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Conserved domains on  [gi|568951451|ref|XP_006508290|]
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protein Atg16l2 isoform X4 [Mus musculus]

Protein Classification

WD repeat ATG16 family protein( domain architecture ID 12095058)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
359-616 3.76e-51

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: 178.30  E-value: 3.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 438
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 439 ETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 515
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 516 WDSRGPHCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRADGFKCSSdwtkAVFSPDRSYALAG 594
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237
                        250       260
                 ....*....|....*....|..
gi 568951451 595 SSNGDLYIWDVNTGKLETSLQG 616
Cdd:cd00200  238 SEDGTIRVWDLRTGECVQTLSG 259
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
59-231 8.54e-46

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: 159.71  E-value: 8.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   59 LFLELVPAYNHLLEKAELLAKFSEKLKSEPKDAISTRHEDwREEVSGTGPDQVSSPASLRVKWQQEKKGLQLVCGEMAYQ 138
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSS-KLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  139 VVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARD 218
Cdd:pfam08614  80 LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRE 159
                         170
                  ....*....|...
gi 568951451  219 LLEQLVQRKARAA 231
Cdd:pfam08614 160 LVERWMKRKGQEA 172
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
359-616 3.76e-51

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: 178.30  E-value: 3.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 438
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 439 ETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 515
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 516 WDSRGPHCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRADGFKCSSdwtkAVFSPDRSYALAG 594
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237
                        250       260
                 ....*....|....*....|..
gi 568951451 595 SSNGDLYIWDVNTGKLETSLQG 616
Cdd:cd00200  238 SEDGTIRVWDLRTGECVQTLSG 259
WD40 COG2319
WD40 repeat [General function prediction only];
354-616 9.99e-47

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 169.71  E-value: 9.99e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 354 SQAQDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQ 433
Cdd:COG2319  110 GLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVR 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 434 LWKVGETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcgDHIIIS 506
Cdd:COG2319  188 LWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTltghsgsVRSVAFSPD----GRLLAS 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 507 GHNDQKIRFWDSRGPHCIQVIPVQ-GRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRADGFKCSSdwtkAVFS 585
Cdd:COG2319  264 GSADGTVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS----VAFS 339
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568951451 586 PDRSYALAGSSNGDLYIWDVNTGKLETSLQG 616
Cdd:COG2319  340 PDGKTLASGSDDGTVRLWDLATGELLRTLTG 370
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
59-231 8.54e-46

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: 159.71  E-value: 8.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   59 LFLELVPAYNHLLEKAELLAKFSEKLKSEPKDAISTRHEDwREEVSGTGPDQVSSPASLRVKWQQEKKGLQLVCGEMAYQ 138
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSS-KLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  139 VVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARD 218
Cdd:pfam08614  80 LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRE 159
                         170
                  ....*....|...
gi 568951451  219 LLEQLVQRKARAA 231
Cdd:pfam08614 160 LVERWMKRKGQEA 172
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
148-231 3.17e-17

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: 76.84  E-value: 3.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 148 TLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRK 227
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                 ....
gi 568951451 228 ARAA 231
Cdd:cd22887   81 QQEA 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
122-286 1.76e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 122 QQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQ 201
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 202 AVHQEAALRRLQEEARDL---LEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISEIPNTLEDGTKEET 278
Cdd:COG1196  395 AAELAAQLEELEEAEEALlerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474

                 ....*...
gi 568951451 279 VALAPAAL 286
Cdd:COG1196  475 LEAALAEL 482
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
359-392 3.96e-07

