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Conserved domains on  [gi|1003976656|ref|WP_061477941|]
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MULTISPECIES: type II toxin-antitoxin system RatA family toxin [Stenotrophomonas]

Protein Classification

type II toxin-antitoxin system RatA family toxin( domain architecture ID 10789869)

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

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List of domain hits

 Name Accession Description Interval E-value
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-136 2.87e-59

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


:

Pssm-ID: 442114  Cd Length: 137  Bit Score: 179.67  E-value: 2.87e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   1 MPTIRRSALVEHSAARMFDLVNDVQAYPSRFRWCSAAQIMEQGEDRLVARLDLGLGSFSTWFQTENTLRRPHSIDMQLRD 80
Cdd:COG2867     1 MPTISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEVVAELTVSFKGLRESFTTRNTLDPPERIDFELVD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1003976656  81 GPFKQLHGRWEFHALAEDACKVTLTLEFEPSSRLLGPALAIGFQGLADRMVNDFVR 136
Cdd:COG2867    81 GPFKHLEGRWRFEPLGEGGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKK 136
 
Name Accession Description Interval E-value
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-136 2.87e-59

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 179.67  E-value: 2.87e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   1 MPTIRRSALVEHSAARMFDLVNDVQAYPSRFRWCSAAQIMEQGEDRLVARLDLGLGSFSTWFQTENTLRRPHSIDMQLRD 80
Cdd:COG2867     1 MPTISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEVVAELTVSFKGLRESFTTRNTLDPPERIDFELVD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1003976656  81 GPFKQLHGRWEFHALAEDACKVTLTLEFEPSSRLLGPALAIGFQGLADRMVNDFVR 136
Cdd:COG2867    81 GPFKHLEGRWRFEPLGEGGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKK 136
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 4-140 2.57e-58

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: 177.28  E-value: 2.57e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   4 IRRSALVEHSAARMFDLVNDVQAYPSRFRWCSAAQIMEQGEDRLVARLDLGLGSFSTWFQTENTLRRPHSIDMQLRDGPF 83
Cdd:cd07813     1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPESIEAELVDGPF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003976656  84 KQLHGRWEFHALAEDACKVTLTLEFEPSSRLLGPALAIGFQGLADRMVNDFVRVADE 140
Cdd:cd07813    81 KHLEGEWRFKPLGENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQ 137
PRK10724 PRK10724
type II toxin-antitoxin system RatA family toxin;
1-140 5.16e-39

type II toxin-antitoxin system RatA family toxin;


Pssm-ID: 182678  Cd Length: 158  Bit Score: 128.89  E-value: 5.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   1 MPTIRRSALVEHSAARMFDLVNDVQAYPSRFRWCSAAQIMEQGEDRLVARLDLGLGSFSTWFQTENTLRRPHSIDMQLRD 80
Cdd:PRK10724   14 MPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMQLVD 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656  81 GPFKQLHGRWEFHALAEDACKVTLTLEFEPSSRLLGPALAIGFQGLADRMVNDFVRVADE 140
Cdd:PRK10724   94 GPFKKLIGGWKFTPLSQEACRIEFHLDFEFTNKLIELAFGRVFKELASNMVQAFTVRAKE 153
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 10-135 1.45e-30

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: 106.43  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656  10 VEHSAARMFDLVNDVQAYPSRFRWCSAAQIMEqgEDRLVARLDLGLGSFSTWFQTENTLRRPHSIDMQLRDGPFKQLHGR 89
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLE--RDGSLADWRVAFGGLRRSFTARVTLQPPERIEMVLVDGDFKRLEGS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1003976656  90 WEFHALA-EDACKVTLTLEFEPSSRLLGPALAIGFQGLADRMVNDFV 135
Cdd:pfam03364  79 WRFEPGGpGTRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
 
Name Accession Description Interval E-value
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-136 2.87e-59

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 179.67  E-value: 2.87e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   1 MPTIRRSALVEHSAARMFDLVNDVQAYPSRFRWCSAAQIMEQGEDRLVARLDLGLGSFSTWFQTENTLRRPHSIDMQLRD 80
Cdd:COG2867     1 MPTISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEVVAELTVSFKGLRESFTTRNTLDPPERIDFELVD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1003976656  81 GPFKQLHGRWEFHALAEDACKVTLTLEFEPSSRLLGPALAIGFQGLADRMVNDFVR 136
Cdd:COG2867    81 GPFKHLEGRWRFEPLGEGGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKK 136
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 4-140 2.57e-58

