSITHSEYYPYPVDKVWDVLVSRELTAS-----QVKEVSDAPVEVGSTRVIVTHPQPavGFDGVVRTTYTSVEPYEHI 80
Cdd:COG3832    4 EDRTITIEREIDAPPERVWRAWTDPELLARwfgpkGWATVAEFDLRVGGRFRFRMRGPD--GEEFGFEGEVLEVEPPERL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491202538  81 EQ---VLTAPGIEVTSRWNLLPEPGGTRLRVTYSRFDPSiPLHRQWRTMLFSGAGPILNSL 138
Cdd:COG3832   82 VFtwgFEDDPEGESTVTVTLEPEGGGTRLTLTHTGFSAE-DRDAVLAEGMEEGWTESLDRL 141
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 17-114 2.80e-05

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: 41.15  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491202538   17 PYPVDKVWDVLVSRELTAsQVKEVSDAPVE--VGSTRVIVTHPQPaVGFDGVVrtTYTSVEPYEHIEQ--VLTAPGIEVT 92
Cdd:pfam08327   1 DAPPERVFRALTDPELLA-RWFTRTVAEMDlrPGGKFRFMRGPDG-EEFGGNG--TYLELVPPKRIVYtwRLDDWPEGGY 76

                          90       100
                  ....*....|....*....|....
gi 491202538   93 S--RWNLLPEPGGTRLRVTYSRFD 114
Cdd:pfam08327  77 StvTVELEEVGGGTRLTLTHTGEP 100
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 8-143 3.69e-04

Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442114  Cd Length: 137  Bit Score: 38.30  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491202538   8 TSITHSEYYPYPVDKVWDVL--VSR------ELTASQVKEVSDAPVEVgstRVIvthpqpaVGFDGVVR--TTYTSVEPY 77
Cdd:COG2867    2 PTISRSVLVPYSAEQMFDLVadVERypeflpWCKAARVLERDGDEVVA---ELT-------VSFKGLREsfTTRNTLDPP 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491202538  78 EHIEQVLTAPGIEV-TSRWNLLPEP-GGTRLRVTYSrFDPSIPLHRqwrtMLFsgaGPILNS-LREMLD 143
Cdd:COG2867   72 ERIDFELVDGPFKHlEGRWRFEPLGeGGTKVTFDLD-FEFKSPLLG----ALL---GPVFNEaARRMVD 132
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 17-120 5.01e-04

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. The family also includes proteins which are involved in the binding/transport of lipids.


Pssm-ID: 397441  Cd Length: 125  Bit Score: 37.86  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491202538   17 PYPVDKVWDVLVSRELTASQVKEVSDapVEVGSTRVIVTHPQPAVGFDGVVRTTYTSVEPYEHIEQVLTAPGIEVTS-RW 95
Cdd:pfam03364   2 PAPAEQVWALVTDVERYPEFLPWCKS--VEVLERDGSLADWRVAFGGLRRSFTARVTLQPPERIEMVLVDGDFKRLEgSW 79

                          90       100
                  ....*....|....*....|....*.
gi 491202538   96 NLLPEPGGTRLRVTYS-RFDPSIPLH 120
Cdd:pfam03364  80 RFEPGGPGTRVKVTLElDFEFASPLP 105
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 19-119 5.01e-04

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. It also includes other proteins of the START superfamily.


Pssm-ID: 431388  Cd Length: 139  Bit Score: 37.85  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491202538   19 PVDKVWDVLVSRELTASQVKEVSDA-PVEVGSTRVIVTHPQPAVGFDGVVRTTYTSVEPYEH---IEQVLTAPGIEVTSR 94
Cdd:pfam10604   8 PPEQVWALLSDFENWPRWHPGVLRVeLEGGGGPLRGVVGTLRVGGRRGTVREELVEYDPAPRllaYRIVEPLGVANYVGT 87

                          90       100
                  ....*....|....*....|....*
gi 491202538   95 WNLLPEPGGTRLRVTYsRFDPSIPL 119
Cdd:pfam10604  88 WTVTPAGGGTRVTWTG-EFDGPPLG 111
SRPBCC_CalC_Aha1-like_6 cd08899
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 2-115 7.53e-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: 176908 [Multi-domain]  Cd Length: 157  Bit Score: 37.66  E-value: 7.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491202538   2 TSSGDPTSITHSEYYPYPVDKVWDVLVSRELTASQVKEVSDAPVEVGSTRVIVTHPQPAVgFDGVVrttyTSVEPYEHIE 81
Cdd:cd08899    5 TRLDGGATLRFERLLPAPIEDVWAALTDPERLARWFAPGTGDLRVGGRVEFVMDDEEGPN-ATGTI----LACEPPRLLA 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491202538  82 qvLTAPGIEVTS--RWNLLPEPGGTRLRVTYSRFDP 115
Cdd:cd08899   80 --FTWGEGGGESevRFELAPEGDGTRLTLTHRLLDE 113
SRPBCC_CalC_Aha1-like_5 cd08898
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 19-126 2.39e-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: 176907 [Multi-domain]  Cd Length: 145  Bit Score: 36.13  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491202538  19 PVDKVWDVLVSRElTASQVKEVSDAPVEVG-STRVIVTHPqpavGFDGVV-RTTYTSVEPYEHIEQVLTAPGIEVTSRWN 96
Cdd:cd08898   12 PRERVWRALTDPE-HFGQWFGVKLGPFVVGeGATGEITYP----GYEHGVfPVTVVEVDPPRRFSFRWHPPAIDPGEDYS 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491202538  97 ----------LLPEPGGTRLRVTYSRFDpSIPLHRQWRTM 126
Cdd:cd08898   87 aepstlveftLEPIAGGTLLTVTESGFD-ALPAERRAEAY 125
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 10-127 8.81e-03

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176854  Cd Length: 141  Bit Score: 34.61  E-value: 8.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491202538  10 ITHSEYYPYPVDKVWDVLVSRELTASQVKEVSDA----PVEVGSTRVIVTHPQPAVGFDGVVRTTYTSVEPYEHIEQVLT 85
Cdd:cd07812    1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVevlgGGEGGVGARFVGGRKGGRRLTLTSEVTEVDPPRPGRFRVTGG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 491202538  86 APGIEVTSRWNLLPEP-GGTRLRVTYsRFDPSIPLHRQWRTML 127
Cdd:cd07812   81 GGGVDGTGEWRLEPEGdGGTRVTYTV-EYDPPGPLLKVFALLL 122
 
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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