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Conserved domains on  [gi|665395407|ref|NP_001138124|]
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Autophagy-related 16, isoform F [Drosophila melanogaster]

Protein Classification

WD repeat ATG16 family protein( domain architecture ID 12095058)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
310-605 7.00e-57

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 197.06  E-value: 7.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 310 LGQANPTKILMKFEAHENESHAVRWSPVERMVATGGADRKVKLWDIGknSTEPRAVLSGSSAGINSVDFDSTGAYILGTS 389
Cdd:COG2319  104 LWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA--TGKLLRTLTGHSGAVTSVAFSPDGKLLASGS 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 390 NDYGARVWTVMDNRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWDLRSIACIET-KFAGSSCNDLV-TTDslGS 467
Cdd:COG2319  182 DDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTlTGHSGSVRSVAfSPD--GR 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 468 TIISGHYDKKIRFWDIRTEKQADDVLMP-AKITSLDLSKDCNYLICSVRDDTIKLLDLRKNQVISTFTNEHFKISCdfar 546
Cdd:COG2319  260 LLASGSADGTVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS---- 335

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 547 ASFNSSGLKIACGSADGAIYIWNVNGFLE-ATLKGHSTAVNAVSWSPNNNMLASVGKNKR 605
Cdd:COG2319  336 VAFSPDGKTLASGSDDGTVRLWDLATGELlRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 27-197 3.54e-42

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: 150.08  E-value: 3.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   27 FKEIIEQNNRLIDHVAQLKADNLKISVENEQLRNAVSTG----GTGSNVAIATLEKKLLSQQEELTELHKRKGENSQMIV 102
Cdd:pfam08614   2 FLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSklskASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  103 DLNQKVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNTMLDEHTALQLAFSSLEEKLRGVQDENRRLL 182
Cdd:pfam08614  82 DLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRELV 161

                         170
                  ....*....|....*
gi 665395407  183 ERLMQYKSKDADKLN 197
Cdd:pfam08614 162 ERWMKRKGQEAEAMN 176
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
310-605 7.00e-57

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 197.06  E-value: 7.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 310 LGQANPTKILMKFEAHENESHAVRWSPVERMVATGGADRKVKLWDIGknSTEPRAVLSGSSAGINSVDFDSTGAYILGTS 389
Cdd:COG2319  104 LWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA--TGKLLRTLTGHSGAVTSVAFSPDGKLLASGS 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 390 NDYGARVWTVMDNRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWDLRSIACIET-KFAGSSCNDLV-TTDslGS 467
Cdd:COG2319  182 DDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTlTGHSGSVRSVAfSPD--GR 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 468 TIISGHYDKKIRFWDIRTEKQADDVLMP-AKITSLDLSKDCNYLICSVRDDTIKLLDLRKNQVISTFTNEHFKISCdfar 546
Cdd:COG2319  260 LLASGSADGTVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS---- 335

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 547 ASFNSSGLKIACGSADGAIYIWNVNGFLE-ATLKGHSTAVNAVSWSPNNNMLASVGKNKR 605
Cdd:COG2319  336 VAFSPDGKTLASGSDDGTVRLWDLATGELlRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 322-605 1.08e-49

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: 174.06  E-value: 1.08e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 322 FEAHENESHAVRWSPVERMVATGGADRKVKLWDIgkNSTEPRAVLSGSSAGINSVDFDSTGAYILGTSNDYGARVWTVMD 401
Cdd:cd00200    5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 402 NRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWDLRSIACIetkFAGSSCNDLVTT---DSLGSTIISGHYDKKI 478
Cdd:cd00200   83 GECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL---TTLRGHTDWVNSvafSPDGTFVASSSQDGTI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 479 RFWDIRTEK-QADDVLMPAKITSLDLSKDCNYLICSVRDDTIKLLDLRKNQVISTFT-NEHFKISCdfaraSFNSSGLKI 556
Cdd:cd00200  160 KLWDLRTGKcVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRgHENGVNSV-----AFSPDGYLL 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 665395407 557 ACGSADGAIYIWNVNGFLE-ATLKGHSTAVNAVSWSPNNNMLASVGKNKR 605
Cdd:cd00200  235 ASGSEDGTIRVWDLRTGECvQTLSGHTNSVTSLAWSPDGKRLASGSADGT 284
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 27-197 3.54e-42

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: 150.08  E-value: 3.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   27 FKEIIEQNNRLIDHVAQLKADNLKISVENEQLRNAVSTG----GTGSNVAIATLEKKLLSQQEELTELHKRKGENSQMIV 102
Cdd:pfam08614   2 FLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSklskASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  103 DLNQKVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNTMLDEHTALQLAFSSLEEKLRGVQDENRRLL 182
Cdd:pfam08614  82 DLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRELV 161

                         170
                  ....*....|....*
gi 665395407  183 ERLMQYKSKDADKLN 197
Cdd:pfam08614 162 ERWMKRKGQEAEAMN 176
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 115-200 5.67e-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: 93.40  E-value: 5.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 115 ISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNTMLDEHTALQLAFSSLEEKLRGVQDENRRLLERLMQYKSKDAD 194
Cdd:cd22887    6 LQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKKQQEAD 85


                 ....*.
gi 665395407 195 KLNEEN 200
Cdd:cd22887   86 KMNEAN 91
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 340-524 3.85e-08