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: 177.28  E-value: 2.57e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   4 IRRSALVEHSAARMFDLVNDVQAYPSRFRWCSAAQIMEQGEDRLVARLDLGLGSFSTWFQTENTLRRPHSIDMQLRDGPF 83
Cdd:cd07813     1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPESIEAELVDGPF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003976656  84 KQLHGRWEFHALAEDACKVTLTLEFEPSSRLLGPALAIGFQGLADRMVNDFVRVADE 140
Cdd:cd07813    81 KHLEGEWRFKPLGENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQ 137
PRK10724 PRK10724
type II toxin-antitoxin system RatA family toxin;
1-140 5.16e-39

type II toxin-antitoxin system RatA family toxin;


Pssm-ID: 182678  Cd Length: 158  Bit Score: 128.89  E-value: 5.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   1 MPTIRRSALVEHSAARMFDLVNDVQAYPSRFRWCSAAQIMEQGEDRLVARLDLGLGSFSTWFQTENTLRRPHSIDMQLRD 80
Cdd:PRK10724   14 MPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMQLVD 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656  81 GPFKQLHGRWEFHALAEDACKVTLTLEFEPSSRLLGPALAIGFQGLADRMVNDFVRVADE 140
Cdd:PRK10724   94 GPFKKLIGGWKFTPLSQEACRIEFHLDFEFTNKLIELAFGRVFKELASNMVQAFTVRAKE 153
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 10-135 1.45e-30

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: 106.43  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656  10 VEHSAARMFDLVNDVQAYPSRFRWCSAAQIMEqgEDRLVARLDLGLGSFSTWFQTENTLRRPHSIDMQLRDGPFKQLHGR 89
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLE--RDGSLADWRVAFGGLRRSFTARVTLQPPERIEMVLVDGDFKRLEGS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1003976656  90 WEFHALA-EDACKVTLTLEFEPSSRLLGPALAIGFQGLADRMVNDFV 135
Cdd:pfam03364  79 WRFEPGGpGTRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
1-133 5.94e-10

Uncharacterized protein, contains SRPBCC domain [Function unknown];


Pssm-ID: 444363  Cd Length: 154  Bit Score: 54.14  E-value: 5.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   1 MPTIRRSALVEHSAARMFDLVNDVQAYPsrfRWCSAAQIMEQGEDRLVA-RLDLGLGSFSTWfQTENTLRRPHS-IDMQL 78
Cdd:COG5637     1 MTTVEKSITINAPVEEVYAYWRDFENLP---RFMKGVESVTVLDDTRSHwVAKGPLGVTVEW-DAEITEQVPGErIAWRS 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1003976656  79 RDGPFKQlHGRWEFHALAEDACKVTLTLEFEPSSRLLGPALAIGFQGLADRMVND 133
Cdd:COG5637    77 VEGDIPN-AGVVRFEPAGGRGTRVTVTIEYDPPGGLLGKALAKLFGGVPERQLRE 130
SRPBCC_8 cd07817
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 3-133 2.47e-08

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176859  Cd Length: 139  Bit Score: 49.53  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   3 TIRRSALVEHSAARMFDLVNDVQAYPSRFRWCSAAQIMeqGEDRLVARLDLGLGSFSTWfQTENTLRRP------HSIDm 76
Cdd:cd07817     1 TVEKSITVNVPVEEVYDFWRDFENLPRFMSHVESVEQL--DDTRSHWKAKGPAGLSVEW-DAEITEQVPneriawRSVE- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003976656  77 qlrdGPFKQLhGRWEFHALAEDACKVTLTLEFEPSSRLLGPALAIGFQGLADRMVND 133
Cdd:cd07817    77 ----GADPNA-GSVRFRPAPGRGTRVTLTIEYEPPGGAEGAAVAGLLGGEPERQLRE 128
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 4-138 1.45e-07

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: 47.32  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   4 IRRSALVEHSAARMFDLVNDVQAYPSRFRWCSAAQIMEQGEDRLVARLDLGLGSFSTWFQ----TENTLRRPHSIDmQLR 79
Cdd:cd07812     1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARFVGGRKGGRRLTLtsevTEVDPPRPGRFR-VTG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003976656  80 DGPFKQLHGRWEFHALAEDACKVTLTLEFEPSS---RLLGPALAIGFQGLADRMVNDFVRVA 138
Cdd:cd07812    80 GGGGVDGTGEWRLEPEGDGGTRVTYTVEYDPPGpllKVFALLLAGALKRELAALLRALKARL 141
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 1-133 2.36e-07

