NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|298229007|ref|NP_001177196|]
View 

autophagy-related protein 16-1 isoform 5 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
141-488 5.49e-61

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 205.15  E-value: 5.49e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 141 VRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRV----PATALCVFDAHDGEVNAVQFSP 216
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSP 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 217 GSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 296
Cdd:COG2319  131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 297 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LL 372
Cdd:COG2319  209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 373 GKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKV 452
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 298229007 453 EKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 488
Cdd:COG2319  365 LRTL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 4-93 1.28e-31

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


:

Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 116.51  E-value: 1.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007   4 KDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKA 83
Cdd:cd22887    2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKKQ 81

                         90
                 ....*....|
gi 298229007  84 QEANRLNAEN 93
Cdd:cd22887   82 QEADKMNEAN 91
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
141-488 5.49e-61

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 205.15  E-value: 5.49e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 141 VRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRV----PATALCVFDAHDGEVNAVQFSP 216
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSP 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 217 GSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 296
Cdd:COG2319  131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 297 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LL 372
Cdd:COG2319  209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 373 GKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKV 452
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 298229007 453 EKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 488
Cdd:COG2319  365 LRTL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 199-489 1.16e-58

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: 195.25  E-value: 1.16e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 199 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVfgEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWT 278
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 279 VDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmS 348
Cdd:cd00200   80 LETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------S 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 349 GHFDKKIRFWDIRSESIVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDW-TRVVF 426
Cdd:cd00200  153 SSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAF 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298229007 427 SPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSkQHSSSINAVAWSPSGSHVVSVDKGCKAVLWA 489
Cdd:cd00200  228 SPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 4-93 1.28e-31

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 116.51  E-value: 1.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007   4 KDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKA 83
Cdd:cd22887    2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKKQ 81

                         90
                 ....*....|
gi 298229007  84 QEANRLNAEN 93
Cdd:cd22887   82 QEADKMNEAN 91
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 1-90 2.43e-28

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: 110.41  E-value: 2.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007    1 MQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMA 80
Cdd:pfam08614  87 LQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRELVERWMK 166

                          90
                  ....*....|
gi 298229007   81 EKAQEANRLN 90
Cdd:pfam08614 167 RKGQEAEAMN 176
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 199-234 8.14e-08

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: 48.46  E-value: 8.14e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 298229007   199 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 234
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
199-234 2.76e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.95  E-value: 2.76e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 298229007  199 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 234
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 209-445 1.49e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.86  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 209 VNAVQFSPGSRLLATGGMDRRVKLWEVF-----GEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASN-DFASRIWTVDDY 282
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 283 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 355
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 356 RFWDIRSESI-VREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNA--IKQT--FSAPGFKCGSDWTRVVFSpDG 430
Cdd:PLN00181 643 YYYDLRNPKLpLCTMIGHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSVS-DG 721

                        250
                 ....*....|....*
gi 298229007 431 sYVAAGSAEGSLYIW 445
Cdd:PLN00181 722 -YIATGSETNEVFVY 735
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-150 9.54e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 9.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007     1 MQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEEnQELVTRWMA 80
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEERIA 750

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298229007    81 EKAQEANRLNAE-NEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATK 150
Cdd:TIGR02168  751 QLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-114 6.15e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007   2 QRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRwMAE 81
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-LEE 320

                         90       100       110
                 ....*....|....*....|....*....|....
gi 298229007  82 KAQEANRLNAENEKDS-RRRQARLQKELAEAAKE 114
Cdd:COG1196  321 LEEELAELEEELEELEeELEELEEELEEAEEELE 354
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
141-488 5.49e-61

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 205.15  E-value: 5.49e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 141 VRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRV----PATALCVFDAHDGEVNAVQFSP 216
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSP 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 217 GSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 296
Cdd:COG2319  131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 297 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LL 372
Cdd:COG2319  209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 373 GKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKV 452
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 298229007 453 EKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 488
Cdd:COG2319  365 LRTL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 199-489 1.16e-58

