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Conserved domains on  [gi|159341093|ref|YP_001542652|]
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putative ATPase [Acidianus rod-shaped virus 1]

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 ...
 13-130 3.63e-05

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 pfam00005:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 150  Bit Score: 42.25  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159341093   13 SLDINtPDFKVGVVlGENGTGKTKLLKTIAKEYEKAS---YID-----------------CLSLQTPLLATKDMVEHIKE 72
Cdd:pfam00005   5 SLTLN-PGEILALV-GPNGAGKSTLLKLIAGLLSPTEgtiLLDgqdltdderkslrkeigYVFQDPQLFPRLTVRENLRL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 159341093   73 VADDINDIHVSEDGQTYVAFT-------NGEKVPLR--ELGHGHRQLISFmAKYTVENPDILLVDAP 130
Cdd:pfam00005  83 GLLLKGLSKREKDARAEEALEklglgdlADRPVGERpgTLSGGQRQRVAI-ARALLTKPKLLLLDEP 148
 
Name Accession Description Interval E-value
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 13-130 3.63e-05

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 42.25  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159341093   13 SLDINtPDFKVGVVlGENGTGKTKLLKTIAKEYEKAS---YID-----------------CLSLQTPLLATKDMVEHIKE 72
Cdd:pfam00005   5 SLTLN-PGEILALV-GPNGAGKSTLLKLIAGLLSPTEgtiLLDgqdltdderkslrkeigYVFQDPQLFPRLTVRENLRL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 159341093   73 VADDINDIHVSEDGQTYVAFT-------NGEKVPLR--ELGHGHRQLISFmAKYTVENPDILLVDAP 130
Cdd:pfam00005  83 GLLLKGLSKREKDARAEEALEklglgdlADRPVGERpgTLSGGQRQRVAI-ARALLTKPKLLLLDEP 148
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
2-42 6.79e-05

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 42.68  E-value: 6.79e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 159341093   2 RIKIDRYKGSKSLDINTPDF-KVGVVLGENGTGKTKLLKTIA 42
Cdd:COG3950    5 SLTIENFRGFEDLEIDFDNPpRLTVLVGENGSGKTTLLEAIA 46
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 27-201 2.35e-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: 37.13  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159341093  27 LGENGTGKTKLLKTIAKEYEKASYiDCLSLQTPLLATKDMVEhikevaddindihvsedgqtyvaftngekvplRELGHG 106
Cdd:cd00009   25 YGPPGTGKTTLARAIANELFRPGA-PFLYLNASDLLEGLVVA--------------------------------ELFGHF 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159341093 107 HRQLISFMAKYtvENPDILLVDapEALLLSPHKMQNFANFIHQhtrlfsmvatqsldiyFQTINVNPSNTIVIILGNNDY 186
Cdd:cd00009   72 LVRLLFELAEK--AKPGVLFID--EIDSLSRGAQNALLRVLET----------------LNDLRIDRENVRVIGATNRPL 131

                        170
                 ....*....|....*
gi 159341093 187 MTIGGEEALDRLDFE 201
Cdd:cd00009  132 LGDLDRALYDRLDIR 146
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 26-201 2.42e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.97  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159341093    26 VLGENGTGKTKLLKTIAKEYEKAS----YIDClslqtpllatkdmvehikevaddinDIHVSEDGQTYVAFTNGEKVPLR 101
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGggviYIDG-------------------------EDILEEVLDQLLLIIVGGKKASG 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159341093   102 ELGHGHRQLISFMAKytvENPDILLVDAPEALLLSPHKMQNfanfihqhtrlfsmvatQSLDIYFQTINVNPSNTIVIIL 181
Cdd:smart00382  62 SGELRLRLALALARK---LKPDVLILDEITSLLDAEQEALL-----------------LLLEELRLLLLLKSEKNLTVIL 121

