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Conserved domains on  [gi|1958803240|ref|XP_038939845|]
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autophagy-related protein 16-1 isoform X3 [Rattus norvegicus]

Protein Classification

WD repeat ATG16 family protein( domain architecture ID 12095058)

WD repeat ATG16 (autophagy-related 16) family protein similar to human ATG16L1 that plays an essential role in autophagy; it interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine to LC3, and thus, controls the elongation of the nascent autophagosomal membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
133-536 1.51e-58

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 199.75  E-value: 1.51e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 133 QARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGLSESPLLGHHSS 212
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 213 DAARRRSvssipvPQDVVDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKC 288
Cdd:COG2319    81 VLSVAFS------PDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 289 EfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 368
Cdd:COG2319   155 L--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 369 LRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLL 444
Cdd:COG2319   233 LATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 445 KIIDLRTNAIKQSFSAPgfkcGSDWTRVVFSPDGSYVAAGSADGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHV 524
Cdd:COG2319   313 RLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRTL 387

                         410
                  ....*....|..
gi 1958803240 525 VSVDKGSRAVLW 536
Cdd:COG2319   388 ASGSADGTVRLW 399
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-146 1.93e-25

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


:

Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 103.09  E-value: 1.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240  31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDVPNRHEISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958803240 111 IDLNNQMQQKDKEIQTNEakRRQARLQKELAEAAKE 146
Cdd:pfam08614  81 VDLNEELQELEKKLREDE--RRLAALEAERAQLEEK 114
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
133-536 1.51e-58

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 199.75  E-value: 1.51e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 133 QARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGLSESPLLGHHSS 212
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 213 DAARRRSvssipvPQDVVDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKC 288
Cdd:COG2319    81 VLSVAFS------PDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 289 EfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 368
Cdd:COG2319   155 L--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 369 LRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLL 444
Cdd:COG2319   233 LATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 445 KIIDLRTNAIKQSFSAPgfkcGSDWTRVVFSPDGSYVAAGSADGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHV 524
Cdd:COG2319   313 RLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRTL 387

                         410
                  ....*....|..
gi 1958803240 525 VSVDKGSRAVLW 536
Cdd:COG2319   388 ASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 249-537 4.52e-56

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: 189.85  E-value: 4.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 249 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 328
Cdd:cd00200     4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR--TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 329 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmSGH 398
Cdd:cd00200    82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------SSS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 399 FDKKIRFWDIRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDW-TRVVFSP 476
Cdd:cd00200   155 QDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAFSP 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958803240 477 DGSYVAAGSADGSLYVWSVLTGKVEKVLSkQHSSSINAVAWAPSGLHVVSVDKGSRAVLWA 537
Cdd:cd00200   230 DGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-146 1.93e-25

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 103.09  E-value: 1.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240  31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDVPNRHEISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958803240 111 IDLNNQMQQKDKEIQTNEakRRQARLQKELAEAAKE 146
Cdd:pfam08614  81 VDLNEELQELEKKLREDE--RRLAALEAERAQLEEK 114
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 248-282 1.92e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 47.31  E-value: 1.92e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958803240  248 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 282
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
248-282 4.99e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.18  E-value: 4.99e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1958803240 248 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 282
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 257-493 2.45e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.47  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 257 VNAVQFSPGSRLLATGGMDRRVKLWEAF-----GDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASN-DFASRIWTVDDY 330
Cdd:PLN00181  486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 331 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 403
Cdd:PLN00181  566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 404 RFWDIRSE-----SVVREMELLGKITALDlnpeRTELLSCSRDDLLKIIDLRTNA--IKQS--FSAPGFKCGSDWTRVVF 474
Cdd:PLN00181  643 YYYDLRNPklplcTMIGHSKTVSYVRFVD----SSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSV 718

                         250
                  ....*....|....*....
gi 1958803240 475 SpDGsYVAAGSADGSLYVW 493
Cdd:PLN00181  719 S-DG-YIATGSETNEVFVY 735
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 80-169 3.33e-03

ATP synthase CF0 B' subunit; Validated


Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 38.43  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240  80 SQLQEMAQLKMKHQEELTELHKKrgelAQLVIdlnNQMQQKDKEIQTNEAKRRQARLQKELAEAAKEpLPVEQDD---DI 156
Cdd:CHL00118   67 EILAKANELTKQYEQELSKARKE----AQLEI---TQSQKEAKEIVENELKQAQKYIDSLLNEATKQ-LEAQKEKalkSL 138

                          90
                  ....*....|...
gi 1958803240 157 EVIVDETSDHTEE 169
Cdd:CHL00118  139 EEQVDTLSDQIEE 151
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
31-146 3.44e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240  31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKhdvPNRHEISPGHDGawnDSQLQEMAQLkmkhQEELTELHKKRGELAQLV 110
Cdd:COG4717   386 ELRAALEQAEEYQELKEELEELEEQLEELL---GELEELLEALDE---EELEEELEEL----EEELEELEEELEELREEL 455

