Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189698 315 GHQELLAQLRQQLRQDESrthtPLVLFGPPGIGKTSLMCKLAQQVPEllghkTVVVLRLLGTsklSLDARSLLRslsfQV 394
Cdd:COG3267    27 SHREALARLEYALAQGGG----FVVLTGEVGTGKTTLLRRLLERLPD-----DVKVAYIPNP---QLSPAELLR----AI 90

                          90       100
                  ....*....|....*....|....*..
gi 1907189698 395 CLAYGLPLPPAQVLEAHSRVGHFFHTL 421
Cdd:COG3267    91 ADELGLEPKGASKADLLRQLQEFLLEL 117

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907189698 870 LRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHT 920
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHT 51

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907189698 315 GHQELLAQLRQQLRQDESRthtPLVLFGPPGIGKTSLMCKLAQQVPE 361
Cdd:cd00009     2 GQEEAIEALREALELPPPK---NLLLYGPPGTGKTTLARAIANELFR 45

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907189698 868 GPLRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWD 906
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907189698 313 FCGHQELLAQLRQQLRQDESRTHTP--LVLFGPPGIGKTSL 351
Cdd:TIGR00635   6 FIGQEKVKEQLQLFIEAAKMRQEALdhLLLYGPPGLGKTTL 46

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907189698 870 LRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHT 920
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHT 51

WD40 repeat [General function prediction only];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907189698 867 GGPLRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHT 920
Cdd:COG2319   235 TGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS 288

WD40 repeat [General function prediction only];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907189698 868 GPLRATLTGcHKG-ITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHT 920
Cdd:COG2319   152 GKLLRTLTG-HSGaVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT 204

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189698 865 PPGGPLRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHT 920
Cdd:cd00200   206 LSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHT 261

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907189698 868 GPLRATLTGcHKG-ITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHT 920
Cdd:cd00200   167 GKCVATLTG-HTGeVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHE 219

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907189698 315 GHQELLAQLRQQLRQDESRthtPLVLFGPPGIGKTSLMCKLAQQVPE 361
Cdd:cd00009     2 GQEEAIEALREALELPPPK---NLLLYGPPGTGKTTLARAIANELFR 45

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907189698 868 GPLRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWD 906
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907189698 313 FCGHQELLAQLRQQLRQDESRTHTP--LVLFGPPGIGKTSL 351
Cdd:TIGR00635   6 FIGQEKVKEQLQLFIEAAKMRQEALdhLLLYGPPGLGKTTL 46

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907189698 881 ITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVL 916
Cdd:pfam12894  41 VTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHF 76

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907189698 867 GGPLRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHT 920
Cdd:cd00200    40 TGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHT 93