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: 195.25  E-value: 1.16e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 199 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVfgEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWT 278
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 279 VDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmS 348
Cdd:cd00200   80 LETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------S 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 349 GHFDKKIRFWDIRSESIVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDW-TRVVF 426
Cdd:cd00200  153 SSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAF 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298229007 427 SPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSkQHSSSINAVAWSPSGSHVVSVDKGCKAVLWA 489
Cdd:cd00200  228 SPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
187-447 3.98e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 173.56  E-value: 3.98e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 187 GSGKEVRV----PATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEFkgSLSGSNAGITSIEFDSAG 262
Cdd:COG2319  139 SADGTVRLwdlaTGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR--TLTGHTGAVRSVAFSPDG 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 263 SYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAGSSC--NDIV 340
Cdd:COG2319  217 KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT-LTGHSGgvNSVA 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 341 CT--EQCVMSGHFDKKIRFWDIRSESIVREME-LLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkc 417
Cdd:COG2319  296 FSpdGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGH---- 371

                        250       260       270
                 ....*....|....*....|....*....|.
gi 298229007 418 gSDW-TRVVFSPDGSYVAAGSAEGSLYIWSV 447
Cdd:COG2319  372 -TGAvTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 284-488 2.69e-35

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: 133.23  E-value: 2.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 284 LRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV----FAGSSCNDIVCTEQCVmSGHFDKKIRFWD 359
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLkghtGPVRDVAASADGTYLA-SGSSDKTIRLWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 360 IRSESIVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDWTR-VVFSPDGSYVAAGS 437
Cdd:cd00200   80 LETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNsVAFSPDGTFVASSS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 298229007 438 AEGSLYIWSVLTGKVEKVLsKQHSSSINAVAWSPSGSHVV--SVDKGCKavLW 488
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSPDGEKLLssSSDGTIK--LW 204
WD40 COG2319
WD40 repeat [General function prediction only];
213-488 4.37e-35

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 135.42  E-value: 4.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 213 QFSPGSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHS 292
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALL--LLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 293 GKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFA-GSSCNDIVCTE--QCVMSGHFDKKIRFWDIRSESIVREM 369
Cdd:COG2319   79 AAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGhTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 370 EL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDW-TRVVFSPDGSYVAAGSAEGSLYIWSV 447
Cdd:COG2319  159 TGhSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH-----TGAvRSVAFSPDGKLLASGSADGTVRLWDL 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 298229007 448 LTGKVEKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 488
Cdd:COG2319  234 ATGKLLRTL-TGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 4-93 1.28e-31

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 116.51  E-value: 1.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007   4 KDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKA 83
Cdd:cd22887    2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKKQ 81

                         90
                 ....*....|
gi 298229007  84 QEANRLNAEN 93
Cdd:cd22887   82 QEADKMNEAN 91
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 1-90 2.43e-28

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: 110.41  E-value: 2.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007    1 MQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMA 80
Cdd:pfam08614  87 LQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRELVERWMK 166

                          90
                  ....*....|
gi 298229007   81 EKAQEANRLN 90
Cdd:pfam08614 167 RKGQEAEAMN 176
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 199-234 8.14e-08

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: 48.46  E-value: 8.14e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 298229007   199 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 234
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 283-320 1.85e-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: 1.85e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 298229007   283 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 320
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
199-234 2.76e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.95  E-value: 2.76e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 298229007  199 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 234
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
283-320 4.92e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.18  E-value: 4.92e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 298229007  283 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 320
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 209-445 1.49e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.86  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 209 VNAVQFSPGSRLLATGGMDRRVKLWEVF-----GEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASN-DFASRIWTVDDY 282
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 283 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 355
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 356 RFWDIRSESI-VREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNA--IKQT--FSAPGFKCGSDWTRVVFSpDG 430
Cdd:PLN00181 643 YYYDLRNPKLpLCTMIGHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSVS-DG 721

                        250
                 ....*....|....*
gi 298229007 431 sYVAAGSAEGSLYIW 445
Cdd:PLN00181 722 -YIATGSETNEVFVY 735
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
242-450 3.43e-06