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958803240 111 IDLNNQMQQ--KDKEIQtnEAKRRQARLQKELAEAAKE 146
Cdd:COG4717   456 AELEAELEQleEDGELA--ELLQELEELKAELRELAEE 491
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
133-536 1.51e-58

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 199.75  E-value: 1.51e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 133 QARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGLSESPLLGHHSS 212
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 213 DAARRRSvssipvPQDVVDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKC 288
Cdd:COG2319    81 VLSVAFS------PDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 289 EfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 368
Cdd:COG2319   155 L--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 369 LRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLL 444
Cdd:COG2319   233 LATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 445 KIIDLRTNAIKQSFSAPgfkcGSDWTRVVFSPDGSYVAAGSADGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHV 524
Cdd:COG2319   313 RLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRTL 387

                         410
                  ....*....|..
gi 1958803240 525 VSVDKGSRAVLW 536
Cdd:COG2319   388 ASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 249-537 4.52e-56

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: 189.85  E-value: 4.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 249 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 328
Cdd:cd00200     4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR--TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 329 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmSGH 398
Cdd:cd00200    82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------SSS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 399 FDKKIRFWDIRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDW-TRVVFSP 476
Cdd:cd00200   155 QDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAFSP 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958803240 477 DGSYVAAGSADGSLYVWSVLTGKVEKVLSkQHSSSINAVAWAPSGLHVVSVDKGSRAVLWA 537
Cdd:cd00200   230 DGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
248-495 1.05e-46

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 168.17  E-value: 1.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 248 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 327
Cdd:COG2319   156 RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR--TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 328 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFAGSSC-NDIVCT--EQCVMSGHFDKKIR 404
Cdd:COG2319   234 ATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGvNSVAFSpdGKLLASGSDDGTVR 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 405 FWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDW-TRVVFSPDGSYVA 482
Cdd:COG2319   314 LWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGH-----TGAvTSVAFSPDGRTLA 388

                         250
                  ....*....|...
gi 1958803240 483 AGSADGSLYVWSV 495
Cdd:COG2319   389 SGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 248-494 1.48e-37

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: 140.16  E-value: 1.48e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 248 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 327
Cdd:cd00200    87 RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT--TLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 328 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvfagsscndivcteqcvMSGHfdkkirfwd 407
Cdd:cd00200   165 RTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT-----------------LRGH--------- 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 408 irsesvvremelLGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPGFKCGSdwtrVVFSPDGSYVAAGSAD 487
Cdd:cd00200   219 ------------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTS----LAWSPDGKRLASGSAD 282


                  ....*..
gi 1958803240 488 GSLYVWS 494
Cdd:cd00200   283 GTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
249-451 1.30e-35

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 137.74  E-value: 1.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 249 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 328
Cdd:COG2319   199 TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLR--TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 329 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG--SSCNDIVCT--EQCVMSGHFDKKIR 404
Cdd:COG2319   277 TGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTGhtGAVRSVAFSpdGKTLASGSDDGTVR 355

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958803240 405 FWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLLKIIDLRT 451
Cdd:COG2319   356 LWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 332-526 5.38e-34

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: 130.15  E-value: 5.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 332 LRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV----FAGSSCNDIVCTEQCVmSGHFDKKIRFWD 407
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLkghtGPVRDVAASADGTYLA-SGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 408 IRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDWTR-VVFSPDGSYVAAGS 485
Cdd:cd00200    80 LETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNsVAFSPDGTFVASSS 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958803240 486 ADGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHVVS 526
Cdd:cd00200   155 QDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSPDGEKLLS 194
WD40 COG2319
WD40 repeat [General function prediction only];
248-410 6.93e-31

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 124.25  E-value: 6.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 248 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCefKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 327
Cdd:COG2319   240 RTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL--LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 328 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAGSScnDIVCT------EQCVMSGHFDK 401
Cdd:COG2319   318 ATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT-LTGHT--GAVTSvafspdGRTLASGSADG 394


                  ....*....
gi 1958803240 402 KIRFWDIRS 410
Cdd:COG2319   395 TVRLWDLAT 403
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-146 1.93e-25

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 103.09  E-value: 1.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240  31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDVPNRHEISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958803240 111 IDLNNQMQQKDKEIQTNEakRRQARLQKELAEAAKE 146
Cdd:pfam08614  81 VDLNEELQELEKKLREDE--RRLAALEAERAQLEEK 114
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 248-282 1.92e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 47.31  E-value: 1.92e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958803240  248 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 282
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 331-368 3.35e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 46.54  E-value: 3.35e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1958803240  331 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 368
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
248-282 4.99e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.18  E-value: 4.99e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1958803240 248 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 282
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
331-368 9.25e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 9.25e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958803240 331 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 368
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
290-498 9.29e-07

