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Conserved domains on  [gi|624388176|gb|KBT47025|]
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hypothetical protein Z548_00907 [Mycobacterium tuberculosis 2233BH]

Protein Classification

SRPBCC family protein( domain architecture ID 10566222)

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

CATH:  3.30.530.20
PubMed:  18922149
SCOP:  3000738

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 7-142 3.78e-21

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: 82.92  E-value: 3.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176    7 SIDVPLPPEEAWMHASDLTRYREWLTihKVWRSKLPEVLEKGTVVESYVEVKGMPNRIKWTIVRYKpPEGMTLNGDGV-- 84
Cdd:pfam10604   2 SIEIAAPPEQVWALLSDFENWPRWHP--GVLRVELEGGGGPLRGVVGTLRVGGRRGTVREELVEYD-PAPRLLAYRIVep 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176   85 -GGVKVKLIAKVAPKEHGSVVSFDVHLGGPALLGPIGMIVAA-ALRADIRESLQNFVTVF 142
Cdd:pfam10604  79 lGVANYVGTWTVTPAGGGTRVTWTGEFDGPPLGGPFRDPAAArAVKGDYRAGLDRLKAVL 138
 
Name Accession Description Interval E-value
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 7-142 3.78e-21

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: 82.92  E-value: 3.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176    7 SIDVPLPPEEAWMHASDLTRYREWLTihKVWRSKLPEVLEKGTVVESYVEVKGMPNRIKWTIVRYKpPEGMTLNGDGV-- 84
Cdd:pfam10604   2 SIEIAAPPEQVWALLSDFENWPRWHP--GVLRVELEGGGGPLRGVVGTLRVGGRRGTVREELVEYD-PAPRLLAYRIVep 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176   85 -GGVKVKLIAKVAPKEHGSVVSFDVHLGGPALLGPIGMIVAA-ALRADIRESLQNFVTVF 142
Cdd:pfam10604  79 lGVANYVGTWTVTPAGGGTRVTWTGEFDGPPLGGPFRDPAAArAVKGDYRAGLDRLKAVL 138
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 4-138 3.52e-11

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: 57.33  E-value: 3.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176   4 LSGSIDVPLPPEEAWMHASDLTRYREWLTIHKVWRSKLPEVLEKGTVVESYVEVkGMPNRIKWTIVRYKPPEGMTLNGDG 83
Cdd:cd07812    1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARFVGGRKG-GRRLTLTSEVTEVDPPRPGRFRVTG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 624388176  84 VG-GVKVKLIAKVAPK-EHGSVVSFDVHL-GGPALLGPIGMIVAAALRADIRESLQNF 138
Cdd:cd07812   80 GGgGVDGTGEWRLEPEgDGGTRVTYTVEYdPPGPLLKVFALLLAGALKRELAALLRAL 137
CoxG COG3427
Carbon monoxide dehydrogenase subunit CoxG [Energy production and conversion];
3-143 6.89e-07

Carbon monoxide dehydrogenase subunit CoxG [Energy production and conversion];


Pssm-ID: 442653  Cd Length: 145  Bit Score: 45.62  E-value: 6.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176   3 KLSGSIDVPLPPEEAWMHASDLtryrewltihKVWRSKLP--EVLE-------KGTVVesyVEVKGMPNRIK--WTIVRY 71
Cdd:COG3427    2 ELSGSFTVPAPPEQVWAALNDP----------EVLAACIPgcESLEvvgdteyEATVK---VKVGPVKATFKgeVTLSEL 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 624388176  72 KPPEGMTLNGDGVGG----VKVKLIAKVAPKEHGSVVSF--DVHLGGP-ALLGPiGMIVAAAlRADIRESLQNFVTVFA 143
Cdd:COG3427   69 DPPESYTLTGEGKGGragfAKGTATVTLEPDGGGTRLTYdaDADVGGKlAQLGR-RLIDGVA-KKLADQFFENLAAKLE 145
 
Name Accession Description Interval E-value
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 7-142 3.78e-21

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: 82.92  E-value: 3.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176    7 SIDVPLPPEEAWMHASDLTRYREWLTihKVWRSKLPEVLEKGTVVESYVEVKGMPNRIKWTIVRYKpPEGMTLNGDGV-- 84
Cdd:pfam10604   2 SIEIAAPPEQVWALLSDFENWPRWHP--GVLRVELEGGGGPLRGVVGTLRVGGRRGTVREELVEYD-PAPRLLAYRIVep 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176   85 -GGVKVKLIAKVAPKEHGSVVSFDVHLGGPALLGPIGMIVAA-ALRADIRESLQNFVTVF 142
Cdd:pfam10604  79 lGVANYVGTWTVTPAGGGTRVTWTGEFDGPPLGGPFRDPAAArAVKGDYRAGLDRLKAVL 138
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 4-138 3.52e-11

