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Conserved domains on  [gi|66820052|ref|XP_643673|]
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autophagy protein 16 [Dictyostelium discoideum AX4]

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 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 317-612 2.61e-79

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: 252.26  E-value: 2.61e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 317 KKRWTGHNSEIYCMAFNSIGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGTSNDNSARLWNTE 396
Cdd:cd00200   2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 397 LGRSRHTLTGHIGKVYTGKFINSNRVVTGSH-DRTIKLWDLQKGYCTRTIFCFS-SCNDLVILgGSGTHLASGHVDHSVR 474
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSrDKTIKVWDVETGKCLTTLRGHTdWVNSVAFS-PDGTFVASSSQDGTIK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 475 FWDSNAGEPTQVLSSiHEGQITSITNSPTNtNQILTNSRDHTLKIIDIRTFDTIRTFKDPEyrNGLNWtkASWSPDGRYI 554
Cdd:cd00200 161 LWDLRTGKCVATLTG-HTGEVNSVAFSPDG-EKLLSSSSDGTIKLWDLSTGKCLGTLRGHE--NGVNS--VAFSPDGYLL 234

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66820052 555 ASGSIDGSICIWDATNGKTVKVLTKvHNNgsSVCCCSWSPLANIFISADKDKNIIQWE 612
Cdd:cd00200 235 ASGSEDGTIRVWDLRTGECVQTLSG-HTN--SVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 63-254 2.50e-45

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: 158.56  E-value: 2.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052    63 YSEFMRIYTDLLKRERTLNDRTLLYEKEIVSLRNekkTQQQPPSGSSKMDssssssssnrvsgmGSTIEEMEQKLFKLQE 142
Cdd:pfam08614   2 FLELIDAYNRLLDRTALLEAENAKLQSEPESVLP---STSSSKLSKASPQ--------------SASIQSLEQLLAQLRE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052   143 DLTNSYKRNADNASSILLLNDKNKDLQNELMSKEIEIERIRSTIQQDLDSIKRLEMVVIEKENVSQIIRDELSSLQTEFL 222
Cdd:pfam08614  65 ELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLN 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 66820052   223 HNESKVVKLEQENSSLVERWLRKKNEEASKMN 254
Cdd:pfam08614 145 MAEEKLRKLEKENRELVERWMKRKGQEAEAMN 176
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 317-612 2.61e-79

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: 252.26  E-value: 2.61e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 317 KKRWTGHNSEIYCMAFNSIGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGTSNDNSARLWNTE 396
Cdd:cd00200   2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 397 LGRSRHTLTGHIGKVYTGKFINSNRVVTGSH-DRTIKLWDLQKGYCTRTIFCFS-SCNDLVILgGSGTHLASGHVDHSVR 474
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSrDKTIKVWDVETGKCLTTLRGHTdWVNSVAFS-PDGTFVASSSQDGTIK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 475 FWDSNAGEPTQVLSSiHEGQITSITNSPTNtNQILTNSRDHTLKIIDIRTFDTIRTFKDPEyrNGLNWtkASWSPDGRYI 554
Cdd:cd00200 161 LWDLRTGKCVATLTG-HTGEVNSVAFSPDG-EKLLSSSSDGTIKLWDLSTGKCLGTLRGHE--NGVNS--VAFSPDGYLL 234

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66820052 555 ASGSIDGSICIWDATNGKTVKVLTKvHNNgsSVCCCSWSPLANIFISADKDKNIIQWE 612
Cdd:cd00200 235 ASGSEDGTIRVWDLRTGECVQTLSG-HTN--SVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
314-611 1.46e-66

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 222.86  E-value: 1.46e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 314 SKAKKRWTGHNSEIYCMAFNSIGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGTSNDNSARLW 393
Cdd:COG2319 110 GLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLW 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 394 NTELGRSRHTLTGHIGKVYTGKFI-NSNRVVTGSHDRTIKLWDLQKGYCTRTIFCFSSCNDLVILGGSGTHLASGHVDHS 472
Cdd:COG2319 190 DLATGKLLRTLTGHTGAVRSVAFSpDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGT 269

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 473 VRFWDSNAGEPTQVLSSiHEGQITSITNSPTNtNQILTNSRDHTLKIIDIRTFDTIRTFKDPEYRnglnWTKASWSPDGR 552
Cdd:COG2319 270 VRLWDLATGELLRTLTG-HSGGVNSVAFSPDG-KLLASGSDDGTVRLWDLATGKLLRTLTGHTGA----VRSVAFSPDGK 343