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 46.54  E-value: 3.96e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568951451   359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWN 392
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
147-562 4.15e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 53.17  E-value: 4.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 147 DTLQSQ-LEERQDRLEALQAcVVQLQEARAQQSRQLE------ERQAENAAQREAYETLLQQAVHQeaALRR---LQEEA 216
Cdd:PLN00181 261 ELLQSEfINEPRENLEEREA-AMELRDRIEEQELLLEflfliqQRKQEAADKLQDTISLLSSDIDQ--VVKRqlvLQQKG 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 217 RDLLEQLVQRK-----ARAAAERNLRNERRERANQALVS------------------------QELKKAAKRTVSISE-I 266
Cdd:PLN00181 338 SDVRSFLASRKrirqgAETLAAEEENDDNSSKLDDTLEStllessrlmrnlkklesvyfatryRQIKAAAAAEKPLARyY 417
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 267 PNTLEDGTKEETVALA-PAALPEFSESETCEK-WKRPFrsasatsltlsrcvdvVKGL---LDFKKRRghsvggapeqry 341
Cdd:PLN00181 418 SALSENGRSSEKSSMSnPAKPPDFYINDSRQGgWIDPF----------------LEGLckyLSFSKLR------------ 469
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 342 qsipvcVSAQIpsQAQDVLDAHlSEVNAVCFGPNSSLLATGGADRLIHLWN----VVGGRLEANQTLEGAGGS-ITSVDF 416
Cdd:PLN00181 470 ------VKADL--KQGDLLNSS-NLVCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICW 540
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 417 DPS-GSQVLAATYNQAAQLWKVGETQSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSyc 494
Cdd:PLN00181 541 NSYiKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA-- 618
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568951451 495 nDVVC------GDHIIISGHNDQKIRFWDSRGPHCIQVIPVQGRVTSLHLSY-DQLHLLSCSRDNTLKVIDLRIS 562
Cdd:PLN00181 619 -NICCvqfpseSGRSLAFGSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFvDSSTLVSSSTDNTLKLWDLSMS 692
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
39-253 7.82e-07

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: 52.37  E-value: 7.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451    39 AVWKRHIVRQLRHRDRTQKALflelvPAYNHLLEKAELLAKFSEKLKSEPKDAISTRHEDWRE---EVSGTGPDQVSSPA 115
Cdd:TIGR02168  228 ALLVLRLEELREELEELQEEL-----KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   116 SLRVKwQQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEA---RAQQSRQLEERQAENAAQR 192
Cdd:TIGR02168  303 QKQIL-RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEleeLEAELEELESRLEELEEQL 381
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568951451   193 EAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVSQEL 253
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
WD40 pfam00400
WD domain, G-beta repeat;
359-392 1.29e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.03  E-value: 1.29e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568951451  359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWN 392
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PRK11281 PRK11281
mechanosensitive channel MscK;
93-229 3.21e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 43.75  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   93 STRHEDWREEVSGTGPDQVSSPASLRVKWQQEkkgLQLVCGEMAYQvvKKSAA-----LDTLQSQLEERQDRLEALQACV 167
Cdd:PRK11281  169 SQRLQQIRNLLKGGKVGGKALRPSQRVLLQAE---QALLNAQNDLQ--RKSLEgntqlQDLLQKQRDYLTARIQRLEHQL 243
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568951451  168 VQLQEARAQQSRQLEERQAENA-AQREAYETLLQQAVHQEAAL-RRLQE---EARDLLEQLVQRKAR 229
Cdd:PRK11281  244 QLLQEAINSKRLTLSEKTVQEAqSQDEAARIQANPLVAQELEInLQLSQrllKATEKLNTLTQQNLR 310
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
359-616 3.76e-51

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: 178.30  E-value: 3.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 438
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 439 ETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 515
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 516 WDSRGPHCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRADGFKCSSdwtkAVFSPDRSYALAG 594
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237
                        250       260
                 ....*....|....*....|..
gi 568951451 595 SSNGDLYIWDVNTGKLETSLQG 616
Cdd:cd00200  238 SEDGTIRVWDLRTGECVQTLSG 259
WD40 COG2319
WD40 repeat [General function prediction only];
354-616 9.99e-47

