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Conserved domains on  [gi|1272484564|gb|PHX81941|]
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hypothetical protein CK540_00405 [Thermoleophilia bacterium]

Protein Classification

SRPBCC family protein( domain architecture ID 10790656)

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 COG4276
Ligand-binding SRPBCC domain [General function prediction only];
1-153 5.39e-41

Ligand-binding SRPBCC domain [General function prediction only];


:

Pssm-ID: 443417  Cd Length: 153  Bit Score: 134.21  E-value: 5.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   1 MPTFERSIEIAAPIKSVYDFHLDTRNAARIASDGQEFVSITG-EFPLVEGGEVELKVKMKPMPgtQTWLVRVTELAEPVL 79
Cdd:COG4276     1 MPTFERETRIPAPLEEVFDFHSRPDNLERLTPPWMGERILSGvPGGLELGDRVTYRLRHFGIP--QRWTSEITEVEPPHY 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1272484564  80 VVDEMLKGPFAKFRHEHRFAPSAhGGTILTDHIEWALPGGAAGRLVA-PIAAKLMEKSFVERQAATKRILEADAA 153
Cdd:COG4276    79 FVDEQVKGPFKSWRHEHRFEEVG-GGTLMTDRVEYELPLGLLGRLAHgLFVKKYLERIFAYRHRVLKELLESHAK 152
 
Name Accession Description Interval E-value
SRPBCC COG4276
Ligand-binding SRPBCC domain [General function prediction only];
1-153 5.39e-41

Ligand-binding SRPBCC domain [General function prediction only];


Pssm-ID: 443417  Cd Length: 153  Bit Score: 134.21  E-value: 5.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   1 MPTFERSIEIAAPIKSVYDFHLDTRNAARIASDGQEFVSITG-EFPLVEGGEVELKVKMKPMPgtQTWLVRVTELAEPVL 79
Cdd:COG4276     1 MPTFERETRIPAPLEEVFDFHSRPDNLERLTPPWMGERILSGvPGGLELGDRVTYRLRHFGIP--QRWTSEITEVEPPHY 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1272484564  80 VVDEMLKGPFAKFRHEHRFAPSAhGGTILTDHIEWALPGGAAGRLVA-PIAAKLMEKSFVERQAATKRILEADAA 153
Cdd:COG4276    79 FVDEQVKGPFKSWRHEHRFEEVG-GGTLMTDRVEYELPLGLLGRLAHgLFVKKYLERIFAYRHRVLKELLESHAK 152
SRPBCC_3 cd07820
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 4-142 1.31e-35

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the 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: 176862  Cd Length: 137  Bit Score: 120.02  E-value: 1.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   4 FERSIEIAAPIKSVYDFHLDTRNAARIASDGQEFVsITGEFPLVEGGEVELKVKMKPMPGTQTWLVRVTELAEPVLVVDE 83
Cdd:cd07820     1 LERSTVIPAPIEEVFDFHSRPDNLERLTPPWLEFA-VLGRTPGLIYGGARVTYRLRHFGIPQRWTTEITEVEPPRRFVDE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1272484564  84 MLKGPFAKFRHEHRFAPSAhGGTILTDHIEWALPGGAAGRLVAPIAAKLMEKSFVERQA 142
Cdd:cd07820    80 QVSGPFRSWRHTHRFEAIG-GGTLMTDRVEYRLPLGPLGRLAAPLVVRRYLERFFAYRH 137
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 6-149 1.26e-03

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: 37.08  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   6 RSIEIAAPIKSVYDFHLDTRNAARIASdgqEFVSITGEFPLVEGGEVELKVKMKPMPGTQTWlvRVTEL-AEPVLVVDEM 84
Cdd:pfam10604   1 VSIEIAAPPEQVWALLSDFENWPRWHP---GVLRVELEGGGGPLRGVVGTLRVGGRRGTVRE--ELVEYdPAPRLLAYRI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1272484564  85 LKG-PFAKFRHEHRFAPSAHGGTiltdhIEWAL---PGGAAGRLVAPIAAKLMEKSFVERQAATKRILE 149
Cdd:pfam10604  76 VEPlGVANYVGTWTVTPAGGGTR-----VTWTGefdGPPLGGPFRDPAAARAVKGDYRAGLDRLKAVLE 139
 
Name Accession Description Interval E-value
SRPBCC COG4276
Ligand-binding SRPBCC domain [General function prediction only];
1-153 5.39e-41

Ligand-binding SRPBCC domain [General function prediction only];


