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Conserved domains on  [gi|21356705|ref|NP_648464|]
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uncharacterized protein Dmel_CG7557, isoform A [Drosophila melanogaster]

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 ...
 151-268 3.19e-03

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 cd00009:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 151  Bit Score: 37.51  E-value: 3.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356705 151 QEQALSRMERALSgSGRFRSVALLGPPGVGKT-LATETLRRCFPWPR-----NAHSYswsTQVSDEASKFR--LIRQFAD 222
Cdd:cd00009   3 QEEAIEALREALE-LPPPKNLLLYGPPGTGKTtLARAIANELFRPGApflylNASDL---LEGLVVAELFGhfLVRLLFE 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21356705 223 GLSECGVNLLIIDNLTTCDHGLVPIYNRLILEREGEPKGNQRVLVV 268
Cdd:cd00009  79 LAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVRVI 124
 
Name Accession Description Interval E-value
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 151-268 3.19e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 37.51  E-value: 3.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356705 151 QEQALSRMERALSgSGRFRSVALLGPPGVGKT-LATETLRRCFPWPR-----NAHSYswsTQVSDEASKFR--LIRQFAD 222
Cdd:cd00009   3 QEEAIEALREALE-LPPPKNLLLYGPPGTGKTtLARAIANELFRPGApflylNASDL---LEGLVVAELFGhfLVRLLFE 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21356705 223 GLSECGVNLLIIDNLTTCDHGLVPIYNRLILEREGEPKGNQRVLVV 268
Cdd:cd00009  79 LAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVRVI 124
PRK04195 PRK04195
replication factor C large subunit; Provisional
 148-203 5.72e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 38.36  E-value: 5.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356705  148 VLNQEQALSRM----ERALSGSGRfRSVALLGPPGVGKTLATETLrrcfpwprnAHSYSW 203
Cdd:PRK04195  16 VVGNEKAKEQLrewiESWLKGKPK-KALLLYGPPGVGKTSLAHAL---------ANDYGW 65
 
Name Accession Description Interval E-value
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 151-268 3.19e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 37.51  E-value: 3.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356705 151 QEQALSRMERALSgSGRFRSVALLGPPGVGKT-LATETLRRCFPWPR-----NAHSYswsTQVSDEASKFR--LIRQFAD 222
Cdd:cd00009   3 QEEAIEALREALE-LPPPKNLLLYGPPGTGKTtLARAIANELFRPGApflylNASDL---LEGLVVAELFGhfLVRLLFE 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21356705 223 GLSECGVNLLIIDNLTTCDHGLVPIYNRLILEREGEPKGNQRVLVV 268
Cdd:cd00009  79 LAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVRVI 124
PRK04195 PRK04195
replication factor C large subunit; Provisional
 148-203 5.72e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 38.36  E-value: 5.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356705  148 VLNQEQALSRM----ERALSGSGRfRSVALLGPPGVGKTLATETLrrcfpwprnAHSYSW 203
Cdd:PRK04195  16 VVGNEKAKEQLrewiESWLKGKPK-KALLLYGPPGVGKTSLAHAL---------ANDYGW 65
 
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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