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: 57.33  E-value: 3.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176   4 LSGSIDVPLPPEEAWMHASDLTRYREWLTIHKVWRSKLPEVLEKGTVVESYVEVkGMPNRIKWTIVRYKPPEGMTLNGDG 83
Cdd:cd07812    1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARFVGGRKG-GRRLTLTSEVTEVDPPRPGRFRVTG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 624388176  84 VG-GVKVKLIAKVAPK-EHGSVVSFDVHL-GGPALLGPIGMIVAAALRADIRESLQNF 138
Cdd:cd07812   80 GGgGVDGTGEWRLEPEgDGGTRVTYTVEYdPPGPLLKVFALLLAGALKRELAALLRAL 137
SRPBCC_10 cd08865
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 4-137 3.05e-08

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: 49.20  E-value: 3.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176   4 LSGSIDVPLPPEEAWMHASDLTRYREWL-TIHKV-WRSklPEVLEKGTVVESYVEVKGMPNRIKWTIVRYKPPEGMTLNG 81
Cdd:cd08865    1 VEESIVIERPVEEVFAYLADFENAPEWDpGVVEVeKIT--DGPVGVGTRYHQVRKFLGRRIELTYEITEYEPGRRVVFRG 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 624388176  82 DGvGGVKVKLIAKVAPKEHGSVVSFDVHLGGPALLGPIGMIVAAALRADIRESLQN 137
Cdd:cd08865   79 SS-GPFPYEDTYTFEPVGGGTRVRYTAELEPGGFARLLDPLMAPAFRRRARAALEN 133
CoxG COG3427
Carbon monoxide dehydrogenase subunit CoxG [Energy production and conversion];
3-143 6.89e-07

Carbon monoxide dehydrogenase subunit CoxG [Energy production and conversion];


Pssm-ID: 442653  Cd Length: 145  Bit Score: 45.62  E-value: 6.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176   3 KLSGSIDVPLPPEEAWMHASDLtryrewltihKVWRSKLP--EVLE-------KGTVVesyVEVKGMPNRIK--WTIVRY 71
Cdd:COG3427    2 ELSGSFTVPAPPEQVWAALNDP----------EVLAACIPgcESLEvvgdteyEATVK---VKVGPVKATFKgeVTLSEL 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 624388176  72 KPPEGMTLNGDGVGG----VKVKLIAKVAPKEHGSVVSF--DVHLGGP-ALLGPiGMIVAAAlRADIRESLQNFVTVFA 143
Cdd:COG3427   69 DPPESYTLTGEGKGGragfAKGTATVTLEPDGGGTRLTYdaDADVGGKlAQLGR-RLIDGVA-KKLADQFFENLAAKLE 145
CoxG cd05018
Carbon monoxide dehydrogenase subunit G (CoxG); CoxG has been shown, in Oligotropha ...
 3-139 3.34e-05

Carbon monoxide dehydrogenase subunit G (CoxG); CoxG has been shown, in Oligotropha carboxidovorans, to anchor the carbon monoxide (CO) dehydrogenase to the cytoplasmic membrane. The gene encoding CoxG is part of the Cox cluster (coxBCMSLDEFGHIK) located on a low-copy-number, circular, megaplasmid pHCG3. This cluster includes genes encoding subunits of CO dehydrogenase and several accessory components involved in the utilization of CO. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands.


Pssm-ID: 176853  Cd Length: 144  Bit Score: 41.03  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176   3 KLSGSIDVPLPPEEAWMHASDltryrewltihkvwrsklPEVLEK---GtvVESYvEVKGmPNRIKWTIV--------RY 71
Cdd:cd05018    2 KISGEFRIPAPPEEVWAALND------------------PEVLARcipG--CESL-EKIG-PNEYEATVKlkvgpvkgTF 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176  72 K---------PPEGMTLNGDGVGG---VKVKLIAKVAPKEHGSVV--SFDVHLGGP-ALLGPIgMIVAAAlRADIRESLQ 136
Cdd:cd05018   60 KgkvelsdldPPESYTITGEGKGGagfVKGTARVTLEPDGGGTRLtyTADAQVGGKlAQLGSR-LIDGAA-RKLINQFFE 137


                 ...
gi 624388176 137 NFV 139
Cdd:cd05018  138 NLA 140
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-139 5.89e-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: 37.53  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624388176   1 MAKLSGSIDVPLPPEEAWMHASDLTRYREWLTihkvWRSKLpEVLEK-GTVVESYVEVKGMPNRIKWTI-VRYKPPEGMT 78
Cdd:COG2867    1 MPTISRSVLVPYSAEQMFDLVADVERYPEFLP----WCKAA-RVLERdGDEVVAELTVSFKGLRESFTTrNTLDPPERID 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 624388176  79 ---LNGD---GVGGVKVKLIAkvapkEHGSVVSFDVH--LGGPALlgpiGMIVAAALRADIRESLQNFV 139
Cdd:COG2867   76 felVDGPfkhLEGRWRFEPLG-----EGGTKVTFDLDfeFKSPLL----GALLGPVFNEAARRMVDAFK 135
 
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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