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Conserved domains on  [gi|1848631517|gb|QKI04558|]
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SRPBCC family protein [Mycobacterium tuberculosis]

Protein Classification

SRPBCC family protein( domain architecture ID 10505808)

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_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 15-140 5.69e-17

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: 72.14  E-value: 5.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517  15 MAAPPDKIWTLIADVRNTGRFSPETFEAEWLDGATGPALGARFRGHVRRNGIGPVYWTVCEPGREFgFAVLLGDRPVNNW 94
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSLADWRVAFGGLRRSFTARVTLQPPERIEMV-LVDGDFKRLEGSW 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1848631517  95 HYRLTPTADGTEVTESFRLPPSVLTTVYYRVFGGWLRQRRNIRDMT 140
Cdd:pfam03364  80 RFEPGGPGTRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
 
Name Accession Description Interval E-value
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 15-140 5.69e-17

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: 72.14  E-value: 5.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517  15 MAAPPDKIWTLIADVRNTGRFSPETFEAEWLDGATGPALGARFRGHVRRNGIGPVYWTVCEPGREFgFAVLLGDRPVNNW 94
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSLADWRVAFGGLRRSFTARVTLQPPERIEMV-LVDGDFKRLEGSW 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1848631517  95 HYRLTPTADGTEVTESFRLPPSVLTTVYYRVFGGWLRQRRNIRDMT 140
Cdd:pfam03364  80 RFEPGGPGTRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 10-150 2.29e-14

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: 65.81  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517  10 SATVHMAAPPDKIWTLIADVRNTGRFSPETFEAEWLDGaTGPALGARFRGHVRRNGIGPVYWTV--CEPGREFGFAVLLG 87
Cdd:cd07812     2 EASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGG-GEGGVGARFVGGRKGGRRLTLTSEVteVDPPRPGRFRVTGG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1848631517  88 DRPV-NNWHYRLTPTAD-GTEVTESFRLPPSVLTtvyyRVFGGWLRQRRNIRDMTKTLQRIKDLV 150
Cdd:cd07812    81 GGGVdGTGEWRLEPEGDgGTRVTYTVEYDPPGPL----LKVFALLLAGALKRELAALLRALKARL 141
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
10-153 8.08e-05

Uncharacterized protein, contains SRPBCC domain [Function unknown];


Pssm-ID: 444363  Cd Length: 154  Bit Score: 40.28  E-value: 8.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517  10 SATVHMAAPPDKIWTLIADVRNTGRFSPETFEAEWLDGAtgpalgaRFRGHVRRNGIGPVYW----TVCEPGREFGFAVL 85
Cdd:COG5637     5 EKSITINAPVEEVYAYWRDFENLPRFMKGVESVTVLDDT-------RSHWVAKGPLGVTVEWdaeiTEQVPGERIAWRSV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1848631517  86 LGDrPVNNWHYRLTPTAD-GTEVTE--SFRLPPSVLTTVYYRVFGGWLRQRrnirdMTKTLQRIKDLVEAG 153
Cdd:COG5637    78 EGD-IPNAGVVRFEPAGGrGTRVTVtiEYDPPGGLLGKALAKLFGGVPERQ-----LREDLERFKQLIETG 142
 
Name Accession Description Interval E-value
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 15-140 5.69e-17

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: 72.14  E-value: 5.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517  15 MAAPPDKIWTLIADVRNTGRFSPETFEAEWLDGATGPALGARFRGHVRRNGIGPVYWTVCEPGREFgFAVLLGDRPVNNW 94
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSLADWRVAFGGLRRSFTARVTLQPPERIEMV-LVDGDFKRLEGSW 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1848631517  95 HYRLTPTADGTEVTESFRLPPSVLTTVYYRVFGGWLRQRRNIRDMT 140
Cdd:pfam03364  80 RFEPGGPGTRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 10-150 2.29e-14