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 169.71  E-value: 9.99e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 354 SQAQDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQ 433
Cdd:COG2319  110 GLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVR 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 434 LWKVGETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcgDHIIIS 506
Cdd:COG2319  188 LWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTltghsgsVRSVAFSPD----GRLLAS 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 507 GHNDQKIRFWDSRGPHCIQVIPVQ-GRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRADGFKCSSdwtkAVFS 585
Cdd:COG2319  264 GSADGTVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS----VAFS 339
                        250       260       270
                 ....*....|....*....|....*....|.
gi 568951451 586 PDRSYALAGSSNGDLYIWDVNTGKLETSLQG 616
Cdd:COG2319  340 PDGKTLASGSDDGTVRLWDLATGELLRTLTG 370
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
59-231 8.54e-46

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: 159.71  E-value: 8.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   59 LFLELVPAYNHLLEKAELLAKFSEKLKSEPKDAISTRHEDwREEVSGTGPDQVSSPASLRVKWQQEKKGLQLVCGEMAYQ 138
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSS-KLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  139 VVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARD 218
Cdd:pfam08614  80 LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRE 159
                         170
                  ....*....|...
gi 568951451  219 LLEQLVQRKARAA 231
Cdd:pfam08614 160 LVERWMKRKGQEA 172
WD40 COG2319
WD40 repeat [General function prediction only];
348-618 6.39e-43

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 158.92  E-value: 6.39e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 348 VSAQIPSQAQDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEAnqTLEGAGGSITSVDFDPSGSQVLAAT 427
Cdd:COG2319   62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLR--TLTGHTGAVRSVAFSPDGKTLASGS 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 428 YNQAAQLWKVGETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcg 500
Cdd:COG2319  140 ADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTltghtgaVRSVAFSPD---- 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 501 DHIIISGHNDQKIRFWDSRGPHCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRADgfkcsSDW 579
Cdd:COG2319  216 GKLLASGSADGTVRLWDLATGKLLRTLTGhSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH-----SGG 290
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568951451 580 TKAV-FSPDRSYALAGSSNGDLYIWDVNTGKLETSLQGPH 618
Cdd:COG2319  291 VNSVaFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT 330
WD40 COG2319
WD40 repeat [General function prediction only];
359-607 4.65e-40

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 151.22  E-value: 4.65e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 438
Cdd:COG2319  157 TLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLL--RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 439 ETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTinvLSYCNDVVCG------DHIIISGHNDQK 512
Cdd:COG2319  235 TGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT---LTGHSGGVNSvafspdGKLLASGSDDGT 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 513 IRFWDSRGPHCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRAdgfkcSSDWTKAV-FSPDRSY 590
Cdd:COG2319  312 VRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTG-----HTGAVTSVaFSPDGRT 386
                        250
                 ....*....|....*..
gi 568951451 591 ALAGSSNGDLYIWDVNT 607
Cdd:COG2319  387 LASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
359-556 2.22e-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: 2.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 438
Cdd:cd00200   88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL--TTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLR 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 439 ETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLgraYCSRTINVLSYCNDVVCG------DHIIISGHNDQK 512
Cdd:cd00200  166 TGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL---STGKCLGTLRGHENGVNSvafspdGYLLASGSEDGT 242
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568951451 513 IRFWDSRGPHCIQVIP-VQGRVTSLHLSYDQLHLLSCSRDNTLKV 556
Cdd:cd00200  243 IRVWDLRTGECVQTLSgHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
402-616 7.77e-34

