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Conserved domains on  [gi|489499504|ref|WP_003404412|]
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MULTISPECIES: SRPBCC family protein [Mycobacterium]

Protein Classification

SRPBCC family protein( domain architecture ID 10167496)

uncharacterized SRPBCC family protein; similar to Streptomyces canus cyclase which catalyzes a chemical reaction to form a cyclic compound

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 2-140 2.12e-61

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: 176861  Cd Length: 140  Bit Score: 185.52  E-value: 2.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   2 AIKESRDIVIEASPEEILDVIADFEAMTEWSPAHQSVEILETGDDGRPSKVKMKVKTAGITDEQVVAYSWTDR-SVRWTL 80
Cdd:cd07819    1 AIKVSREFEIEAPPAAVMDVLADVEAYPEWSPKVKSVEVLLRDNDGRPEMVRIGVGAYGIKDTYALEYTWDGAgSVSWTL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504  81 VSSTQQRSQDGKYELTPKGDNTLVQFEITVDPQVPLPGFVLKRAIKGTIDTATEALRSQV 140
Cdd:cd07819   81 VEGEGNRSQEGSYTLTPKGDGTRVTFDLTVELTVPLPGFLKRKAEPLVLDEALKGLKKRV 140
 
Name Accession Description Interval E-value
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 2-140 2.12e-61

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: 176861  Cd Length: 140  Bit Score: 185.52  E-value: 2.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   2 AIKESRDIVIEASPEEILDVIADFEAMTEWSPAHQSVEILETGDDGRPSKVKMKVKTAGITDEQVVAYSWTDR-SVRWTL 80
Cdd:cd07819    1 AIKVSREFEIEAPPAAVMDVLADVEAYPEWSPKVKSVEVLLRDNDGRPEMVRIGVGAYGIKDTYALEYTWDGAgSVSWTL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504  81 VSSTQQRSQDGKYELTPKGDNTLVQFEITVDPQVPLPGFVLKRAIKGTIDTATEALRSQV 140
Cdd:cd07819   81 VEGEGNRSQEGSYTLTPKGDGTRVTFDLTVELTVPLPGFLKRKAEPLVLDEALKGLKKRV 140
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 6-137 6.94e-18

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 74.51  E-value: 6.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   6 SRDIVIEASPEEILDVIADFEAMTEWSPAHQSVEILETGDDGRpsKVKMKVKTAGITDEQVVAYSWT-DRSVRWTLVSSt 84
Cdd:COG2867    5 SRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEV--VAELTVSFKGLRESFTTRNTLDpPERIDFELVDG- 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489499504  85 QQRSQDGKYELTPKGDN-TLVQFEITVDPQVPLPGFVLKRAIKGTIDTATEALR 137
Cdd:COG2867   82 PFKHLEGRWRFEPLGEGgTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFK 135
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 9-140 9.57e-18

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: 74.06  E-value: 9.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504    9 IVIEASPEEILDVIADFEAMTEWSPAHQSVEILETGDDGRPSKVKMKVK-TAGITDEQVVAYSWTDRSVRWTLVSSTQQR 87
Cdd:pfam10604   3 IEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGGGGPLRGVVGTLRVGgRRGTVREELVEYDPAPRLLAYRIVEPLGVA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489499504   88 SQDGKYELTPKGDNTLVQFEITVDPQVPLPGF---VLKRAIKGTIDTATEALRSQV 140
Cdd:pfam10604  83 NYVGTWTVTPAGGGTRVTWTGEFDGPPLGGPFrdpAAARAVKGDYRAGLDRLKAVL 138
 
Name Accession Description Interval E-value
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 2-140 2.12e-61

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: 176861  Cd Length: 140  Bit Score: 185.52  E-value: 2.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   2 AIKESRDIVIEASPEEILDVIADFEAMTEWSPAHQSVEILETGDDGRPSKVKMKVKTAGITDEQVVAYSWTDR-SVRWTL 80
Cdd:cd07819    1 AIKVSREFEIEAPPAAVMDVLADVEAYPEWSPKVKSVEVLLRDNDGRPEMVRIGVGAYGIKDTYALEYTWDGAgSVSWTL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504  81 VSSTQQRSQDGKYELTPKGDNTLVQFEITVDPQVPLPGFVLKRAIKGTIDTATEALRSQV 140
Cdd:cd07819   81 VEGEGNRSQEGSYTLTPKGDGTRVTFDLTVELTVPLPGFLKRKAEPLVLDEALKGLKKRV 140
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 6-137 6.94e-18

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 74.51  E-value: 6.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   6 SRDIVIEASPEEILDVIADFEAMTEWSPAHQSVEILETGDDGRpsKVKMKVKTAGITDEQVVAYSWT-DRSVRWTLVSSt 84
Cdd:COG2867    5 SRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEV--VAELTVSFKGLRESFTTRNTLDpPERIDFELVDG- 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489499504  85 QQRSQDGKYELTPKGDN-TLVQFEITVDPQVPLPGFVLKRAIKGTIDTATEALR 137
Cdd:COG2867   82 PFKHLEGRWRFEPLGEGgTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFK 135
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 9-140 9.57e-18

