NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|504405312|ref|WP_014592414|]
View 

MULTISPECIES: type II toxin-antitoxin system RatA family toxin [Pseudomonas]

Protein Classification

type II toxin-antitoxin system RatA family toxin( domain architecture ID 10167417)

type II toxin-antitoxin (TA) system RatA family toxin similar to Escherichia coli ribosome association toxin RatA, which binds to 50S ribosomal subunits, preventing them from associating with 30S subunits to form 70S ribosomes, and is the toxin component of the RatA (PasT)-RatB (PasI) TA module

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 5-142 7.41e-72

Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and similar proteins. COQ10p is a hydrophobic protein located in the inner membrane of mitochondria that binds coenzyme Q (CoQ), also called ubiquinone, which is an essential electron carrier of the respiratory chain. Deletion of the gene encoding COQ10p (COQ10 or YOL008W) in Saccharomyces cerevisiae results in respiratory defect because of the inability to oxidize NADH and succinate. COQ10p may function in the delivery of CoQ (Q6 in budding yeast) to its proper location for electron transport. The human homolog, called Q-binding protein COQ10 homolog A (COQ10A), is able to fully complement for the absence of COQ10p in fission yeast. Human COQ10A also has a splice variant COQ10B. COQ10p 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: 176855  Cd Length: 138  Bit Score: 211.56  E-value: 7.41e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   5 IQRSALLPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTHMRAKLEVAKGGMSQHFVTRNVLVPGQSIEMNLEEGPF 84
Cdd:cd07813    1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPESIEAELVDGPF 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504405312  85 TQLHGVWVFKALGEKACKISLDLSFDYAGPIVRATLGPLFNQAANTLVDAFCQRAKQL 142
Cdd:cd07813   81 KHLEGEWRFKPLGENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQL 138
 
Name Accession Description Interval E-value
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 5-142 7.41e-72

Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and similar proteins. COQ10p is a hydrophobic protein located in the inner membrane of mitochondria that binds coenzyme Q (CoQ), also called ubiquinone, which is an essential electron carrier of the respiratory chain. Deletion of the gene encoding COQ10p (COQ10 or YOL008W) in Saccharomyces cerevisiae results in respiratory defect because of the inability to oxidize NADH and succinate. COQ10p may function in the delivery of CoQ (Q6 in budding yeast) to its proper location for electron transport. The human homolog, called Q-binding protein COQ10 homolog A (COQ10A), is able to fully complement for the absence of COQ10p in fission yeast. Human COQ10A also has a splice variant COQ10B. COQ10p 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: 176855  Cd Length: 138  Bit Score: 211.56  E-value: 7.41e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   5 IQRSALLPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTHMRAKLEVAKGGMSQHFVTRNVLVPGQSIEMNLEEGPF 84
Cdd:cd07813    1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPESIEAELVDGPF 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504405312  85 TQLHGVWVFKALGEKACKISLDLSFDYAGPIVRATLGPLFNQAANTLVDAFCQRAKQL 142
Cdd:cd07813   81 KHLEGEWRFKPLGENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQL 138
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 3-138 1.47e-68

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 203.17  E-value: 1.47e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   3 THIQRSALLPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTHMRAKLEVAKGGMSQHFVTRNVLVPGQSIEMNLEEG 82
Cdd:COG2867    2 PTISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEVVAELTVSFKGLRESFTTRNTLDPPERIDFELVDG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504405312  83 PFTQLHGVWVFKALGEKACKISLDLSFDYAGPIVRATLGPLFNQAANTLVDAFCQR 138
Cdd:COG2867   82 PFKHLEGRWRFEPLGEGGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
PRK10724 PRK10724
type II toxin-antitoxin system RatA family toxin;
5-142 8.31e-47

type II toxin-antitoxin system RatA family toxin;


