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Conserved domains on  [gi|298229005|ref|NP_001177195|]
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autophagy-related protein 16-1 isoform 4 [Homo sapiens]

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];
173-520 1.17e-61

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 207.84  E-value: 1.17e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 173 VRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRV----PATALCVFDAHDGEVNAVQFSP 248
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSP 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 249 GSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 328
Cdd:COG2319  131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 329 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LL 404
Cdd:COG2319  209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 405 GKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKV 484
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 298229005 485 EKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 520
Cdd:COG2319  365 LRTL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 1-122 1.29e-43

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: 152.39  E-value: 1.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005    1 MAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKD 80
Cdd:pfam08614  55 LEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 298229005   81 EYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRLN 122
Cdd:pfam08614 135 ELVALQLQLNMAEEKLRKLEKENRELVERWMKRKGQEAEAMN 176
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
173-520 1.17e-61

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 207.84  E-value: 1.17e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 173 VRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRV----PATALCVFDAHDGEVNAVQFSP 248
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSP 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 249 GSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 328
Cdd:COG2319  131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 329 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LL 404
Cdd:COG2319  209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 405 GKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKV 484
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 298229005 485 EKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 520
Cdd:COG2319  365 LRTL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 231-521 3.78e-59

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: 197.56  E-value: 3.78e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 231 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVfgEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWT 310
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 311 VDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmS 380
Cdd:cd00200   80 LETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------S 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 381 GHFDKKIRFWDIRSESIVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDW-TRVVF 458
Cdd:cd00200  153 SSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAF 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298229005 459 SPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSkQHSSSINAVAWSPSGSHVVSVDKGCKAVLWA 521
Cdd:cd00200  228 SPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 1-122 1.29e-43

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: 152.39  E-value: 1.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005    1 MAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKD 80
Cdd:pfam08614  55 LEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 298229005   81 EYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRLN 122
Cdd:pfam08614 135 ELVALQLQLNMAEEKLRKLEKENRELVERWMKRKGQEAEAMN 176
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 36-125 2.42e-30

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: 113.43  E-value: 2.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005  36 KDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKA 115
Cdd:cd22887    2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKKQ 81

                         90
                 ....*....|
gi 298229005 116 QEANRLNAEN 125
Cdd:cd22887   82 QEADKMNEAN 91
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-186 8.52e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 8.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   2 AQLRIKHQEELTELHKKRGELAQL---VIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTL 78
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELlaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005  79 KDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEV 158
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429

                        170       180
                 ....*....|....*....|....*...
gi 298229005 159 IVDETSDHTEETSPVRAISRAATKRLSQ 186
Cdd:COG1196  430 LAELEEEEEEEEEALEEAAEEEAELEEE 457
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 231-266 5.86e-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: 5.86e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 298229005   231 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 266
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
231-266 2.06e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.06e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 298229005  231 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 266
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 241-477 1.54e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.86  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 241 VNAVQFSPGSRLLATGGMDRRVKLWEVF-----GEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASN-DFASRIWTVDDY 314
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 315 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 387
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 388 RFWDIRSESI-VREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNA--IKQT--FSAPGFKCGSDWTRVVFSpDG 462
Cdd:PLN00181 643 YYYDLRNPKLpLCTMIGHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSVS-DG 721

                        250
                 ....*....|....*
gi 298229005 463 sYVAAGSAEGSLYIW 477
Cdd:PLN00181 722 -YIATGSETNEVFVY 735
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-154 4.84e-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: 4.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005     2 AQLRIKHQEELTELHKKRGELAQLVIDLNnqmqRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDE 81
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEIS----RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005    82 YDALQITFTALEGKLRKTTEENQELVTRW-------------MAEKAQEANRLNAENE------KDSRRRQARLQKELAE 142
Cdd:TIGR02168  346 LEELKEELESLEAELEELEAELEELESRLeeleeqletlrskVAQLELQIASLNNEIErlearlERLEDRRERLQQEIEE 425