Pssm-ID: 443417  Cd Length: 153  Bit Score: 134.21  E-value: 5.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   1 MPTFERSIEIAAPIKSVYDFHLDTRNAARIASDGQEFVSITG-EFPLVEGGEVELKVKMKPMPgtQTWLVRVTELAEPVL 79
Cdd:COG4276     1 MPTFERETRIPAPLEEVFDFHSRPDNLERLTPPWMGERILSGvPGGLELGDRVTYRLRHFGIP--QRWTSEITEVEPPHY 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1272484564  80 VVDEMLKGPFAKFRHEHRFAPSAhGGTILTDHIEWALPGGAAGRLVA-PIAAKLMEKSFVERQAATKRILEADAA 153
Cdd:COG4276    79 FVDEQVKGPFKSWRHEHRFEEVG-GGTLMTDRVEYELPLGLLGRLAHgLFVKKYLERIFAYRHRVLKELLESHAK 152
SRPBCC_3 cd07820
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 4-142 1.31e-35

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the 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: 176862  Cd Length: 137  Bit Score: 120.02  E-value: 1.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   4 FERSIEIAAPIKSVYDFHLDTRNAARIASDGQEFVsITGEFPLVEGGEVELKVKMKPMPGTQTWLVRVTELAEPVLVVDE 83
Cdd:cd07820     1 LERSTVIPAPIEEVFDFHSRPDNLERLTPPWLEFA-VLGRTPGLIYGGARVTYRLRHFGIPQRWTTEITEVEPPRRFVDE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1272484564  84 MLKGPFAKFRHEHRFAPSAhGGTILTDHIEWALPGGAAGRLVAPIAAKLMEKSFVERQA 142
Cdd:cd07820    80 QVSGPFRSWRHTHRFEAIG-GGTLMTDRVEYRLPLGPLGRLAAPLVVRRYLERFFAYRH 137
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
1-156 9.84e-14

Uncharacterized protein, contains SRPBCC domain [Function unknown];


Pssm-ID: 444363  Cd Length: 154  Bit Score: 64.55  E-value: 9.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   1 MPTFERSIEIAAPIKSVYDFHLDTRNAARIASdgqEFVSITgefpLVEGGEVELKVKMkPMPGTQTWLVRVTELAEPVLV 80
Cdd:COG5637     1 MTTVEKSITINAPVEEVYAYWRDFENLPRFMK---GVESVT----VLDDTRSHWVAKG-PLGVTVEWDAEITEQVPGERI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564  81 VDEMLKGPFakfrhEH----RFAPSAHGGTILTDHIEWALPGGAAGRLVapiaAKLMEKsFVERQAAT-----KRILEAD 151
Cdd:COG5637    73 AWRSVEGDI-----PNagvvRFEPAGGRGTRVTVTIEYDPPGGLLGKAL----AKLFGG-VPERQLREdlerfKQLIETG 142


                  ....*
gi 1272484564 152 AAAQS 156
Cdd:COG5637   143 EIPTG 147
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-140 3.42e-09

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 52.17  E-value: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   1 MPTFERSIEIAAPIKSVYDFHLDTRN---------AARIASDgqefvsitgefplvEGGEVELKVKMKPMPGTQTWLVRV 71
Cdd:COG2867     1 MPTISRSVLVPYSAEQMFDLVADVERypeflpwckAARVLER--------------DGDEVVAELTVSFKGLRESFTTRN 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1272484564  72 TeLAEPVLVVDEMLKGPFAKFRHEHRFAPSAHGGTILTDHIE----WALPGGAAGRLVAPIAAKLMEkSFVER 140
Cdd:COG2867    67 T-LDPPERIDFELVDGPFKHLEGRWRFEPLGEGGTKVTFDLDfefkSPLLGALLGPVFNEAARRMVD-AFKKR 137
SRPBCC_10 cd08865
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 4-150 1.46e-07

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the 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: 176874  Cd Length: 140  Bit Score: 47.66  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   4 FERSIEIAAPIKSVYDFHLDTRNAARIASDGQEFVSITGEfPLVEGGEVELKVKMkpMPGTQTWLVRVTELAEPVLVVDE 83
Cdd:cd08865     1 VEESIVIERPVEEVFAYLADFENAPEWDPGVVEVEKITDG-PVGVGTRYHQVRKF--LGRRIELTYEITEYEPGRRVVFR 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1272484564  84 MLKGPFAkFRHEHRFAPSAhGGTILTDHIEwALPGGAAgRLVAPIAAKLMEKSFVERQAATKRILEA 150
Cdd:cd08865    78 GSSGPFP-YEDTYTFEPVG-GGTRVRYTAE-LEPGGFA-RLLDPLMAPAFRRRARAALENLKALLEA 140
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 4-148 1.04e-06

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: 45.39  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   4 FERSIEIAAPIKSVYDFHLDTRNAARIASDGQEFVSITGEFPlvEGGEVELKVKMKPMPGTQTWLVRVTELAEPVLVVDE 83
Cdd:cd07812     1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEG--GVGARFVGGRKGGRRLTLTSEVTEVDPPRPGRFRVT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1272484564  84 MLKGPFaKFRHEHRFAPSAHGGTILTDHIEwALPGGAAGRLVAPIAAKLMEKSFVERQAATKRIL 148
Cdd:cd07812    79 GGGGGV-DGTGEWRLEPEGDGGTRVTYTVE-YDPPGPLLKVFALLLAGALKRELAALLRALKARL 141
SRPBCC_8 cd07817
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 5-139 1.52e-06

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the 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: 176859  Cd Length: 139  Bit Score: 44.90  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   5 ERSIEIAAPIKSVYDFHLDTRNAARIASdGQEFVSITGEfplvegGEVELKVKMkPMPGTQTWLVRVTELAEPVLVVDEM 84
Cdd:cd07817     3 EKSITVNVPVEEVYDFWRDFENLPRFMS-HVESVEQLDD------TRSHWKAKG-PAGLSVEWDAEITEQVPNERIAWRS 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1272484564  85 LKGPfakfrHEH----RFAPSAHGGTILTDHIEWALPGGAAGRLVAPIAAKLME----------KSFVE 139
Cdd:cd07817    75 VEGA-----DPNagsvRFRPAPGRGTRVTLTIEYEPPGGAEGAAVAGLLGGEPErqlredlrrfKQLVE 138
SRPBCC_Smu440-like cd08862
Ligand-binding SRPBCC domain of Streptococcus mutans Smu.440 and related proteins; This family ...
 4-150 1.07e-03

Ligand-binding SRPBCC domain of Streptococcus mutans Smu.440 and related proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Streptococcus mutans Smu.440 and related proteins. This domain belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Streptococcus mutans is a dental pathogen, and the leading cause of dental caries. In this pathogen, the gene encoding Smu.440 is in the same operon as the gene encoding SMU.441, a member of the MarR protein family of transcriptional regulators involved in multiple antibiotic resistance. It has been suggested that SMU.440 is involved in polyketide-like antibiotic resistance.


Pssm-ID: 176871  Cd Length: 138  Bit Score: 36.95  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   4 FERSIEIAAPIKSVYDFHLDTRNAARIASDgQEFVSITGEFPlveggEVELKVKMKPmPGTQTWLVRVTELAEPVLVVDe 83
Cdd:cd08862     3 FEATIVIDAPPERVWAVLTDVENWPAWTPS-VETVRLEGPPP-----AVGSSFKMKP-PGLVRSTFTVTELRPGHSFTW- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1272484564  84 MLKGPFAKFRHEHRFAPSAHGGTILTDHIEWAlpgGAAGRLVAPIAAKLMEKSFVERQAATKRILEA 150
Cdd:cd08862    75 TGPAPGISAVHRHEFEAKPDGGVRVTTSESLS---GPLAFLFGLFVGKKLRALLPEWLEGLKAAAEQ 138
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 6-149 1.26e-03

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: 37.08  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   6 RSIEIAAPIKSVYDFHLDTRNAARIASdgqEFVSITGEFPLVEGGEVELKVKMKPMPGTQTWlvRVTEL-AEPVLVVDEM 84
Cdd:pfam10604   1 VSIEIAAPPEQVWALLSDFENWPRWHP---GVLRVELEGGGGPLRGVVGTLRVGGRRGTVRE--ELVEYdPAPRLLAYRI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1272484564  85 LKG-PFAKFRHEHRFAPSAHGGTiltdhIEWAL---PGGAAGRLVAPIAAKLMEKSFVERQAATKRILE 149
Cdd:pfam10604  76 VEPlGVANYVGTWTVTPAGGGTR-----VTWTGefdGPPLGGPFRDPAAARAVKGDYRAGLDRLKAVLE 139
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 10-135 1.26e-03

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: 36.71  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564  10 IAAPIKSVYDFHLDTRNAARIASDGQEfVSITGEfplvEGGEVELKVKMKPMpgTQTWLVRVTELaEPVLVVDEMLKGPF 89
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKS-VEVLER----DGSLADWRVAFGGL--RRSFTARVTLQ-PPERIEMVLVDGDF 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1272484564  90 AKFRHEHRFAPSAhGGTILTDHIEWALPGGaaGRLVAPIAAKLMEK 135
Cdd:pfam03364  73 KRLEGSWRFEPGG-PGTRVKVTLELDFEFA--SPLPGALLGFVFRR 115
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 1-109 3.65e-03

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 35.78  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1272484564   1 MPTFERSIEIAAPIKSVYDFHLDtrnAARIAS-DGQEFVSITGEFPLVEGGEVELkvKMKPMPGTQTWL-VRVTELAEPV 78
Cdd:COG3832     5 DRTITIEREIDAPPERVWRAWTD---PELLARwFGPKGWATVAEFDLRVGGRFRF--RMRGPDGEEFGFeGEVLEVEPPE 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1272484564  79 LVV--DEMLKGPFAKFRHEHRFAPSAhGGTILT 109
Cdd:COG3832    80 RLVftWGFEDDPEGESTVTVTLEPEG-GGTRLT 111
 
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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