Pssm-ID: 182678  Cd Length: 158  Bit Score: 148.92  E-value: 8.31e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   5 IQRSALLPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTHMRAKLEVAKGGMSQHFVTRNVLVPGQSIEMNLEEGPF 84
Cdd:PRK10724  17 ISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMQLVDGPF 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504405312  85 TQLHGVWVFKALGEKACKISLDLSFDYAGPIVRATLGPLFNQAANTLVDAFCQRAKQL 142
Cdd:PRK10724  97 KKLIGGWKFTPLSQEACRIEFHLDFEFTNKLIELAFGRVFKELASNMVQAFTVRAKEV 154
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 11-136 2.43e-38

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: 126.46  E-value: 2.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   11 LPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTHmrAKLEVAKGGMSQHFVTRNVLVPGQSIEMNLEEGPFTQLHGV 90
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSL--ADWRVAFGGLRRSFTARVTLQPPERIEMVLVDGDFKRLEGS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 504405312   91 WVFKALG-EKACKISLDLSFDYAGPIVRATLGPLFNQAANTLVDAFC 136
Cdd:pfam03364  79 WRFEPGGpGTRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
 
Name Accession Description Interval E-value
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 5-142 7.41e-72

Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and similar proteins. COQ10p is a hydrophobic protein located in the inner membrane of mitochondria that binds coenzyme Q (CoQ), also called ubiquinone, which is an essential electron carrier of the respiratory chain. Deletion of the gene encoding COQ10p (COQ10 or YOL008W) in Saccharomyces cerevisiae results in respiratory defect because of the inability to oxidize NADH and succinate. COQ10p may function in the delivery of CoQ (Q6 in budding yeast) to its proper location for electron transport. The human homolog, called Q-binding protein COQ10 homolog A (COQ10A), is able to fully complement for the absence of COQ10p in fission yeast. Human COQ10A also has a splice variant COQ10B. COQ10p 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: 176855  Cd Length: 138  Bit Score: 211.56  E-value: 7.41e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   5 IQRSALLPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTHMRAKLEVAKGGMSQHFVTRNVLVPGQSIEMNLEEGPF 84
Cdd:cd07813    1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPESIEAELVDGPF 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504405312  85 TQLHGVWVFKALGEKACKISLDLSFDYAGPIVRATLGPLFNQAANTLVDAFCQRAKQL 142
Cdd:cd07813   81 KHLEGEWRFKPLGENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQL 138
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 3-138 1.47e-68

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 203.17  E-value: 1.47e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   3 THIQRSALLPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTHMRAKLEVAKGGMSQHFVTRNVLVPGQSIEMNLEEG 82
Cdd:COG2867    2 PTISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEVVAELTVSFKGLRESFTTRNTLDPPERIDFELVDG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504405312  83 PFTQLHGVWVFKALGEKACKISLDLSFDYAGPIVRATLGPLFNQAANTLVDAFCQR 138
Cdd:COG2867   82 PFKHLEGRWRFEPLGEGGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
PRK10724 PRK10724
type II toxin-antitoxin system RatA family toxin;
5-142 8.31e-47

type II toxin-antitoxin system RatA family toxin;


Pssm-ID: 182678  Cd Length: 158  Bit Score: 148.92  E-value: 8.31e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   5 IQRSALLPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTHMRAKLEVAKGGMSQHFVTRNVLVPGQSIEMNLEEGPF 84
Cdd:PRK10724  17 ISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMQLVDGPF 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504405312  85 TQLHGVWVFKALGEKACKISLDLSFDYAGPIVRATLGPLFNQAANTLVDAFCQRAKQL 142
Cdd:PRK10724  97 KKLIGGWKFTPLSQEACRIEFHLDFEFTNKLIELAFGRVFKELASNMVQAFTVRAKEV 154
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 11-136 2.43e-38

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: 126.46  E-value: 2.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   11 LPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTHmrAKLEVAKGGMSQHFVTRNVLVPGQSIEMNLEEGPFTQLHGV 90
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSL--ADWRVAFGGLRRSFTARVTLQPPERIEMVLVDGDFKRLEGS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 504405312   91 WVFKALG-EKACKISLDLSFDYAGPIVRATLGPLFNQAANTLVDAFC 136
Cdd:pfam03364  79 WRFEPGGpGTRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
2-142 8.93e-12

Uncharacterized protein, contains SRPBCC domain [Function unknown];


