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Conserved domains on  [gi|685371973|ref|XP_009119627|]
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uncharacterized protein LOC103844579 isoform X2 [Brassica rapa]

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 ...
 84-205 3.80e-27

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 cd07817:

Pssm-ID: 472699  Cd Length: 139  Bit Score: 100.37  E-value: 3.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685371973  84 DITVKMVVDAPASVAYKLYADRELFPKWLPFLSSVEAVegSPDLSRYLVKFEsFGKKFEyyFLAKNLEPIPDRKLHWRSI 163
Cdd:cd07817    1 TVEKSITVNVPVEEVYDFWRDFENLPRFMSHVESVEQL--DDTRSHWKAKGP-AGLSVE--WDAEITEQVPNERIAWRSV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 685371973 164 EGFA-NRGSVRFFQRGPSSCLVEINFSFEVPHAFAPVAFVSLL 205
Cdd:cd07817   76 EGADpNAGSVRFRPAPGRGTRVTLTIEYEPPGGAEGAAVAGLL 118
 
Name Accession Description Interval E-value
SRPBCC_8 cd07817
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 84-205 3.80e-27

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: 100.37  E-value: 3.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685371973  84 DITVKMVVDAPASVAYKLYADRELFPKWLPFLSSVEAVegSPDLSRYLVKFEsFGKKFEyyFLAKNLEPIPDRKLHWRSI 163
Cdd:cd07817    1 TVEKSITVNVPVEEVYDFWRDFENLPRFMSHVESVEQL--DDTRSHWKAKGP-AGLSVE--WDAEITEQVPNERIAWRSV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 685371973 164 EGFA-NRGSVRFFQRGPSSCLVEINFSFEVPHAFAPVAFVSLL 205
Cdd:cd07817   76 EGADpNAGSVRFRPAPGRGTRVTLTIEYEPPGGAEGAAVAGLL 118
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
82-197 1.14e-19

Uncharacterized protein, contains SRPBCC domain [Function unknown];


Pssm-ID: 444363  Cd Length: 154  Bit Score: 81.49  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685371973  82 WQDITVKMVVDAPASVAYKLYADRELFPKWLPFLSSVEAVEGspDLSRYLVKFeSFGKKFEyyFLAKNLEPIPDRKLHWR 161
Cdd:COG5637    1 MTTVEKSITINAPVEEVYAYWRDFENLPRFMKGVESVTVLDD--TRSHWVAKG-PLGVTVE--WDAEITEQVPGERIAWR 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 685371973 162 SIEG-FANRGSVRFFQRGPSSCLVEINFSFEVPHAFA 197
Cdd:COG5637   76 SVEGdIPNAGVVRFEPAGGRGTRVTVTIEYDPPGGLL 112
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 91-207 5.89e-12

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: 60.59  E-value: 5.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685371973   91 VDAPASVAYKLYADRELFPKWLPFLSSVEAVEGSPDLSRYLVKFESFGKKFEyyflAKNLEPIPDRKlHWRSIEGFANRG 170
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSLADWRVAFGGLRRSFT----ARVTLQPPERI-EMVLVDGDFKRL 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 685371973  171 SVRF-FQRGPSSCLVEINFSFEVPHAFAPVAFVSLLVF 207
Cdd:pfam03364  76 EGSWrFEPGGPGTRVKVTLELDFEFASPLPGALLGFVF 113
 
Name Accession Description Interval E-value
SRPBCC_8 cd07817
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 84-205 3.80e-27

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: 100.37  E-value: 3.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685371973  84 DITVKMVVDAPASVAYKLYADRELFPKWLPFLSSVEAVegSPDLSRYLVKFEsFGKKFEyyFLAKNLEPIPDRKLHWRSI 163
Cdd:cd07817    1 TVEKSITVNVPVEEVYDFWRDFENLPRFMSHVESVEQL--DDTRSHWKAKGP-AGLSVE--WDAEITEQVPNERIAWRSV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 685371973 164 EGFA-NRGSVRFFQRGPSSCLVEINFSFEVPHAFAPVAFVSLL 205
Cdd:cd07817   76 EGADpNAGSVRFRPAPGRGTRVTLTIEYEPPGGAEGAAVAGLL 118
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
82-197 1.14e-19

Uncharacterized protein, contains SRPBCC domain [Function unknown];


Pssm-ID: 444363  Cd Length: 154  Bit Score: 81.49  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685371973  82 WQDITVKMVVDAPASVAYKLYADRELFPKWLPFLSSVEAVEGspDLSRYLVKFeSFGKKFEyyFLAKNLEPIPDRKLHWR 161
Cdd:COG5637    1 MTTVEKSITINAPVEEVYAYWRDFENLPRFMKGVESVTVLDD--TRSHWVAKG-PLGVTVE--WDAEITEQVPGERIAWR 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 685371973 162 SIEG-FANRGSVRFFQRGPSSCLVEINFSFEVPHAFA 197
Cdd:COG5637   76 SVEGdIPNAGVVRFEPAGGRGTRVTVTIEYDPPGGLL 112
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 91-207 5.89e-12

