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Conserved domains on  [gi|50058172|dbj|BAD27429|]
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adenosine monophosphate deaminase 1, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AMP_deaminase super family cl44756
AMP deaminase;
1-42 5.93e-20

AMP deaminase;


The actual alignment was detected with superfamily member pfam19326:

Pssm-ID: 437158 [Multi-domain]  Cd Length: 622  Bit Score: 79.81  E-value: 5.93e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 50058172     1 DVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKH 42
Cdd:pfam19326 342 DIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPELHVFLKR 383
 
Name Accession Description Interval E-value
AMP_deaminase pfam19326
AMP deaminase;
1-42 5.93e-20

AMP deaminase;


Pssm-ID: 437158 [Multi-domain]  Cd Length: 622  Bit Score: 79.81  E-value: 5.93e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 50058172     1 DVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKH 42
Cdd:pfam19326 342 DIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPELHVFLKR 383
AMPD cd01319
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ...
 1-42 6.77e-17

AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at position 6 of the adenine nucleotide ring. AMPD is a diverse and highly regulated eukaryotic key enzyme of the adenylate catabolic pathway.


Pssm-ID: 238644  Cd Length: 496  Bit Score: 71.24  E-value: 6.77e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 50058172   1 DVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKH 42
Cdd:cd01319 225 DVYKKSGIVNSFQEMLENIFEPLFEATKDPSSHPELHVFLQQ 266
AMP_deaminase TIGR01429
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ...
 1-42 2.13e-13

AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein involved in energy metabolism. Most members of the family have an additional, poorly alignable region of 150 amino acids or more N-terminal to the region included in the model.


Pssm-ID: 273618 [Multi-domain]  Cd Length: 611  Bit Score: 61.40  E-value: 2.13e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 50058172     1 DVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKH 42
Cdd:TIGR01429 336 DVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQ 377
PTZ00310 PTZ00310
AMP deaminase; Provisional
 2-42 9.04e-09

AMP deaminase; Provisional


Pssm-ID: 240354 [Multi-domain]  Cd Length: 1453  Bit Score: 48.27  E-value: 9.04e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 50058172     2 VFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKH 42
Cdd:PTZ00310 1011 VFRAQNVIGSFGQYLDNIFQPLWEASLHPSKHPKFHYFLNH 1051
 
Name Accession Description Interval E-value
AMP_deaminase pfam19326
AMP deaminase;
1-42 5.93e-20

AMP deaminase;


Pssm-ID: 437158 [Multi-domain]  Cd Length: 622  Bit Score: 79.81  E-value: 5.93e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 50058172     1 DVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKH 42
Cdd:pfam19326 342 DIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPELHVFLKR 383
AMPD cd01319
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ...
 1-42 6.77e-17

AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at position 6 of the adenine nucleotide ring. AMPD is a diverse and highly regulated eukaryotic key enzyme of the adenylate catabolic pathway.


Pssm-ID: 238644  Cd Length: 496  Bit Score: 71.24  E-value: 6.77e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 50058172   1 DVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKH 42
Cdd:cd01319 225 DVYKKSGIVNSFQEMLENIFEPLFEATKDPSSHPELHVFLQQ 266
AMP_deaminase TIGR01429
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ...
 1-42 2.13e-13

AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein involved in energy metabolism. Most members of the family have an additional, poorly alignable region of 150 amino acids or more N-terminal to the region included in the model.


Pssm-ID: 273618 [Multi-domain]  Cd Length: 611  Bit Score: 61.40  E-value: 2.13e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 50058172     1 DVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKH 42
Cdd:TIGR01429 336 DVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQ 377
PTZ00310 PTZ00310
AMP deaminase; Provisional
 2-42 9.04e-09

AMP deaminase; Provisional


Pssm-ID: 240354 [Multi-domain]  Cd Length: 1453  Bit Score: 48.27  E-value: 9.04e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 50058172     2 VFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKH 42
Cdd:PTZ00310 1011 VFRAQNVIGSFGQYLDNIFQPLWEASLHPSKHPKFHYFLNH 1051
PLN02768 PLN02768
AMP deaminase
 1-41 1.22e-08

AMP deaminase


Pssm-ID: 215411  Cd Length: 835  Bit Score: 47.55  E-value: 1.22e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 50058172    1 DVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLK 41
Cdd:PLN02768 548 NVYKEMGIVTSFQNILDNIFIPLFEVTVDPDSHPQLHVFLK 588
PLN03055 PLN03055
AMP deaminase; Provisional
 1-42 4.66e-08

AMP deaminase; Provisional


Pssm-ID: 178613  Cd Length: 602  Bit Score: 46.01  E-value: 4.66e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 50058172    1 DVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKH 42
Cdd:PLN03055 315 NVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKM 356
 
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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