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Conserved domains on  [gi|1735182646|gb|KAA0025401|]
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protein transport protein SEC31-like protein B [Cucumis melo var. makuwa]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

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 ...
157-208 1.08e-10

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 cd18787:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 131  Bit Score: 57.90  E-value: 1.08e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1735182646 157 QAAHRLNILFGLAGFEATELHGNLTQVQLLDALEIFRKQQVYFLISTDVAAR 208
Cdd:cd18787    38 KRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAAR 89
 
Name Accession Description Interval E-value
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
157-208 1.08e-10

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 57.90  E-value: 1.08e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1735182646 157 QAAHRLNILFGLAGFEATELHGNLTQVQLLDALEIFRKQQVYFLISTDVAAR 208
Cdd:cd18787    38 KRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAAR 89
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
169-208 2.27e-07

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 51.30  E-value: 2.27e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1735182646 169 AGFEATELHGNLTQVQLLDALEIFRKQQVYFLISTDVAAR 208
Cdd:COG0513   264 RGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
162-208 9.90e-07

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 46.43  E-value: 9.90e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1735182646 162 LNILFGLAGFEATELHGNLTQVQLLDALEIFRKQQVYFLISTDVAAR 208
Cdd:pfam00271  30 AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
HELICc smart00490
helicase superfamily c-terminal domain;
161-208 9.50e-06

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 42.97  E-value: 9.50e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1735182646  161 RLNILFGLAGFEATELHGNLTQVQLLDALEIFRKQQVYFLISTDVAAR 208
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAER 49
 
Name Accession Description Interval E-value
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
157-208 1.08e-10

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 57.90  E-value: 1.08e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1735182646 157 QAAHRLNILFGLAGFEATELHGNLTQVQLLDALEIFRKQQVYFLISTDVAAR 208
Cdd:cd18787    38 KRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAAR 89
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
169-208 2.27e-07

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 51.30  E-value: 2.27e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1735182646 169 AGFEATELHGNLTQVQLLDALEIFRKQQVYFLISTDVAAR 208
Cdd:COG0513   264 RGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
162-208 9.90e-07

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 46.43  E-value: 9.90e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1735182646 162 LNILFGLAGFEATELHGNLTQVQLLDALEIFRKQQVYFLISTDVAAR 208
Cdd:pfam00271  30 AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
HELICc smart00490
helicase superfamily c-terminal domain;
161-208 9.50e-06

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 42.97  E-value: 9.50e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1735182646  161 RLNILFGLAGFEATELHGNLTQVQLLDALEIFRKQQVYFLISTDVAAR 208
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAER 49
 
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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