Pssm-ID: 444363  Cd Length: 154  Bit Score: 58.77  E-value: 8.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   2 TTHIQRSALLPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTHMRAKlevAKGGMSQHFVTRNV-LVPGQSIEMNLE 80
Cdd:COG5637    1 MTTVEKSITINAPVEEVYAYWRDFENLPRFMKGVESVTVLDDTRSHWVAK---GPLGVTVEWDAEITeQVPGERIAWRSV 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504405312  81 EGPFTQlHGVWVFKALGEKACKISLDLSFDYAGPIVRATLGPLFNQAANTLVDAFCQRAKQL 142
Cdd:COG5637   78 EGDIPN-AGVVRFEPAGGRGTRVTVTIEYDPPGGLLGKALAKLFGGVPERQLREDLERFKQL 138
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 5-139 2.21e-10

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: 55.02  E-value: 2.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   5 IQRSALLPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTHMRAK-LEVAKGGMSQHFVTR-NVLVPGQSIEMNLEEG 82
Cdd:cd07812    1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARfVGGRKGGRRLTLTSEvTEVDPPRPGRFRVTGG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504405312  83 PF-TQLHGVWVFKALGEKACKISLDLSFDYAGP---IVRATLGPLFNQAANTLVDAFCQRA 139
Cdd:cd07812   81 GGgVDGTGEWRLEPEGDGGTRVTYTVEYDPPGPllkVFALLLAGALKRELAALLRALKARL 141
OtcD1_ARO-CYC_like cd08861
N-terminal and C-terminal aromatase/cyclase domains of Streptomyces rimosus OtcD1 and related ...
 14-118 1.88e-09

N-terminal and C-terminal aromatase/cyclase domains of Streptomyces rimosus OtcD1 and related domains; This family includes the N- and C- terminal aromatase/cyclase (ARO/CYC) domains of Streptomyces rimosus OtcD1 and related domains. It 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. ARO/CYC domains participate in the diversification of aromatic polyketides by promoting polyketide cyclization. They occur in two architectural forms, didomain and monodomain. Didomain aromatase/cyclases (ARO/CYCs), contain two ARO/CYC domains, and are associated with C7-C12 first ring cyclized polyketides. Streptomyces rimosus OtcD1 is a didomain ARO/CYC. The polyketide Oxytetracycline (OTC) is a broad spectrum antibiotic made by Streptomyces rimosus. The gene encoding OtcD1 is part of oxytetracycline (OTC) gene cluster. Disruption of this gene results in the production of novel polyketides having shorter chain lengths (by up to 10 carbons) than OTC. Monodomain ARO/CYCs have a single ARO/CYC domain, and are often associated with C9-C14 first ring cyclizations, these latter domains belong to a different subfamily in the SRPBCC superfamily.


Pssm-ID: 176870  Cd Length: 142  Bit Score: 52.71  E-value: 1.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312  14 PAQALYDLVNDVASYPEFLPWCSASTV-IETSDTHMRAkLEVAKGGMSQHFVTRNVLVP-GQSIEMNLEE--GPFTQLHG 89
Cdd:cd08861   10 PAEDVYDLLADAERWPEFLPTVHVERLeLDGGVERLRM-WATAFDGSVHTWTSRRVLDPeGRRIVFRQEEppPPVASMSG 88

                         90       100
                 ....*....|....*....|....*....
gi 504405312  90 VWVFKALGEKACKISLDLSFDYAGPIVRA 118
Cdd:cd08861   89 EWRFEPLGGGGTRVTLRHDFTLGIDSPEA 117
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 2-144 6.96e-09

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: 51.08  E-value: 6.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   2 TTHIQRSALLPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDT---HMrAKLEVAKGGMSQHFVTRNVLVPGQSIEMN 78
Cdd:cd07819    1 AIKVSREFEIEAPPAAVMDVLADVEAYPEWSPKVKSVEVLLRDNDgrpEM-VRIGVGAYGIKDTYALEYTWDGAGSVSWT 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504405312  79 LEEGP-FTQLHGVWVFKALGEKaCKISLDLSFDYAGPIvratLGPLFNQAANTLVDAFcqrAKQLNA 144
Cdd:cd07819   80 LVEGEgNRSQEGSYTLTPKGDG-TRVTFDLTVELTVPL----PGFLKRKAEPLVLDEA---LKGLKK 138
SRPBCC_8 cd07817
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 4-142 1.37e-05