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 48.15  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 242 FKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARI-VSGSHDRTLKLWD 320
Cdd:COG3391   17 ALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLyVANSGSGRVSVID 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 321 LRSKVCIKTVFAGSSCNDIVCTE---QCVMSGHFDKKIRFWDIRSESIVREMELLGKITALDLNPERTELLSCSRDD--- 394
Cdd:COG3391   97 LATGKVVATIPVGGGPRGLAVDPdggRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSntv 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 298229007 395 --LLKVIDLRTNAIKQTFSApgfkcGSDWTRVVFSPDGS--YVA------AGSAEGSLYIWSVLTG 450
Cdd:COG3391  177 svIVSVIDTATGKVVATIPV-----GGGPVGVAVSPDGRrlYVAnrgsntSNGGSNTVSVIDLATL 237
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 205-321 6.31e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.93  E-value: 6.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 205 HDGEVNAVQFSPGS-RLLATGGMDRRVKLWEVFgekcefKGSLSGS---NAGITSIEFDSAGSYLLAasndFASRIWTVD 280
Cdd:PLN00181 574 HEKRVWSIDYSSADpTLLASGSDDGSVKLWSIN------QGVSIGTiktKANICCVQFPSESGRSLA----FGSADHKVY 643

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 298229007 281 DYRLRH------TLTGHSGKVLSAKFLlDNARIVSGSHDRTLKLWDL 321
Cdd:PLN00181 644 YYDLRNpklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 398-477 3.27e-05

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: 44.28  E-value: 3.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 398 VIDLRTNAIKQTFSAPGFKCGSDWtrvvfSPDGSYVAAGSAEGS---LYIWSVLTGKVEKVLSKQHSSSinAVAWSPSGS 474
Cdd:COG0823   15 VVDLDGGEPRRLTNSPGIDTSPAW-----SPDGRRIAFTSDRGGgpqIYVVDADGGEPRRLTFGGGYNA--SPSWSPDGK 87


                 ...
gi 298229007 475 HVV 477
Cdd:COG0823   88 RLA 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-150 9.54e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 9.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007     1 MQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEEnQELVTRWMA 80
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEERIA 750

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298229007    81 EKAQEANRLNAE-NEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATK 150
Cdd:TIGR02168  751 QLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 425-473 2.51e-04

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 43.87  E-value: 2.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 298229007  425 VFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSKQHSSSINAVAWSPSG 473
Cdd:COG4946   395 VWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISDLAWSPDS 443
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 449-488 2.65e-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: 38.45  E-value: 2.65e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 298229007   449 TGKVEKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 488
Cdd:smart00320   1 SGELLKTL-KGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 398-488 3.38e-04

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: 41.20  E-value: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007 398 VIDLRTNAIKQ-TFSapgfkcGSDWTRVVFSPDGSYVA-AGSAEGSLYIWSV-LTGKVEKVLSKqhssSINAVAWSPSGS 474
Cdd:COG0823   59 VVDADGGEPRRlTFG------GGYNASPSWSPDGKRLAfVSRSDGRFDIYVLdLDGGAPRRLTD----GPGSPSWSPDGR 128

                         90
                 ....*....|....*
gi 298229007 475 HVV-SVDKGCKAVLW 488
Cdd:COG0823  129 RIVfSSDRGGRPDLY 143
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-114 6.15e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007   2 QRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRwMAE 81
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-LEE 320

                         90       100       110
                 ....*....|....*....|....*....|....
gi 298229007  82 KAQEANRLNAENEKDS-RRRQARLQKELAEAAKE 114
Cdd:COG1196  321 LEEELAELEEELEELEeELEELEEELEEAEEELE 354
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-137 6.82e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007   2 QRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAE 81
Cdd:COG1196  305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298229007  82 KAQEANRLNAENEK------------DSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEE 137
Cdd:COG1196  385 AEELLEALRAAAELaaqleeleeaeeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 1-110 9.58e-04

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 39.61  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007    1 MQRKDREMQMNEAKiaecLQTISDLETECLDLR-------TKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQE 73
Cdd:pfam11559  44 LQQRDRDLEFRESL----NETIRTLEAEIERLQskierlkTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQR 119

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 298229007   74 LVTRWMAEKAQeanrlnAENEKDSRRRQ-ARLQKELAE 110
Cdd:pfam11559 120 LKNALQQIKTQ------FAHEVKKRDREiEKLKERLAQ 151
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 11-137 1.02e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007   11 NEAKIAECLQTISDLETECLDLRT--------------KLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELvt 76
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESensekqreleekqnEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK-- 410