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 130.53  E-value: 7.77e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 402 QTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVGETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGR 481
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 482 AYCSRTINvlSYCNDVVCGD-----HIIISGHNDQKIRFWDSRGPHCIQVIP-VQGRVTSLHLSYDQLHLLSCSRDNTLK 555
Cdd:cd00200   83 GECVRTLT--GHTSYVSSVAfspdgRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAFSPDGTFVASSSQDGTIK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568951451 556 VIDLRISNIRQVFRAdgfkcSSDWTKAV-FSPDRSYALAGSSNGDLYIWDVNTGKLETSLQG 616
Cdd:cd00200  161 LWDLRTGKCVATLTG-----HTGEVNSVaFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRG 217
WD40 COG2319
WD40 repeat [General function prediction only];
332-617 2.09e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 132.34  E-value: 2.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 332 SVGGAPEQRYQSIPVCVSAQIPSQAQDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEAnqTLEGAGGSI 411
Cdd:COG2319    4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLA--TLLGHTAAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 412 TSVDFDPSGSQVLAATYNQAAQLWKVGETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT---- 487
Cdd:COG2319   82 LSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTltgh 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 488 ---INVLSYCNDvvcgDHIIISGHNDQKIRFWDSRGPHCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISN 563
Cdd:COG2319  162 sgaVTSVAFSPD----GKLLASGSDDGTVRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGK 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568951451 564 IRQVFRADgfkcsSDWTKAV-FSPDRSYALAGSSNGDLYIWDVNTGKLETSLQGP 617
Cdd:COG2319  238 LLRTLTGH-----SGSVRSVaFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
355-517 3.97e-26

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: 108.58  E-value: 3.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 355 QAQDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLeaNQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQL 434
Cdd:cd00200  126 KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC--VATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKL 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 435 WKVGETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDVvcgdHIIISG 507
Cdd:cd00200  204 WDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTlsghtnsVTSLAWSPDG----KRLASG 279
                        170
                 ....*....|
gi 568951451 508 HNDQKIRFWD 517
Cdd:cd00200  280 SADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
372-617 4.00e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.07  E-value: 4.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 372 FGPNSSLLATGGADRLIHLWNVVGGRLEAnqTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVGETQSKETLSGHKD 451
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLL--LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 452 KVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVL-SYCNDVVC--GDHIIISGHNDQKIRFWDSRGPHCIQVIP 528
Cdd:COG2319   80 AVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHtGAVRSVAFspDGKTLASGSADGTVRLWDLATGKLLRTLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 529 V-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRAdgfkcSSDWTKAV-FSPDRSYALAGSSNGDLYIWDVN 606
Cdd:COG2319  160 GhSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG-----HTGAVRSVaFSPDGKLLASGSADGTVRLWDLA 234
                        250
                 ....*....|.
gi 568951451 607 TGKLETSLQGP 617
Cdd:COG2319  235 TGKLLRTLTGH 245
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
148-231 3.17e-17

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: 76.84  E-value: 3.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 148 TLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRK 227
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                 ....
gi 568951451 228 ARAA 231
Cdd:cd22887   81 QQEA 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
122-286 1.76e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 122 QQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQ 201
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 202 AVHQEAALRRLQEEARDL---LEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISEIPNTLEDGTKEET 278
Cdd:COG1196  395 AAELAAQLEELEEAEEALlerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474

                 ....*...
gi 568951451 279 VALAPAAL 286
Cdd:COG1196  475 LEAALAEL 482
WD40 COG2319
WD40 repeat [General function prediction only];
458-618 2.20e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.46  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 458 FKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVLSYCNDVVC---GDHIIISGHNDQKIRFWDSRGPHCIQVIPV-QGRV 533
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAaspDGARLAAGAGDLTLLLLDAAAGALLATLLGhTAAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 534 TSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRAdgfkcSSDWTKAV-FSPDRSYALAGSSNGDLYIWDVNTGKLET 612
Cdd:COG2319   82 LSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTG-----HTGAVRSVaFSPDGKTLASGSADGTVRLWDLATGKLLR 156

                 ....*.
gi 568951451 613 SLQGPH 618
Cdd:COG2319  157 TLTGHS 162
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
120-260 2.86e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 120 KWQQEKKGLQLVcgEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLL 199
Cdd:COG1196  217 ELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568951451 200 QQAVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRT 260
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
120-265 1.87e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  120 KWQQEKKGLQLVCGEMAYQVVKK-----SAALDTLQSQLEERQDRLEALQACVVQLQEARAQQS-----------RQLEE 183
Cdd:COG4913   273 ELEYLRAALRLWFAQRRLELLEAeleelRAELARLEAELERLEARLDALREELDELEAQIRGNGgdrleqlereiERLER 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  184 RQAENAAQREAYETLLQQ----AVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQAL--VSQELKKAA 257
Cdd:COG4913   353 ELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELreLEAEIASLE 432