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: 65.81  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517  10 SATVHMAAPPDKIWTLIADVRNTGRFSPETFEAEWLDGaTGPALGARFRGHVRRNGIGPVYWTV--CEPGREFGFAVLLG 87
Cdd:cd07812     2 EASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGG-GEGGVGARFVGGRKGGRRLTLTSEVteVDPPRPGRFRVTGG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1848631517  88 DRPV-NNWHYRLTPTAD-GTEVTESFRLPPSVLTtvyyRVFGGWLRQRRNIRDMTKTLQRIKDLV 150
Cdd:cd07812    81 GGGVdGTGEWRLEPEGDgGTRVTYTVEYDPPGPL----LKVFALLLAGALKRELAALLRALKARL 141
SRPBCC_10 cd08865
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 10-152 2.01e-11

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: 58.06  E-value: 2.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517  10 SATVHMAAPPDKIWTLIADVRNTGRFSPETFEAEWLDGATgPALGARFRGHVRRNGIGPVY-WTVC--EPGREFGFAVLL 86
Cdd:cd08865     2 EESIVIERPVEEVFAYLADFENAPEWDPGVVEVEKITDGP-VGVGTRYHQVRKFLGRRIELtYEITeyEPGRRVVFRGSS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1848631517  87 GDRPVNNwHYRLTPTADGTEVTESFRLPPSVLTTVYYRVFGGWLRqrrniRDMTKTLQRIKDLVEA 152
Cdd:cd08865    81 GPFPYED-TYTFEPVGGGTRVRYTAELEPGGFARLLDPLMAPAFR-----RRARAALENLKALLEA 140
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 11-151 4.47e-10

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: 54.41  E-value: 4.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517  11 ATVHMAAPPDKIWTLIADVRNTGRFSPETFEAEWlDGATGPalGARFRGHVRRNGI-GPVYWTVCE---PGREFGFAVlL 86
Cdd:pfam10604   1 VSIEIAAPPEQVWALLSDFENWPRWHPGVLRVEL-EGGGGP--LRGVVGTLRVGGRrGTVREELVEydpAPRLLAYRI-V 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1848631517  87 GDRPVNN--WHYRLTPTADGTEVTESFrlppsvltTVYYRVFGGWLR----QRRNIRDMTKTLQRIKDLVE 151
Cdd:pfam10604  77 EPLGVANyvGTWTVTPAGGGTRVTWTG--------EFDGPPLGGPFRdpaaARAVKGDYRAGLDRLKAVLE 139
SRPBCC_CalC_Aha1-like_5 cd08898
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 12-152 1.41e-06

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: 44.99  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517  12 TVHMAAPPDKIWTLIADvrntgrfsPETFEAEWLDGATGPALGARFRGHVRRNGIGPVYWTV----CEPGREFGF----- 82
Cdd:cd08898     6 TILIDAPRERVWRALTD--------PEHFGQWFGVKLGPFVVGEGATGEITYPGYEHGVFPVtvveVDPPRRFSFrwhpp 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1848631517  83 AVLLGDRPVNN----WHYRLTPTADGTE--VTES-FR-LPPSVLTTVYYRVFGGWLRQrrnirdmtktLQRIKDLVEA 152
Cdd:cd08898    78 AIDPGEDYSAEpstlVEFTLEPIAGGTLltVTESgFDaLPAERRAEAYRMNEGGWDEQ----------LENLVAYVEA 145
SRPBCC_7 cd07825
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 10-146 2.40e-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: 176867  Cd Length: 144  Bit Score: 44.65  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517  10 SATVHMAAPPDKIWTLIADVRNTGRFSPETFEAEWLDGATGPALGARFRGHVRRNGIG---PVYWTVCEPGREFGFA-VL 85
Cdd:cd07825     3 SVSRTVDAPAEAVFAVLADPRRHPEIDGSGTVREAIDGPRILAVGDVFRMAMRLDGGPyriTNHVVAFEENRLIAWRpGP 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1848631517  86 LGDRPV-NNWHYRLTPTADG-TEVTESFRLPPsvlTTVYYRVFGGWLRQRRNIRDMTKTLQRI 146
Cdd:cd07825    83 AGQEPGgHRWRWELEPIGPGrTRVTETYDWSA---VTDLKELLGFPAFPEVQLEASLDRLATL 142
SRPBCC_Smu440-like cd08862
Ligand-binding SRPBCC domain of Streptococcus mutans Smu.440 and related proteins; This family ...
 7-152 5.16e-06