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66820052 553 YIASGSIDGSICIWDATNGKTVKVLTkvhNNGSSVCCCSWSPLANIFISADKDKNIIQW 611
Cdd:COG2319 344 TLASGSDDGTVRLWDLATGELLRTLT---GHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 63-254 2.50e-45

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: 158.56  E-value: 2.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052    63 YSEFMRIYTDLLKRERTLNDRTLLYEKEIVSLRNekkTQQQPPSGSSKMDssssssssnrvsgmGSTIEEMEQKLFKLQE 142
Cdd:pfam08614   2 FLELIDAYNRLLDRTALLEAENAKLQSEPESVLP---STSSSKLSKASPQ--------------SASIQSLEQLLAQLRE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052   143 DLTNSYKRNADNASSILLLNDKNKDLQNELMSKEIEIERIRSTIQQDLDSIKRLEMVVIEKENVSQIIRDELSSLQTEFL 222
Cdd:pfam08614  65 ELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLN 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 66820052   223 HNESKVVKLEQENSSLVERWLRKKNEEASKMN 254
Cdd:pfam08614 145 MAEEKLRKLEKENRELVERWMKRKGQEAEAMN 176
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 167-257 2.16e-23

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: 94.55  E-value: 2.16e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 167 DLQNELMSKEIEIERIRSTIQQDLDSIKRLEMVVIEKENVSQIIRDELSSLQTEFLHNESKVVKLEQENSSLVERWLRKK 246
Cdd:cd22887   1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                        90
                ....*....|.
gi 66820052 247 NEEASKMNEAN 257
Cdd:cd22887  81 QQEADKMNEAN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 313-352 6.15e-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: 48.85  E-value: 6.15e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 66820052    313 PSKAKKRWTGHNSEIYCMAFNSIGNLLATGGGDKCVKVWD 352
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
314-352 3.27e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.95  E-value: 3.27e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 66820052   314 SKAKKRWTGHNSEIYCMAFNSIGNLLATGGGDKCVKVWD 352
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 325-436 1.32e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052  325 SEIYCMAFNS-IGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGT-SNDNSARLWN-------- 394
Cdd:PLN00181 533 SKLSGICWNSyIKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASgSDDGSVKLWSinqgvsig 612

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66820052  395 --------------TELGRS---------------RH------TLTGHIGKVYTGKFINSNRVVTGSHDRTIKLWDL 436
Cdd:PLN00181 613 tiktkaniccvqfpSESGRSlafgsadhkvyyydlRNpklplcTMIGHSKTVSYVRFVDSSTLVSSSTDNTLKLWDL 689
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 130-285 4.42e-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: 46.59  E-value: 4.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052    130 IEEMEQKLFKLQEDLTNSYKRNADNASSILLLNDKNKDLQNELMSKEIEI-------ERIRSTIQQDLDSIKRLEMVVIE 202
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalrkdlARLEAEVEQLEERIAQLSKELTE 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052    203 KENVSQIIRDELSSLQTEFLHNESKVVKLEQ------ENSSLVERWLRKKNEEASKMNEA---NDFYQKMVEQRDSTPAK 273
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAqieqlkEELKALREALDELRAELTLLNEEaanLRERLESLERRIAATER 838

                          170
                   ....*....|..
gi 66820052    274 AAVQLSESISNL 285
Cdd:TIGR02168  839 RLEDLEEQIEEL 850
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 129-267 3.54e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 3.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 129 TIEEMEQKLFKLQEDLTNSYKRNADNASSILLLNDKNKDLQNELMSKEIEIERIRSTIQQDLDSIKRLEMVVIEKENvsq 208
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE--- 351

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66820052 209 iirdELSSLQTEFLHNESKVVKLEQENSSLVERWLRKKNEEASKMNEANDFYQKMVEQR 267
Cdd:COG1196 352 ----ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 317-612 2.61e-79

