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Conserved domains on  [gi|485706721|ref|WP_001339419|]
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MULTISPECIES: type II toxin-antitoxin system toxin RatA [Enterobacteriaceae]

Protein Classification

type II toxin-antitoxin system RatA family toxin( domain architecture ID 10793454)

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
PRK10724 PRK10724
type II toxin-antitoxin system RatA family toxin;
1-145 1.19e-107

type II toxin-antitoxin system RatA family toxin;


:

Pssm-ID: 182678  Cd Length: 158  Bit Score: 303.00  E-value: 1.19e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   1 MPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMSLVD 80
Cdd:PRK10724  14 MPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMQLVD 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485706721  81 GPFKKLIGGWKFTPLSQDACRIEFHLDFEFTNKLIELAFGRVFKELAANMVQAFTVRAKEVYSAR 145
Cdd:PRK10724  94 GPFKKLIGGWKFTPLSQEACRIEFHLDFEFTNKLIELAFGRVFKELASNMVQAFTVRAKEVYSAR 158
 
Name Accession Description Interval E-value
PRK10724 PRK10724
type II toxin-antitoxin system RatA family toxin;
1-145 1.19e-107

type II toxin-antitoxin system RatA family toxin;


Pssm-ID: 182678  Cd Length: 158  Bit Score: 303.00  E-value: 1.19e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   1 MPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMSLVD 80
Cdd:PRK10724  14 MPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMQLVD 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485706721  81 GPFKKLIGGWKFTPLSQDACRIEFHLDFEFTNKLIELAFGRVFKELAANMVQAFTVRAKEVYSAR 145
Cdd:PRK10724  94 GPFKKLIGGWKFTPLSQEACRIEFHLDFEFTNKLIELAFGRVFKELASNMVQAFTVRAKEVYSAR 158
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 4-141 2.58e-74

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: 217.72  E-value: 2.58e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   4 ISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMSLVDGPF 83
Cdd:cd07813    1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPESIEAELVDGPF 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 485706721  84 KKLIGGWKFTPLSQDACRIEFHLDFEFTNKLIELAFGRVFKELAANMVQAFTVRAKEV 141
Cdd:cd07813   81 KHLEGEWRFKPLGENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQL 138
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-137 4.70e-73

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 214.73  E-value: 4.70e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   1 MPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMSLVD 80
Cdd:COG2867    1 MPTISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEVVAELTVSFKGLRESFTTRNTLDPPERIDFELVD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 485706721  81 GPFKKLIGGWKFTPLSQDACRIEFHLDFEFTNKLIELAFGRVFKELAANMVQAFTVR 137
Cdd:COG2867   81 GPFKHLEGRWRFEPLGEGGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 10-135 6.37e-40

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: 130.31  E-value: 6.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   10 VPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPGQmtAAVDVSKAGISKTFTTRNQLTSNQSILMSLVDGPFKKLIGG 89
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSL--ADWRVAFGGLRRSFTARVTLQPPERIEMVLVDGDFKRLEGS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 485706721   90 WKFTPLSQ-DACRIEFHLDFEFTNKLIELAFGRVFKELAANMVQAFT 135
Cdd:pfam03364  79 WRFEPGGPgTRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
 
Name Accession Description Interval E-value
PRK10724 PRK10724
type II toxin-antitoxin system RatA family toxin;
1-145 1.19e-107

type II toxin-antitoxin system RatA family toxin;


Pssm-ID: 182678  Cd Length: 158  Bit Score: 303.00  E-value: 1.19e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   1 MPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMSLVD 80
Cdd:PRK10724  14 MPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMQLVD 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485706721  81 GPFKKLIGGWKFTPLSQDACRIEFHLDFEFTNKLIELAFGRVFKELAANMVQAFTVRAKEVYSAR 145
Cdd:PRK10724  94 GPFKKLIGGWKFTPLSQEACRIEFHLDFEFTNKLIELAFGRVFKELASNMVQAFTVRAKEVYSAR 158
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 4-141 2.58e-74

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: 217.72  E-value: 2.58e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   4 ISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMSLVDGPF 83
Cdd:cd07813    1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPESIEAELVDGPF 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 485706721  84 KKLIGGWKFTPLSQDACRIEFHLDFEFTNKLIELAFGRVFKELAANMVQAFTVRAKEV 141
Cdd:cd07813   81 KHLEGEWRFKPLGENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQL 138
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-137 4.70e-73

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 214.73  E-value: 4.70e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   1 MPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMSLVD 80
Cdd:COG2867    1 MPTISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEVVAELTVSFKGLRESFTTRNTLDPPERIDFELVD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 485706721  81 GPFKKLIGGWKFTPLSQDACRIEFHLDFEFTNKLIELAFGRVFKELAANMVQAFTVR 137
Cdd:COG2867   81 GPFKHLEGRWRFEPLGEGGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 10-135 6.37e-40

