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Conserved domains on  [gi|296439460|sp|Q96QE3|]
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RecName: Full=ATPase family AAA domain-containing protein 5; AltName: Full=Chromosome fragility-associated gene 1 protein

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RuvB_N super family cl25701
Holliday junction DNA helicase ruvB N-terminus; The RuvB protein makes up part of the RuvABC ...
1051-1167 3.74e-14

Holliday junction DNA helicase ruvB N-terminus; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


The actual alignment was detected with superfamily member PRK04195:

Pssm-ID: 330522  Cd Length: 482  Bit Score: 77.27  E-value: 3.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439460 1051 DMLWTEKYQPQTASELIGNELAIKKLHSWLKDWKRraeleerqnlkgkrdekhedfsgGIDFKgssddeeesrlcnTVLI 1130
Cdd:PRK04195    1 MMPWVEKYRPKTLSDVVGNEKAKEQLREWIESWLK-----------------------GKPKK-------------ALLL 44
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 296439460 1131 TGPTGVGKTAAVYACAQELGFKIFEVNASSQRSGRQI 1167
Cdd:PRK04195   45 YGPPGVGKTSLAHALANDYGWEVIELNASDQRTADVI 81
 
Name Accession Description Interval E-value
PRK04195 PRK04195
replication factor C large subunit; Provisional
1051-1167 3.74e-14

replication factor C large subunit; Provisional


Pssm-ID: 235250  Cd Length: 482  Bit Score: 77.27  E-value: 3.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439460 1051 DMLWTEKYQPQTASELIGNELAIKKLHSWLKDWKRraeleerqnlkgkrdekhedfsgGIDFKgssddeeesrlcnTVLI 1130
Cdd:PRK04195    1 MMPWVEKYRPKTLSDVVGNEKAKEQLREWIESWLK-----------------------GKPKK-------------ALLL 44
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 296439460 1131 TGPTGVGKTAAVYACAQELGFKIFEVNASSQRSGRQI 1167
Cdd:PRK04195   45 YGPPGVGKTSLAHALANDYGWEVIELNASDQRTADVI 81
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
1128-1173 3.31e-06

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 306510  Cd Length: 130  Bit Score: 48.75  E-value: 3.31e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 296439460  1128 VLITGPTGVGKTAAVYACAQELGFKIFEVNASSQRSG---------RQILSQLKE 1173
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKyvgesekrlRELFEAAKK 55
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
1126-1160 8.07e-05

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  Cd Length: 151  Bit Score: 44.44  E-value: 8.07e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 296439460 1126 NTVLITGPTGVGKTAAVYACAQEL---GFKIFEVNASS 1160
Cdd:cd00009    20 KNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASD 57
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1126-1164 2.81e-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  Cd Length: 148  Bit Score: 40.05  E-value: 2.81e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 296439460   1126 NTVLITGPTGVGKTAAVYACAQEL---GFKIFEVNASSQRSG 1164
Cdd:smart00382    3 EVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEE 44
 
Name Accession Description Interval E-value
PRK04195 PRK04195
replication factor C large subunit; Provisional
1051-1167 3.74e-14

replication factor C large subunit; Provisional


Pssm-ID: 235250  Cd Length: 482  Bit Score: 77.27  E-value: 3.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439460 1051 DMLWTEKYQPQTASELIGNELAIKKLHSWLKDWKRraeleerqnlkgkrdekhedfsgGIDFKgssddeeesrlcnTVLI 1130
Cdd:PRK04195    1 MMPWVEKYRPKTLSDVVGNEKAKEQLREWIESWLK-----------------------GKPKK-------------ALLL 44
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 296439460 1131 TGPTGVGKTAAVYACAQELGFKIFEVNASSQRSGRQI 1167
Cdd:PRK04195   45 YGPPGVGKTSLAHALANDYGWEVIELNASDQRTADVI 81
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
1128-1173 3.31e-06

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 306510  Cd Length: 130  Bit Score: 48.75  E-value: 3.31e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 296439460  1128 VLITGPTGVGKTAAVYACAQELGFKIFEVNASSQRSG---------RQILSQLKE 1173
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKyvgesekrlRELFEAAKK 55
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
1126-1160 8.07e-05

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  Cd Length: 151  Bit Score: 44.44  E-value: 8.07e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 296439460 1126 NTVLITGPTGVGKTAAVYACAQEL---GFKIFEVNASS 1160
Cdd:cd00009    20 KNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASD 57
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1126-1164 2.81e-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  Cd Length: 148  Bit Score: 40.05  E-value: 2.81e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 296439460   1126 NTVLITGPTGVGKTAAVYACAQEL---GFKIFEVNASSQRSG 1164
Cdd:smart00382    3 EVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEE 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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