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: 60.59  E-value: 5.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685371973   91 VDAPASVAYKLYADRELFPKWLPFLSSVEAVEGSPDLSRYLVKFESFGKKFEyyflAKNLEPIPDRKlHWRSIEGFANRG 170
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSLADWRVAFGGLRRSFT----ARVTLQPPERI-EMVLVDGDFKRL 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 685371973  171 SVRF-FQRGPSSCLVEINFSFEVPHAFAPVAFVSLLVF 207
Cdd:pfam03364  76 EGSWrFEPGGPGTRVKVTLELDFEFASPLPGALLGFVF 113
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 85-191 1.53e-07

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 48.70  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685371973  85 ITVKMVVDAPASVAYKLYADRELFPKWLPFLSSVEAVEGSPD--LSRYLVKFESFGKKF-EYYFLaknlepIPDRKLHWR 161
Cdd:COG2867    4 ISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDevVAELTVSFKGLRESFtTRNTL------DPPERIDFE 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 685371973 162 SIEG-F-ANRGSVRFFQRGPSSCLVEINFSFE 191
Cdd:COG2867   78 LVDGpFkHLEGRWRFEPLGEGGTKVTFDLDFE 109
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 83-205 3.17e-06

Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid receptors (RCARs), and related proteins; The PYR/PYL/RCAR-like 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. PYR/PYL/RCAR plant proteins are receptors involved in signal transduction. They bind abscisic acid (ABA) and mediate its signaling. ABA is a vital plant hormone, which regulates plant growth, development, and response to environmental stresses. Upon binding ABA, these plant proteins interact with a type 2C protein phosphatase (PP2C), such as ABI1 and ABI2, and inhibit their activity. When ABA is bound, a loop (designated the gate/CL2 loop) closes over the ligand binding pocket, resulting in the weakening of the inactive PYL dimer and facilitating type 2C protein phosphatase binding. In the ABA:PYL1:ABI1 complex, the gate blocks substrate access to the phosphatase active site. A conserved Trp from PP2C inserts into PYL to lock the receptor in a closed formation. This group also contains Methylobacterium extorquens AM1 MxaD. The mxaD gene is located within the mxaFJGIR(S)ACKLDEHB cluster which encodes proteins involved in methanol oxidation. MxaD may participate in the periplasmic electron transport chain for oxidation of methanol. Mutants lacking MxaD exhibit a reduced growth on methanol, and a lower rate of respiration with methanol.


Pssm-ID: 176863 [Multi-domain]  Cd Length: 140  Bit Score: 45.01  E-value: 3.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685371973  83 QDITVKMVVDAPASVAYKLYADRELFPKWLPFLSSVEAVEGSPDL-SRYLVKFESFGK---KFEYYflaknlEPiPDRKL 158
Cdd:cd07821    1 AKVTVSVTIDAPADKVWALLSDFGGLHKWHPAVASCELEGGGPGVgAVRTVTLKDGGTvreRLLAL------DD-AERRY 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 685371973 159 HWRSIEG---FAN-RGSVRFFQRGPSSCLVEINFSFEVPHAFAPVAFVSLL 205
Cdd:cd07821   74 SYRIVEGplpVKNyVATIRVTPEGDGGTRVTWTAEFDPPEGLTDELARAFL 124
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 85-201 1.87e-04

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: 40.00  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685371973  85 ITVKMVVDAPASVAYKLYADRELFPKWLPFLSSVEAVEGSPDLSRYLVKFESFGKKfEYYFLAKNLEPIPDRKLHWRSIE 164
Cdd:cd07812    1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARFVGGRKGGR-RLTLTSEVTEVDPPRPGRFRVTG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 685371973 165 G---FANRGSVRFFQRGPSSCLVEINFSFEVPHAFAPVAF 201
Cdd:cd07812   80 GgggVDGTGEWRLEPEGDGGTRVTYTVEYDPPGPLLKVFA 119
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 87-199 2.06e-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: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685371973   87 VKMVVDAPASVAYKLYADRELFPKWLPFLSSVEAVEGSPDLSRYLVKFESFGK----KFEYYflakNLEPIPdRKLHWRS 162
Cdd:pfam10604   1 VSIEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGGGGPLRGVVGTLRVGGRrgtvREELV----EYDPAP-RLLAYRI 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 685371973  163 IE--GFAN-RGSVRFFQRGPsSCLVEINFSFEVPHAFAPV 199
Cdd:pfam10604  76 VEplGVANyVGTWTVTPAGG-GTRVTWTGEFDGPPLGGPF 114
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 88-131 6.79e-03

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. The START domain 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. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease.


Pssm-ID: 176885  Cd Length: 195  Bit Score: 36.10  E-value: 6.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 685371973  88 KMVVDAPASVAYKLYADRELFPKWLPFLSSVEAVEGSPDLSRYL 131
Cdd:cd08876   46 VAEVDASIEAFLALLRDTESYPQWMPNCKESRVLKRTDDNERSV 89
 
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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