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: 43.50  E-value: 5.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517   7 MEGSATVHMAAPPDKIWTLIADVRNTGRFSPETFEAEWLDGatGPALGARFRghVRRNGIGPVYWTV--CEPGREFGF-A 83
Cdd:cd08862     1 MKFEATIVIDAPPERVWAVLTDVENWPAWTPSVETVRLEGP--PPAVGSSFK--MKPPGLVRSTFTVteLRPGHSFTWtG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1848631517  84 VLLGDRPVNNWHYRLTPtADGTEVT--ESFRLPPSVLttvyyrvfGGWLRQRRNIRDMTKTLQRIKDLVEA 152
Cdd:cd08862    77 PAPGISAVHRHEFEAKP-DGGVRVTtsESLSGPLAFL--------FGLFVGKKLRALLPEWLEGLKAAAEQ 138
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 7-112 6.04e-05

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: 40.39  E-value: 6.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517   7 MEGSATVHMAAPPDKIWTLIADVRNTGRFSPETFEAEWLDGATGPalgarfrGHVRRNGIGPVYW-----TVCEPG-REF 80
Cdd:cd07821     1 AKVTVSVTIDAPADKVWALLSDFGGLHKWHPAVASCELEGGGPGV-------GAVRTVTLKDGGTvrerlLALDDAeRRY 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1848631517  81 GFAVLLGDRPVNNWH--YRLTPTAD-GTEVTESFR 112
Cdd:cd07821    74 SYRIVEGPLPVKNYVatIRVTPEGDgGTRVTWTAE 108
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
10-153 8.08e-05

Uncharacterized protein, contains SRPBCC domain [Function unknown];


Pssm-ID: 444363  Cd Length: 154  Bit Score: 40.28  E-value: 8.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517  10 SATVHMAAPPDKIWTLIADVRNTGRFSPETFEAEWLDGAtgpalgaRFRGHVRRNGIGPVYW----TVCEPGREFGFAVL 85
Cdd:COG5637     5 EKSITINAPVEEVYAYWRDFENLPRFMKGVESVTVLDDT-------RSHWVAKGPLGVTVEWdaeiTEQVPGERIAWRSV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1848631517  86 LGDrPVNNWHYRLTPTAD-GTEVTE--SFRLPPSVLTTVYYRVFGGWLRQRrnirdMTKTLQRIKDLVEAG 153
Cdd:COG5637    78 EGD-IPNAGVVRFEPAGGrGTRVTVtiEYDPPGGLLGKALAKLFGGVPERQ-----LREDLERFKQLIETG 142
SRPBCC_4 cd07822
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 10-151 2.68e-03

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: 36.15  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517  10 SATVHMAAPPDKIWTLIADVRNTGRFSPETFEAEwldgATGPALGARFRGHVRRNGIGPVYW----TVCEPGREFGFAVL 85
Cdd:cd07822     3 STEIEINAPPEKVWEVLTDFPSYPEWNPFVRSAT----GLSLALGARLRFVVKLPGGPPRSFkprvTEVEPPRRLAWRGG 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1848631517  86 LGDRPVNNWH--YRLTPTADG-TEVT--ESFRlppSVLTTVYYRVFGGWLrqRRNIRDMTKTLqriKDLVE 151
Cdd:cd07822    79 LPFPGLLDGEhsFELEPLGDGgTRFVhrETFS---GLLAPLVLLGLGRDL--RAGFEAMNEAL---KARAE 141
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 12-115 4.05e-03

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 35.40  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848631517  12 TVHMAAPPDKIWTLIADVRNTGRFSPETFEAEWLDGAtgPALGARFRgHVRRNGIGPVYW-----TVCEPGREFGFAVLL 86
Cdd:COG3832    11 EREIDAPPERVWRAWTDPELLARWFGPKGWATVAEFD--LRVGGRFR-FRMRGPDGEEFGfegevLEVEPPERLVFTWGF 87

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1848631517  87 GDRPVNNWH--YRLTPTADGTEVTESFRLPP 115
Cdd:COG3832    88 EDDPEGESTvtVTLEPEGGGTRLTLTHTGFS 118
 
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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