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: 46.85  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   1 MPTIRRSALVEHSAARMFDLVNDVQAYPSRFRWCSAAQIMEQGEDRLVARLDLGLGSFStwFQTENTLR----RPHSIDM 76
Cdd:cd07819     1 AIKVSREFEIEAPPAAVMDVLADVEAYPEWSPKVKSVEVLLRDNDGRPEMVRIGVGAYG--IKDTYALEytwdGAGSVSW 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656  77 QLRDGP-FKQLHGRWEfhaLAE--DACKVTLTLEFEPSSRLLGPalaigFQGLADRMVND 133
Cdd:cd07819    79 TLVEGEgNRSQEGSYT---LTPkgDGTRVTFDLTVELTVPLPGF-----LKRKAEPLVLD 130
OtcD1_ARO-CYC_like cd08861
N-terminal and C-terminal aromatase/cyclase domains of Streptomyces rimosus OtcD1 and related ...
 7-108 3.06e-04

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: 38.46  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   7 SALVEHSAARMFDLVNDVQAYPSRFRwCSAAQIMEQGEDRLVARLD--LGLGSFSTWFQTENTLRRPHSIDM-QLR-DGP 82
Cdd:cd08861     4 SVTVAAPAEDVYDLLADAERWPEFLP-TVHVERLELDGGVERLRMWatAFDGSVHTWTSRRVLDPEGRRIVFrQEEpPPP 82

                          90       100
                  ....*....|....*....|....*.
gi 1003976656  83 FKQLHGRWEFHALAEDACKVTLTLEF 108
Cdd:cd08861    83 VASMSGEWRFEPLGGGGTRVTLRHDF 108
TcmN_ARO-CYC_like cd08860
N-terminal aromatase/cyclase domain of the multifunctional protein tetracenomycin (TcmN) and ...
 18-130 1.82e-03

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: 36.30  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656  18 FDLVNDVQAYPSRFRWCSAAQIMEQGEDRLVARL----DLGlGSFSTWFQTENTLRRPHSIDMQ-LRDGPFKQLHGRWEF 92
Cdd:cd08860    17 WDMTNDIATWPDLFSEYAEAEVLEEDGDTVRFRLtmhpDAN-GTVWSWVSERTLDPVNRTVRARrVETGPFAYMNIRWEY 95

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1003976656  93 HALAEdACKVTLTLEFEpssrlLGPALAIGFQGLADRM 130
Cdd:cd08860    96 TEVPE-GTRMRWVQDFE-----MKPGAPVDDAAMTDRL 127
SRPBCC_1 cd07818
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 3-134 3.96e-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: 176860  Cd Length: 150  Bit Score: 35.32  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   3 TIRRSALVEHSAARMFDLVNDVQAYPsrfRWCSAAQI---ME---QGEDRlvarldlGLGSFSTWfQTENT--------- 67
Cdd:cd07818     3 RVERSIVINAPPEEVFPYVNDLKNWP---EWSPWEKLdpdMKrtySGPDS-------GVGASYSW-EGNDKvgegemeit 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1003976656  68 -LRRPHSIDMQLRDG-PFK-QLHGRWEFHAlAEDACKVTLTLefepSSRLLGPALAIGFQGLADRMV-NDF 134
Cdd:cd07818    72 eSVPNERIEYELRFIkPFEaTNDVEFTLEP-VGGGTKVTWGM----SGELPFPLKLMYLFLDMDKMIgKDF 137
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 3-139 7.83e-03

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: 34.61  E-value: 7.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003976656   3 TIRRSALVEHSAARMFDLVNDVQAYPsrfRWCSAAQ--IMEQGEDRLVARLDLGLGSFSTwfQTENTLRR---PHSIDMQ 77
Cdd:cd07821     2 KVTVSVTIDAPADKVWALLSDFGGLH---KWHPAVAscELEGGGPGVGAVRTVTLKDGGT--VRERLLALddaERRYSYR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003976656  78 LRDG--PFKQLHGRWEFHALAEDACKVTLTLEFEPSSRLLGPALAIGFQGLADRMVNDFVRVAD 139
Cdd:cd07821    77 IVEGplPVKNYVATIRVTPEGDGGTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALKAALE 140
 
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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