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Conserved domains on  [gi|446370085|ref|WP_000447940|]
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MULTISPECIES: hypothetical protein [Leptospira]

Protein Classification

SRPBCC family protein( domain architecture ID 51693)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 3-150 1.42e-05

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.


The actual alignment was detected with superfamily member cd07814:

Pssm-ID: 472699 [Multi-domain]  Cd Length: 139  Bit Score: 42.35  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370085   3 TIRFSILIDADVKTVWhKMLEDSsyRIWAKEFHEGSYFEGSWEKGSEIRFLAQDENDKPQGMYAKIRENIPYQFISIEHI 82
Cdd:cd07814    1 TITIEREFDAPPELVW-RALTDP--ELLAQWFGPTTTAEMDLRVGGRWFFFMTGPDGEEGWVSGEVLEVEPPRRLVFTWA 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370085  83 GLISGGVIDTESEevkkwtpafenYTFQEESnGKTKLIIEMQTI------EEYKSMFEEMWPKALKSLKELCEK 150
Cdd:cd07814   78 FSDETPGPETTVT-----------VTLEETG-GGTRLTLTHSGFpeedaeQEAREGMEEGWTGTLDRLKALLEK 139
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 3-150 1.42e-05

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: 42.35  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370085   3 TIRFSILIDADVKTVWhKMLEDSsyRIWAKEFHEGSYFEGSWEKGSEIRFLAQDENDKPQGMYAKIRENIPYQFISIEHI 82
Cdd:cd07814    1 TITIEREFDAPPELVW-RALTDP--ELLAQWFGPTTTAEMDLRVGGRWFFFMTGPDGEEGWVSGEVLEVEPPRRLVFTWA 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370085  83 GLISGGVIDTESEevkkwtpafenYTFQEESnGKTKLIIEMQTI------EEYKSMFEEMWPKALKSLKELCEK 150
Cdd:cd07814   78 FSDETPGPETTVT-----------VTLEETG-GGTRLTLTHSGFpeedaeQEAREGMEEGWTGTLDRLKALLEK 139
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 1-145 1.10e-03

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 36.94  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370085   1 METIRFSILIDADVKTVWHKMLEDSSYRIWAKEFHEGSYFEGSWEKGSEIRFLAQDENDKPQGMYAKIRENIPYQFISIE 80
Cdd:COG3832    5 DRTITIEREIDAPPERVWRAWTDPELLARWFGPKGWATVAEFDLRVGGRFRFRMRGPDGEEFGFEGEVLEVEPPERLVFT 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446370085  81 HiglisggVIDTESEEVKKWTpafenYTFqEESNGKTKLIIEMQTIEE------YKSMFEEMWPKALKSLK 145
Cdd:COG3832   85 W-------GFEDDPEGESTVT-----VTL-EPEGGGTRLTLTHTGFSAedrdavLAEGMEEGWTESLDRLK 142
 
Name Accession Description Interval E-value
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 3-150 1.42e-05

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: 42.35  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370085   3 TIRFSILIDADVKTVWhKMLEDSsyRIWAKEFHEGSYFEGSWEKGSEIRFLAQDENDKPQGMYAKIRENIPYQFISIEHI 82
Cdd:cd07814    1 TITIEREFDAPPELVW-RALTDP--ELLAQWFGPTTTAEMDLRVGGRWFFFMTGPDGEEGWVSGEVLEVEPPRRLVFTWA 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446370085  83 GLISGGVIDTESEevkkwtpafenYTFQEESnGKTKLIIEMQTI------EEYKSMFEEMWPKALKSLKELCEK 150
Cdd:cd07814   78 FSDETPGPETTVT-----------VTLEETG-GGTRLTLTHSGFpeedaeQEAREGMEEGWTGTLDRLKALLEK 139
SRPBCC_4 cd07822
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 3-75 2.32e-04

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: 176864  Cd Length: 141  Bit Score: 38.85  E-value: 2.32e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446370085   3 TIRFSILIDADVKTVWHKMLEDSSYRIW--AKEFHEGSyfegSWEKGSEIRFLAQDENDKPQGMYAKIRENIPYQ 75
Cdd:cd07822    1 TISTEIEINAPPEKVWEVLTDFPSYPEWnpFVRSATGL----SLALGARLRFVVKLPGGPPRSFKPRVTEVEPPR 71
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 1-145 1.10e-03

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 36.94  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370085   1 METIRFSILIDADVKTVWHKMLEDSSYRIWAKEFHEGSYFEGSWEKGSEIRFLAQDENDKPQGMYAKIRENIPYQFISIE 80
Cdd:COG3832    5 DRTITIEREIDAPPERVWRAWTDPELLARWFGPKGWATVAEFDLRVGGRFRFRMRGPDGEEFGFEGEVLEVEPPERLVFT 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446370085  81 HiglisggVIDTESEEVKKWTpafenYTFqEESNGKTKLIIEMQTIEE------YKSMFEEMWPKALKSLK 145
Cdd:COG3832   85 W-------GFEDDPEGESTVT-----VTL-EPEGGGTRLTLTHTGFSAedrdavLAEGMEEGWTESLDRLK 142
 
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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