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: 252.26  E-value: 2.61e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 317 KKRWTGHNSEIYCMAFNSIGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGTSNDNSARLWNTE 396
Cdd:cd00200   2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 397 LGRSRHTLTGHIGKVYTGKFINSNRVVTGSH-DRTIKLWDLQKGYCTRTIFCFS-SCNDLVILgGSGTHLASGHVDHSVR 474
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSrDKTIKVWDVETGKCLTTLRGHTdWVNSVAFS-PDGTFVASSSQDGTIK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 475 FWDSNAGEPTQVLSSiHEGQITSITNSPTNtNQILTNSRDHTLKIIDIRTFDTIRTFKDPEyrNGLNWtkASWSPDGRYI 554
Cdd:cd00200 161 LWDLRTGKCVATLTG-HTGEVNSVAFSPDG-EKLLSSSSDGTIKLWDLSTGKCLGTLRGHE--NGVNS--VAFSPDGYLL 234

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66820052 555 ASGSIDGSICIWDATNGKTVKVLTKvHNNgsSVCCCSWSPLANIFISADKDKNIIQWE 612
Cdd:cd00200 235 ASGSEDGTIRVWDLRTGECVQTLSG-HTN--SVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
314-611 1.46e-66

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 222.86  E-value: 1.46e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 314 SKAKKRWTGHNSEIYCMAFNSIGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGTSNDNSARLW 393
Cdd:COG2319 110 GLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLW 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 394 NTELGRSRHTLTGHIGKVYTGKFI-NSNRVVTGSHDRTIKLWDLQKGYCTRTIFCFSSCNDLVILGGSGTHLASGHVDHS 472
Cdd:COG2319 190 DLATGKLLRTLTGHTGAVRSVAFSpDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGT 269

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 473 VRFWDSNAGEPTQVLSSiHEGQITSITNSPTNtNQILTNSRDHTLKIIDIRTFDTIRTFKDPEYRnglnWTKASWSPDGR 552
Cdd:COG2319 270 VRLWDLATGELLRTLTG-HSGGVNSVAFSPDG-KLLASGSDDGTVRLWDLATGKLLRTLTGHTGA----VRSVAFSPDGK 343

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66820052 553 YIASGSIDGSICIWDATNGKTVKVLTkvhNNGSSVCCCSWSPLANIFISADKDKNIIQW 611
Cdd:COG2319 344 TLASGSDDGTVRLWDLATGELLRTLT---GHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 COG2319
WD40 repeat [General function prediction only];
310-612 1.65e-62

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 212.08  E-value: 1.65e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 310 AMLPSKAKKRWTGHNSEIYCMAFNSIGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGTSNDNS 389
Cdd:COG2319  64 DAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGT 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 390 ARLWNTELGRSRHTLTGHIGKVYTGKFI-NSNRVVTGSHDRTIKLWDLQKGYCTRTI---------FCFSScndlvilgg 459
Cdd:COG2319 144 VRLWDLATGKLLRTLTGHSGAVTSVAFSpDGKLLASGSDDGTVRLWDLATGKLLRTLtghtgavrsVAFSP--------- 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 460 SGTHLASGHVDHSVRFWDSNAGEPTQVLSSiHEGQITSITNSPTNTnQILTNSRDHTLKIIDIRTFDTIRTFKDPEyrng 539
Cdd:COG2319 215 DGKLLASGSADGTVRLWDLATGKLLRTLTG-HSGSVRSVAFSPDGR-LLASGSADGTVRLWDLATGELLRTLTGHS---- 288

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66820052 540 lNW-TKASWSPDGRYIASGSIDGSICIWDATNGKTVKVLTkvhNNGSSVCCCSWSPLANIFISADKDKNIIQWE 612
Cdd:COG2319 289 -GGvNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVRSVAFSPDGKTLASGSDDGTVRLWD 358
WD40 COG2319
WD40 repeat [General function prediction only];
315-570 3.70e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 203.22  E-value: 3.70e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 315 KAKKRWTGHNSEIYCMAFNSIGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGTSNDNSARLWN 394
Cdd:COG2319 153 KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD 232

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 395 TELGRSRHTLTGHIGKVYT------GKfinsnRVVTGSHDRTIKLWDLQKGYCTRTI---------FCFSscndlvilgG 459
Cdd:COG2319 233 LATGKLLRTLTGHSGSVRSvafspdGR-----LLASGSADGTVRLWDLATGELLRTLtghsggvnsVAFS---------P 298

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 460 SGTHLASGHVDHSVRFWDSNAGEPTQVLSSiHEGQITSITNSPtNTNQILTNSRDHTLKIIDIRTFDTIRTFKDPEyrng 539
Cdd:COG2319 299 DGKLLASGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSP-DGKTLASGSDDGTVRLWDLATGELLRTLTGHT---- 372

                       250       260       270
                ....*....|....*....|....*....|..
gi 66820052 540 lNW-TKASWSPDGRYIASGSIDGSICIWDATN 570
Cdd:COG2319 373 -GAvTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
321-612 7.17e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 186.27  E-value: 7.17e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 321 TGHNSEIYCMAFNSIGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGTSNDNSARLWNTELGRS 400
Cdd:COG2319  33 LGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 401 RHTLTGHIGKVYTGKF-INSNRVVTGSHDRTIKLWDLQKGYCTRTIFCFSSCNDLVILGGSGTHLASGHVDHSVRFWDSN 479
Cdd:COG2319 113 LRTLTGHTGAVRSVAFsPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 480 AGEPTQVLSSiHEGQITSITNSPTNtNQILTNSRDHTLKIIDIRTFDTIRTFKDPEYRnglnWTKASWSPDGRYIASGSI 559
Cdd:COG2319 193 TGKLLRTLTG-HTGAVRSVAFSPDG-KLLASGSADGTVRLWDLATGKLLRTLTGHSGS----VRSVAFSPDGRLLASGSA 266

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 66820052 560 DGSICIWDATNGKTVKVLTkvhNNGSSVCCCSWSPLANIFISADKDKNIIQWE 612
Cdd:COG2319 267 DGTVRLWDLATGELLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWD 316
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 63-254 2.50e-45

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: 158.56  E-value: 2.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052    63 YSEFMRIYTDLLKRERTLNDRTLLYEKEIVSLRNekkTQQQPPSGSSKMDssssssssnrvsgmGSTIEEMEQKLFKLQE 142
Cdd:pfam08614   2 FLELIDAYNRLLDRTALLEAENAKLQSEPESVLP---STSSSKLSKASPQ--------------SASIQSLEQLLAQLRE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052   143 DLTNSYKRNADNASSILLLNDKNKDLQNELMSKEIEIERIRSTIQQDLDSIKRLEMVVIEKENVSQIIRDELSSLQTEFL 222
Cdd:pfam08614  65 ELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLN 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 66820052   223 HNESKVVKLEQENSSLVERWLRKKNEEASKMN 254
Cdd:pfam08614 145 MAEEKLRKLEKENRELVERWMKRKGQEAEAMN 176
WD40 COG2319
WD40 repeat [General function prediction only];
331-611 6.65e-42

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 156.22  E-value: 6.65e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 331 AFNSIGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGTSNDNSARLWNTELGRSRHTLTGHIGK 410
Cdd:COG2319   1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 411 VYTGKFI-NSNRVVTGSHDRTIKLWDLQKGYCTRTIF---------CFSScndlvilggSGTHLASGHVDHSVRFWDSNA 480
Cdd:COG2319  81 VLSVAFSpDGRLLASASADGTVRLWDLATGLLLRTLTghtgavrsvAFSP---------DGKTLASGSADGTVRLWDLAT 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 481 GEPTQVLSSiHEGQITSITNSPTNTnQILTNSRDHTLKIIDIRTFDTIRTFKDPEYRnglnWTKASWSPDGRYIASGSID 560
Cdd:COG2319 152 GKLLRTLTG-HSGAVTSVAFSPDGK-LLASGSDDGTVRLWDLATGKLLRTLTGHTGA----VRSVAFSPDGKLLASGSAD 225

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 66820052 561 GSICIWDATNGKTVKVLTkvhNNGSSVCCCSWSPLANIFISADKDKNIIQW 611
Cdd:COG2319 226 GTVRLWDLATGKLLRTLT---GHSGSVRSVAFSPDGRLLASGSADGTVRLW 273
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 315-477 2.33e-32

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: 126.30  E-value: 2.33e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 315 KAKKRWTGHNSEIYCMAFNSIGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGTSNDNSARLWN 394
Cdd:cd00200 126 KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWD 205

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 395 TELGRSRHTLTGHIGKVYTGKFINSNR-VVTGSHDRTIKLWDLQKGYCTRT-------IFCFSSCNDlvilggsGTHLAS 466
Cdd:cd00200 206 LSTGKCLGTLRGHENGVNSVAFSPDGYlLASGSEDGTIRVWDLRTGECVQTlsghtnsVTSLAWSPD-------GKRLAS 278

                       170
                ....*....|.
gi 66820052 467 GHVDHSVRFWD 477
Cdd:cd00200 279 GSADGTIRIWD 289
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 167-257 2.16e-23

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: 94.55  E-value: 2.16e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 167 DLQNELMSKEIEIERIRSTIQQDLDSIKRLEMVVIEKENVSQIIRDELSSLQTEFLHNESKVVKLEQENSSLVERWLRKK 246
Cdd:cd22887   1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                        90
                ....*....|.
gi 66820052 247 NEEASKMNEAN 257
Cdd:cd22887  81 QQEADKMNEAN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 313-352 6.15e-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: 48.85  E-value: 6.15e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 66820052    313 PSKAKKRWTGHNSEIYCMAFNSIGNLLATGGGDKCVKVWD 352
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
314-352 3.27e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.95  E-value: 3.27e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 66820052   314 SKAKKRWTGHNSEIYCMAFNSIGNLLATGGGDKCVKVWD 352
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 481-594 6.10e-06

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 49.65  E-value: 6.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052  481 GEPTQvLSSIHEGQITSITNSPTNTnQILTNSRDHTLKIIDIRTfDTIRTFKDPEYrNGLNWTkASWSPDGRYIASGSID 560
Cdd:COG4946  378 GEPKQ-LTLGDLGRVFNPVWSPDGK-KIAFTDNRGRLWVVDLAS-GKVRKVDTDGY-GDGISD-LAWSPDSKWLAYSKPG 452

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 66820052  561 GS----ICIWDATNGKTVKVLTKVHNNGSSVcccsWSP 594
Cdd:COG4946  453 PNqlsqIFLYDVETGKTVQLTDGRYDDGSPA----FSP 486
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 543-567 1.25e-05

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: 42.30  E-value: 1.25e-05
                           10        20
                   ....*....|....*....|....*
gi 66820052    543 TKASWSPDGRYIASGSIDGSICIWD 567
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 325-436 1.32e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052  325 SEIYCMAFNS-IGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGT-SNDNSARLWN-------- 394
Cdd:PLN00181 533 SKLSGICWNSyIKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASgSDDGSVKLWSinqgvsig 612

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66820052  395 --------------TELGRS---------------RH------TLTGHIGKVYTGKFINSNRVVTGSHDRTIKLWDL 436
Cdd:PLN00181 613 tiktkaniccvqfpSESGRSlafgsadhkvyyydlRNpklplcTMIGHSKTVSYVRFVDSSTLVSSSTDNTLKLWDL 689
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 132-289 2.41e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.41  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052   132 EMEQKLFKLQEDLTNSYKRNADNASSILLLNDKNKDLQNELMSKEIEIERIRSTIQQDLD----SIKRLEMVVIEKENVS 207
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDkseeNARSIEYEVLKKEKQM 589

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052   208 QIIRDELSSLQTEFLHNESKVVKLEQENSSLVerwlRKKNEEASKMN---------------------EANDFYQKMVEQ 266
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKALK----KKGSAENKQLNayeikvnklelelasakqkfeEIIDNYQKEIED 665

                         170       180
                  ....*....|....*....|....*
gi 66820052   267 RDSTPAK--AAVQLSESISNLVVKL 289
Cdd:pfam05483 666 KKISEEKllEEVEKAKAIADEAVKL 690
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 398-435 4.19e-05

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: 40.76  E-value: 4.19e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 66820052    398 GRSRHTLTGHIGKVYTGKFI-NSNRVVTGSHDRTIKLWD 435
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSpDGKYLASGSDDGTIKLWD 40
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 130-285 4.42e-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: 46.59  E-value: 4.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052    130 IEEMEQKLFKLQEDLTNSYKRNADNASSILLLNDKNKDLQNELMSKEIEI-------ERIRSTIQQDLDSIKRLEMVVIE 202
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalrkdlARLEAEVEQLEERIAQLSKELTE 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052    203 KENVSQIIRDELSSLQTEFLHNESKVVKLEQ------ENSSLVERWLRKKNEEASKMNEA---NDFYQKMVEQRDSTPAK 273
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAqieqlkEELKALREALDELRAELTLLNEEaanLRERLESLERRIAATER 838

                          170
                   ....*....|..
gi 66820052    274 AAVQLSESISNL 285
Cdd:TIGR02168  839 RLEDLEEQIEEL 850
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 323-522 5.16e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 46.23  E-value: 5.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052  323 HNSEIYC-MAFNSIGNLLATGGGDKCVKVWDVISGQQKS-------TLLGASQSIVSVSFSPNDESILGTSN-DNSARLW 393
Cdd:PLN00181 481 NSSNLVCaIGFDRDGEFFATAGVNKKIKIFECESIIKDGrdihypvVELASRSKLSGICWNSYIKSQVASSNfEGVVQVW 560

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052  394 NTELGRSRHTLTGHIGKVYTGKFINSNRVV--TGSHDRTIKLWDLQKGYCTRTIFCFSSCNDLVILGGSGTHLASGHVDH 471
Cdd:PLN00181 561 DVARSQLVTEMKEHEKRVWSIDYSSADPTLlaSGSDDGSVKLWSINQGVSIGTIKTKANICCVQFPSESGRSLAFGSADH 640

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 66820052  472 SVRFWDSNagEPTQVLSSI--HEGQITSITNSPTNTnqILTNSRDHTLKIIDI 522
Cdd:PLN00181 641 KVYYYDLR--NPKLPLCTMigHSKTVSYVRFVDSST--LVSSSTDNTLKLWDL 689
WD40 pfam00400
WD domain, G-beta repeat;
546-567 6.29e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 6.29e-05
                          10        20
                  ....*....|....*....|..
gi 66820052   546 SWSPDGRYIASGSIDGSICIWD 567
Cdd:pfam00400  18 AFSPDGKLLASGSDDGTVKVWD 39
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
 313-580 8.13e-05

WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and plants is an essential factor for ribosome assembly. In cooperation with the assembly factor NVL2, WDR74 participates in an early cleavage of the pre-rRNA processing pathway. NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of WDR74 from nucleolar pre-60S particles. WDR74 has been implicated in tumorigenesis. In lung cancer, it regulates cell proliferation, cell cycle progression, chemoresistance and cell aggressiveness, by inducing nuclear beta-catenin accumulation and driving downstream Wnt-responsive genes expression. In melanoma, it promotes apoptosis resistance and aggressive behavior by regulating the RPL5-MDM2-p53 pathway. WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.


Pssm-ID: 439303 [Multi-domain]  Cd Length: 325  Bit Score: 44.91  E-value: 8.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 313 PSKAKKRW--TGHNSEIYCMAFNSIG--NLLATGGGDKCVKVWDVISGqqksTLLGASQSIVSVSFSPNDESILG----- 383
Cdd:cd22857  17 APKVVDRWggPDKSKAVQALSIADREsePLLAVARKNGTVEVLDPENG----DLLASFSDSEPATKLSEEDHFVGlhlfs 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 384 ----TSNDN-SARLWN----TELGRSRHTLTGHIGKVYTGK-FINSNRVVTGSHDRTIKLWDLqKGYCTRtifCFSSCN- 452
Cdd:cd22857  93 gtllTCTSKgSLRSTKlpddSTASSSPTAWVCLGGNLLCMRvDPNENYFAFGGKEVELNVWDL-EEKPGK---IWRAKNv 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 453 --------------DLVILGGSGTH-LASGHVDHSVRFWDSNAGEPTQVLSSIHEGQITSITnSPTNTNQIL--TNSRDh 515
Cdd:cd22857 169 pndslglrvpvwvtDLTFLSKDDHRkIVTGTGYHQVRLYDTRAQRRPVVSVDFGETPIKAVA-EDPDGHTVYvgDTSGD- 246

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66820052 516 tLKIIDIRTFDTIRTFKdpeyrnGLN--WTKASWS-PDGRYIASGSIDGSICIWDAtngKTVKVLTKV 580
Cdd:cd22857 247 -LASIDLRTGKLLGCFK------GKCggSIRSIARhPELPLIASCGLDRYLRIWDT---ETRQLLSKV 304
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
411-571 1.50e-04

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 43.53  E-value: 1.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 411 VYTGKFINSNRV-VTGSHDRTIKLWDLQKGYCTRTIFCFSSCNDLVILGGSGTHLASGHVDHSVRFWDSNAGEptqVLSS 489
Cdd:COG3391  71 DGADAGADGRRLyVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGK---VVAT 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 490 IHEG-QITSITNSPTNTNQILTNSRDHT----LKIIDIRTFDTIRTFKDPEYRNGLnwtkaSWSPDGRYI--------AS 556
Cdd:COG3391 148 IPVGaGPHGIAVDPDGKRLYVANSGSNTvsviVSVIDTATGKVVATIPVGGGPVGV-----AVSPDGRRLyvanrgsnTS 222

                       170
                ....*....|....*
gi 66820052 557 GSIDGSICIWDATNG 571
Cdd:COG3391 223 NGGSNTVSVIDLATL 237
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 538-593 1.84e-04

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


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 40.72  E-value: 1.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 66820052   538 NGLNWTKASWSPDGRYIASGSIDGSICIWDATNGKTVKVLTkVHNngSSVCCCSWS 593
Cdd:pfam12894  37 EDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFS-AGS--DLITCLGWG 89
WD40 pfam00400
WD domain, G-beta repeat;
398-435 1.91e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 1.91e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 66820052   398 GRSRHTLTGHIGKVYTGKFI-NSNRVVTGSHDRTIKLWD 435
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSpDGKLLASGSDDGTVKVWD 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 129-267 3.54e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 3.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 129 TIEEMEQKLFKLQEDLTNSYKRNADNASSILLLNDKNKDLQNELMSKEIEIERIRSTIQQDLDSIKRLEMVVIEKENvsq 208
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE--- 351

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66820052 209 iirdELSSLQTEFLHNESKVVKLEQENSSLVERWLRKKNEEASKMNEANDFYQKMVEQR 267
Cdd:COG1196 352 ----ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
PTZ00421 PTZ00421
coronin; Provisional
 322-461 5.61e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 42.96  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052  322 GHNSEIYCMAFN-SIGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGTSNDNSARLWNTELGRS 400
Cdd:PTZ00421 123 GHTKKVGIVSFHpSAMNVLASAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTI 202

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66820052  401 RHTLTGHIGkVYTGKFINSNR---VVT----GSHDRTIKLWD---LQKGYCTRTIFCFSSC--------NDLVILGGSG 461
Cdd:PTZ00421 203 VSSVEAHAS-AKSQRCLWAKRkdlIITlgcsKSQQRQIMLWDtrkMASPYSTVDLDQSSALfipffdedTNLLYIGSKG 280
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
465-578 1.64e-03

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 40.45  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 465 ASGHVDHSVRFWDSNAGEPTQVLSSIheGQITSITNSPTNTNQILTNSRDHTLKIIDIRTFDTIRTFKDPEYRNGLnwtk 544
Cdd:COG3391  84 VANSGSGRVSVIDLATGKVVATIPVG--GGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGI---- 157

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 66820052 545 aSWSPDGRYIASGSIDGS-----ICIWDATNGKTVKVLT 578
Cdd:COG3391 158 -AVDPDGKRLYVANSGSNtvsviVSVIDTATGKVVATIP 195
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 130-278 2.28e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.96  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052   130 IEEMEQKLFKLQEDLTNSykrnaDNASSILllndknkdlQNELMSKEIEIERIRSTIQQDlDSIKRLEMVVIEKENvsQI 209
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNT-----DTALTTL---------EEALSEKERIIERLKEQRERE-DRERLEELESLKKEN--KD 479

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66820052   210 IRDELSSLQTEFLHNESKVVKLEQENSSLVERWLRKKNEeaSKMNEANdfyqkmVEQRDSTPAKAAVQL 278
Cdd:pfam10174 480 LKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSK--LKSLEIA------VEQKKEECSKLENQL 540
PTZ00421 PTZ00421
coronin; Provisional
 362-449 2.52e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 40.65  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052  362 LLGASQSIVSVSFSPNDESILGT-SNDNSARLWNT-ELGRSRHT------LTGHIGKVYTGKFINSNRVVTGSH--DRTI 431
Cdd:PTZ00421  71 LLGQEGPIIDVAFNPFDPQKLFTaSEDGTIMGWGIpEEGLTQNIsdpivhLQGHTKKVGIVSFHPSAMNVLASAgaDMVV 150

                         90
                 ....*....|....*...
gi 66820052  432 KLWDLQKGYCTRTIFCFS 449
Cdd:PTZ00421 151 NVWDVERGKAVEVIKCHS 168
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
130-328 2.53e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 2.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 130 IEEMEQKLFKLQEDLTNSYKRNADNASSILLLNDKNKDLQNELMSKEIEIERIRSTIQQDLDSIKRLEMVVIEKENVSQI 209
Cdd:COG4372  75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 210 IRDELSSLQTEFLHNESKVVKLEQEN-SSLVERWLRKKNEEASKMNEANDFYQK-MVEQRDSTPAKAAVQLSESISNLVV 287
Cdd:COG4372 155 LEEQLESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLiESLPRELAEELLEAKDSLEAKLGLA 234

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 66820052 288 KLPDANDVPIPIVLERGVFSSEAMLPSKAKKRWTGHNSEIY 328
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 355-394 3.83e-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: 35.37  E-value: 3.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 66820052    355 SGQQKSTLLGASQSIVSVSFSPNDESILGTSNDNSARLWN 394
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00421 PTZ00421
coronin; Provisional
 399-609 3.92e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 40.26  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052  399 RSRHTlTGHIGKvYTGKFINsnrvVTGShdrtIKLWDlqkgyCTRTIfcfsSCNDLVI------LGGSGT--HLASGHVd 470
Cdd:PTZ00421   5 RFRHT-QGVPAR-PDRHFLN----VTPS----TALWD-----CSNTI----ACNDRFIavpwqqLGSTAVlkHTDYGKL- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052  471 hsvrfwdsnAGEPTQVLSsiHEGQITSITNSPTNTNQILTNSRDHTLKIIDI-------RTFDTIRTFKDPEYRNGLnwt 543
Cdd:PTZ00421  65 ---------ASNPPILLG--QEGPIIDVAFNPFDPQKLFTASEDGTIMGWGIpeegltqNISDPIVHLQGHTKKVGI--- 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66820052  544 kASWSPDGR-YIASGSIDGSICIWDATNGKTVKVLTKVHNNGSSVcccSWSPLANIFISADKDK--NII 609
Cdd:PTZ00421 131 -VSFHPSAMnVLASAGADMVVNVWDVERGKAVEVIKCHSDQITSL---EWNLDGSLLCTTSKDKklNII 195
WD40 pfam00400
WD domain, G-beta repeat;
356-394 4.24e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 4.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 66820052   356 GQQKSTLLGASQSIVSVSFSPNDESILGTSNDNSARLWN 394
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 404-528 4.78e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 39.88  E-value: 4.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052  404 LTGHIGKVYTGKF--INSNRVVTGSHDRTIKLWDLQKGYCTrtifcfSSCND-LVILGGSGTH-------------LASG 467
Cdd:PTZ00421  71 LLGQEGPIIDVAFnpFDPQKLFTASEDGTIMGWGIPEEGLT------QNISDpIVHLQGHTKKvgivsfhpsamnvLASA 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66820052  468 HVDHSVRFWDSNAGEPTQVLSSiHEGQITSITNSpTNTNQILTNSRDHTLKIIDIRTFDTI 528
Cdd:PTZ00421 145 GADMVVNVWDVERGKAVEVIKC-HSDQITSLEWN-LDGSLLCTTSKDKKLNIIDPRDGTIV 203
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 573-612 5.00e-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: 34.98  E-value: 5.00e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 66820052    573 TVKVLTKVHNNGSSVCCCSWSPLANIFISADKDKNIIQWE 612
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 130-281 6.97e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 6.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 130 IEEMEQKLFKLQEDLTNSYKRNADNASSILLLNDKNKDLQNELMSKEIEI--------ERIRStIQQDLDSIKRLEMVV- 200
Cdd:COG3883  32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeerreelgERARA-LYRSGGSVSYLDVLLg 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66820052 201 -------IEK-ENVSQIIR------DELSSLQTEFLHNESKVVKLEQENSSLVERWLRKKNEEASKMNEANDFYQKMVEQ 266
Cdd:COG3883 111 sesfsdfLDRlSALSKIADadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190

                       170
                ....*....|....*
gi 66820052 267 RDSTPAKAAVQLSES 281
Cdd:COG3883 191 EAAAEAQLAELEAEL 205
 
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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