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: 42.21  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   4 HIQRSALLPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTHMRAKlevAKGGMSQHFVTRNVL-VPGQSIEMNLEEG 82
Cdd:cd07817    1 TVEKSITVNVPVEEVYDFWRDFENLPRFMSHVESVEQLDDTRSHWKAK---GPAGLSVEWDAEITEqVPNERIAWRSVEG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312  83 PFTQLhGVWVFKALGEKACKISLDLSFDYAGPIVRATLGPLFNQAANTLVDAFCQRAKQL 142
Cdd:cd07817   78 ADPNA-GSVRFRPAPGRGTRVTLTIEYEPPGGAEGAAVAGLLGGEPERQLREDLRRFKQL 136
SRPBCC_1 cd07818
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 4-126 9.18e-05

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: 39.94  E-value: 9.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   4 HIQRSALLPYPAQALYDLVNDVASYPEFLPWcsastviETSDTHMRAKL-EVAKG-GMSQHFVTRNV----------LVP 71
Cdd:cd07818    3 RVERSIVINAPPEEVFPYVNDLKNWPEWSPW-------EKLDPDMKRTYsGPDSGvGASYSWEGNDKvgegemeiteSVP 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504405312  72 GQSIEMNLE-EGPFT-QLHGVWVFKALGEKaCKISLDLSFDYAGPIVRATLGPLFNQ 126
Cdd:cd07818   76 NERIEYELRfIKPFEaTNDVEFTLEPVGGG-TKVTWGMSGELPFPLKLMYLFLDMDK 131
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 11-47 6.76e-04

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: 38.02  E-value: 6.76e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 504405312  11 LPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTH 47
Cdd:cd08876   49 VDASIEAFLALLRDTESYPQWMPNCKESRVLKRTDDN 85
TcmN_ARO-CYC_like cd08860
N-terminal aromatase/cyclase domain of the multifunctional protein tetracenomycin (TcmN) and ...
 4-98 7.74e-04

N-terminal aromatase/cyclase domain of the multifunctional protein tetracenomycin (TcmN) and related domains; This family includes the N-terminal aromatase/cyclase (ARO/CYC) domain of Streptomyces glaucescens TcmN, and related domains. It 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. ARO/CYC domains participate in the diversification of aromatic polyketides by promoting polyketide cyclization. They occur in two architectural forms, monodomain and didomain. Monodomain aromatase/cyclases have a single ARO/CYC domain. For some, such as TcmN, this single domain is linked to a second domain of unrelated function. TcmN is a multifunctional cyclase-dehydratase-O-methyl transferase. Its N-terminal ARO/CYC domain participates in polyketide binding and catalysis; it promotes C9-C14 first-ring (and C7-C16 second-ring) cyclizations. Its C-terminal domain has O-methyltransferase activity. Didomain aromatase/cyclases contain two ARO/CYC domains, and they biosynthesize C7-C12 first ring cyclized polyketides. These latter domains belong to a different subfamily in the SRPBCC superfamily.


Pssm-ID: 176869  Cd Length: 146  Bit Score: 37.46  E-value: 7.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504405312   4 HIQRSALLPYPAQALYDLVNDVASYPEFLPWCSASTVIETSDTHMRAKLEVA--KGGMSQHFVTRNVLVPG--QSIEMNL 79
Cdd:cd08860    2 RTDNSIVIDAPLDLVWDMTNDIATWPDLFSEYAEAEVLEEDGDTVRFRLTMHpdANGTVWSWVSERTLDPVnrTVRARRV 81

                         90
                 ....*....|....*....
gi 504405312  80 EEGPFTQLHGVWVFKALGE 98
Cdd:cd08860   82 ETGPFAYMNIRWEYTEVPE 100
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH