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Conserved domains on  [gi|1958675964|ref|XP_038947850|]
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WD repeat-containing protein 19 isoform X1 [Rattus norvegicus]

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 5.66e-31

WD domain, G-beta repeat;


:

Pssm-ID: 464937  Cd Length: 57  Bit Score: 115.77  E-value: 5.66e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958675964  508 VNDYRHPVGVKKLFPDPNGTRLVFIDEKSDGFVYCPVNDATYEIPDFSPTIKGVLWE 564
Cdd:pfam15911    1 VNEYRHSVGIKKLFPNPSGTRLVFIDEKGDGFLYNPVSDELLEIPDFPPTVKGVLWD 57
WD40 COG2319
WD40 repeat [General function prediction only];
24-345 3.32e-12

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 69.94  E-value: 3.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964   24 SSGNYLAVTGADSVVKIFDRHGQK--RSEISLPGNCVAMDWDKDGDILAVIAEKSScIYLWDANTNKTSQLDNGMRDQMS 101
Cdd:COG2319     88 PDGRLLASASADGTVRLWDLATGLllRTLTGHTGAVRSVAFSPDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGAVT 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  102 FLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNTE-NLLALGGEDRMITVSNQEGDTIRQTPV--K 178
Cdd:COG2319    167 SVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDgKLLASGSADGTVRLWDLATGKLLRTLTghS 246

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  179 SEPSDIKFStskTDERissaesTISAVVGKKMLFLFHLNEPDNPVDLEFQQAYGNIVCYSwyGDG-YIMIGFSRGT--FL 255
Cdd:COG2319    247 GSVRSVAFS---PDGR------LLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFS--PDGkLLASGSDDGTvrLW 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  256 AISThfpevGQEIFKTRDHKDNLTSVALS---QTLnkAATCGDNCIKIHDLTELRdmyAIINLDDENKGLGTLSWTDDGQ 332
Cdd:COG2319    316 DLAT-----GKLLRTLTGHTGAVRSVAFSpdgKTL--ASGSDDGTVRLWDLATGE---LLRTLTGHTGAVTSVAFSPDGR 385

                          330
                   ....*....|...
gi 1958675964  333 LLALSTQRGSLHV 345
Cdd:COG2319    386 TLASGSADGTVRL 398
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 782-1008 1.25e-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: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  782 AIQLEFTGDYVNALAHYEKGITGDNkEHDEVCLAgVAQMSIRMGDIRRganqALKHPSRVLKRDcgailenmkpkfPLSL 861
Cdd:COG2956     15 GLNYLLNGQPDKAIDLLEEALELDP-ETVEAHLA-LGNLYRRRGEYDR----AIRIHQKLLERD------------PDRA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  862 QQFSEAAQLYEKGQYYDRAASVYIRC---------------------KNWAK---VGELLPHVS--SPKIHLQYAKAKEA 915
Cdd:COG2956     77 EALLELAQDYLKAGLLDRAEELLEKLleldpddaealrllaeiyeqeGDWEKaieVLERLLKLGpeNAHAYCELAELYLE 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  916 DGRYKEAVVAYENA--KQWNSV------IRIYLDHlNNPEKAVSIVRET-----QSLDGAKMVARFFLQLGDYGSAIQFL 982
Cdd:COG2956    157 QGDYDEAIEALEKAlkLDPDCArallllAELYLEQ-GDYEEAIAALERAleqdpDYLPALPRLAELYEKLGDPEEALELL 235

                          250       260
                   ....*....|....*....|....*.
gi 1958675964  983 vlskcnNEAFTLAQQHNKMEIYADII 1008
Cdd:COG2956    236 ------RKALELDPSDDLLLALADLL 255
DZR pfam12773
Double zinc ribbon; This family consists of a pair of zinc ribbon domains.
 1261-1304 4.09e-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: 4.09e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958675964 1261 CPFCQFLLPECELLCPGCKNNIPY--CIATGRhMLKDDWTMCPHCG 1304
Cdd:pfam12773    1 CPNCGHPNPPGAKFCPACGTPLKPdrCPNCGA-PVPPNARFCPYCG 45
 
Name Accession Description Interval E-value
WD40_3 pfam15911
WD domain, G-beta repeat;
508-564 5.66e-31

WD domain, G-beta repeat;


Pssm-ID: 464937  Cd Length: 57  Bit Score: 115.77  E-value: 5.66e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958675964  508 VNDYRHPVGVKKLFPDPNGTRLVFIDEKSDGFVYCPVNDATYEIPDFSPTIKGVLWE 564
Cdd:pfam15911    1 VNEYRHSVGIKKLFPNPSGTRLVFIDEKGDGFLYNPVSDELLEIPDFPPTVKGVLWD 57
WD40 COG2319
WD40 repeat [General function prediction only];
24-345 3.32e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 69.94  E-value: 3.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964   24 SSGNYLAVTGADSVVKIFDRHGQK--RSEISLPGNCVAMDWDKDGDILAVIAEKSScIYLWDANTNKTSQLDNGMRDQMS 101
Cdd:COG2319     88 PDGRLLASASADGTVRLWDLATGLllRTLTGHTGAVRSVAFSPDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGAVT 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  102 FLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNTE-NLLALGGEDRMITVSNQEGDTIRQTPV--K 178
Cdd:COG2319    167 SVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDgKLLASGSADGTVRLWDLATGKLLRTLTghS 246

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  179 SEPSDIKFStskTDERissaesTISAVVGKKMLFLFHLNEPDNPVDLEFQQAYGNIVCYSwyGDG-YIMIGFSRGT--FL 255
Cdd:COG2319    247 GSVRSVAFS---PDGR------LLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFS--PDGkLLASGSDDGTvrLW 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  256 AISThfpevGQEIFKTRDHKDNLTSVALS---QTLnkAATCGDNCIKIHDLTELRdmyAIINLDDENKGLGTLSWTDDGQ 332
Cdd:COG2319    316 DLAT-----GKLLRTLTGHTGAVRSVAFSpdgKTL--ASGSDDGTVRLWDLATGE---LLRTLTGHTGAVTSVAFSPDGR 385

                          330
                   ....*....|...
gi 1958675964  333 LLALSTQRGSLHV 345
Cdd:COG2319    386 TLASGSADGTVRL 398
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 25-157 5.19e-10

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: 61.97  E-value: 5.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964   25 SGNYLAVTGADSVVKIFDRHgQKRSEISLPG-----NCVAMDWDKDgdiLAVIAEKSSCIYLWDANTNKTSQLDNGMRDQ 99
Cdd:cd00200    104 DGRILSSSSRDKTIKVWDVE-TGKCLTTLRGhtdwvNSVAFSPDGT---FVASSSQDGTIKLWDLRTGKCVATLTGHTGE 179

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958675964  100 MSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNTENLLALGG 157
Cdd:cd00200    180 VNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASG 237
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 782-1008 1.25e-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: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  782 AIQLEFTGDYVNALAHYEKGITGDNkEHDEVCLAgVAQMSIRMGDIRRganqALKHPSRVLKRDcgailenmkpkfPLSL 861
Cdd:COG2956     15 GLNYLLNGQPDKAIDLLEEALELDP-ETVEAHLA-LGNLYRRRGEYDR----AIRIHQKLLERD------------PDRA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  862 QQFSEAAQLYEKGQYYDRAASVYIRC---------------------KNWAK---VGELLPHVS--SPKIHLQYAKAKEA 915
Cdd:COG2956     77 EALLELAQDYLKAGLLDRAEELLEKLleldpddaealrllaeiyeqeGDWEKaieVLERLLKLGpeNAHAYCELAELYLE 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  916 DGRYKEAVVAYENA--KQWNSV------IRIYLDHlNNPEKAVSIVRET-----QSLDGAKMVARFFLQLGDYGSAIQFL 982
Cdd:COG2956    157 QGDYDEAIEALEKAlkLDPDCArallllAELYLEQ-GDYEEAIAALERAleqdpDYLPALPRLAELYEKLGDPEEALELL 235

                          250       260
                   ....*....|....*....|....*.
gi 1958675964  983 vlskcnNEAFTLAQQHNKMEIYADII 1008
Cdd:COG2956    236 ------RKALELDPSDDLLLALADLL 255
DZR pfam12773
Double zinc ribbon; This family consists of a pair of zinc ribbon domains.
 1261-1304 4.09e-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: 4.09e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958675964 1261 CPFCQFLLPECELLCPGCKNNIPY--CIATGRhMLKDDWTMCPHCG 1304
Cdd:pfam12773    1 CPNCGHPNPPGAKFCPACGTPLKPdrCPNCGA-PVPPNARFCPYCG 45
CLH smart00299
Clathrin heavy chain repeat homology;
919-972 2.04e-03

Clathrin heavy chain repeat homology;


Pssm-ID: 128594 [Multi-domain]  Cd Length: 140  Bit Score: 39.95  E-value: 2.04e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958675964   919 YKEAVVAYENAKQWNSVIRIYLDHLNNPEKAVSIVRETQSLDGAKMVARFFLQL 972
Cdd:smart00299   85 YEEAVELYKKDGNFKDAIVTLIEHLGNYEKAIEYFVKQNNPELWAEVLKALLDK 138
IKI3 pfam04762
IKI3 family; Members of this family are components of the elongator multi-subunit component of ...
 20-82 4.95e-03

IKI3 family; Members of this family are components of the elongator multi-subunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. This region contains WD40 like repeats.


Pssm-ID: 428111 [Multi-domain]  Cd Length: 933  Bit Score: 41.54  E-value: 4.95e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958675964   20 AWqKSSGNYLAVT-GADSVVKI--FDRHGQKRSEISLPGN-----CVAMDWDKDGDILAVIAEksSCIYLW 82
Cdd:pfam04762  264 SW-RPSGSLIASIqRKDDRLDVvfFERNGLRHGEFTLRLNpaeekVQSLAWNSDSEVLAVVLE--DRVQLW 331
SNAP cd15832
Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the ...
 910-1073 5.92e-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: 40.26  E-value: 5.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  910 AKAKEADGRYKEAVVAYENAKQWNSVIRIYLdhlnnpeKAVSIVRETQSLDGAkmvARFFLQLGD-------------YG 976
Cdd:cd15832     26 SKYEEAAELYEKAANAFKLAKNWEEAGDAFL-------KAAECQLKLDSKHDA---ANAYVEAAKcykkvdpqeavncLE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  977 SAIQFLVlskCNNEAFTLAQQHNKM-EIYADIIGAEDTTNEDYQSIALYFEGEKRHFQAGKFFLLCGQYSRALKHFLKcp 1055
Cdd:cd15832     96 KAIEIYT---EMGRFRQAAKHLKEIaELYENELGDLDKAIEAYEQAADYYEGEGANSLANKCYLKVADLAAQLEDYDK-- 170

                          170
                   ....*....|....*...
gi 1958675964 1056 ssednvAIEmAIETVGQA 1073
Cdd:cd15832    171 ------AIE-IYEQVARS 181
 
Name Accession Description Interval E-value
WD40_3 pfam15911
WD domain, G-beta repeat;
508-564 5.66e-31

WD domain, G-beta repeat;


Pssm-ID: 464937  Cd Length: 57  Bit Score: 115.77  E-value: 5.66e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958675964  508 VNDYRHPVGVKKLFPDPNGTRLVFIDEKSDGFVYCPVNDATYEIPDFSPTIKGVLWE 564
Cdd:pfam15911    1 VNEYRHSVGIKKLFPNPSGTRLVFIDEKGDGFLYNPVSDELLEIPDFPPTVKGVLWD 57
WD40 COG2319
WD40 repeat [General function prediction only];
24-345 3.32e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 69.94  E-value: 3.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964   24 SSGNYLAVTGADSVVKIFDRHGQK--RSEISLPGNCVAMDWDKDGDILAVIAEKSScIYLWDANTNKTSQLDNGMRDQMS 101
Cdd:COG2319     88 PDGRLLASASADGTVRLWDLATGLllRTLTGHTGAVRSVAFSPDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGAVT 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  102 FLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNTE-NLLALGGEDRMITVSNQEGDTIRQTPV--K 178
Cdd:COG2319    167 SVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDgKLLASGSADGTVRLWDLATGKLLRTLTghS 246

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  179 SEPSDIKFStskTDERissaesTISAVVGKKMLFLFHLNEPDNPVDLEFQQAYGNIVCYSwyGDG-YIMIGFSRGT--FL 255
Cdd:COG2319    247 GSVRSVAFS---PDGR------LLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFS--PDGkLLASGSDDGTvrLW 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  256 AISThfpevGQEIFKTRDHKDNLTSVALS---QTLnkAATCGDNCIKIHDLTELRdmyAIINLDDENKGLGTLSWTDDGQ 332
Cdd:COG2319    316 DLAT-----GKLLRTLTGHTGAVRSVAFSpdgKTL--ASGSDDGTVRLWDLATGE---LLRTLTGHTGAVTSVAFSPDGR 385

                          330
                   ....*....|...
gi 1958675964  333 LLALSTQRGSLHV 345
Cdd:COG2319    386 TLASGSADGTVRL 398
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 25-157 5.19e-10

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: 61.97  E-value: 5.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964   25 SGNYLAVTGADSVVKIFDRHgQKRSEISLPG-----NCVAMDWDKDgdiLAVIAEKSSCIYLWDANTNKTSQLDNGMRDQ 99
Cdd:cd00200    104 DGRILSSSSRDKTIKVWDVE-TGKCLTTLRGhtdwvNSVAFSPDGT---FVASSSQDGTIKLWDLRTGKCVATLTGHTGE 179

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958675964  100 MSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNTENLLALGG 157
Cdd:cd00200    180 VNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASG 237
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 59-346 1.75e-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: 57.34  E-value: 1.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964   59 AMDWDKDGDILAVIAEkSSCIYLWDANTNKTSQLDNGMRDQMSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKH 138
Cdd:cd00200     14 CVAFSPDGKLLATGSG-DGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGH 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  139 TKKITCGCWNTEN-LLALGGEDRMITVSNQEGDTIRQTpvksepsdikfstsktderISSAESTISAVVgkkmlflFHln 217
Cdd:cd00200     93 TSYVSSVAFSPDGrILSSSSRDKTIKVWDVETGKCLTT-------------------LRGHTDWVNSVA-------FS-- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  218 ePDNPVdlefqqaygnIVCYSWygDGYIMI-----GFSRGTFLAisthfpevgqeifktrdHKDNLTSVALSQTLNK-AA 291
Cdd:cd00200    145 -PDGTF----------VASSSQ--DGTIKLwdlrtGKCVATLTG-----------------HTGEVNSVAFSPDGEKlLS 194

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958675964  292 TCGDNCIKIHDLTELRdmyAIINLDDENKGLGTLSWTDDGQLLALSTQRGSLHVF 346
Cdd:cd00200    195 SSSDGTIKLWDLSTGK---CLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVW 246
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 24-174 5.63e-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: 55.80  E-value: 5.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964   24 SSGNYLAVTGADSVVKIFDRHGQKRSEIsLPG-----NCVamDWDKDGDILAVIAEKSSCIyLWDANTNKTSQLDNGMRD 98
Cdd:cd00200     61 ADGTYLASGSSDKTIRLWDLETGECVRT-LTGhtsyvSSV--AFSPDGRILSSSSRDKTIK-VWDVETGKCLTTLRGHTD 136

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958675964   99 QMSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCW-NTENLLALGGEDRMITVSN-QEGDTIRQ 174
Cdd:cd00200    137 WVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFsPDGEKLLSSSSDGTIKLWDlSTGKCLGT 214
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 25-162 4.81e-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: 53.11  E-value: 4.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964   25 SGNYLAVTGADSVVKIFDRHGQKRSEiSLPG-----NCVAmdWDKDGDILAVIAEkSSCIYLWDANTNKTSQLDNGMRDQ 99
Cdd:cd00200    146 DGTFVASSSQDGTIKLWDLRTGKCVA-TLTGhtgevNSVA--FSPDGEKLLSSSS-DGTIKLWDLSTGKCLGTLRGHENG 221

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958675964  100 MSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCW-NTENLLALGGEDRMI 162
Cdd:cd00200    222 VNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWsPDGKRLASGSADGTI 285
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 782-1008 1.25e-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: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  782 AIQLEFTGDYVNALAHYEKGITGDNkEHDEVCLAgVAQMSIRMGDIRRganqALKHPSRVLKRDcgailenmkpkfPLSL 861
Cdd:COG2956     15 GLNYLLNGQPDKAIDLLEEALELDP-ETVEAHLA-LGNLYRRRGEYDR----AIRIHQKLLERD------------PDRA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  862 QQFSEAAQLYEKGQYYDRAASVYIRC---------------------KNWAK---VGELLPHVS--SPKIHLQYAKAKEA 915
Cdd:COG2956     77 EALLELAQDYLKAGLLDRAEELLEKLleldpddaealrllaeiyeqeGDWEKaieVLERLLKLGpeNAHAYCELAELYLE 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  916 DGRYKEAVVAYENA--KQWNSV------IRIYLDHlNNPEKAVSIVRET-----QSLDGAKMVARFFLQLGDYGSAIQFL 982
Cdd:COG2956    157 QGDYDEAIEALEKAlkLDPDCArallllAELYLEQ-GDYEEAIAALERAleqdpDYLPALPRLAELYEKLGDPEEALELL 235

                          250       260
                   ....*....|....*....|....*.
gi 1958675964  983 vlskcnNEAFTLAQQHNKMEIYADII 1008
Cdd:COG2956    236 ------RKALELDPSDDLLLALADLL 255
WD40 COG2319
WD40 repeat [General function prediction only];
65-346 4.85e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 50.68  E-value: 4.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964   65 DGDILAVIAEKSScIYLWDANTNKTSQLDNGMRDQMSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITC 144
Cdd:COG2319     89 DGRLLASASADGT-VRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTS 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  145 GCWNTE-NLLALGGEDRMITV-SNQEGDTIRqtpvksepsdikfstsktdeRISSAESTISAVVgkkmlflFHlnePDnp 222
Cdd:COG2319    168 VAFSPDgKLLASGSDDGTVRLwDLATGKLLR--------------------TLTGHTGAVRSVA-------FS---PD-- 215

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  223 vdlefqqayGNIVcYSWYGDGYIMIgFSRGTflaisthfpevGQEIFKTRDHKDNLTSVALS---QTLnkAATCGDNCIK 299
Cdd:COG2319    216 ---------GKLL-ASGSADGTVRL-WDLAT-----------GKLLRTLTGHSGSVRSVAFSpdgRLL--ASGSADGTVR 271

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1958675964  300 IHDLTELRdmyAIINLDDENKGLGTLSWTDDGQLLALSTQRGSLHVF 346
Cdd:COG2319    272 LWDLATGE---LLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW 315
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 690-929 1.11e-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: 48.57  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  690 EVEFAIRVsrtmgdvgtvmsLEQIKGIEDYNLLA----GHLAMFTNDFNLAQDLY-----LASNCPVAALEMRR---DLQ 757
Cdd:COG2956     57 EYDRAIRI------------HQKLLERDPDRAEAllelAQDYLKAGLLDRAEELLeklleLDPDDAEALRLLAEiyeQEG 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  758 HWDSALQLAKRLAP--DQIPFISKEYAIQLEFTGDYVNALAHYEKGITgDNKEHDEVCLAgVAQMSIRMGDirrgANQAL 835
Cdd:COG2956    125 DWEKAIEVLERLLKlgPENAHAYCELAELYLEQGDYDEAIEALEKALK-LDPDCARALLL-LAELYLEQGD----YEEAI 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  836 KHPSRVLKRDcgailenmkpkfPLSLQQFSEAAQLYEKGQYYDRAASVYIRCknwakvgelLPHVSSPKIHLQYAKAKEA 915
Cdd:COG2956    199 AALERALEQD------------PDYLPALPRLAELYEKLGDPEEALELLRKA---------LELDPSDDLLLALADLLER 257

                          250
                   ....*....|....
gi 1958675964  916 DGRYKEAVVAYENA 929
Cdd:COG2956    258 KEGLEAALALLERQ 271
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 25-300 4.11e-05

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: 46.94  E-value: 4.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964   25 SGNYLAVTGADSVVKIFDRHGQkRSEISLPG------NCVAMDWDKdgdiLAVIAEKSSCIYLWDANTNKTSQLDNGMRD 98
Cdd:cd00200     20 DGKLLATGSGDGTIKVWDLETG-ELLRTLKGhtgpvrDVAASADGT----YLASGSSDKTIRLWDLETGECVRTLTGHTS 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964   99 QMSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNTENLLALGG-EDRMITVSNQEGDTIRQT-- 175
Cdd:cd00200     95 YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSsQDGTIKLWDLRTGKCVATlt 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  176 ----PVKSepsdIKFSTSKTDERISSAESTIsavvgkkmlFLFHLNEPDNPVDLEFQQAYgnIVCYSWYGDGYIMIGFSR 251
Cdd:cd00200    175 ghtgEVNS----VAFSPDGEKLLSSSSDGTI---------KLWDLSTGKCLGTLRGHENG--VNSVAFSPDGYLLASGSE 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958675964  252 -GTFLAISTHFPEVGQEIFKtrdHKDNLTSVALSQTLNKAATCG-DNCIKI 300
Cdd:cd00200    240 dGTIRVWDLRTGECVQTLSG---HTNSVTSLAWSPDGKRLASGSaDGTIRI 287
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
859-929 1.96e-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: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  859 LSLQQFSEAAQLYEK---GQYYD------RAASVYIRCKNWAKVGELL-------PHVSSPKIHLQYAKAKEADGRYKEA 922
Cdd:COG4700    100 LELGRYDEAIELYEEaltGIFADdphillGLAQALFELGRYAEALETLekliaknPDFKSSDAHLLYARALEALGDLEAA 179


                   ....*..
gi 1958675964  923 VVAYENA 929
Cdd:COG4700    180 EAELEAL 186
DZR pfam12773
Double zinc ribbon; This family consists of a pair of zinc ribbon domains.
 1261-1304 4.09e-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: 4.09e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958675964 1261 CPFCQFLLPECELLCPGCKNNIPY--CIATGRhMLKDDWTMCPHCG 1304
Cdd:pfam12773    1 CPNCGHPNPPGAKFCPACGTPLKPdrCPNCGA-PVPPNARFCPYCG 45
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 859-1115 5.29e-04

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: 43.56  E-value: 5.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  859 LSLQQFSEAAQLYEKGQYyDRAASVYIrcknwaKVGELLPhvSSPKIHLQYAKAKEADGRYKEAVVAYENAKQWNS---- 934
Cdd:COG2956      7 AALGWYFKGLNYLLNGQP-DKAIDLLE------EALELDP--ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPdrae 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  935 ----VIRIYLDhLNNPEKAVSIVRETQSLDG-----AKMVARFFLQLGDYGSAIQFL--VLSKCNNEA---FTLAQQHNK 1000
Cdd:COG2956     78 alleLAQDYLK-AGLLDRAEELLEKLLELDPddaeaLRLLAEIYEQEGDWEKAIEVLerLLKLGPENAhayCELAELYLE 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964 1001 MEIYADIIGA-EDTTNEDYQSIALYFEgekrhfqAGKFFLLCGQYSRALKHFLKCPSSE-DNVAIEMAIETVGQAKDEll 1078
Cdd:COG2956    157 QGDYDEAIEAlEKALKLDPDCARALLL-------LAELYLEQGDYEEAIAALERALEQDpDYLPALPRLAELYEKLGD-- 227

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1958675964 1079 TNQLIDHLMG--ESDGMPKDAKYLFRLYMALKQYREAAR 1115
Cdd:COG2956    228 PEEALELLRKalELDPSDDLLLALADLLERKEGLEAALA 266
WD40 COG2319
WD40 repeat [General function prediction only];
81-346 1.05e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.98  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964   81 LWDANTNKTSQLDNGMRDQMSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNTE-NLLALGGED 159
Cdd:COG2319     62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDgKTLASGSAD 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  160 RMITVSNQEGDTIRQTpvksepsdikfstsktderISSAESTISAVVgkkmlflFHlnePDnpvdlefqqayGNIVcYSW 239
Cdd:COG2319    142 GTVRLWDLATGKLLRT-------------------LTGHSGAVTSVA-------FS---PD-----------GKLL-ASG 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  240 YGDGYIMIgFSRGTflaisthfpevGQEIFKTRDHKDNLTSVALS---QTLnkAATCGDNCIKIHDLTELRdmyAIINLD 316
Cdd:COG2319    181 SDDGTVRL-WDLAT-----------GKLLRTLTGHTGAVRSVAFSpdgKLL--ASGSADGTVRLWDLATGK---LLRTLT 243

                          250       260       270
                   ....*....|....*....|....*....|
gi 1958675964  317 DENKGLGTLSWTDDGQLLALSTQRGSLHVF 346
Cdd:COG2319    244 GHSGSVRSVAFSPDGRLLASGSADGTVRLW 273
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 780-933 1.15e-03

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: 40.56  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  780 EYAIQLEFTGDYVNALAHYEKGITgDNKEHDEVcLAGVAQMSIRMGDIRrganQALKHPSRVLKRDcgailenmkPKFPL 859
Cdd:COG4783      9 ALAQALLLAGDYDEAEALLEKALE-LDPDNPEA-FALLGEILLQLGDLD----EAIVLLHEALELD---------PDEPE 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958675964  860 SLQQFseaAQLYEKGQYYDRAASVYircknwAKVGELLPhvSSPKIHLQYAKAKEADGRYKEAVVAYENAKQWN 933
Cdd:COG4783     74 ARLNL---GLALLKAGDYDEALALL------EKALKLDP--EHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 710-931 1.31e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.06  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  710 LEQIKGIEDYNLLAGHLAMFTNDFNLAQDLYLASNCPVAALEMRRDLQHWDSALQLAKRLAPDQIP-----FISKEYAIQ 784
Cdd:COG3914      8 ALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAAllllaALLELAALL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  785 LEFTGDYVNALAHYEKGITGDNKEHDEVCLAGVAQMsiRMGDIrrgaNQALKHPSRVLKRDcgailenmkPKFPLSLQQF 864
Cdd:COG3914     88 LQALGRYEEALALYRRALALNPDNAEALFNLGNLLL--ALGRL----EEALAALRRALALN---------PDFAEAYLNL 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958675964  865 SEAaqLYEKGQYYDRAASvyircknWAKVGELLPHvsSPKIHLQYAKAKEADGRYKEAVVAYENAKQ 931
Cdd:COG3914    153 GEA--LRRLGRLEEAIAA-------LRRALELDPD--NAEALNNLGNALQDLGRLEEAIAAYRRALE 208
CLH smart00299
Clathrin heavy chain repeat homology;
919-972 2.04e-03

Clathrin heavy chain repeat homology;


Pssm-ID: 128594 [Multi-domain]  Cd Length: 140  Bit Score: 39.95  E-value: 2.04e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958675964   919 YKEAVVAYENAKQWNSVIRIYLDHLNNPEKAVSIVRETQSLDGAKMVARFFLQL 972
Cdd:smart00299   85 YEEAVELYKKDGNFKDAIVTLIEHLGNYEKAIEYFVKQNNPELWAEVLKALLDK 138
IKI3 pfam04762
IKI3 family; Members of this family are components of the elongator multi-subunit component of ...
 20-82 4.95e-03

IKI3 family; Members of this family are components of the elongator multi-subunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. This region contains WD40 like repeats.


Pssm-ID: 428111 [Multi-domain]  Cd Length: 933  Bit Score: 41.54  E-value: 4.95e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958675964   20 AWqKSSGNYLAVT-GADSVVKI--FDRHGQKRSEISLPGN-----CVAMDWDKDGDILAVIAEksSCIYLW 82
Cdd:pfam04762  264 SW-RPSGSLIASIqRKDDRLDVvfFERNGLRHGEFTLRLNpaeekVQSLAWNSDSEVLAVVLE--DRVQLW 331
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 906-982 5.72e-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: 5.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  906 HLQYAKAKEADGRYKEAVVAYENA---KQWNSVIRIYL----DHLNNPEKAVSIVRETQSLDGAKMVARFFL-----QLG 973
Cdd:COG4235     20 WLLLGRAYLRLGRYDEALAAYEKAlrlDPDNADALLDLaealLAAGDTEEAEELLERALALDPDNPEALYLLglaafQQG 99


                   ....*....
gi 1958675964  974 DYGSAIQFL 982
Cdd:COG4235    100 DYAEAIAAW 108
SNAP cd15832
Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the ...
 910-1073 5.92e-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: 40.26  E-value: 5.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  910 AKAKEADGRYKEAVVAYENAKQWNSVIRIYLdhlnnpeKAVSIVRETQSLDGAkmvARFFLQLGD-------------YG 976
Cdd:cd15832     26 SKYEEAAELYEKAANAFKLAKNWEEAGDAFL-------KAAECQLKLDSKHDA---ANAYVEAAKcykkvdpqeavncLE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675964  977 SAIQFLVlskCNNEAFTLAQQHNKM-EIYADIIGAEDTTNEDYQSIALYFEGEKRHFQAGKFFLLCGQYSRALKHFLKcp 1055
Cdd:cd15832     96 KAIEIYT---EMGRFRQAAKHLKEIaELYENELGDLDKAIEAYEQAADYYEGEGANSLANKCYLKVADLAAQLEDYDK-- 170

                          170
                   ....*....|....*...
gi 1958675964 1056 ssednvAIEmAIETVGQA 1073
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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