                          170       180
                   ....*....|....*....|
gi 159341093   182 GNNDYMTIGGEEALDRLDFE 201
Cdd:smart00382 122 TTNDEKDLGPALLRRRFDRR 141
 
Name Accession Description Interval E-value
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 13-130 3.63e-05

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 42.25  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159341093   13 SLDINtPDFKVGVVlGENGTGKTKLLKTIAKEYEKAS---YID-----------------CLSLQTPLLATKDMVEHIKE 72
Cdd:pfam00005   5 SLTLN-PGEILALV-GPNGAGKSTLLKLIAGLLSPTEgtiLLDgqdltdderkslrkeigYVFQDPQLFPRLTVRENLRL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 159341093   73 VADDINDIHVSEDGQTYVAFT-------NGEKVPLR--ELGHGHRQLISFmAKYTVENPDILLVDAP 130
Cdd:pfam00005  83 GLLLKGLSKREKDARAEEALEklglgdlADRPVGERpgTLSGGQRQRVAI-ARALLTKPKLLLLDEP 148
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
2-42 6.79e-05

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 42.68  E-value: 6.79e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 159341093   2 RIKIDRYKGSKSLDINTPDF-KVGVVLGENGTGKTKLLKTIA 42
Cdd:COG3950    5 SLTIENFRGFEDLEIDFDNPpRLTVLVGENGSGKTTLLEAIA 46
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 13-130 1.19e-04

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 41.97  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159341093  13 SLDINTPDfKVGVVlGENGTGKTKLLKTIAKEYE------------KASYIDclSLQTPLLATKDMVEHIKEVADDINDI 80
Cdd:COG0488  335 SLRIDRGD-RIGLI-GPNGAGKSTLLKLLAGELEpdsgtvklgetvKIGYFD--QHQEELDPDKTVLDELRDGAPGGTEQ 410

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159341093  81 HVS----------EDGQTYVA-FTNGEKVPLRelghghrqlisfMAKYTVENPDILLVDAP 130
Cdd:COG0488  411 EVRgylgrflfsgDDAFKPVGvLSGGEKARLA------------LAKLLLSPPNVLLLDEP 459
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 27-201 2.35e-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: 37.13  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159341093  27 LGENGTGKTKLLKTIAKEYEKASYiDCLSLQTPLLATKDMVEhikevaddindihvsedgqtyvaftngekvplRELGHG 106
Cdd:cd00009   25 YGPPGTGKTTLARAIANELFRPGA-PFLYLNASDLLEGLVVA--------------------------------ELFGHF 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159341093 107 HRQLISFMAKYtvENPDILLVDapEALLLSPHKMQNFANFIHQhtrlfsmvatqsldiyFQTINVNPSNTIVIILGNNDY 186
Cdd:cd00009   72 LVRLLFELAEK--AKPGVLFID--EIDSLSRGAQNALLRVLET----------------LNDLRIDRENVRVIGATNRPL 131

                        170
                 ....*....|....*
gi 159341093 187 MTIGGEEALDRLDFE 201
Cdd:cd00009  132 LGDLDRALYDRLDIR 146
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 26-201 2.42e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.97  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159341093    26 VLGENGTGKTKLLKTIAKEYEKAS----YIDClslqtpllatkdmvehikevaddinDIHVSEDGQTYVAFTNGEKVPLR 101
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGggviYIDG-------------------------EDILEEVLDQLLLIIVGGKKASG 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159341093   102 ELGHGHRQLISFMAKytvENPDILLVDAPEALLLSPHKMQNfanfihqhtrlfsmvatQSLDIYFQTINVNPSNTIVIIL 181
Cdd:smart00382  62 SGELRLRLALALARK---LKPDVLILDEITSLLDAEQEALL-----------------LLLEELRLLLLLKSEKNLTVIL 121

                          170       180
                   ....*....|....*....|
gi 159341093   182 GNNDYMTIGGEEALDRLDFE 201
Cdd:smart00382 122 TTNDEKDLGPALLRRRFDRR 141
 
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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