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Conserved domains on  [gi|15224406|ref|NP_178929|]
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P-loop containing nucleoside triphosphate hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
1-74 6.59e-55

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PLN02759:

Pssm-ID: 476819  Cd Length: 637  Bit Score: 179.20  E-value: 6.59e-55
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224406    1 MYTQQGFSNLPICMSKTQYSFSHDASKKGAPSGFVLPIRDVRGSIGAGFIYPLVGTMSTMPGLPTRPCFYEIDI 74
Cdd:PLN02759 553 MYTRQGFSNLPICMAKTQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDI 626
 
Name Accession Description Interval E-value
PLN02759 PLN02759
Formate--tetrahydrofolate ligase
1-74 6.59e-55

Formate--tetrahydrofolate ligase


Pssm-ID: 178359  Cd Length: 637  Bit Score: 179.20  E-value: 6.59e-55
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224406    1 MYTQQGFSNLPICMSKTQYSFSHDASKKGAPSGFVLPIRDVRGSIGAGFIYPLVGTMSTMPGLPTRPCFYEIDI 74
Cdd:PLN02759 553 MYTRQGFSNLPICMAKTQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDI 626
FTHFS pfam01268
Formate--tetrahydrofolate ligase;
1-74 2.02e-48

Formate--tetrahydrofolate ligase;


Pssm-ID: 460143  Cd Length: 555  Bit Score: 160.57  E-value: 2.02e-48
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224406     1 MYTQQGFSNLPICMSKTQYSFSHDASKKGAPSGFVLPIRDVRGSIGAGFIYPLVGTMSTMPGLPTRPCFYEIDI 74
Cdd:pfam01268 472 RIEELGFGKLPVCMAKTQYSLSDDPKLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDV 545
FTHFS cd00477
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ...
1-74 5.75e-48

formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ATP-dependent activation of formate ion via its addition to the N10 position of tetrahydrofolate. FTHFS is a highly expressed key enzyme in both the Wood-Ljungdahl pathway of autotrophic CO2 fixation (acetogenesis) and the glycine synthase/reductase pathways of purinolysis. The key physiological role of this enzyme in acetogens is to catalyze the formylation of tetrahydrofolate, an initial step in the reduction of carbon dioxide and other one-carbon precursors to acetate. In purinolytic organisms, the enzymatic reaction is reversed, liberating formate from 10-formyltetrahydrofolate with concurrent production of ATP.


Pssm-ID: 349750  Cd Length: 540  Bit Score: 159.24  E-value: 5.75e-48
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224406   1 MYTQQGFSNLPICMSKTQYSFSHDASKKGAPSGFVLPIRDVRGSIGAGFIYPLVGTMSTMPGLPTRPCFYEIDI 74
Cdd:cd00477 458 RYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIRDVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDI 531
MIS1 COG2759
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
1-74 5.35e-41

Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];


Pssm-ID: 442046  Cd Length: 556  Bit Score: 140.56  E-value: 5.35e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224406   1 MYTQQGFSNLPICMSKTQYSFSHDASKKGAPSGFVLPIRDVRGSIGAGFIYPLVGTMSTMPGLPTRPCFYEIDI 74
Cdd:COG2759 473 RIEELGYGKLPVCMAKTQYSLSDDPKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDI 546
 
Name Accession Description Interval E-value
PLN02759 PLN02759
Formate--tetrahydrofolate ligase
1-74 6.59e-55

Formate--tetrahydrofolate ligase


Pssm-ID: 178359  Cd Length: 637  Bit Score: 179.20  E-value: 6.59e-55
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224406    1 MYTQQGFSNLPICMSKTQYSFSHDASKKGAPSGFVLPIRDVRGSIGAGFIYPLVGTMSTMPGLPTRPCFYEIDI 74
Cdd:PLN02759 553 MYTRQGFSNLPICMAKTQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDI 626
FTHFS pfam01268
Formate--tetrahydrofolate ligase;
1-74 2.02e-48

Formate--tetrahydrofolate ligase;


