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Conserved domains on  [gi|194597715|gb|ACF78094|]
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ammonia monooxygenase subunit A, partial [beta proteobacterium enrichment culture clone SF06E-BA10-C02]

Protein Classification

methane monooxygenase/ammonia monooxygenase subunit A family protein( domain architecture ID 229400)

methane monooxygenase/ammonia monooxygenase subunit A is part of the methane or ammonia monooxygenase complex that catalyzes the oxidation of methane to methanol or ammonia to hydroxylamine, respectively

CATH:  1.20.1450.10
EC:  1.14.-.-
Gene Ontology:  GO:0004497
SCOP:  3002268

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AMO super family cl21655
Ammonia monooxygenase; Ammonia monooxygenase plays a key role in the nitrogen cycle and ...
1-132 1.18e-69

Ammonia monooxygenase; Ammonia monooxygenase plays a key role in the nitrogen cycle and degrades a wide range of hydrocarbons and halogenated hydrocarbons.


The actual alignment was detected with superfamily member NF041557:

Pssm-ID: 473928  Cd Length: 234  Bit Score: 209.86  E-value: 1.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194597715   1 HYPINFVLPSTMIPGALIMDTCLLLTRNWMITALFGGGAFGLLFYPGNWPIFGPTHLPLVVEGVLLSLADYTGFLYVRTG 80
Cdd:NF041557 102 YFPINFVFPATLIPGALVLDIVLMLSGSWLVTAIVGGMGWGLLFYPANWPIIAPYHVPVEYNGSLMSLADLIGYHYVRTG 181
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 194597715  81 TPEYVRLIEQGSLRTFGGHTTVIAAFFAAFVSMLMFVVWWYLGRFYCTSFYY 132
Cdd:NF041557 182 TPEYIRMVERGTLRTFGKDVTPVSAFFSAFVSILMYFLWWFIGKWFATTKFI 233
 
Name Accession Description Interval E-value
AmoA_BACT NF041557
bacterial ammonia monooxygenase, subunit AmoA;
1-132 1.18e-69

bacterial ammonia monooxygenase, subunit AmoA;


Pssm-ID: 469442  Cd Length: 234  Bit Score: 209.86  E-value: 1.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194597715   1 HYPINFVLPSTMIPGALIMDTCLLLTRNWMITALFGGGAFGLLFYPGNWPIFGPTHLPLVVEGVLLSLADYTGFLYVRTG 80
Cdd:NF041557 102 YFPINFVFPATLIPGALVLDIVLMLSGSWLVTAIVGGMGWGLLFYPANWPIIAPYHVPVEYNGSLMSLADLIGYHYVRTG 181
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 194597715  81 TPEYVRLIEQGSLRTFGGHTTVIAAFFAAFVSMLMFVVWWYLGRFYCTSFYY 132
Cdd:NF041557 182 TPEYIRMVERGTLRTFGKDVTPVSAFFSAFVSILMYFLWWFIGKWFATTKFI 233
AMO pfam02461
Ammonia monooxygenase; Ammonia monooxygenase plays a key role in the nitrogen cycle and ...
1-131 2.42e-66

Ammonia monooxygenase; Ammonia monooxygenase plays a key role in the nitrogen cycle and degrades a wide range of hydrocarbons and halogenated hydrocarbons.


Pssm-ID: 426783  Cd Length: 238  Bit Score: 201.48  E-value: 2.42e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194597715    1 HYPINFVLPSTMIPGALIMDTCLLLTRNWMITALFGGGAFGLLFYPGNWPIFGPTHLPLVVEGVLLSLADYTGFLYVRTG 80
Cdd:pfam02461 106 YFPINFVFPSTLIPGALVLDAVLMLSGSYTITAIVGGLAWGLLFYPGNWPIIAPFHVPVEYNGVLMTLADLIGFQYVRTG 185
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 194597715   81 TPEYVRLIEQGSLRTFGGHTTVIAAFFAAFVSMLMFVVWWYLGRFYCTSFY 131
Cdd:pfam02461 186 TPEYIRMVERGTLRTFGKDVVPVAAFFSGFVSMLMYFLWWFFGKWFSTTKY 236
 
Name Accession Description Interval E-value
AmoA_BACT NF041557
bacterial ammonia monooxygenase, subunit AmoA;
1-132 1.18e-69

bacterial ammonia monooxygenase, subunit AmoA;


Pssm-ID: 469442  Cd Length: 234  Bit Score: 209.86  E-value: 1.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194597715   1 HYPINFVLPSTMIPGALIMDTCLLLTRNWMITALFGGGAFGLLFYPGNWPIFGPTHLPLVVEGVLLSLADYTGFLYVRTG 80
Cdd:NF041557 102 YFPINFVFPATLIPGALVLDIVLMLSGSWLVTAIVGGMGWGLLFYPANWPIIAPYHVPVEYNGSLMSLADLIGYHYVRTG 181
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 194597715  81 TPEYVRLIEQGSLRTFGGHTTVIAAFFAAFVSMLMFVVWWYLGRFYCTSFYY 132
Cdd:NF041557 182 TPEYIRMVERGTLRTFGKDVTPVSAFFSAFVSILMYFLWWFIGKWFATTKFI 233
AMO pfam02461
Ammonia monooxygenase; Ammonia monooxygenase plays a key role in the nitrogen cycle and ...
1-131 2.42e-66

Ammonia monooxygenase; Ammonia monooxygenase plays a key role in the nitrogen cycle and degrades a wide range of hydrocarbons and halogenated hydrocarbons.


Pssm-ID: 426783  Cd Length: 238  Bit Score: 201.48  E-value: 2.42e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194597715    1 HYPINFVLPSTMIPGALIMDTCLLLTRNWMITALFGGGAFGLLFYPGNWPIFGPTHLPLVVEGVLLSLADYTGFLYVRTG 80
Cdd:pfam02461 106 YFPINFVFPSTLIPGALVLDAVLMLSGSYTITAIVGGLAWGLLFYPGNWPIIAPFHVPVEYNGVLMTLADLIGFQYVRTG 185
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 194597715   81 TPEYVRLIEQGSLRTFGGHTTVIAAFFAAFVSMLMFVVWWYLGRFYCTSFY 131
Cdd:pfam02461 186 TPEYIRMVERGTLRTFGKDVVPVAAFFSGFVSMLMYFLWWFFGKWFSTTKY 236
 
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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