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: 130.31  E-value: 6.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   10 VPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPGQmtAAVDVSKAGISKTFTTRNQLTSNQSILMSLVDGPFKKLIGG 89
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSL--ADWRVAFGGLRRSFTARVTLQPPERIEMVLVDGDFKRLEGS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 485706721   90 WKFTPLSQ-DACRIEFHLDFEFTNKLIELAFGRVFKELAANMVQAFT 135
Cdd:pfam03364  79 WRFEPGGPgTRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 4-138 2.09e-12

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: 60.41  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   4 ISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPGQMTAAVDVSKAGIsKTFTTRNQLT---SNQSILMSLVD 80
Cdd:cd07812    1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARFVGGRKGG-RRLTLTSEVTevdPPRPGRFRVTG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485706721  81 GPFK-KLIGGWKFTPLSQDACRIEFHLDFEFTN---KLIELAFGRVFKELAANMVQAFTVRA 138
Cdd:cd07812   80 GGGGvDGTGEWRLEPEGDGGTRVTYTVEYDPPGpllKVFALLLAGALKRELAALLRALKARL 141
OtcD1_ARO-CYC_like cd08861
N-terminal and C-terminal aromatase/cyclase domains of Streptomyces rimosus OtcD1 and related ...
 7-118 3.34e-06

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: 43.85  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   7 TALVPYSAEQMYQLVNDVQSYPQFLPgCTGSRILESTPGQMTAAVD-VSKAGISKTFTTR------------NQLTSnqs 73
Cdd:cd08861    4 SVTVAAPAEDVYDLLADAERWPEFLP-TVHVERLELDGGVERLRMWaTAFDGSVHTWTSRrvldpegrrivfRQEEP--- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 485706721  74 ilmslvDGPFKKLIGGWKFTPLSQDACRIEFHLDFEFTNKLIELA 118
Cdd:cd08861   80 ------PPPVASMSGEWRFEPLGGGGTRVTLRHDFTLGIDSPEAV 118
SRPBCC_11 cd08866
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 4-131 5.45e-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: 176875  Cd Length: 144  Bit Score: 43.37  E-value: 5.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   4 ISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPGQM----TAAVDVSKAGISKTFTTRNQLTSN--QSILMS 77
Cdd:cd08866    1 VVARVRVPAPPETVWAVLTDYDNLAEFIPNLAESRLLERNGNRVvleqTGKQGILFFKFEARVVLELREREEfpRELDFE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 485706721  78 LVDGPFKKLIGGWKFTPLSQD-ACRIEFHL----DFEFTNKLIElafGRVFKELAANMV 131
Cdd:cd08866   81 MVEGDFKRFEGSWRLEPLADGgGTLLTYEVevkpDFFAPVFLVE---FVLRQDLPTNLL 136
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 10-107 5.55e-06

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: 43.80  E-value: 5.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721  10 VPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTP--GQMTAAV----------DVskagISKTFTTRNQltSNQSILMS 77
Cdd:cd08876   49 VDASIEAFLALLRDTESYPQWMPNCKESRVLKRTDdnERSVYTVidlpwpvkdrDM----VLRSTTEQDA--DDGSVTIT 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 485706721  78 LVDGP-----------FKKLIGGWKFTPLSQDACRIE--FHLD 107
Cdd:cd08876  123 LEAAPealpeqkgyvrIKTVEGQWTFTPLGNGKTRVTyqAYAD 165
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 3-134 2.14e-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: 41.54  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   3 QISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPGqmtaavdvskAGISKTFTTRNQLTSNQSILM------ 76
Cdd:cd07821    2 KVTVSVTIDAPADKVWALLSDFGGLHKWHPAVASCELEGGGPG----------VGAVRTVTLKDGGTVRERLLAlddaer 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485706721  77 ----SLVDG--PFKKLIGGWKFTPLSQDACRIEFHLDFE----FTNKLIELAFGRVFKELAANMVQAF 134
Cdd:cd07821   72 rysyRIVEGplPVKNYVATIRVTPEGDGGTRVTWTAEFDppegLTDELARAFLTGVYRAGLAALKAAL 139
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 1-131 1.72e-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: 176861  Cd Length: 140  Bit Score: 39.14  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485706721   1 MPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPG---QMtAAVDVSKAGISKTFTTRNQLTSNQSILMS 77
Cdd:cd07819    1 AIKVSREFEIEAPPAAVMDVLADVEAYPEWSPKVKSVEVLLRDNDgrpEM-VRIGVGAYGIKDTYALEYTWDGAGSVSWT 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 485706721  78 LVDGP-FKKLIGGWKFTPLSqDACRIEFHLDFEFTNKLIELafgrvFKELAANMV 131
Cdd:cd07819   80 LVEGEgNRSQEGSYTLTPKG-DGTRVTFDLTVELTVPLPGF-----LKRKAEPLV 128
 
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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