                          170
                   ....*....|..
gi 298229005   143 AAKEPLPVEQDD 154
Cdd:TIGR02168  426 LLKKLEEAELKE 437
46 PHA02562
endonuclease subunit; Provisional
 9-160 9.83e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.46  E-value: 9.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   9 QEELTELHKKRGE-------LAQLVIDLNNQMQRKDREMQMNE--AKIAECLQTISD-------LETECLDLRTKLCDLE 72
Cdd:PHA02562 240 TDELLNLVMDIEDpsaalnkLNTAAAKIKSKIEQFQKVIKMYEkgGVCPTCTQQISEgpdritkIKDKLKELQHSLEKLD 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005  73 RANQTLK---DEYDALQITFTALEGKLRKtteENQELVT-RWMAEKAQEA-NRLNAENeKDSRRRQARLQKELAEAAKEP 147
Cdd:PHA02562 320 TAIDELEeimDEFNEQSKKLLELKNKIST---NKQSLITlVDKAKKVKAAiEELQAEF-VDNAEELAKLQDELDKIVKTK 395

                        170
                 ....*....|...
gi 298229005 148 LPVEQDDDIEVIV 160
Cdd:PHA02562 396 SELVKEKYHRGIV 408
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
173-520 1.17e-61

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 207.84  E-value: 1.17e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 173 VRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRV----PATALCVFDAHDGEVNAVQFSP 248
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSP 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 249 GSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 328
Cdd:COG2319  131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 329 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LL 404
Cdd:COG2319  209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 405 GKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKV 484
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 298229005 485 EKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 520
Cdd:COG2319  365 LRTL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 231-521 3.78e-59

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: 197.56  E-value: 3.78e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 231 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVfgEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWT 310
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 311 VDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmS 380
Cdd:cd00200   80 LETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------S 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 381 GHFDKKIRFWDIRSESIVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDW-TRVVF 458
Cdd:cd00200  153 SSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAF 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298229005 459 SPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSkQHSSSINAVAWSPSGSHVVSVDKGCKAVLWA 521
Cdd:cd00200  228 SPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
219-479 1.12e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 175.87  E-value: 1.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 219 GSGKEVRV----PATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEFkgSLSGSNAGITSIEFDSAG 294
Cdd:COG2319  139 SADGTVRLwdlaTGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR--TLTGHTGAVRSVAFSPDG 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 295 SYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAGSSC--NDIV 372
Cdd:COG2319  217 KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT-LTGHSGgvNSVA 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 373 CT--EQCVMSGHFDKKIRFWDIRSESIVREME-LLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkc 449
Cdd:COG2319  296 FSpdGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGH---- 371

                        250       260       270
                 ....*....|....*....|....*....|.
gi 298229005 450 gSDW-TRVVFSPDGSYVAAGSAEGSLYIWSV 479
Cdd:COG2319  372 -TGAvTSVAFSPDGRTLASGSADGTVRLWDL 401
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 1-122 1.29e-43

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: 152.39  E-value: 1.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005    1 MAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKD 80
Cdd:pfam08614  55 LEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 298229005   81 EYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRLN 122
Cdd:pfam08614 135 ELVALQLQLNMAEEKLRKLEKENRELVERWMKRKGQEAEAMN 176
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 316-520 1.09e-35

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 134.77  E-value: 1.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 316 LRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV----FAGSSCNDIVCTEQCVmSGHFDKKIRFWD 391
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLkghtGPVRDVAASADGTYLA-SGSSDKTIRLWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 392 IRSESIVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDWTR-VVFSPDGSYVAAGS 469
Cdd:cd00200   80 LETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNsVAFSPDGTFVASSS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 298229005 470 AEGSLYIWSVLTGKVEKVLsKQHSSSINAVAWSPSGSHVV--SVDKGCKavLW 520
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSPDGEKLLssSSDGTIK--LW 204
WD40 COG2319
WD40 repeat [General function prediction only];
245-520 1.20e-35

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 137.35  E-value: 1.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 245 QFSPGSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHS 324
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALL--LLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 325 GKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFA-GSSCNDIVCTE--QCVMSGHFDKKIRFWDIRSESIVREM 401
Cdd:COG2319   79 AAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGhTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 402 EL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDW-TRVVFSPDGSYVAAGSAEGSLYIWSV 479
Cdd:COG2319  159 TGhSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH-----TGAvRSVAFSPDGKLLASGSADGTVRLWDL 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 298229005 480 LTGKVEKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 520
Cdd:COG2319  234 ATGKLLRTL-TGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 36-125 2.42e-30

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: 113.43  E-value: 2.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005  36 KDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKA 115
Cdd:cd22887    2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKKQ 81

                         90
                 ....*....|
gi 298229005 116 QEANRLNAEN 125
Cdd:cd22887   82 QEADKMNEAN 91
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-186 8.52e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 8.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   2 AQLRIKHQEELTELHKKRGELAQL---VIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTL 78
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELlaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005  79 KDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEV 158
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429

                        170       180
                 ....*....|....*....|....*...
gi 298229005 159 IVDETSDHTEETSPVRAISRAATKRLSQ 186
Cdd:COG1196  430 LAELEEEEEEEEEALEEAAEEEAELEEE 457
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 231-266 5.86e-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: 5.86e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 298229005   231 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 266
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 315-352 1.39e-07

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 47.69  E-value: 1.39e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 298229005   315 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 352
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
231-266 2.06e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.06e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 298229005  231 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 266
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-180 3.06e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   1 MAQLRIKHQEELTELHKKRGELAQL---VIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQT 77
Cdd:COG4372   47 LEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005  78 LKDEYDALQITFTALEGKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPVEQDDDI 156
Cdd:COG4372  127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEA 205

                        170       180
                 ....*....|....*....|....
gi 298229005 157 EVIVDETSDHTEETSPVRAISRAA 180
Cdd:COG4372  206 EKLIESLPRELAEELLEAKDSLEA 229
WD40 pfam00400
WD domain, G-beta repeat;
315-352 3.72e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 3.72e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 298229005  315 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 352
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
4-154 6.54e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 6.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   4 LRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYD 83
Cdd:COG4717   47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298229005  84 ALQitftaLEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQ-ARLQKELAEAAKEPLPVEQDD 154
Cdd:COG4717  127 LLP-----LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElAELQEELEELLEQLSLATEEE 193
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 241-477 1.54e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.86  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 241 VNAVQFSPGSRLLATGGMDRRVKLWEVF-----GEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASN-DFASRIWTVDDY 314
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 315 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 387
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 388 RFWDIRSESI-VREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNA--IKQT--FSAPGFKCGSDWTRVVFSpDG 462
Cdd:PLN00181 643 YYYDLRNPKLpLCTMIGHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSVS-DG 721

                        250
                 ....*....|....*
gi 298229005 463 sYVAAGSAEGSLYIW 477
Cdd:PLN00181 722 -YIATGSETNEVFVY 735
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-146 2.12e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   7 KHQEELTELHKKRGELAQLVID-LNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDAL 85
Cdd:COG1196  214 RYRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298229005  86 QITFTALEGKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDS-RRRQARLQKELAEAAKE 146
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEER-LEELEEELAELEEELEELEeELEELEEELEEAEEELE 354
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
274-482 3.74e-06

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 48.15  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 274 FKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARI-VSGSHDRTLKLWD 352
Cdd:COG3391   17 ALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLyVANSGSGRVSVID 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 353 LRSKVCIKTVFAGSSCNDIVCTE---QCVMSGHFDKKIRFWDIRSESIVREMELLGKITALDLNPERTELLSCSRDD--- 426
Cdd:COG3391   97 LATGKVVATIPVGGGPRGLAVDPdggRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSntv 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 298229005 427 --LLKVIDLRTNAIKQTFSApgfkcGSDWTRVVFSPDGS--YVA------AGSAEGSLYIWSVLTG 482
Cdd:COG3391  177 svIVSVIDTATGKVVATIPV-----GGGPVGVAVSPDGRrlYVAnrgsntSNGGSNTVSVIDLATL 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-154 4.84e-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: 4.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005     2 AQLRIKHQEELTELHKKRGELAQLVIDLNnqmqRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDE 81
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEIS----RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005    82 YDALQITFTALEGKLRKTTEENQELVTRW-------------MAEKAQEANRLNAENE------KDSRRRQARLQKELAE 142
Cdd:TIGR02168  346 LEELKEELESLEAELEELEAELEELESRLeeleeqletlrskVAQLELQIASLNNEIErlearlERLEDRRERLQQEIEE 425

                          170
                   ....*....|..
gi 298229005   143 AAKEPLPVEQDD 154
Cdd:TIGR02168  426 LLKKLEEAELKE 437
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 237-353 6.40e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.93  E-value: 6.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 237 HDGEVNAVQFSPGS-RLLATGGMDRRVKLWEVFgekcefKGSLSGS---NAGITSIEFDSAGSYLLAasndFASRIWTVD 312
Cdd:PLN00181 574 HEKRVWSIDYSSADpTLLASGSDDGSVKLWSIN------QGVSIGTiktKANICCVQFPSESGRSLA----FGSADHKVY 643