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 56.63  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 340 MVATGGADRKVKLWDI------GKNSTEPRAVLSGSSAgINSVDFDSTGAYILGTSNDYGA-RVWTVMDNRLRHTLTGHS 412
Cdd:PLN00181 497 FFATAGVNKKIKIFECesiikdGRDIHYPVVELASRSK-LSGICWNSYIKSQVASSNFEGVvQVWDVARSQLVTEMKEHE 575

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 413 GKVMAAKYVQ-EPIKVVTGSHDRTLKIWDLR---SIACIETKfaGSSCNDLVTTDSlGSTIISGHYDKKIRFWDIRTEKQ 488
Cdd:PLN00181 576 KRVWSIDYSSaDPTLLASGSDDGSVKLWSINqgvSIGTIKTK--ANICCVQFPSES-GRSLAFGSADHKVYYYDLRNPKL 652

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 665395407 489 ADDVLMP-AKITSLDLSKDCNYLICSVRDDTIKLLDL 524
Cdd:PLN00181 653 PLCTMIGhSKTVSYVRFVDSSTLVSSSTDNTLKLWDL 689
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 317-354 1.07e-06

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: 45.38  E-value: 1.07e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 665395407   317 KILMKFEAHENESHAVRWSPVERMVATGGADRKVKLWD 354
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 25-201 1.18e-06

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: 51.56  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   25 DNFKEIIEQNNRLIDHVAQLKADNLKISVENEQlrnavstggtGSNVAIATLEKKLLSQQEELTELHKRKGENSQMIVDL 104
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ----------KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  105 NQKVEQqriIISEKEHSlveqQTNNNRLRAEVQLLHSSLEELKKLNNTMLDEHTALQLAFSSLEEKLRGVQDENRRLLER 184
Cdd:TIGR04523 341 NEQISQ---LKKELTNS----ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ 413

                         170
                  ....*....|....*..
gi 665395407  185 LmQYKSKDADKLNEENE 201
Cdd:TIGR04523 414 I-KKLQQEKELLEKEIE 429
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
28-187 2.17e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.79  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  28 KEIIEQNNRLIDHVAQLKADNLKISVENEQLRNAVSTGGT-----GSNVAIATLEKKLLSQQEELTELHKRKGENSQMIV 102
Cdd:COG3206  215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDalpelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 103 DLNQKVEQ-QRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNTMldehTALQLAFSSLEEKLrgvqDENRRL 181
Cdd:COG3206  295 ALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL----PELEAELRRLEREV----EVAREL 366


                 ....*.
gi 665395407 182 LERLMQ 187
Cdd:COG3206  367 YESLLQ 372
WD40 pfam00400
WD domain, G-beta repeat;
317-354 1.21e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 1.21e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 665395407  317 KILMKFEAHENESHAVRWSPVERMVATGGADRKVKLWD 354
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PRK11637 PRK11637
AmiB activator; Provisional
 73-188 3.53e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 43.53  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  73 IATLEKKLLSQQEELTELhkrkgensqmivdLNQkVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNT 152
Cdd:PRK11637  56 IAAKEKSVRQQQQQRASL-------------LAQ-LKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAA 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 665395407 153 -------MLD------EHTALQLAFSSlEEKLRGvqdenrrllERLMQY 188
Cdd:PRK11637 122 qerllaaQLDaafrqgEHTGLQLILSG-EESQRG---------ERILAY 160
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
 120-229 6.02e-04

Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p


Pssm-ID: 214699 [Multi-domain]  Cd Length: 117  Bit Score: 40.02  E-value: 6.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   120 HSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNTMLDEHTALqlafSSLEEKLRGVQDENRRLLERLmQYKSKDADKLNEE 199
Cdd:smart00503   1 SNLDEFFEKVEEIRANIQKISQNVAELQKLHEELLTPPDAD----KELREKLERLIDDIKRLAKEI-RAKLKELEKENLE 75

                           90       100       110
                   ....*....|....*....|....*....|...
gi 665395407   200 NesiiRKRLPSIFRKRSA---KLKRDLEDAVRE 229
Cdd:smart00503  76 N----RASGSASDRTRKAqteKLRKKFKEVMNE 104
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
310-605 7.00e-57

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 197.06  E-value: 7.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 310 LGQANPTKILMKFEAHENESHAVRWSPVERMVATGGADRKVKLWDIGknSTEPRAVLSGSSAGINSVDFDSTGAYILGTS 389
Cdd:COG2319  104 LWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA--TGKLLRTLTGHSGAVTSVAFSPDGKLLASGS 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 390 NDYGARVWTVMDNRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWDLRSIACIET-KFAGSSCNDLV-TTDslGS 467
Cdd:COG2319  182 DDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTlTGHSGSVRSVAfSPD--GR 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 468 TIISGHYDKKIRFWDIRTEKQADDVLMP-AKITSLDLSKDCNYLICSVRDDTIKLLDLRKNQVISTFTNEHFKISCdfar 546
Cdd:COG2319  260 LLASGSADGTVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS---- 335

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 547 ASFNSSGLKIACGSADGAIYIWNVNGFLE-ATLKGHSTAVNAVSWSPNNNMLASVGKNKR 605
Cdd:COG2319  336 VAFSPDGKTLASGSDDGTVRLWDLATGELlRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395
WD40 COG2319
WD40 repeat [General function prediction only];
258-605 4.16e-50