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: 74.06  E-value: 9.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504    9 IVIEASPEEILDVIADFEAMTEWSPAHQSVEILETGDDGRPSKVKMKVK-TAGITDEQVVAYSWTDRSVRWTLVSSTQQR 87
Cdd:pfam10604   3 IEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGGGGPLRGVVGTLRVGgRRGTVREELVEYDPAPRLLAYRIVEPLGVA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489499504   88 SQDGKYELTPKGDNTLVQFEITVDPQVPLPGF---VLKRAIKGTIDTATEALRSQV 140
Cdd:pfam10604  83 NYVGTWTVTPAGGGTRVTWTGEFDGPPLGGPFrdpAAARAVKGDYRAGLDRLKAVL 138
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 6-140 1.56e-13

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: 63.50  E-value: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   6 SRDIVIEASPEEILDVIADFEAMTEWSPAHQSVEILETGDDGRPSKVKMKVKTAGI--TDEQVVAYSWtDRSVRWTLVSS 83
Cdd:cd07812    2 EASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARFVGGRKGGRRltLTSEVTEVDP-PRPGRFRVTGG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489499504  84 TQQRSQDGKYELTPKGDN-TLVQFEITVDPQVPLP---GFVLKRAIKGTIDTATEALRSQV 140
Cdd:cd07812   81 GGGVDGTGEWRLEPEGDGgTRVTYTVEYDPPGPLLkvfALLLAGALKRELAALLRALKARL 141
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 11-137 4.52e-13

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: 61.74  E-value: 4.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   11 IEASPEEILDVIADFEAMTEWSPAHQSVEILetgdDGRPSKVKMKVKTAGITdeqvvaYSWTDRSVR------WTLVSST 84
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVL----ERDGSLADWRVAFGGLR------RSFTARVTLqpperiEMVLVDG 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489499504   85 QQRSQDGKYELTPKGDNTL--VQFEITVDPQVPLPGFVLKRAIKGTIDTATEALR 137
Cdd:pfam03364  71 DFKRLEGSWRFEPGGPGTRvkVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 9-137 2.19e-12

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: 60.42  E-value: 2.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   9 IVIEASPEEILDVIADFEAMTEWSPAHQSVEIleTGDDGRPSKV-KMKVKTAGITDEQVVAYSWTDRSVRWTLVSSTQ-Q 86
Cdd:cd07821    7 VTIDAPADKVWALLSDFGGLHKWHPAVASCEL--EGGGPGVGAVrTVTLKDGGTVRERLLALDDAERRYSYRIVEGPLpV 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489499504  87 RSQDGKYELTPKGDN-TLVQFEITVDPQVPLPGFVLKRAIKGTIDTATEALR 137
Cdd:cd07821   85 KNYVATIRVTPEGDGgTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALK 136
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 10-140 1.87e-07

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: 48.04  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504  10 VIEASPEEILDVIADFEAMTEWSPAHQSVEILETGDDGR---------PSKVK-----MKVKTAGITDEQVVAYSWTDRS 75
Cdd:cd08876   48 EVDASIEAFLALLRDTESYPQWMPNCKESRVLKRTDDNErsvytvidlPWPVKdrdmvLRSTTEQDADDGSVTITLEAAP 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489499504  76 ---------VRWTLVsstqqrsqDGKYELTPKGDN-TLVQFEITVDPQVPLPGFVLKRAIKGTIDTATEALRSQV 140
Cdd:cd08876  128 ealpeqkgyVRIKTV--------EGQWTFTPLGNGkTRVTYQAYADPGGSIPGWLANAFAKDAPYNTLENLRKQL 194
SRPBCC_Smu440-like cd08862
Ligand-binding SRPBCC domain of Streptococcus mutans Smu.440 and related proteins; This family ...
 6-138 2.39e-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: 44.27  E-value: 2.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   6 SRDIVIEASPEEILDVIADFEAMTEWSPAHQSVEILETGdDGRPSKVKMKVKTAGITDEQVVAYSWTdRSVRWTLVSSTQ 85
Cdd:cd08862    4 EATIVIDAPPERVWAVLTDVENWPAWTPSVETVRLEGPP-PAVGSSFKMKPPGLVRSTFTVTELRPG-HSFTWTGPAPGI 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489499504  86 QRSQDgkYELTPKGD-NTLVQFEITV-DPQVPLPGFVLKRAIKGTIDTATEALRS 138
Cdd:cd08862   82 SAVHR--HEFEAKPDgGVRVTTSESLsGPLAFLFGLFVGKKLRALLPEWLEGLKA 134
SRPBCC_10 cd08865
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 6-138 4.62e-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: 176874  Cd Length: 140  Bit Score: 43.43  E-value: 4.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   6 SRDIVIEASPEEILDVIADFEAMTEWSPAHQSVEILETGDDGRPSKVKMKVKTAGITDE---QVVAYSwTDRSVrWTLVS 82
Cdd:cd08865    2 EESIVIERPVEEVFAYLADFENAPEWDPGVVEVEKITDGPVGVGTRYHQVRKFLGRRIEltyEITEYE-PGRRV-VFRGS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489499504  83 STQQRSQDGkYELTPKGDNTLVQFEITVDPQVP--LPGFVLKRAIKGTIDTATEALRS 138
Cdd:cd08865   80 SGPFPYEDT-YTFEPVGGGTRVRYTAELEPGGFarLLDPLMAPAFRRRARAALENLKA 136
SRPBCC_1 cd07818
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 6-104 8.37e-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: 176860  Cd Length: 150  Bit Score: 43.02  E-value: 8.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   6 SRDIVIEASPEEILDVIADFEAMTEWSPahqsveiLETGDDgrpskvKMKVKTAGiTDEQVVA-YSWT-DRSV---RWTL 80
Cdd:cd07818    5 ERSIVINAPPEEVFPYVNDLKNWPEWSP-------WEKLDP------DMKRTYSG-PDSGVGAsYSWEgNDKVgegEMEI 70