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 298229005 313 DYRLRH------TLTGHSGKVLSAKFLlDNARIVSGSHDRTLKLWDL 353
Cdd:PLN00181 644 YYDLRNpklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 30-182 3.00e-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: 46.97  E-value: 3.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005    30 NNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEEnQELVTR 109
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEE 747

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298229005   110 WMAEKAQEANRLNAE-NEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATK 182
Cdd:TIGR02168  748 RIAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 430-509 3.53e-05

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


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 44.28  E-value: 3.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 430 VIDLRTNAIKQTFSAPGFKCGSDWtrvvfSPDGSYVAAGSAEGS---LYIWSVLTGKVEKVLSKQHSSSinAVAWSPSGS 506
Cdd:COG0823   15 VVDLDGGEPRRLTNSPGIDTSPAW-----SPDGRRIAFTSDRGGgpqIYVVDADGGEPRRLTFGGGYNA--SPSWSPDGK 87


                 ...
gi 298229005 507 HVV 509
Cdd:COG0823   88 RLA 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 9-169 7.27e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 7.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005     9 QEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDL--------------ERA 74
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELeseleallneraslEEA 888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005    75 NQTLKDEYDALQITFTALEGKLRKTTEENQELvtrwMAEKAQEANRLN-AENEKDSRRRQARLQKELAEAAKEPLPVEQD 153
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEEL----REKLAQLELRLEgLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964

                          170
                   ....*....|....*.
gi 298229005   154 DDIEVIVDETSDHTEE 169
Cdd:TIGR02168  965 DDEEEARRRLKRLENK 980
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 11-146 7.72e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.15  E-value: 7.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005  11 ELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKlcdLERANQTLK-----DEYDAL 85
Cdd:COG1579   18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---IKKYEEQLGnvrnnKEYEAL 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298229005  86 QITFTALEGKLRKTTEENQELVTRwmAEKAQ----EANRLNAENEKDSRRRQARLQKELAEAAKE 146
Cdd:COG1579   95 QKEIESLKRRISDLEDEILELMER--IEELEeelaELEAELAELEAELEEKKAELDEELAELEAE 157
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 481-520 2.06e-04

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.83  E-value: 2.06e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 298229005   481 TGKVEKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 520
Cdd:smart00320   1 SGELLKTL-KGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 457-505 2.76e-04

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 43.87  E-value: 2.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 298229005  457 VFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSKQHSSSINAVAWSPSG 505
Cdd:COG4946   395 VWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISDLAWSPDS 443
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1-186 3.17e-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: 3.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005     1 MAQLRIKHQEELTELHKKRGELAQLVIDLnnQMQRKDREMQMNEakiaeclqtISDLETECLDLRTKLCDLERANQTLKD 80
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREI--EEERKRRDKLTEE---------YAELKEELEDLRAELEEVDKEFAETRD 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005    81 EYDALQitfTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENE-KDSRRRQARLQKELAEAAKEPLPVEQddDIEVI 159
Cdd:TIGR02169  386 ELKDYR---EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAiAGIEAKINELEEEKEDKALEIKKQEW--KLEQL 460

                          170       180
                   ....*....|....*....|....*..
gi 298229005   160 VDETSDHTEETSPVRAISRAATKRLSQ 186
Cdd:TIGR02169  461 AADLSKYEQELYDLKEEYDRVEKELSK 487
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 430-520 3.64e-04

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


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 41.20  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 430 VIDLRTNAIKQ-TFSapgfkcGSDWTRVVFSPDGSYVA-AGSAEGSLYIWSV-LTGKVEKVLSKqhssSINAVAWSPSGS 506
Cdd:COG0823   59 VVDADGGEPRRlTFG------GGYNASPSWSPDGKRLAfVSRSDGRFDIYVLdLDGGAPRRLTD----GPGSPSWSPDGR 128

                         90
                 ....*....|....*
gi 298229005 507 HVV-SVDKGCKAVLW 520
Cdd:COG0823  129 RIVfSSDRGGRPDLY 143
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-190 3.83e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   2 AQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDE 81
Cdd:COG1196  336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005  82 YDALQitftalegklrkttEENQELVTrwmAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPL--PVEQDDDIEVI 159
Cdd:COG1196  416 LERLE--------------EELEELEE---ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLaeLLEEAALLEAA 478

                        170       180       190
                 ....*....|....*....|....*....|.
gi 298229005 160 VDETSDHTEETSPVRAISRAATKRLSQPAGG 190
Cdd:COG1196  479 LAELLEELAEAAARLLLLLEAEADYEGFLEG 509
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 11-169 4.43e-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: 43.09  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   11 ELTELHKKRGElaQLVIDLNNQMQRKDREMQM-------NEAKIAECLQTISDLETECLDLRT--------------KLC 69
Cdd:TIGR04523 296 EISDLNNQKEQ--DWNKELKSELKNQEKKLEEiqnqisqNNKIISQLNEQISQLKKELTNSESensekqreleekqnEIE 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   70 DLERANQTLKDEYDALQITFTALEGKLRKTTEENQELvtrwmaekaqEANRLNAENEKDSRRRQARLQKELAEAAKEPLP 149
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK----------DEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443

                         170       180
                  ....*....|....*....|..
gi 298229005  150 --VEQDDDIEVIVDETSDHTEE 169
Cdd:TIGR04523 444 dlTNQDSVKELIIKNLDNTRES 465
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1-137 4.86e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 4.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005     1 MAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAE-------CLQTISDLETECLDLRTKLcDLER 73
Cdd:pfam01576  206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEetaqknnALKKIRELEAQISELQEDL-ESER 284

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298229005    74 ANQT--------LKDEYDALQitfTALEGKLrKTTEENQELVTRwmaeKAQEANRLNAENEKDSRRRQARLQ 137
Cdd:pfam01576  285 AARNkaekqrrdLGEELEALK---TELEDTL-DTTAAQQELRSK----REQEVTELKKALEEETRSHEAQLQ 348
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
9-157 5.34e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005    9 QEELTELHKKRGELAQLVIDLNNQMQRKDR---------EMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLK 79
Cdd:COG4913   616 EAELAELEEELAEAEERLEALEAELDALQErrealqrlaEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLE 695

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   80 D---EYDALQITFTALEGKLRKTTEENQELVTRWmaekAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDI 156
Cdd:COG4913   696 EleaELEELEEELDELKGEIGRLEKELEQAEEEL----DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771


                  .
gi 298229005  157 E 157
Cdd:COG4913   772 E 772
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-165 5.82e-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: 42.75  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005     7 KHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMN--------EAKIAECLQTISDLETEcldlrtkLCDLERANQTL 78
Cdd:TIGR02169  255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekigelEAEIASLERSIAEKERE-------LEDAEERLAKL 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005    79 KDEYDALQITFTALEGKLR-------KTTEENQELVTRwMAEKAQEANRLNAENeKDSRRRQARLQKELAEAAKE--PLP 149
Cdd:TIGR02169  328 EAEIDKLLAEIEELEREIEeerkrrdKLTEEYAELKEE-LEDLRAELEEVDKEF-AETRDELKDYREKLEKLKREinELK 405

                          170
                   ....*....|....*.
gi 298229005   150 VEQDDDIEVIVDETSD 165
Cdd:TIGR02169  406 RELDRLQEELQRLSEE 421
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 4-142 8.37e-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: 42.31  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005    4 LRIKHQEELTELHKKRGELAQLvidlnnQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYD 83
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQ------EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK 471

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 298229005   84 ALQITFTALEGKLRKTTEEnqelvtrwMAEKAQEANRLNAENeKDSRRRQARLQKELAE 142
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKE--------LKSKEKELKKLNEEK-KELEEKVKDLTKKISS 521
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-142 2.35e-03

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: 40.82  E-value: 2.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005     7 KHQEELTELhKKRGELAQLVID-LNNQMQRKDREMQMNEakiaeclqtisdletECLDLRTKLCDLE-----RANQTLKD 80
Cdd:TIGR02169  174 KALEELEEV-EENIERLDLIIDeKRQQLERLRREREKAE---------------RYQALLKEKREYEgyellKEKEALER 237

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298229005    81 EYDALQITFTALEGKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRRQARLQKELAE 142
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKR-LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 30-186 2.49e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005  30 NNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTR 109
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005 110 WMAEKAQEANR----------------LNAENEKDSRRRQARLQ------KELAEAAKeplpvEQDDDIEVIVDETSDHT 167
Cdd:COG4942   99 LEAQKEELAELlralyrlgrqpplallLSPEDFLDAVRRLQYLKylaparREQAEELR-----ADLAELAALRAELEAER 173

                        170
                 ....*....|....*....
gi 298229005 168 EETSPVRAISRAATKRLSQ 186
Cdd:COG4942  174 AELEALLAELEEERAALEA 192
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 456-520 2.51e-03