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.57  E-value: 4.16e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 258 LIGDEDFDEAAINGAMEAIGLDDNEYISARFTAGEIAENSRASIDTLKATGYLGQANPTKILMKFEAHENESHAVRWSPV 337
Cdd:COG2319   10 AAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 338 ERMVATGGADRKVKLWDIgkNSTEPRAVLSGSSAGINSVDFDSTGAYILGTSNDYGARVWTVMDNRLRHTLTGHSGKVMA 417
Cdd:COG2319   90 GRLLASASADGTVRLWDL--ATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 418 A------KYvqepikVVTGSHDRTLKIWDLRSIACIETkFAGSScnDLVTtdSL-----GSTIISGHYDKKIRFWDIRTE 486
Cdd:COG2319  168 VafspdgKL------LASGSDDGTVRLWDLATGKLLRT-LTGHT--GAVR--SVafspdGKLLASGSADGTVRLWDLATG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 487 KQAdDVLM--PAKITSLDLSKDCNYLICSVRDDTIKLLDLRKNQVISTFTNEHFKISCdfarASFNSSGLKIACGSADGA 564
Cdd:COG2319  237 KLL-RTLTghSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNS----VAFSPDGKLLASGSDDGT 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 665395407 565 IYIWNVN-GFLEATLKGHSTAVNAVSWSPNNNMLASVGKNKR 605
Cdd:COG2319  312 VRLWDLAtGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGT 353
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 322-605 1.08e-49

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: 174.06  E-value: 1.08e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 322 FEAHENESHAVRWSPVERMVATGGADRKVKLWDIgkNSTEPRAVLSGSSAGINSVDFDSTGAYILGTSNDYGARVWTVMD 401
Cdd:cd00200    5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 402 NRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWDLRSIACIetkFAGSSCNDLVTT---DSLGSTIISGHYDKKI 478
Cdd:cd00200   83 GECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL---TTLRGHTDWVNSvafSPDGTFVASSSQDGTI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 479 RFWDIRTEK-QADDVLMPAKITSLDLSKDCNYLICSVRDDTIKLLDLRKNQVISTFT-NEHFKISCdfaraSFNSSGLKI 556
Cdd:cd00200  160 KLWDLRTGKcVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRgHENGVNSV-----AFSPDGYLL 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 665395407 557 ACGSADGAIYIWNVNGFLE-ATLKGHSTAVNAVSWSPNNNMLASVGKNKR 605
Cdd:cd00200  235 ASGSEDGTIRVWDLRTGECvQTLSGHTNSVTSLAWSPDGKRLASGSADGT 284
WD40 COG2319
WD40 repeat [General function prediction only];
297-610 6.34e-45

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 164.70  E-value: 6.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 297 SRASIDTLKATGYLGQANPTKILMKFEAHENESHAVRWSPVERMVATGGADRKVKLWDIGknSTEPRAVLSGSSAGINSV 376
Cdd:COG2319    7 AALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAA--AGALLATLLGHTAAVLSV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 377 DFDSTGAYILGTSNDYGARVWTVMDNRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWDLRSIACIETKFAGSSC 456
Cdd:COG2319   85 AFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 457 NDLVTTDSLGSTIISGHYDKKIRFWDIRTEKQADDVL-MPAKITSLDLSKDCNYLICSVRDDTIKLLDLRKNQVISTFTN 535
Cdd:COG2319  165 VTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTG 244

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665395407 536 EHFKISCdfarASFNSSGLKIACGSADGAIYIWNVN-GFLEATLKGHSTAVNAVSWSPNNNMLASVGKNKRCTIYS 610
Cdd:COG2319  245 HSGSVRS----VAFSPDGRLLASGSADGTVRLWDLAtGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWD 316
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 27-197 3.54e-42

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: 150.08  E-value: 3.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   27 FKEIIEQNNRLIDHVAQLKADNLKISVENEQLRNAVSTG----GTGSNVAIATLEKKLLSQQEELTELHKRKGENSQMIV 102
Cdd:pfam08614   2 FLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSklskASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  103 DLNQKVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNTMLDEHTALQLAFSSLEEKLRGVQDENRRLL 182
Cdd:pfam08614  82 DLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRELV 161

                         170
                  ....*....|....*
gi 665395407  183 ERLMQYKSKDADKLN 197
Cdd:pfam08614 162 ERWMKRKGQEAEAMN 176
WD40 COG2319
WD40 repeat [General function prediction only];
322-572 1.06e-41

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 155.45  E-value: 1.06e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 322 FEAHENESHAVRWSPVERMVATGGADRKVKLWDIgkNSTEPRAVLSGSSAGINSVDFDSTGAYILGTSNDYGARVWTVMD 401
Cdd:COG2319  158 LTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDL--ATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 402 NRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWDLRSIACIETkFAGSSC--NDLVTTDSlGSTIISGHYDKKIR 479
Cdd:COG2319  236 GKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT-LTGHSGgvNSVAFSPD-GKLLASGSDDGTVR 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 480 FWDIRTEKQADDVLMP-AKITSLDLSKDCNYLICSVRDDTIKLLDLRKNQVISTFTNEHFKISCdfarASFNSSGLKIAC 558
Cdd:COG2319  314 LWDLATGKLLRTLTGHtGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTS----VAFSPDGRTLAS 389