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 50.08  E-value: 9.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 290 FKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARI-VSGSHDRTLKLWD 368
Cdd:COG3391    17 ALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLyVANSGSGRVSVID 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 369 LRSKVCIKTVFAGSSCNDIVCTE---QCVMSGHFDKKIRFWDIRSESVVREMELLGKITALDLNPERTELLSCSRDD--- 442
Cdd:COG3391    97 LATGKVVATIPVGGGPRGLAVDPdggRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSntv 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958803240 443 --LLKIIDLRTNAIKQSFSApgfkcGSDWTRVVFSPDGS--YVA------AGSADGSLYVWSVLTG 498
Cdd:COG3391   177 svIVSVIDTATGKVVATIPV-----GGGPVGVAVSPDGRrlYVAnrgsntSNGGSNTVSVIDLATL 237
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 257-493 2.45e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.47  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 257 VNAVQFSPGSRLLATGGMDRRVKLWEAF-----GDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASN-DFASRIWTVDDY 330
Cdd:PLN00181  486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 331 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 403
Cdd:PLN00181  566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 404 RFWDIRSE-----SVVREMELLGKITALDlnpeRTELLSCSRDDLLKIIDLRTNA--IKQS--FSAPGFKCGSDWTRVVF 474
Cdd:PLN00181  643 YYYDLRNPklplcTMIGHSKTVSYVRFVD----SSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSV 718

                         250
                  ....*....|....*....
gi 1958803240 475 SpDGsYVAAGSADGSLYVW 493
Cdd:PLN00181  719 S-DG-YIATGSETNEVFVY 735
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 253-369 9.87e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.54  E-value: 9.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 253 HDGEVNAVQFSPGS-RLLATGGMDRRVKLWEAfgDKCEFKGSLSgSNAGITSIEFDSAGAYLLAasndFASRIWTVDDYR 331
Cdd:PLN00181  574 HEKRVWSIDYSSADpTLLASGSDDGSVKLWSI--NQGVSIGTIK-TKANICCVQFPSESGRSLA----FGSADHKVYYYD 646

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958803240 332 LRH------TLTGHSGKVLSAKFLlDNARIVSGSHDRTLKLWDL 369
Cdd:PLN00181  647 LRNpklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 473-539 4.06e-04

Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 43.49  E-value: 4.06e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958803240  473 VFSPDGSYVAAGSADGSLYVWSVLTGKVEKVLSKQHSSSINAVAWAPsglhvvsvDkgSRAVLWAQP 539
Cdd:COG4946    395 VWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISDLAWSP--------D--SKWLAYSKP 451
PTZ00420 PTZ00420
coronin; Provisional
 301-458 5.02e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 42.63  E-value: 5.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 301 ITSIEFDSAGaylLAASNDFASRIWTVDD------YRLRHT--------LTGHSGKVLSAKFLLDNARIV-SGSHDRTLK 365
Cdd:PTZ00420   24 ICSRVIDSCG---IACSSGFVAVPWEVEGggligaIRLENQmrkppvikLKGHTSSILDLQFNPCFSEILaSGSEDLTIR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 366 LWDLRSKvciktvfaGSSCNDIVcTEQCVMSGH---------------------FDKKIRFWDIRSESVVREMELLGKIT 424
Cdd:PTZ00420  101 VWEIPHN--------DESVKEIK-DPQCILKGHkkkisiidwnpmnyyimcssgFDSFVNIWDIENEKRAFQINMPKKLS 171

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958803240 425 ALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSF 458
Cdd:PTZ00420  172 SLKWNIKGNLLSGTCVGKHMHIIDPRKQEIASSF 205
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 470-494 5.14e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 37.68  E-value: 5.14e-04
                           10        20
                   ....*....|....*....|....*
gi 1958803240  470 TRVVFSPDGSYVAAGSADGSLYVWS 494
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
470-494 9.32e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 9.32e-04
                          10        20
                  ....*....|....*....|....*
gi 1958803240 470 TRVVFSPDGSYVAAGSADGSLYVWS 494
Cdd:pfam00400  15 TSLAFSPDGKLLASGSDDGTVKVWD 39
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 41-142 2.41e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240   41 KLLEK--SDLHSVLTQKLQAEKH--DVPNRHE--ISPGHDGAWNDSQL-QEMAQLKMKHQEELTELHKKRGELAQLVIDL 113
Cdd:pfam01576  155 KLLEEriSEFTSNLAEEEEKAKSlsKLKNKHEamISDLEERLKKEEKGrQELEKAKRKLEGESTDLQEQIAELQAQIAEL 234