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298229007   77 rwmaekaqEANRLNAENEKDSRRRQARLQKELAEAAKEPLP--VEQDDDIEVIVDETSDHTEE 137
Cdd:TIGR04523 411 --------DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKdlTNQDSVKELIIKNLDNTRES 465
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-193 1.99e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007    2 QRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYD--ALQITFTALEGKLRKTTEENQEL--VTR 77
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDLaaLEE 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007   78 WMAEKAQEANRLNAENEK--------DSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAAT 149
Cdd:COG4913   693 QLEELEAELEELEEELDElkgeigrlEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE 772

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 298229007  150 KRLSQ---PAGGLLDSITNIFgRRSVSSFPVPQDNVDTHPGSGKEVR 193
Cdd:COG4913   773 ERIDAlraRLNRAEEELERAM-RAFNREWPAETADLDADLESLPEYL 818
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-154 2.07e-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: 40.52  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007   2 QRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAE 81
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007  82 KAQEANR----------------LNAENEKDSRRRQARLQ------KELAEAAKeplpvEQDDDIEVIVDETSDHTEETS 139
Cdd:COG4942  103 KEELAELlralyrlgrqpplallLSPEDFLDAVRRLQYLKylaparREQAEELR-----ADLAELAALRAELEAERAELE 177

                        170
                 ....*....|....*
gi 298229007 140 PVRAISRAATKRLSQ 154
Cdd:COG4942  178 ALLAELEEERAALEA 192
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 424-488 2.30e-03

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 40.79  E-value: 2.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298229007  424 VVFSPDGSYVAAGS-AEGS--LYIWSVLTGKVEKVLSKQHSSSINAVAWSPSGSHVVSVDKGCKavLW 488
Cdd:COG4946   348 PAWSPDGKSIAYFSdASGEyeLYIAPADGSGEPKQLTLGDLGRVFNPVWSPDGKKIAFTDNRGR--LW 413
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 372-475 3.21e-03

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 40.41  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007  372 LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPGFKCGSDwtrVVFSPDGSYVA----AGSAEGSLYIWSV 447
Cdd:COG4946   388 LGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISD---LAWSPDSKWLAyskpGPNQLSQIFLYDV 464

                          90       100
                  ....*....|....*....|....*...
gi 298229007  448 LTGKVEKVLSKQHSSSinAVAWSPSGSH 475
Cdd:COG4946   465 ETGKTVQLTDGRYDDG--SPAFSPDGKY 490
Ge1_WD40 pfam16529
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ...
 249-330 3.52e-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: 39.36  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007  249 SNAGITSIEFDSAGSYLLAASNDFASRIWTV-----DDYRLRHTLTGHSGKVLSAKFLLDNAR----------IVSGS-H 312
Cdd:pfam16529 185 EHSLLVDAAFSPDGTALATASLDGEVKFFQIylfdnRNPRCLHEWKPHDGKPLSSLFFLDNHKkppevqfwrfAITGAdN 264

                          90
                  ....*....|....*...
gi 298229007  313 DRTLKLWDLRSKVCIKTV 330
Cdd:pfam16529 265 NSELKLWSCESWTCLQTI 282
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 2-110 4.31e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007    2 QRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEEnqelvtrwMAE 81
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE--------LKS 493

                          90       100
                  ....*....|....*....|....*....
gi 298229007   82 KAQEANRLNAENeKDSRRRQARLQKELAE 110
Cdd:TIGR04523 494 KEKELKKLNEEK-KELEEKVKDLTKKISS 521
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 422-446 6.25e-03

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: 34.60  E-value: 6.25e-03
                           10        20
                   ....*....|....*....|....*
gi 298229007   422 TRVVFSPDGSYVAAGSAEGSLYIWS 446
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLWD 40
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
19-114 7.50e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 7.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229007  19 LQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRwMAEKAQEANRLNAENEKdSR 98
Cdd:COG4372   37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE-LAQAQEELESLQEEAEE-LQ 114

                         90
                 ....*....|....*.
gi 298229007  99 RRQARLQKELAEAAKE 114
Cdd:COG4372  115 EELEELQKERQDLEQQ 130
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH