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Conserved domains on  [gi|730237985|ref|WP_033942634|]
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HOASN domain-containing protein [Pseudomonas aeruginosa]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HOASN pfam14515
Haem-oxygenase-associated N-terminal helices; This domain represents a pair of alpha helices, ...
20-106 4.25e-47

Haem-oxygenase-associated N-terminal helices; This domain represents a pair of alpha helices, which are found at the N-terminus of some Haem-oxygenase globular domain.


:

Pssm-ID: 405239  Cd Length: 92  Bit Score: 154.54  E-value: 4.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730237985   20 SQRTMSEPAR-----NASALLAEALKPGASLDQITLALEAILAVTAKGLGGDASAYAQYQALLLELHVGSDPHTEPTRRW 94
Cdd:pfam14515   1 NQRNFSEPALqnlpiEAAAILADALAPGASLDQIDLAAEAIAALAAAGLGGDAQAYAAYQALLLELHLGDDPATAPTRRW 80
                          90
                  ....*....|..
gi 730237985   95 MASQVYLVEDRF 106
Cdd:pfam14515  81 LARAIYLVEDRF 92
PqqC COG5424
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];
115-340 2.64e-40

Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];


:

Pssm-ID: 444176  Cd Length: 228  Bit Score: 141.57  E-value: 2.64e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730237985 115 AVPVEEFCKKVDAEIEARSRVRHPMSVHLFQGTPPVEDVRFFLEHHWVRSYNFYSLLAELAFRFENIEDASVFYRNLYGE 194
Cdd:COG5424    1 LLSPEEFEARLRAEIARRYLLKHPFLQRLREGKLTREQLRAFALQRYHYVKHFPRYLAAILSRCPDEELRRALLENLYEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730237985 195 AGAEtPERSHPALLSHLMTYFDIPL-RIDFPALHPLEKAYLNNRIRCVRHTDVAWGLALLYAVESVSCVNHRRIYELLQR 273
Cdd:COG5424   81 DGEG-PEEGHIELWLRFAEALGLDReEVDARPPLPETRAAVDAYVNFCRRRSLLEAVAASLTAEGFAPEISRERLEGLLE 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730237985 274 -LGVP-EQPSEFHRLHGTQDEIDTEEMWALIAKFAPSEDFQRKFMQSLARHFEINRAYFDLLWEQMQAN 340
Cdd:COG5424  160 hYGLPdEEALEYFRLHAELDPRHAEEALELVLRLADTPEDQEAALEAARFKLDLLWAFLDALYRAYVAP 228
 
Name Accession Description Interval E-value
HOASN pfam14515
Haem-oxygenase-associated N-terminal helices; This domain represents a pair of alpha helices, ...
20-106 4.25e-47

Haem-oxygenase-associated N-terminal helices; This domain represents a pair of alpha helices, which are found at the N-terminus of some Haem-oxygenase globular domain.


Pssm-ID: 405239  Cd Length: 92  Bit Score: 154.54  E-value: 4.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730237985   20 SQRTMSEPAR-----NASALLAEALKPGASLDQITLALEAILAVTAKGLGGDASAYAQYQALLLELHVGSDPHTEPTRRW 94
Cdd:pfam14515   1 NQRNFSEPALqnlpiEAAAILADALAPGASLDQIDLAAEAIAALAAAGLGGDAQAYAAYQALLLELHLGDDPATAPTRRW 80
                          90
                  ....*....|..
gi 730237985   95 MASQVYLVEDRF 106
Cdd:pfam14515  81 LARAIYLVEDRF 92
PqqC COG5424
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];
115-340 2.64e-40

Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];


Pssm-ID: 444176  Cd Length: 228  Bit Score: 141.57  E-value: 2.64e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730237985 115 AVPVEEFCKKVDAEIEARSRVRHPMSVHLFQGTPPVEDVRFFLEHHWVRSYNFYSLLAELAFRFENIEDASVFYRNLYGE 194
Cdd:COG5424    1 LLSPEEFEARLRAEIARRYLLKHPFLQRLREGKLTREQLRAFALQRYHYVKHFPRYLAAILSRCPDEELRRALLENLYEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730237985 195 AGAEtPERSHPALLSHLMTYFDIPL-RIDFPALHPLEKAYLNNRIRCVRHTDVAWGLALLYAVESVSCVNHRRIYELLQR 273
Cdd:COG5424   81 DGEG-PEEGHIELWLRFAEALGLDReEVDARPPLPETRAAVDAYVNFCRRRSLLEAVAASLTAEGFAPEISRERLEGLLE 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730237985 274 -LGVP-EQPSEFHRLHGTQDEIDTEEMWALIAKFAPSEDFQRKFMQSLARHFEINRAYFDLLWEQMQAN 340
Cdd:COG5424  160 hYGLPdEEALEYFRLHAELDPRHAEEALELVLRLADTPEDQEAALEAARFKLDLLWAFLDALYRAYVAP 228
Haem_oxygenas_2 pfam14518
Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, ...
154-310 5.01e-13

Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, crystal structure reveals a dimer of seven-helical bundles. Each bundle contains a di-iron centre adjacent to an internal cavity that forms an active site similar to that of methane mono-oxygenase hydrolase.


Pssm-ID: 434009  Cd Length: 178  Bit Score: 66.64  E-value: 5.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730237985  154 RFFLEHHWVRSYNFYSLLAELAFRFENIEDASVFYRNLYGEAGAETPERSHPALLSHLMTYFDIPL-RIDFPALHPLEKA 232
Cdd:pfam14518   1 REFLRQRYPYVLVFADWLALVIPRLPDGRAKAALVENLWEELGDGDPERNHVELFRRLLAALGLDPeYLEYLPELPETLA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730237985  233 YLNNRIRCVRHTD-VAWGLALLYAVESVSCVNHRRIYELLQRLGVPEQPSEFHRLHGTQDEIDTEEMWALIAKFAPSED 310
Cdd:pfam14518  81 LVNLMSLFGLHRRlRGALLGALAALELTSPPPALRLAKGLRRLGLDDEALYYFDEHVEIDAAHAQMALEDVLEPLADEE 159
 
Name Accession Description Interval E-value
HOASN pfam14515
Haem-oxygenase-associated N-terminal helices; This domain represents a pair of alpha helices, ...
20-106 4.25e-47

Haem-oxygenase-associated N-terminal helices; This domain represents a pair of alpha helices, which are found at the N-terminus of some Haem-oxygenase globular domain.


Pssm-ID: 405239  Cd Length: 92  Bit Score: 154.54  E-value: 4.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730237985   20 SQRTMSEPAR-----NASALLAEALKPGASLDQITLALEAILAVTAKGLGGDASAYAQYQALLLELHVGSDPHTEPTRRW 94
Cdd:pfam14515   1 NQRNFSEPALqnlpiEAAAILADALAPGASLDQIDLAAEAIAALAAAGLGGDAQAYAAYQALLLELHLGDDPATAPTRRW 80
                          90
                  ....*....|..
gi 730237985   95 MASQVYLVEDRF 106
Cdd:pfam14515  81 LARAIYLVEDRF 92
PqqC COG5424
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];
115-340 2.64e-40

Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];


Pssm-ID: 444176  Cd Length: 228  Bit Score: 141.57  E-value: 2.64e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730237985 115 AVPVEEFCKKVDAEIEARSRVRHPMSVHLFQGTPPVEDVRFFLEHHWVRSYNFYSLLAELAFRFENIEDASVFYRNLYGE 194
Cdd:COG5424    1 LLSPEEFEARLRAEIARRYLLKHPFLQRLREGKLTREQLRAFALQRYHYVKHFPRYLAAILSRCPDEELRRALLENLYEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730237985 195 AGAEtPERSHPALLSHLMTYFDIPL-RIDFPALHPLEKAYLNNRIRCVRHTDVAWGLALLYAVESVSCVNHRRIYELLQR 273
Cdd:COG5424   81 DGEG-PEEGHIELWLRFAEALGLDReEVDARPPLPETRAAVDAYVNFCRRRSLLEAVAASLTAEGFAPEISRERLEGLLE 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730237985 274 -LGVP-EQPSEFHRLHGTQDEIDTEEMWALIAKFAPSEDFQRKFMQSLARHFEINRAYFDLLWEQMQAN 340
Cdd:COG5424  160 hYGLPdEEALEYFRLHAELDPRHAEEALELVLRLADTPEDQEAALEAARFKLDLLWAFLDALYRAYVAP 228
Haem_oxygenas_2 pfam14518
Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, ...
154-310 5.01e-13

Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, crystal structure reveals a dimer of seven-helical bundles. Each bundle contains a di-iron centre adjacent to an internal cavity that forms an active site similar to that of methane mono-oxygenase hydrolase.


Pssm-ID: 434009  Cd Length: 178  Bit Score: 66.64  E-value: 5.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730237985  154 RFFLEHHWVRSYNFYSLLAELAFRFENIEDASVFYRNLYGEAGAETPERSHPALLSHLMTYFDIPL-RIDFPALHPLEKA 232
Cdd:pfam14518   1 REFLRQRYPYVLVFADWLALVIPRLPDGRAKAALVENLWEELGDGDPERNHVELFRRLLAALGLDPeYLEYLPELPETLA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730237985  233 YLNNRIRCVRHTD-VAWGLALLYAVESVSCVNHRRIYELLQRLGVPEQPSEFHRLHGTQDEIDTEEMWALIAKFAPSED 310
Cdd:pfam14518  81 LVNLMSLFGLHRRlRGALLGALAALELTSPPPALRLAKGLRRLGLDDEALYYFDEHVEIDAAHAQMALEDVLEPLADEE 159
 
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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