Pssm-ID: 460143  Cd Length: 555  Bit Score: 160.57  E-value: 2.02e-48
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224406     1 MYTQQGFSNLPICMSKTQYSFSHDASKKGAPSGFVLPIRDVRGSIGAGFIYPLVGTMSTMPGLPTRPCFYEIDI 74
Cdd:pfam01268 472 RIEELGFGKLPVCMAKTQYSLSDDPKLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDV 545
FTHFS cd00477
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ...
1-74 5.75e-48

formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ATP-dependent activation of formate ion via its addition to the N10 position of tetrahydrofolate. FTHFS is a highly expressed key enzyme in both the Wood-Ljungdahl pathway of autotrophic CO2 fixation (acetogenesis) and the glycine synthase/reductase pathways of purinolysis. The key physiological role of this enzyme in acetogens is to catalyze the formylation of tetrahydrofolate, an initial step in the reduction of carbon dioxide and other one-carbon precursors to acetate. In purinolytic organisms, the enzymatic reaction is reversed, liberating formate from 10-formyltetrahydrofolate with concurrent production of ATP.


Pssm-ID: 349750  Cd Length: 540  Bit Score: 159.24  E-value: 5.75e-48
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224406   1 MYTQQGFSNLPICMSKTQYSFSHDASKKGAPSGFVLPIRDVRGSIGAGFIYPLVGTMSTMPGLPTRPCFYEIDI 74
Cdd:cd00477 458 RYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIRDVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDI 531
PTZ00386 PTZ00386
formyl tetrahydrofolate synthetase; Provisional
2-78 1.29e-42

formyl tetrahydrofolate synthetase; Provisional


Pssm-ID: 240394  Cd Length: 625  Bit Score: 145.74  E-value: 1.29e-42
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224406    2 YTQQGFSNLPICMSKTQYSFSHDASKKGAPSGFVLPIRDVRGSIGAGFIYPLVGTMSTMPGLPTRPCFYEIDISQSF 78
Cdd:PTZ00386 542 FERMGYGKFPVCMAKTQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCET 618
MIS1 COG2759
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
1-74 5.35e-41

Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];


Pssm-ID: 442046  Cd Length: 556  Bit Score: 140.56  E-value: 5.35e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224406   1 MYTQQGFSNLPICMSKTQYSFSHDASKKGAPSGFVLPIRDVRGSIGAGFIYPLVGTMSTMPGLPTRPCFYEIDI 74
Cdd:COG2759 473 RIEELGYGKLPVCMAKTQYSLSDDPKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDI 546
PRK13505 PRK13505
formate--tetrahydrofolate ligase; Provisional
2-74 9.09e-34

formate--tetrahydrofolate ligase; Provisional


Pssm-ID: 237403  Cd Length: 557  Bit Score: 121.06  E-value: 9.09e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224406    2 YTQQGFSNLPICMSKTQYSFSHDASKKGAPSGFVLPIRDVRGSIGAGFIYPLVGTMSTMPGLPTRPCFYEIDI 74
Cdd:PRK13505 475 IEKNGWDKLPVCMAKTQYSFSDDPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDV 547
PRK13506 PRK13506
formate--tetrahydrofolate ligase; Provisional
1-76 3.97e-32

formate--tetrahydrofolate ligase; Provisional


Pssm-ID: 237404  Cd Length: 578  Bit Score: 116.64  E-value: 3.97e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15224406    1 MYTQQGFSNLPICMSKTQYSFSHDASKKGAPSGFVLPIRDVRGSIGAGFIYPLVGTMSTMPGLPTRPCFYEIDISQ 76
Cdd:PRK13506 495 QLTALGYDHLPVCMAKTPLSISHDPALKGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDIDA 570
PRK13507 PRK13507
formate--tetrahydrofolate ligase; Provisional
7-74 3.26e-22

formate--tetrahydrofolate ligase; Provisional


Pssm-ID: 184098  Cd Length: 587  Bit Score: 88.62  E-value: 3.26e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15224406    7 FSNLPICMSKTQYSFSHDASKKGAPSGFVLPIRDVRGSIGAGFIYPLVGTMSTMPGLPTRPCFYEIDI 74
Cdd:PRK13507 509 TADFGTCMVKTHLSLSHDPALKGVPKGWTLPIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDV 576
 
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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