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489499504  81 VSSTQQRS--------------QDGKYELTPKGDNTLV 104
Cdd:cd07818   71 TESVPNERieyelrfikpfeatNDVEFTLEPVGGGTKV 108
SRPBCC_11 cd08866
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 9-142 1.43e-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: 176875  Cd Length: 144  Bit Score: 39.52  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   9 IVIEASPEEILDVIADFEAMTEWSPAHQSVEILETGDD-------GRPSKVKMKVKTAGITDeqVVAYSWTDRSVRWTLV 81
Cdd:cd08866    5 VRVPAPPETVWAVLTDYDNLAEFIPNLAESRLLERNGNrvvleqtGKQGILFFKFEARVVLE--LREREEFPRELDFEMV 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489499504  82 SSTQQRSQdGKYELTPKGDN--TLVQFEITVDPQVPLPGFVLKRAIKGTIDTATEALRSQVLK 142
Cdd:cd08866   83 EGDFKRFE-GSWRLEPLADGggTLLTYEVEVKPDFFAPVFLVEFVLRQDLPTNLLAIRAEAES 144
COG4891 COG4891
Uncharacterized conserved protein [Function unknown];
8-60 5.63e-04

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443919  Cd Length: 138  Bit Score: 37.59  E-value: 5.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489499504   8 DIVIEASPEEILDVIADFEAMTEWSPAHQSVEiletGDDGRPSKVKMKVKTAG 60
Cdd:COG4891    2 EIEIDAPPERVWQVLTDFPSYPEWNPFIRSIE----GELRVGARLTLRLRPPG 50
SRPBCC_CalC_Aha1-like_5 cd08898
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 6-104 6.09e-04

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: 37.67  E-value: 6.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   6 SRDIVIEASPEEILDVIADFEAMTEWSPAHQSVEILETGDDGR---PS--KVKMKVKTAGITDEQVVAYSW--------- 71
Cdd:cd08898    4 ERTILIDAPRERVWRALTDPEHFGQWFGVKLGPFVVGEGATGEityPGyeHGVFPVTVVEVDPPRRFSFRWhppaidpge 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489499504  72 TDRSVRWTLVsstqqrsqdgKYELTPKGDNTLV 104
Cdd:cd08898   84 DYSAEPSTLV----------EFTLEPIAGGTLL 106
SRPBCC_6 cd07824
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 11-46 1.07e-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: 176866  Cd Length: 146  Bit Score: 36.91  E-value: 1.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 489499504  11 IEASPEEILDVIADFEAMTEWSPAHQSVEILETGDD 46
Cdd:cd07824    9 IPAPPEAVWDVLVDAESWPDWWPGVERVVELEPGDE 44
SRPBCC_4 cd07822
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 6-42 1.73e-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: 36.54  E-value: 1.73e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 489499504   6 SRDIVIEASPEEILDVIADFEAMTEWSPAHQSVEILE 42
Cdd:cd07822    3 STEIEINAPPEKVWEVLTDFPSYPEWNPFVRSATGLS 39
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 9-127 9.71e-03

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: 34.26  E-value: 9.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489499504   9 IVIEASPEEILDVIADFEAMTEWSPAHQSVEILE----------TGDDGRPSKVKMKVKTagITDEQVVAYSWTDRSVRW 78
Cdd:cd07814    6 REFDAPPELVWRALTDPELLAQWFGPTTTAEMDLrvggrwfffmTGPDGEEGWVSGEVLE--VEPPRRLVFTWAFSDETP 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489499504  79 TLVSSTqqrsqdgKYELTPKGDNTLVQFEITVDPQVPLPGFVLKRAIKG 127
Cdd:cd07814   84 GPETTV-------TVTLEETGGGTRLTLTHSGFPEEDAEQEAREGMEEG 125
 
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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