                        250
                 ....*....|....
gi 665395407 559 GSADGAIYIWNVNG 572
Cdd:COG2319  390 GSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 362-609 6.70e-39

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: 144.79  E-value: 6.70e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 362 PRAVLSGSSAGINSVDFDSTGAYILGTSNDYGARVWTVMDNRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWDL 441
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 442 RSIACIETkFAG-----SSCnDLVTTDSLgstIISGHYDKKIRFWDIRTEKQ-------ADDVlmpakiTSLDLSKDCNY 509
Cdd:cd00200   81 ETGECVRT-LTGhtsyvSSV-AFSPDGRI---LSSSSRDKTIKVWDVETGKClttlrghTDWV------NSVAFSPDGTF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 510 LICSVRDDTIKLLDLRKNQVISTFTNEHFKISCdfarASFNSSGLKIACGSADGAIYIWNVN-GFLEATLKGHSTAVNAV 588
Cdd:cd00200  150 VASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS----VAFSPDGEKLLSSSSDGTIKLWDLStGKCLGTLRGHENGVNSV 225

                        250       260
                 ....*....|....*....|.
gi 665395407 589 SWSPNNNMLASVGKNkrCTIY 609
Cdd:cd00200  226 AFSPDGYLLASGSED--GTIR 244
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 317-521 1.16e-34

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 132.84  E-value: 1.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 317 KILMKFEAHENESHAVRWSPVERMVATGGADRKVKLWDIgkNSTEPRAVLSGSSAGINSVDFDSTGAYILGTSNDYGARV 396
Cdd:cd00200   84 ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV--ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 397 WTVMDNRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWDLRSIACIETkfaGSSCNDLVTT---DSLGSTIISGH 473
Cdd:cd00200  162 WDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT---LRGHENGVNSvafSPDGYLLASGS 238

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 665395407 474 YDKKIRFWDIRTEKQADDVLMPAK-ITSLDLSKDCNYLICSVRDDTIKL 521
Cdd:cd00200  239 EDGTIRVWDLRTGECVQTLSGHTNsVTSLAWSPDGKRLASGSADGTIRI 287
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 404-610 1.38e-34

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 132.84  E-value: 1.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 404 LRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWDLRSIACIETKFAGSSCNDLVTTDSLGSTIISGHYDKKIRFWDI 483
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 484 RTEKQADDVLM-PAKITSLDLSKDCNYLICSVRDDTIKLLDLRKNQVISTFTNeHFK-ISCdfarASFNSSGLKIACGSA 561
Cdd:cd00200   81 ETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRG-HTDwVNS----VAFSPDGTFVASSSQ 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 665395407 562 DGAIYIWNV-NGFLEATLKGHSTAVNAVSWSPNNNMLASVGKNKRCTIYS 610
Cdd:cd00200  156 DGTIKLWDLrTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWD 205
WD40 COG2319
WD40 repeat [General function prediction only];
333-610 3.37e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 134.65  E-value: 3.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 333 RWSPVERMVATGGADRKVKLWDIgkNSTEPRAVLSGSSAGINSVDFDSTGAYILGTSNDYGARVWTVMDNRLRHTLTGHS 412
Cdd:COG2319    1 ALSADGAALAAASADLALALLAA--ALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 413 GKVMAAKYVQEPIKVVTGSHDRTLKIWDLRSIACIETKFAGSSCNDLVTTDSLGSTIISGHYDKKIRFWDIRTEKQADDV 492
Cdd:COG2319   79 AAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 493 LMPAK-ITSLDLSKDCNYLICSVRDDTIKLLDLRKNQVISTFTNEHFKISCdfarASFNSSGLKIACGSADGAIYIWNVN 571
Cdd:COG2319  159 TGHSGaVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS----VAFSPDGKLLASGSADGTVRLWDLA 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 665395407 572 -GFLEATLKGHSTAVNAVSWSPNNNMLASVGKNKRCTIYS 610
Cdd:COG2319  235 tGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD 274
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 317-482 6.22e-27

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: 110.89  E-value: 6.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 317 KILMKFEAHENESHAVRWSPVERMVATGGADRKVKLWDIgkNSTEPRAVLSGSSAGINSVDFDSTGAYILGTSNDYGARV 396
Cdd:cd00200  126 KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL--RTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKL 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 397 WTVMDNRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWDLRSIACIETkFAG--SSCNDlVTTDSLGSTIISGHY 474
Cdd:cd00200  204 WDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQT-LSGhtNSVTS-LAWSPDGKRLASGSA 281


                 ....*...
gi 665395407 475 DKKIRFWD 482
Cdd:cd00200  282 DGTIRIWD 289
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 115-200 5.67e-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: 93.40  E-value: 5.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 115 ISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNTMLDEHTALQLAFSSLEEKLRGVQDENRRLLERLMQYKSKDAD 194
Cdd:cd22887    6 LQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKKQQEAD 85


                 ....*.
gi 665395407 195 KLNEEN 200
Cdd:cd22887   86 KMNEAN 91
WD40 COG2319
WD40 repeat [General function prediction only];
317-399 2.45e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 72.25  E-value: 2.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 317 KILMKFEAHENESHAVRWSPVERMVATGGADRKVKLWDIgkNSTEPRAVLSGSSAGINSVDFDSTGAYILGTSNDYGARV 396
Cdd:COG2319  321 KLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL--ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398