                           90       100
                   ....*....|....*....|....*....
gi 1958803240  114 NNQMQQKDKEIQTneakrRQARLQKELAE 142
Cdd:pfam01576  235 RAQLAKKEEELQA-----ALARLEEETAQ 258
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 247-282 2.98e-03

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: 39.63  E-value: 2.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958803240 247 SYVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 282
Cdd:cd00200   254 VQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 466-536 2.99e-03

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 38.50  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 466 GSDWTRV----------VFSPDGSYVA-AGSADGSLYVWSV-LTGKVEKVLSKqhssSINAVAWAPSGLHVV-SVDKGSR 532
Cdd:COG0823    64 GGEPRRLtfgggynaspSWSPDGKRLAfVSRSDGRFDIYVLdLDGGAPRRLTD----GPGSPSWSPDGRRIVfSSDRGGR 139


                  ....
gi 1958803240 533 AVLW 536
Cdd:COG0823   140 PDLY 143
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 81-146 3.05e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.55  E-value: 3.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958803240  81 QLQEMAQLKMKHQEELteLHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKRRQARlqKELAEAAKE 146
Cdd:pfam13863  13 LALDAKREEIERLEEL--LKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRAL--KKAEEETKL 74
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 80-169 3.33e-03

ATP synthase CF0 B' subunit; Validated


Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 38.43  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240  80 SQLQEMAQLKMKHQEELTELHKKrgelAQLVIdlnNQMQQKDKEIQTNEAKRRQARLQKELAEAAKEpLPVEQDD---DI 156
Cdd:CHL00118   67 EILAKANELTKQYEQELSKARKE----AQLEI---TQSQKEAKEIVENELKQAQKYIDSLLNEATKQ-LEAQKEKalkSL 138

                          90
                  ....*....|...
gi 1958803240 157 EVIVDETSDHTEE 169
Cdd:CHL00118  139 EEQVDTLSDQIEE 151
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
31-146 3.44e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240  31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKhdvPNRHEISPGHDGawnDSQLQEMAQLkmkhQEELTELHKKRGELAQLV 110
Cdd:COG4717   386 ELRAALEQAEEYQELKEELEELEEQLEELL---GELEELLEALDE---EELEEELEEL----EEELEELEEELEELREEL 455

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958803240 111 IDLNNQMQQ--KDKEIQtnEAKRRQARLQKELAEAAKE 146
Cdd:COG4717   456 AELEAELEQleEDGELA--ELLQELEELKAELRELAEE 491
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 446-525 3.54e-03

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 38.50  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 446 IIDLRTNAIKQSFSAPGFKCGSDWtrvvfSPDGSYVAAGSADGS---LYVWSVLTGKVEKVLSKQHSSSinAVAWAPSGL 522
Cdd:COG0823    15 VVDLDGGEPRRLTNSPGIDTSPAW-----SPDGRRIAFTSDRGGgpqIYVVDADGGEPRRLTFGGGYNA--SPSWSPDGK 87


                  ...
gi 1958803240 523 HVV 525
Cdd:COG0823    88 RLA 90
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 81-145 5.55e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.40  E-value: 5.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958803240  81 QLQEMAQLKMKHQEELTELHKKRgelaqlvidLNNQMQQKDKEiqtnEAKRRQARLQKELAEAAK 145
Cdd:PRK09510   88 QAEELQQKQAAEQERLKQLEKER---------LAAQEQKKQAE----EAAKQAALKQKQAEEAAA 139
Ge1_WD40 pfam16529
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ...
 297-378 7.18e-03

WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of Ge-1 or enhancer of mRNA-decapping proteins. WD40-repeat regions are involved in protein-protein interactions.


Pssm-ID: 465162 [Multi-domain]  Cd Length: 328  Bit Score: 38.59  E-value: 7.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803240 297 SNAGITSIEFDSAGAYLLAASNDFASRIWTV-----DDYRLRHTLTGHSGKVLSAKFLLDNAR----------IVSGS-H 360
Cdd:pfam16529 185 EHSLLVDAAFSPDGTALATASLDGEVKFFQIylfdnRNPRCLHEWKPHDGKPLSSLFFLDNHKkppevqfwrfAITGAdN 264

                          90
                  ....*....|....*...
gi 1958803240 361 DRTLKLWDLRSKVCIKTV 378
Cdd:pfam16529 265 NSELKLWSCESWTCLQTI 282
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 80-142 7.98e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 7.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958803240  80 SQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIqtNEAKRRQARLQKELAE 142
Cdd:COG4942    41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL--AELEKEIAELRAELEA 101
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 79-146 8.10e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.98  E-value: 8.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958803240  79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNE-----AKRRQARLQKELAEA--AKE 146
Cdd:COG1579    16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleieeVEARIKKYEEQLGNVrnNKE 90
 
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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