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Conserved domains on  [gi|154240688|ref|NP_700440|]
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WD repeat-containing protein 19 isoform a [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40_3 pfam15911
WD domain, G-beta repeat;
508-564 5.41e-31

WD domain, G-beta repeat;


:

Pssm-ID: 464937  Cd Length: 57  Bit Score: 116.15  E-value: 5.41e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 154240688   508 VNDYRHPVGVKKLFPDPNGTRLVFIDEKSDGFVYCPVNDATYEIPDFSPTIKGVLWE 564
Cdd:pfam15911    1 VNEYRHSVGIKKLFPNPSGTRLVFIDEKGDGFLYNPVSDELLEIPDFPPTVKGVLWD 57
WD40 COG2319
WD40 repeat [General function prediction only];
24-345 1.42e-12

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 71.10  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688   24 SSGNYLAVTGADYIVKIFDRHGQK--RSEISLPGNCVTMDWDKDGDILAVIAEKSScIYLWDANTNKTSQLDNGMRDQMS 101
Cdd:COG2319    88 PDGRLLASASADGTVRLWDLATGLllRTLTGHTGAVRSVAFSPDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGAVT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  102 FLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNSE-NLLALGGEDKMITVSNQEGDTIRQTPV--K 178
Cdd:COG2319   167 SVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDgKLLASGSADGTVRLWDLATGKLLRTLTghS 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  179 SEPSDIKFSmskTDERI---SSAENTIsavvgkkmlFLFHLNEPDNPVDLEFQQAYGNIVCYSwyGDG-YIMIGFSRGT- 253
Cdd:COG2319   247 GSVRSVAFS---PDGRLlasGSADGTV---------RLWDLATGELLRTLTGHSGGVNSVAFS--PDGkLLASGSDDGTv 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  254 -FLAISThfpevGQEIFKARDHKDNLTSVALS---QTLnkAATCGDNCIKIHDLTELRdmyAIINLDDENKGLGTLSWTD 329
Cdd:COG2319   313 rLWDLAT-----GKLLRTLTGHTGAVRSVAFSpdgKTL--ASGSDDGTVRLWDLATGE---LLRTLTGHTGAVTSVAFSP 382

                         330
                  ....*....|....*.
gi 154240688  330 DGQLLALSTQRGSLHV 345
Cdd:COG2319   383 DGRTLASGSADGTVRL 398
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 782-1000 1.08e-06

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 51.65  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  782 AIQLEFTGDYVNALAHYEKGITGDNkEHDEVCLAgVAQMSIRMGDIRRganqALkhpsRVLKRdcgaILENMKQFSEA-- 859
Cdd:COG2956    15 GLNYLLNGQPDKAIDLLEEALELDP-ETVEAHLA-LGNLYRRRGEYDR----AI----RIHQK----LLERDPDRAEAll 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  860 --AQLYEKGQYYDRAASVYIRC---------------------KNWAK---VGELLPHVS--SPKIHLQYAKAKEADGRY 911
Cdd:COG2956    81 elAQDYLKAGLLDRAEELLEKLleldpddaealrllaeiyeqeGDWEKaieVLERLLKLGpeNAHAYCELAELYLEQGDY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  912 KEAVVAYENA--KQWNSV------IRIYLDHlNNPEKAVSIVRET-----QSLDGAKMVARFFLQLGDYGSAIQFLvlsk 978
Cdd:COG2956   161 DEAIEALEKAlkLDPDCArallllAELYLEQ-GDYEEAIAALERAleqdpDYLPALPRLAELYEKLGDPEEALELL---- 235

                         250       260
                  ....*....|....*....|..
gi 154240688  979 cnNEAFTLAQQHNKMEIYADII 1000
Cdd:COG2956   236 --RKALELDPSDDLLLALADLL 255
DZR pfam12773
Double zinc ribbon; This family consists of a pair of zinc ribbon domains.
 1253-1296 3.94e-04

Double zinc ribbon; This family consists of a pair of zinc ribbon domains.


:

Pssm-ID: 432773 [Multi-domain]  Cd Length: 45  Bit Score: 39.28  E-value: 3.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 154240688  1253 CPFCQFLLPECELLCPGCKNNIPY--CIATGRhMLKDDWTMCPHCG 1296
Cdd:pfam12773    1 CPNCGHPNPPGAKFCPACGTPLKPdrCPNCGA-PVPPNARFCPYCG 45
 
Name Accession Description Interval E-value
WD40_3 pfam15911
WD domain, G-beta repeat;
508-564 5.41e-31

WD domain, G-beta repeat;


Pssm-ID: 464937  Cd Length: 57  Bit Score: 116.15  E-value: 5.41e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 154240688   508 VNDYRHPVGVKKLFPDPNGTRLVFIDEKSDGFVYCPVNDATYEIPDFSPTIKGVLWE 564
Cdd:pfam15911    1 VNEYRHSVGIKKLFPNPSGTRLVFIDEKGDGFLYNPVSDELLEIPDFPPTVKGVLWD 57
WD40 COG2319
WD40 repeat [General function prediction only];
24-345 1.42e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 71.10  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688   24 SSGNYLAVTGADYIVKIFDRHGQK--RSEISLPGNCVTMDWDKDGDILAVIAEKSScIYLWDANTNKTSQLDNGMRDQMS 101
Cdd:COG2319    88 PDGRLLASASADGTVRLWDLATGLllRTLTGHTGAVRSVAFSPDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGAVT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  102 FLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNSE-NLLALGGEDKMITVSNQEGDTIRQTPV--K 178
Cdd:COG2319   167 SVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDgKLLASGSADGTVRLWDLATGKLLRTLTghS 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  179 SEPSDIKFSmskTDERI---SSAENTIsavvgkkmlFLFHLNEPDNPVDLEFQQAYGNIVCYSwyGDG-YIMIGFSRGT- 253
Cdd:COG2319   247 GSVRSVAFS---PDGRLlasGSADGTV---------RLWDLATGELLRTLTGHSGGVNSVAFS--PDGkLLASGSDDGTv 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  254 -FLAISThfpevGQEIFKARDHKDNLTSVALS---QTLnkAATCGDNCIKIHDLTELRdmyAIINLDDENKGLGTLSWTD 329
Cdd:COG2319   313 rLWDLAT-----GKLLRTLTGHTGAVRSVAFSpdgKTL--ASGSDDGTVRLWDLATGE---LLRTLTGHTGAVTSVAFSP 382

                         330
                  ....*....|....*.
gi 154240688  330 DGQLLALSTQRGSLHV 345
Cdd:COG2319   383 DGRTLASGSADGTVRL 398
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 25-157 1.16e-08

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 58.12  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688   25 SGNYLAVTGADYIVKIFDRHgQKRSEISLPG-----NCVTMDWDKDgdiLAVIAEKSSCIYLWDANTNKTSQLDNGMRDQ 99
Cdd:cd00200   104 DGRILSSSSRDKTIKVWDVE-TGKCLTTLRGhtdwvNSVAFSPDGT---FVASSSQDGTIKLWDLRTGKCVATLTGHTGE 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 154240688  100 MSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNSENLLALGG 157
Cdd:cd00200   180 VNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASG 237
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 782-1000 1.08e-06

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 51.65  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  782 AIQLEFTGDYVNALAHYEKGITGDNkEHDEVCLAgVAQMSIRMGDIRRganqALkhpsRVLKRdcgaILENMKQFSEA-- 859
Cdd:COG2956    15 GLNYLLNGQPDKAIDLLEEALELDP-ETVEAHLA-LGNLYRRRGEYDR----AI----RIHQK----LLERDPDRAEAll 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  860 --AQLYEKGQYYDRAASVYIRC---------------------KNWAK---VGELLPHVS--SPKIHLQYAKAKEADGRY 911
Cdd:COG2956    81 elAQDYLKAGLLDRAEELLEKLleldpddaealrllaeiyeqeGDWEKaieVLERLLKLGpeNAHAYCELAELYLEQGDY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  912 KEAVVAYENA--KQWNSV------IRIYLDHlNNPEKAVSIVRET-----QSLDGAKMVARFFLQLGDYGSAIQFLvlsk 978
Cdd:COG2956   161 DEAIEALEKAlkLDPDCArallllAELYLEQ-GDYEEAIAALERAleqdpDYLPALPRLAELYEKLGDPEEALELL---- 235

                         250       260
                  ....*....|....*....|..
gi 154240688  979 cnNEAFTLAQQHNKMEIYADII 1000
Cdd:COG2956   236 --RKALELDPSDDLLLALADLL 255
DZR pfam12773
Double zinc ribbon; This family consists of a pair of zinc ribbon domains.
 1253-1296 3.94e-04

Double zinc ribbon; This family consists of a pair of zinc ribbon domains.


Pssm-ID: 432773 [Multi-domain]  Cd Length: 45  Bit Score: 39.28  E-value: 3.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 154240688  1253 CPFCQFLLPECELLCPGCKNNIPY--CIATGRhMLKDDWTMCPHCG 1296
Cdd:pfam12773    1 CPNCGHPNPPGAKFCPACGTPLKPdrCPNCGA-PVPPNARFCPYCG 45
CLH smart00299
Clathrin heavy chain repeat homology;
851-964 1.09e-03

Clathrin heavy chain repeat homology;


Pssm-ID: 128594 [Multi-domain]  Cd Length: 140  Bit Score: 40.72  E-value: 1.09e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688    851 ENMKQFSEAAQLYEKgqyYDRAASVYIRCKNWakvgellPHVSSPKIhlqYAKAKEADGrYKEAVVAYENAKQWNSVIRI 930
Cdd:smart00299   39 ENPALQTKLIELYAK---YDPQKEIERLDNKS-------NHYDIEKV---GKLCEKAKL-YEEAVELYKKDGNFKDAIVT 104

                            90       100       110
                    ....*....|....*....|....*....|....
gi 154240688    931 YLDHLNNPEKAVSIVRETQSLDGAKMVARFFLQL 964
Cdd:smart00299  105 LIEHLGNYEKAIEYFVKQNNPELWAEVLKALLDK 138
SNAP cd15832
Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the ...
 902-1065 8.16e-03

Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the soluble NSF attachment protein (SNAP) family are involved in intracellular membrane trafficking, including vesicular transport between the endoplasmic reticulum and Golgi apparatus. Higher eukaryotes contain three isoforms of SNAPs: alpha, beta, and gamma. Alpha-SNAP is universally present in eukaryotes and acts as an adaptor protein between SNARE (integral membrane SNAP receptor) and NSF for recruitment to the 20S complex. Beta-SNAP is brain-specific and shares high sequence identity (about 85%) with alpha-SNAP. Gamma-SNAP is weakly related (about 20-25% identity) to the two other isoforms, and is ubiquitous. It may help regulate the activity of the 20S complex. The X-ray structures of vertebrate gamma-SNAP and yeast Sec17, a SNAP family member, show similar all-helical structures consisting of an N-terminal extended twisted sheet of four Tetratricopeptide repeat (TPR)-like helical hairpins and a C-terminal helical bundle.


Pssm-ID: 276937 [Multi-domain]  Cd Length: 278  Bit Score: 39.87  E-value: 8.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  902 AKAKEADGRYKEAVVAYENAKQWNSVIRIYLdhlnnpeKAVSIVRETQSLDGAkmvARFFLQLGD-------------YG 968
Cdd:cd15832    26 SKYEEAAELYEKAANAFKLAKNWEEAGDAFL-------KAAECQLKLDSKHDA---ANAYVEAAKcykkvdpqeavncLE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  969 SAIQFLVlskCNNEAFTLAQQHNKM-EIYADIIGAEDTTNEDYQSIALYFEGEKRHFQAGKFFLLCGQYSRALKHFLKcp 1047
Cdd:cd15832    96 KAIEIYT---EMGRFRQAAKHLKEIaELYENELGDLDKAIEAYEQAADYYEGEGANSLANKCYLKVADLAAQLEDYDK-- 170

                         170
                  ....*....|....*...
gi 154240688 1048 ssednvAIEmAIETVGQA 1065
Cdd:cd15832   171 ------AIE-IYEQVARS 181
 
Name Accession Description Interval E-value
WD40_3 pfam15911
WD domain, G-beta repeat;
508-564 5.41e-31

WD domain, G-beta repeat;


Pssm-ID: 464937  Cd Length: 57  Bit Score: 116.15  E-value: 5.41e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 154240688   508 VNDYRHPVGVKKLFPDPNGTRLVFIDEKSDGFVYCPVNDATYEIPDFSPTIKGVLWE 564
Cdd:pfam15911    1 VNEYRHSVGIKKLFPNPSGTRLVFIDEKGDGFLYNPVSDELLEIPDFPPTVKGVLWD 57
WD40 COG2319
WD40 repeat [General function prediction only];
24-345 1.42e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 71.10  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688   24 SSGNYLAVTGADYIVKIFDRHGQK--RSEISLPGNCVTMDWDKDGDILAVIAEKSScIYLWDANTNKTSQLDNGMRDQMS 101
Cdd:COG2319    88 PDGRLLASASADGTVRLWDLATGLllRTLTGHTGAVRSVAFSPDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGAVT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  102 FLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNSE-NLLALGGEDKMITVSNQEGDTIRQTPV--K 178
Cdd:COG2319   167 SVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDgKLLASGSADGTVRLWDLATGKLLRTLTghS 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  179 SEPSDIKFSmskTDERI---SSAENTIsavvgkkmlFLFHLNEPDNPVDLEFQQAYGNIVCYSwyGDG-YIMIGFSRGT- 253
Cdd:COG2319   247 GSVRSVAFS---PDGRLlasGSADGTV---------RLWDLATGELLRTLTGHSGGVNSVAFS--PDGkLLASGSDDGTv 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  254 -FLAISThfpevGQEIFKARDHKDNLTSVALS---QTLnkAATCGDNCIKIHDLTELRdmyAIINLDDENKGLGTLSWTD 329
Cdd:COG2319   313 rLWDLAT-----GKLLRTLTGHTGAVRSVAFSpdgKTL--ASGSDDGTVRLWDLATGE---LLRTLTGHTGAVTSVAFSP 382

                         330
                  ....*....|....*.
gi 154240688  330 DGQLLALSTQRGSLHV 345
Cdd:COG2319   383 DGRTLASGSADGTVRL 398
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 25-157 1.16e-08

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 58.12  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688   25 SGNYLAVTGADYIVKIFDRHgQKRSEISLPG-----NCVTMDWDKDgdiLAVIAEKSSCIYLWDANTNKTSQLDNGMRDQ 99
Cdd:cd00200   104 DGRILSSSSRDKTIKVWDVE-TGKCLTTLRGhtdwvNSVAFSPDGT---FVASSSQDGTIKLWDLRTGKCVATLTGHTGE 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 154240688  100 MSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNSENLLALGG 157
Cdd:cd00200   180 VNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASG 237
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 60-346 1.57e-08

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 57.73  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688   60 MDWDKDGDILAVIAEkSSCIYLWDANTNKTSQLDNGMRDQMSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHT 139
Cdd:cd00200    15 VAFSPDGKLLATGSG-DGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  140 KKITCGCWNSEN-LLALGGEDKMITVSNQEGDTIRQTpvksepsdikfsmsktderISSAENTISAVVgkkmlflFHlne 218
Cdd:cd00200    94 SYVSSVAFSPDGrILSSSSRDKTIKVWDVETGKCLTT-------------------LRGHTDWVNSVA-------FS--- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  219 PDNPVdlefqqaygnIVCYSWygDGYIMI-----GFSRGTFLAisthfpevgqeifkardHKDNLTSVALSQTLNK-AAT 292
Cdd:cd00200   145 PDGTF----------VASSSQ--DGTIKLwdlrtGKCVATLTG-----------------HTGEVNSVAFSPDGEKlLSS 195

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 154240688  293 CGDNCIKIHDLTELRdmyAIINLDDENKGLGTLSWTDDGQLLALSTQRGSLHVF 346
Cdd:cd00200   196 SSDGTIKLWDLSTGK---CLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVW 246
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 24-174 1.02e-07

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 55.03  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688   24 SSGNYLAVTGADYIVKIFDRHGQKRSEIsLPG-----NCVtmDWDKDGDILAVIAEKSSCIyLWDANTNKTSQLDNGMRD 98
Cdd:cd00200    61 ADGTYLASGSSDKTIRLWDLETGECVRT-LTGhtsyvSSV--AFSPDGRILSSSSRDKTIK-VWDVETGKCLTTLRGHTD 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154240688   99 QMSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCW-NSENLLALGGEDKMITVSN-QEGDTIRQ 174
Cdd:cd00200   137 WVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFsPDGEKLLSSSSDGTIKLWDlSTGKCLGT 214
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 782-1000 1.08e-06

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 51.65  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  782 AIQLEFTGDYVNALAHYEKGITGDNkEHDEVCLAgVAQMSIRMGDIRRganqALkhpsRVLKRdcgaILENMKQFSEA-- 859
Cdd:COG2956    15 GLNYLLNGQPDKAIDLLEEALELDP-ETVEAHLA-LGNLYRRRGEYDR----AI----RIHQK----LLERDPDRAEAll 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  860 --AQLYEKGQYYDRAASVYIRC---------------------KNWAK---VGELLPHVS--SPKIHLQYAKAKEADGRY 911
Cdd:COG2956    81 elAQDYLKAGLLDRAEELLEKLleldpddaealrllaeiyeqeGDWEKaieVLERLLKLGpeNAHAYCELAELYLEQGDY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  912 KEAVVAYENA--KQWNSV------IRIYLDHlNNPEKAVSIVRET-----QSLDGAKMVARFFLQLGDYGSAIQFLvlsk 978
Cdd:COG2956   161 DEAIEALEKAlkLDPDCArallllAELYLEQ-GDYEEAIAALERAleqdpDYLPALPRLAELYEKLGDPEEALELL---- 235

                         250       260
                  ....*....|....*....|..
gi 154240688  979 cnNEAFTLAQQHNKMEIYADII 1000
Cdd:COG2956   236 --RKALELDPSDDLLLALADLL 255
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 25-162 1.31e-06

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 51.57  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688   25 SGNYLAVTGADYIVKIFDRHGQKRSEiSLPG-----NCVTmdWDKDGDILAVIAEkSSCIYLWDANTNKTSQLDNGMRDQ 99
Cdd:cd00200   146 DGTFVASSSQDGTIKLWDLRTGKCVA-TLTGhtgevNSVA--FSPDGEKLLSSSS-DGTIKLWDLSTGKCLGTLRGHENG 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154240688  100 MSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCW-NSENLLALGGEDKMI 162
Cdd:cd00200   222 VNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWsPDGKRLASGSADGTI 285
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 690-921 1.45e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.19  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  690 EVEFAIRVsrtmgdvgtvmsLEQIKGIEDYNLLA----GHLAMFTNDFNLAQDLY-----LASNCPVAALEMRR---DLQ 757
Cdd:COG2956    57 EYDRAIRI------------HQKLLERDPDRAEAllelAQDYLKAGLLDRAEELLeklleLDPDDAEALRLLAEiyeQEG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  758 HWDSALQLAKRLAP--DQIPFISKEYAIQLEFTGDYVNALAHYEKGITgDNKEHDEVCLAgVAQMSIRMGDirrgANQAL 835
Cdd:COG2956   125 DWEKAIEVLERLLKlgPENAHAYCELAELYLEQGDYDEAIEALEKALK-LDPDCARALLL-LAELYLEQGD----YEEAI 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  836 KHPSRVLKRD--CGAILENMkqfseaAQLYEKGQYYDRAASVYIRCknwakvgelLPHVSSPKIHLQYAKAKEADGRYKE 913
Cdd:COG2956   199 AALERALEQDpdYLPALPRL------AELYEKLGDPEEALELLRKA---------LELDPSDDLLLALADLLERKEGLEA 263


                  ....*...
gi 154240688  914 AVVAYENA 921
Cdd:COG2956   264 ALALLERQ 271
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 710-923 1.27e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 46.52  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  710 LEQIKGIEDYNLLAGHLAMFTNDFNLAQDLYLASNCPVAALEMRRDLQHWDSALQLAKRLAPDQIP-----FISKEYAIQ 784
Cdd:COG3914     8 ALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAAllllaALLELAALL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  785 LEFTGDYVNALAHYEKGITGDNKEHDEVCLAGVAQMsiRMGDIrrgaNQALKHPSRVLKRD---------CGAILENMKQ 855
Cdd:COG3914    88 LQALGRYEEALALYRRALALNPDNAEALFNLGNLLL--ALGRL----EEALAALRRALALNpdfaeaylnLGEALRRLGR 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154240688  856 FSEAAQLYEkgqyydRAAsvyircknwakvgELLPHvsSPKIHLQYAKAKEADGRYKEAVVAYENAKQ 923
Cdd:COG3914   162 LEEAIAALR------RAL-------------ELDPD--NAEALNNLGNALQDLGRLEEAIAAYRRALE 208
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
847-921 2.35e-04

Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 44.49  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  847 GAILENMKQFSEAAQLYEK---GQYYD------RAASVYIRCKNWAKVGELL-------PHVSSPKIHLQYAKAKEADGR 910
Cdd:COG4700    96 ADALLELGRYDEAIELYEEaltGIFADdphillGLAQALFELGRYAEALETLekliaknPDFKSSDAHLLYARALEALGD 175

                          90
                  ....*....|.
gi 154240688  911 YKEAVVAYENA 921
Cdd:COG4700   176 LEAAEAELEAL 186
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 818-925 2.57e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 42.49  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  818 AQMSIRMGDirrgANQALKHPSRVLKRD---------CGAILENMKQFSEAAQLYEKG--------QYYDRAASVYIRCK 880
Cdd:COG4783    11 AQALLLAGD----YDEAEALLEKALELDpdnpeafalLGEILLQLGDLDEAIVLLHEAleldpdepEARLNLGLALLKAG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 154240688  881 NWAKVGELL-------PhvSSPKIHLQYAKAKEADGRYKEAVVAYENAKQWN 925
Cdd:COG4783    87 DYDEALALLekalkldP--EHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
WD40 COG2319
WD40 repeat [General function prediction only];
81-346 3.19e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 44.90  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688   81 LWDANTNKTSQLDNGMRDQMSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNSE-NLLALGGED 159
Cdd:COG2319    62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDgKTLASGSAD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  160 KMITVSNQEGDTIRQTpvksepsdikfsmsktderISSAENTISAVVgkkmlflFHlnePDnpvdlefqqayGNIVcYSW 239
Cdd:COG2319   142 GTVRLWDLATGKLLRT-------------------LTGHSGAVTSVA-------FS---PD-----------GKLL-ASG 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  240 YGDGYIMIgFSRGTflaisthfpevGQEIFKARDHKDNLTSVALS---QTLnkAATCGDNCIKIHDLTELRdmyAIINLD 316
Cdd:COG2319   181 SDDGTVRL-WDLAT-----------GKLLRTLTGHTGAVRSVAFSpdgKLL--ASGSADGTVRLWDLATGK---LLRTLT 243

                         250       260       270
                  ....*....|....*....|....*....|
gi 154240688  317 DENKGLGTLSWTDDGQLLALSTQRGSLHVF 346
Cdd:COG2319   244 GHSGSVRSVAFSPDGRLLASGSADGTVRLW 273
DZR pfam12773
Double zinc ribbon; This family consists of a pair of zinc ribbon domains.
 1253-1296 3.94e-04

Double zinc ribbon; This family consists of a pair of zinc ribbon domains.


Pssm-ID: 432773 [Multi-domain]  Cd Length: 45  Bit Score: 39.28  E-value: 3.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 154240688  1253 CPFCQFLLPECELLCPGCKNNIPY--CIATGRhMLKDDWTMCPHCG 1296
Cdd:pfam12773    1 CPNCGHPNPPGAKFCPACGTPLKPdrCPNCGA-PVPPNARFCPYCG 45
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 25-300 6.07e-04

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 43.48  E-value: 6.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688   25 SGNYLAVTGADYIVKIFDRHG--QKRSEISLPGNCVTMDWDKDGDILAvIAEKSSCIYLWDANTNKTSQLDNGMRDQMSF 102
Cdd:cd00200    20 DGKLLATGSGDGTIKVWDLETgeLLRTLKGHTGPVRDVAASADGTYLA-SGSSDKTIRLWDLETGECVRTLTGHTSYVSS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  103 LLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNSENLLALGG-EDKMITVSNQEGDTIRQT------ 175
Cdd:cd00200    99 VAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSsQDGTIKLWDLRTGKCVATltghtg 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  176 PVKSepsdIKFSMSKTDERISSAENTIsavvgkkmlFLFHLNEPDNPVDLEFQQAYgnIVCYSWYGDGYIMIGFSR-GTF 254
Cdd:cd00200   179 EVNS----VAFSPDGEKLLSSSSDGTI---------KLWDLSTGKCLGTLRGHENG--VNSVAFSPDGYLLASGSEdGTI 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 154240688  255 LAISTHFPEVGQEIFKardHKDNLTSVALSQTLNKAATCG-DNCIKI 300
Cdd:cd00200   244 RVWDLRTGECVQTLSG---HTNSVTSLAWSPDGKRLASGSaDGTIRI 287
CLH smart00299
Clathrin heavy chain repeat homology;
851-964 1.09e-03

Clathrin heavy chain repeat homology;


Pssm-ID: 128594 [Multi-domain]  Cd Length: 140  Bit Score: 40.72  E-value: 1.09e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688    851 ENMKQFSEAAQLYEKgqyYDRAASVYIRCKNWakvgellPHVSSPKIhlqYAKAKEADGrYKEAVVAYENAKQWNSVIRI 930
Cdd:smart00299   39 ENPALQTKLIELYAK---YDPQKEIERLDNKS-------NHYDIEKV---GKLCEKAKL-YEEAVELYKKDGNFKDAIVT 104

                            90       100       110
                    ....*....|....*....|....*....|....
gi 154240688    931 YLDHLNNPEKAVSIVRETQSLDGAKMVARFFLQL 964
Cdd:smart00299  105 LIEHLGNYEKAIEYFVKQNNPELWAEVLKALLDK 138
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
789-1022 2.37e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 41.15  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  789 GDYVNALAHYEKGITGDNKEHDEVCLAGVAQMsiRMGDIRrganQALKHPSRVLKRD---------CGAILENMKQFSEA 859
Cdd:COG0457    22 GRYEEAIEDYEKALELDPDDAEALYNLGLAYL--RLGRYE----EALADYEQALELDpddaealnnLGLALQALGRYEEA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  860 AQLYEKgqyydraasvyircknwakVGELLPhvSSPKIHLQYAKAKEADGRYKEAVVAYE--------NAKQWNSVIRIY 931
Cdd:COG0457    96 LEDYDK-------------------ALELDP--DDAEALYNLGLALLELGRYDEAIEAYEraleldpdDADALYNLGIAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  932 LdHLNNPEKAVSIVRETQSLDGAKMVARFFLQLGDYGSAIQFLVLSKCNNEAFTLAQQHNKMEIYADIIGAEDTTNEDYQ 1011
Cdd:COG0457   155 E-KLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLAL 233

                         250
                  ....*....|.
gi 154240688 1012 SIALYFEGEKR 1022
Cdd:COG0457   234 RLAALALYQYR 244
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
847-974 3.98e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 40.76  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  847 GAILENMKQFSEAAQLYEK--------GQYYDRAASVYIRCKNWA-------KVGELLPHvsSPKIHLQYAKAKEADGRY 911
Cdd:COG0457    15 GLAYRRLGRYEEAIEDYEKaleldpddAEALYNLGLAYLRLGRYEealadyeQALELDPD--DAEALNNLGLALQALGRY 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154240688  912 KEAVVAYENAKQ--------WNSVIRIYLdHLNNPEKAVSIVRETQSLDGAKMVARFFL-----QLGDYGSAIQFL 974
Cdd:COG0457    93 EEALEDYDKALEldpddaeaLYNLGLALL-ELGRYDEAIEAYERALELDPDDADALYNLgialeKLGRYEEALELL 167
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 898-974 6.44e-03

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 38.45  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  898 HLQYAKAKEADGRYKEAVVAYENA---KQWNSVIRIYL----DHLNNPEKAVSIVRETQSLDGAKMVARFFL-----QLG 965
Cdd:COG4235    20 WLLLGRAYLRLGRYDEALAAYEKAlrlDPDNADALLDLaealLAAGDTEEAEELLERALALDPDNPEALYLLglaafQQG 99


                  ....*....
gi 154240688  966 DYGSAIQFL 974
Cdd:COG4235   100 DYAEAIAAW 108
SNAP cd15832
Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the ...
 902-1065 8.16e-03

Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the soluble NSF attachment protein (SNAP) family are involved in intracellular membrane trafficking, including vesicular transport between the endoplasmic reticulum and Golgi apparatus. Higher eukaryotes contain three isoforms of SNAPs: alpha, beta, and gamma. Alpha-SNAP is universally present in eukaryotes and acts as an adaptor protein between SNARE (integral membrane SNAP receptor) and NSF for recruitment to the 20S complex. Beta-SNAP is brain-specific and shares high sequence identity (about 85%) with alpha-SNAP. Gamma-SNAP is weakly related (about 20-25% identity) to the two other isoforms, and is ubiquitous. It may help regulate the activity of the 20S complex. The X-ray structures of vertebrate gamma-SNAP and yeast Sec17, a SNAP family member, show similar all-helical structures consisting of an N-terminal extended twisted sheet of four Tetratricopeptide repeat (TPR)-like helical hairpins and a C-terminal helical bundle.


Pssm-ID: 276937 [Multi-domain]  Cd Length: 278  Bit Score: 39.87  E-value: 8.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  902 AKAKEADGRYKEAVVAYENAKQWNSVIRIYLdhlnnpeKAVSIVRETQSLDGAkmvARFFLQLGD-------------YG 968
Cdd:cd15832    26 SKYEEAAELYEKAANAFKLAKNWEEAGDAFL-------KAAECQLKLDSKHDA---ANAYVEAAKcykkvdpqeavncLE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154240688  969 SAIQFLVlskCNNEAFTLAQQHNKM-EIYADIIGAEDTTNEDYQSIALYFEGEKRHFQAGKFFLLCGQYSRALKHFLKcp 1047
Cdd:cd15832    96 KAIEIYT---EMGRFRQAAKHLKEIaELYENELGDLDKAIEAYEQAADYYEGEGANSLANKCYLKVADLAAQLEDYDK-- 170

                         170
                  ....*....|....*...
gi 154240688 1048 ssednvAIEmAIETVGQA 1065
Cdd:cd15832   171 ------AIE-IYEQVARS 181
 
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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