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 40.79  E-value: 2.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298229005  456 VVFSPDGSYVAAGS-AEGS--LYIWSVLTGKVEKVLSKQHSSSINAVAWSPSGSHVVSVDKGCKavLW 520
Cdd:COG4946   348 PAWSPDGKSIAYFSdASGEyeLYIAPADGSGEPKQLTLGDLGRVFNPVWSPDGKKIAFTDNRGR--LW 413
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 33-142 3.31e-03

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


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 38.07  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   33 MQRKDREMQMNEAKiaecLQTISDLETECLDLR-------TKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQE 105
Cdd:pfam11559  44 LQQRDRDLEFRESL----NETIRTLEAEIERLQskierlkTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQR 119

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 298229005  106 LVTRWMAEKAQeanrlnAENEKDSRRRQ-ARLQKELAE 142
Cdd:pfam11559 120 LKNALQQIKTQ------FAHEVKKRDREiEKLKERLAQ 151
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 404-507 3.51e-03

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 40.41  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005  404 LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPGFKCGSDwtrVVFSPDGSYVA----AGSAEGSLYIWSV 479
Cdd:COG4946   388 LGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISD---LAWSPDSKWLAyskpGPNQLSQIFLYDV 464

                          90       100
                  ....*....|....*....|....*...
gi 298229005  480 LTGKVEKVLSKQHSSSinAVAWSPSGSH 507
Cdd:COG4946   465 ETGKTVQLTDGRYDDG--SPAFSPDGKY 490
Ge1_WD40 pfam16529
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ...
 281-362 3.60e-03

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


Pssm-ID: 465162 [Multi-domain]  Cd Length: 328  Bit Score: 39.75  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005  281 SNAGITSIEFDSAGSYLLAASNDFASRIWTV-----DDYRLRHTLTGHSGKVLSAKFLLDNAR----------IVSGS-H 344
Cdd:pfam16529 185 EHSLLVDAAFSPDGTALATASLDGEVKFFQIylfdnRNPRCLHEWKPHDGKPLSSLFFLDNHKkppevqfwrfAITGAdN 264

                          90
                  ....*....|....*...
gi 298229005  345 DRTLKLWDLRSKVCIKTV 362
Cdd:pfam16529 265 NSELKLWSCESWTCLQTI 282
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 454-478 4.95e-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: 4.95e-03
                           10        20
                   ....*....|....*....|....*
gi 298229005   454 TRVVFSPDGSYVAAGSAEGSLYIWS 478
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLWD 40
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-146 5.55e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 5.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   2 AQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDE 81
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298229005  82 YDALQITFTALEGKLRKT-----------TEENQELVTRWMAEKA-QEANRLNAENEKDSRRRQARLQKELAEAAKE 146
Cdd:COG4942   99 LEAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAE 175
46 PHA02562
endonuclease subunit; Provisional
 9-160 9.83e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.46  E-value: 9.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   9 QEELTELHKKRGE-------LAQLVIDLNNQMQRKDREMQMNE--AKIAECLQTISD-------LETECLDLRTKLCDLE 72
Cdd:PHA02562 240 TDELLNLVMDIEDpsaalnkLNTAAAKIKSKIEQFQKVIKMYEkgGVCPTCTQQISEgpdritkIKDKLKELQHSLEKLD 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005  73 RANQTLK---DEYDALQITFTALEGKLRKtteENQELVT-RWMAEKAQEA-NRLNAENeKDSRRRQARLQKELAEAAKEP 147
Cdd:PHA02562 320 TAIDELEeimDEFNEQSKKLLELKNKIST---NKQSLITlVDKAKKVKAAiEELQAEF-VDNAEELAKLQDELDKIVKTK 395

                        170
                 ....*....|...
gi 298229005 148 LPVEQDDDIEVIV 160
Cdd:PHA02562 396 SELVKEKYHRGIV 408
PRK12704 PRK12704
phosphodiesterase; Provisional
 6-146 9.99e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 9.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298229005   6 IKHQEELT---ELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEY 82
Cdd:PRK12704  54 IKKEALLEakeEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298229005  83 DALQitftalegklrktTEENQELvTRWMAEKAQEA-NRLNAENEKDSRRRQARLQKELAEAAKE 146
Cdd:PRK12704 134 EELI-------------EEQLQEL-ERISGLTAEEAkEILLEKVEEEARHEAAVLIKEIEEEAKE 184
 
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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