                 ...
gi 665395407 397 WTV 399
Cdd:COG2319  399 WDL 401
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 340-524 3.85e-08

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 56.63  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 340 MVATGGADRKVKLWDI------GKNSTEPRAVLSGSSAgINSVDFDSTGAYILGTSNDYGA-RVWTVMDNRLRHTLTGHS 412
Cdd:PLN00181 497 FFATAGVNKKIKIFECesiikdGRDIHYPVVELASRSK-LSGICWNSYIKSQVASSNFEGVvQVWDVARSQLVTEMKEHE 575

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 413 GKVMAAKYVQ-EPIKVVTGSHDRTLKIWDLR---SIACIETKfaGSSCNDLVTTDSlGSTIISGHYDKKIRFWDIRTEKQ 488
Cdd:PLN00181 576 KRVWSIDYSSaDPTLLASGSDDGSVKLWSINqgvSIGTIKTK--ANICCVQFPSES-GRSLAFGSADHKVYYYDLRNPKL 652

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 665395407 489 ADDVLMP-AKITSLDLSKDCNYLICSVRDDTIKLLDL 524
Cdd:PLN00181 653 PLCTMIGhSKTVSYVRFVDSSTLVSSSTDNTLKLWDL 689
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 317-354 1.07e-06

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: 45.38  E-value: 1.07e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 665395407   317 KILMKFEAHENESHAVRWSPVERMVATGGADRKVKLWD 354
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 25-201 1.18e-06

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: 51.56  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   25 DNFKEIIEQNNRLIDHVAQLKADNLKISVENEQlrnavstggtGSNVAIATLEKKLLSQQEELTELHKRKGENSQMIVDL 104
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ----------KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  105 NQKVEQqriIISEKEHSlveqQTNNNRLRAEVQLLHSSLEELKKLNNTMLDEHTALQLAFSSLEEKLRGVQDENRRLLER 184
Cdd:TIGR04523 341 NEQISQ---LKKELTNS----ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ 413

                         170
                  ....*....|....*..
gi 665395407  185 LmQYKSKDADKLNEENE 201
Cdd:TIGR04523 414 I-KKLQQEKELLEKEIE 429
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
28-187 2.17e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.79  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  28 KEIIEQNNRLIDHVAQLKADNLKISVENEQLRNAVSTGGT-----GSNVAIATLEKKLLSQQEELTELHKRKGENSQMIV 102
Cdd:COG3206  215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDalpelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 103 DLNQKVEQ-QRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNTMldehTALQLAFSSLEEKLrgvqDENRRL 181
Cdd:COG3206  295 ALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL----PELEAELRRLEREV----EVAREL 366


                 ....*.
gi 665395407 182 LERLMQ 187
Cdd:COG3206  367 YESLLQ 372
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 571-610 3.01e-06

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: 44.23  E-value: 3.01e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 665395407   571 NGFLEATLKGHSTAVNAVSWSPNNNMLASVGKNKRCTIYS 610
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
76-229 5.27e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 5.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  76 LEKKLlsqQEELTELHKRKGENSQMIVDLNQKVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNTM-- 153
Cdd:COG4717   47 LLERL---EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLek 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665395407 154 LDEHTALQLAFSSLEEKLRGVQDENRRLLERLMQYKSKDADKLNEENE-SIIRKRLPSIFRKRSAKLKRDLEDAVRE 229
Cdd:COG4717  124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElAELQEELEELLEQLSLATEEELQDLAEE 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 16-186 6.15e-06

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: 49.67  E-value: 6.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407    16 LRERNRKECDNFKEIIEQNNRLIDHVAQLKADNLKISVENEQLRNAVS-TGGTGSNVA--IATLEKKLLSQQEELTELHK 92
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTlLNEEAANLRerLESLERRIAATERRLEDLEE 845

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407    93 RKGENSQMIVDLNQKVEQQRIIISEKEHSLVE-------QQTNNNRLRAEVQLLHSSLEELKKLNNTMLDEHTALQLAFS 165
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925

                          170       180
                   ....*....|....*....|.
gi 665395407   166 SLEEKLRGVQDENRRLLERLM 186
Cdd:TIGR02168  926 QLELRLEGLEVRIDNLQERLS 946
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 73-290 1.07e-05

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: 48.22  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  73 IATLEKKLLSQQEELTELHKRKGENSQMIVDLNQKVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNT 152
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 153 MLD------EHTALQLAFSSleeklRGVQDENRRL--LERLMQYKSKDADKLNEENESIIRKR-LPSIFRKRSAKLKRDL 223
Cdd:COG4942  109 LLRalyrlgRQPPLALLLSP-----EDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRaELEAERAELEALLAEL 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665395407 224 EDAVREPSSSSNAASSPGAASLQRNSSPAQFVGGLIGDEDFDEAAINGAMEAIGLDDNEYISARFTA 290
Cdd:COG4942  184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 13-220 1.17e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407    13 VRRLRERNRKECDNFKEIIEQNNRLI-----DHVAQLKADNLKISVENEQLRNAvstggtgsnvaIATLEKKLLSQQEEL 87
Cdd:TIGR02169  256 LTEEISELEKRLEEIEQLLEELNKKIkdlgeEEQLRVKEKIGELEAEIASLERS-----------IAEKERELEDAEERL 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407    88 TELHKRKGENSQMIVDLNQKVEQQRIiisEKEhSLVEQQTNnnrLRAEVQLLHSSLEELKKLNNTMLDEHTALQLAFSSL 167
Cdd:TIGR02169  325 AKLEAEIDKLLAEIEELEREIEEERK---RRD-KLTEEYAE---LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 665395407   168 EEKLRGVQDENRRLLERLMQYKSKDADkLNEENESIIRKRLPSIFRKRSAKLK 220
Cdd:TIGR02169  398 KREINELKRELDRLQEELQRLSEELAD-LNAAIAGIEAKINELEEEKEDKALE 449
WD40 pfam00400
WD domain, G-beta repeat;
317-354 1.21e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 1.21e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 665395407  317 KILMKFEAHENESHAVRWSPVERMVATGGADRKVKLWD 354
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 401-440 1.85e-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: 41.91  E-value: 1.85e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 665395407   401 DNRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWD 440
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
402-440 1.99e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.95  E-value: 1.99e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 665395407  402 NRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWD 440
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 13-225 2.05e-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: 47.79  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   13 VRRLRERNRKECDNFKEIIEQNNRLIDHVaqlkaDNLKISveneqLRNAVSTGGT-GSNVAIATLEKKLLSQQEE--LTE 89
Cdd:pfam05483 270 ANQLEEKTKLQDENLKELIEKKDHLTKEL-----EDIKMS-----LQRSMSTQKAlEEDLQIATKTICQLTEEKEaqMEE 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   90 LHKRKGENSQMIVDLNQKVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNN----------TMLDEHTA 159
Cdd:pfam05483 340 LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNnkeveleelkKILAEDEK 419

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665395407  160 L---QLAFSSLEEKLRGVQDEnrrlLERLMQYKSKDADKLneENESIIRKRLPSIFRKRSAKLKRDLED 225
Cdd:pfam05483 420 LldeKKQFEKIAEELKGKEQE----LIFLLQAREKEIHDL--EIQLTAIKTSEEHYLKEVEDLKTELEK 482
WD40 pfam00400
WD domain, G-beta repeat;
572-610 7.51e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.02  E-value: 7.51e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 665395407  572 GFLEATLKGHSTAVNAVSWSPNNNMLASVGKNKRCTIYS 610
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 72-229 7.81e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 7.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  72 AIATLEKKLLSQQEELTELHKRKGENSQMIVDLNQKVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNN 151
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665395407 152 TMLDEHTALQLAFSSLEEKLRGVQDENRRLLERLMQYKSKDADKLNEENESiiRKRLPSIFRKRSAKLKRDLEDAVRE 229
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA--EEALLEAEAELAEAEEELEELAEEL 388
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 42-229 1.04e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  42 AQLKADNLKISVENEQLRNAVStggtgsnvAIATLEKKLLSQQEELTELHKRKGENSQMIVDLNQKVEQQRiiiSEKEHS 121
Cdd:COG1196  274 LELEELELELEEAQAEEYELLA--------ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE---EELEEL 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 122 LVEQQTNNNRLRAEVQLLHSSLEELKKLNNTMLDEHTALQLAFSSLEEKLRGVQDENRRLLERLMQYKSKDADKLNEENE 201
Cdd:COG1196  343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422

                        170       180
                 ....*....|....*....|....*...
gi 665395407 202 SIIRKRLPSIFRKRSAKLKRDLEDAVRE 229
Cdd:COG1196  423 LEELEEALAELEEEEEEEEEALEEAAEE 450
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 22-214 2.19e-04

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: 44.24  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   22 KECDNFKEIIEQNNRLI------DHVAQLKADNLKISVEneQLRNAVSTGGTGSNVAIATLEKK---LLSQQEELTELHK 92
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIkdltnqDSVKELIIKNLDNTRE--SLETQLKVLSRSINKIKQNLEQKqkeLKSKEKELKKLNE 503

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   93 RKGENSQMIVDLNQ-------KVEQQRIIISEKEHSLVEQQT---------NNNRLRAEVQLLHSSLEELKKLNNTMLDE 156
Cdd:TIGR04523 504 EKKELEEKVKDLTKkisslkeKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKKK 583

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  157 HTALQL---------------------AFSSLEEKLRGVQDENRRLLERLMQYKSKdADKLNEENESI------IRKRLP 209
Cdd:TIGR04523 584 QEEKQElidqkekekkdlikeieekekKISSLEKELEKAKKENEKLSSIIKNIKSK-KNKLKQEVKQIketikeIRNKWP 662


                  ....*
gi 665395407  210 SIFRK 214
Cdd:TIGR04523 663 EIIKK 667
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-229 2.33e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   5 EHVWRAHVVRRLRERNRKEcdnFKEIIEQNNRLIDHVAQLKADNLKIsvenEQLRNAvstggtgsnvaIATLEKKLLSQQ 84
Cdd:COG1196  226 EAELLLLKLRELEAELEEL---EAELEELEAELEELEAELAELEAEL----EELRLE-----------LEELELELEEAQ 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  85 EELTELHKRKGENSQMIVDLNQKVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKlnntmldEHTALQLAF 164
Cdd:COG1196  288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE-------ELEEAEAEL 360

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665395407 165 SSLEEKLrgvQDENRRLLERLMQYKSKDADKLNEENESIIRKRLPSIFRKRSAKLKRDLEDAVRE 229
Cdd:COG1196  361 AEAEEAL---LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 73-230 2.54e-04

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: 44.28  E-value: 2.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407    73 IATLEKKLLSQQEELTELHKRKGENSQMIVDLNQKVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNT 152
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   153 MLDEHTALQLAFSSLEEKLRGVQDENRRL-------------LERLMQYKSKDADKLNEENESI------IRKRLPSIfR 213
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELeaeleelesrleeLEEQLETLRSKVAQLELQIASLnneierLEARLERL-E 413

                          170
                   ....*....|....*..
gi 665395407   214 KRSAKLKRDLEDAVREP 230
Cdd:TIGR02168  414 DRRERLQQEIEELLKKL 430
PTZ00420 PTZ00420
coronin; Provisional
 471-533 2.55e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 44.17  E-value: 2.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665395407 471 SGHYDKKIRFWDIRTEKQADDVLMPAKITSLDLSKDCNYLICSVRDDTIKLLDLRKNQVISTF 533
Cdd:PTZ00420 143 SSGFDSFVNIWDIENEKRAFQINMPKKLSSLKWNIKGNLLSGTCVGKHMHIIDPRKQEIASSF 205
PRK11637 PRK11637
AmiB activator; Provisional
 73-188 3.53e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 43.53  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  73 IATLEKKLLSQQEELTELhkrkgensqmivdLNQkVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNT 152
Cdd:PRK11637  56 IAAKEKSVRQQQQQRASL-------------LAQ-LKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAA 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 665395407 153 -------MLD------EHTALQLAFSSlEEKLRGvqdenrrllERLMQY 188
Cdd:PRK11637 122 qerllaaQLDaafrqgEHTGLQLILSG-EESQRG---------ERILAY 160
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 29-217 4.69e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 4.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407    29 EIIEQNNRLIDHVAQLKADNLKISVENEQLRNAvstggtgsNVAIATLEKKLLSQQEELTELHKRKGENSQMIVDLNQKV 108
Cdd:TIGR02169  841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEEL--------EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   109 EQQRIIISEKEHSLVEQQTNNN--------------------RLRAEVQLLHSSLEELKKLNNTMLDEHTALQLAFSSLE 168
Cdd:TIGR02169  913 EKKRKRLSELKAKLEALEEELSeiedpkgedeeipeeelsleDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK 992

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 665395407   169 EKLRGVQDENRRLLERLMQYKSKDADKLNEENESIIRKrLPSIFRKRSA 217
Cdd:TIGR02169  993 EKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINEN-FNEIFAELSG 1040
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 13-226 5.24e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 5.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407    13 VRRLRERnRKECDNFKEIIEQNNRLID-HVAQLKAdnlKISVENEQLRNAVSTggtgsnvaIATLEKKLLSQQEELTELH 91
Cdd:TIGR02169  676 LQRLRER-LEGLKRELSSLQSELRRIEnRLDELSQ---ELSDASRKIGEIEKE--------IEQLEQEEEKLKERLEELE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407    92 KRKGENSQMIVDLNQKVEQQRIIISEKEHSLVEQQTNNNRLRAEvqLLHSSLEELKKLNNTMLDEHTALQLAFSSLEEKL 171
Cdd:TIGR02169  744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 665395407   172 RGVQDEnRRLLERLMQYKSKDADKLnEENESIIRKRLPSIfRKRSAKLKRDLEDA 226
Cdd:TIGR02169  822 NRLTLE-KEYLEKEIQELQEQRIDL-KEQIKSIEKEIENL-NGKKEELEEELEEL 873
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
 120-229 6.02e-04

Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p


Pssm-ID: 214699 [Multi-domain]  Cd Length: 117  Bit Score: 40.02  E-value: 6.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   120 HSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNTMLDEHTALqlafSSLEEKLRGVQDENRRLLERLmQYKSKDADKLNEE 199
Cdd:smart00503   1 SNLDEFFEKVEEIRANIQKISQNVAELQKLHEELLTPPDAD----KELREKLERLIDDIKRLAKEI-RAKLKELEKENLE 75

                           90       100       110
                   ....*....|....*....|....*....|...
gi 665395407   200 NesiiRKRLPSIFRKRSA---KLKRDLEDAVRE 229
Cdd:smart00503  76 N----RASGSASDRTRKAqteKLRKKFKEVMNE 104
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 14-209 8.06e-04

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: 42.06  E-value: 8.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  14 RRLRERNRKECDNFKEIIEQNNRLIDHVAQLKADNLKISVENEQLRNAvstggtgsNVAIATLEKKLLSQQEELTELHK- 92
Cdd:COG4942   41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL--------EKEIAELRAELEAQKEELAELLRa 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  93 --RKGENSQMIVDLNQ-------------------------KVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEE 145
Cdd:COG4942  113 lyRLGRQPPLALLLSPedfldavrrlqylkylaparreqaeELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665395407 146 LKKLNNTMLDEHTALQLAFSSLEEKLRGVQDENRRLLERLMQYKSKDADKLNEENESIIRKRLP 209
Cdd:COG4942  193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 45-226 9.92e-04

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: 42.40  E-value: 9.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   45 KADNLKISVENEQLRNAVSTggtgSNVAIATLEKKLLSQqeeltelhkrkgENSQMIVDLnqKVEQQRIIISEKEHSLVE 124
Cdd:pfam05483 472 EVEDLKTELEKEKLKNIELT----AHCDKLLLENKELTQ------------EASDMTLEL--KKHQEDIINCKKQEERML 533

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  125 QQTNN-----NRLRAEVQLLHSSLEELKKLNNTMLD--EHTALQLAFSSLEEKLRGVQDENR-RLLERLMQYKSKDADKL 196
Cdd:pfam05483 534 KQIENleekeMNLRDELESVREEFIQKGDEVKCKLDksEENARSIEYEVLKKEKQMKILENKcNNLKKQIENKNKNIEEL 613

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 665395407  197 NEENESIIRK-----RLPSIFRKRSAKLKRDLEDA 226
Cdd:pfam05483 614 HQENKALKKKgsaenKQLNAYEIKVNKLELELASA 648
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
74-225 1.10e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  74 ATLEKKLLSQQEELTELHKRKGENS-QMIVDLNQKVEQ---------------QRIIISEK-----EHSLVEQQTNNNRL 132
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGfESVEELEERLKElepfyneylelkdaeKELEREEKelkklEEELDKAFEELAET 638

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 133 RAEVQLLHSSLEELKKLNNTmlDEHTALQLAFSSLEEKLRGVQDENRRLLERLMQYKsKDADKLNEENESIIRKrlpsif 212
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIK-KTLEKLKEELEEREKA------ 709

                        170
                 ....*....|...
gi 665395407 213 RKRSAKLKRDLED 225
Cdd:PRK03918 710 KKELEKLEKALER 722
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 23-213 3.56e-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: 40.58  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   23 ECDNFKEIIEQNNRLIDhVAQLKADNLKisvenEQLRN-------------AVSTGGTGSNVAIATLEKKL--------- 80
Cdd:pfam10174 381 EIRDLKDMLDVKERKIN-VLQKKIENLQ-----EQLRDkdkqlaglkervkSLQTDSSNTDTALTTLEEALsekeriier 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   81 ------LSQQEELTELHKRKGENSqmivDLNQKVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNTML 154
Cdd:pfam10174 455 lkeqreREDRERLEELESLKKENK----DLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKK 530

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665395407  155 DEHTALQ---LAFSSLEEKLRGVQDENRRL--LERLMQYKSKDADKLNEENEsiirkRLPSIFR 213
Cdd:pfam10174 531 EECSKLEnqlKKAHNAEEAVRTNPEINDRIrlLEQEVARYKEESGKAQAEVE-----RLLGILR 589
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
13-224 4.05e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  13 VRRLRERNRKECDNFKEIIEQNNRLIDHVAQLKADNLK----ISVENEQLRNAVStggtgsnvAIATLEKKLLSQQEELT 88
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReineISSELPELREELE--------KLEKEVKELEELKEEIE 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  89 ELHKRKGENSQMIVDLNQKVEQQRIIISEKEHSLVEQQTNNNRLRaEVQLLHSSLEELKKLNNTMLDEHTALQLAFSSLE 168
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 665395407 169 EKLRGVQdenrrlleRLMQYKSKDADKLNEenesiIRKRLPSIfRKRSAKLKRDLE 224
Cdd:PRK03918 321 EEINGIE--------ERIKELEEKEERLEE-----LKKKLKEL-EKRLEELEERHE 362
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
25-184 5.51e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407  25 DNFKEIIEQNNRLIDHVAQLKADNLKISVENEQLRNAVSTGGTGS-NVAIATLEKKLLSQQEELTELHKRKGEnsqmivd 103
Cdd:COG4717  385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAE------- 457

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407 104 LNQKVEQQriiisEKEHSLVEqqtnnnrLRAEvqllhssLEELKKLNNTMLDEHTALQLAFSSLEEKLRGVQDENR-RLL 182
Cdd:COG4717  458 LEAELEQL-----EEDGELAE-------LLQE-------LEELKAELRELAEEWAALKLALELLEEAREEYREERLpPVL 518


                 ..
gi 665395407 183 ER 184
Cdd:COG4717  519 ER 520
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 20-199 8.63e-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: 39.23  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   20 NRKECD---NFKEIIEQN-NRLIDHVAQLKADNLKISVENEQLRNAVSTGgTGSNVAIATLEKKLLSQQEELTELHKRKG 95
Cdd:TIGR04523 302 NQKEQDwnkELKSELKNQeKKLEEIQNQISQNNKIISQLNEQISQLKKEL-TNSESENSEKQRELEEKQNEIEKLKKENQ 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395407   96 ENSQMIV-------DLNQKVEQQRIIISEKEHSLVEQQTNNNRLRAEVQLLHSSLEELKKLNNTMLDEHTALQLAFSSLe 168
Cdd:TIGR04523 381 SYKQEIKnlesqinDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL- 459

                         170       180       190
                  ....*....|....*....|....*....|.
gi 665395407  169 EKLRGVQDENRRLLERLMQYKSKDADKLNEE 199
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKE 490
 
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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