                  ....*...
gi 568951451  258 KRTVSISE 265
Cdd:COG4913   433 RRKSNIPA 440
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
141-285 3.43e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 3.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 141 KKSAALDTLQSQLEERQDRLE----ALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEA 216
Cdd:COG1196  400 AQLEELEEAEEALLERLERLEeeleELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568951451 217 RDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISEIpntLEDGTKEETVALAPAA 285
Cdd:COG1196  480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL---IGVEAAYEAALEAALA 545
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
359-392 3.96e-07

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 46.54  E-value: 3.96e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568951451   359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWN 392
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
147-562 4.15e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 53.17  E-value: 4.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 147 DTLQSQ-LEERQDRLEALQAcVVQLQEARAQQSRQLE------ERQAENAAQREAYETLLQQAVHQeaALRR---LQEEA 216
Cdd:PLN00181 261 ELLQSEfINEPRENLEEREA-AMELRDRIEEQELLLEflfliqQRKQEAADKLQDTISLLSSDIDQ--VVKRqlvLQQKG 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 217 RDLLEQLVQRK-----ARAAAERNLRNERRERANQALVS------------------------QELKKAAKRTVSISE-I 266
Cdd:PLN00181 338 SDVRSFLASRKrirqgAETLAAEEENDDNSSKLDDTLEStllessrlmrnlkklesvyfatryRQIKAAAAAEKPLARyY 417
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 267 PNTLEDGTKEETVALA-PAALPEFSESETCEK-WKRPFrsasatsltlsrcvdvVKGL---LDFKKRRghsvggapeqry 341
Cdd:PLN00181 418 SALSENGRSSEKSSMSnPAKPPDFYINDSRQGgWIDPF----------------LEGLckyLSFSKLR------------ 469
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 342 qsipvcVSAQIpsQAQDVLDAHlSEVNAVCFGPNSSLLATGGADRLIHLWN----VVGGRLEANQTLEGAGGS-ITSVDF 416
Cdd:PLN00181 470 ------VKADL--KQGDLLNSS-NLVCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICW 540
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 417 DPS-GSQVLAATYNQAAQLWKVGETQSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSyc 494
Cdd:PLN00181 541 NSYiKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA-- 618
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568951451 495 nDVVC------GDHIIISGHNDQKIRFWDSRGPHCIQVIPVQGRVTSLHLSY-DQLHLLSCSRDNTLKVIDLRIS 562
Cdd:PLN00181 619 -NICCvqfpseSGRSLAFGSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFvDSSTLVSSSTDNTLKLWDLSMS 692
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
39-253 7.82e-07

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: 52.37  E-value: 7.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451    39 AVWKRHIVRQLRHRDRTQKALflelvPAYNHLLEKAELLAKFSEKLKSEPKDAISTRHEDWRE---EVSGTGPDQVSSPA 115
Cdd:TIGR02168  228 ALLVLRLEELREELEELQEEL-----KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   116 SLRVKwQQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEA---RAQQSRQLEERQAENAAQR 192
Cdd:TIGR02168  303 QKQIL-RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEleeLEAELEELESRLEELEEQL 381
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568951451   193 EAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVSQEL 253
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
WD40 pfam00400
WD domain, G-beta repeat;
359-392 1.29e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.03  E-value: 1.29e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568951451  359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWN 392
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
144-252 1.88e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 144 AALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQL 223
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
                         90       100
                 ....*....|....*....|....*....
gi 568951451 224 VQRKARAAAERNLRNERRERANQALVSQE 252
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAEE 410
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
138-260 3.71e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARA---QQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQE 214
Cdd:COG1196  268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568951451 215 EARDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRT 260
Cdd:COG1196  348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
149-260 6.69e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 6.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 149 LQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRKA 228
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568951451 229 RAAAERNLRNERRERANQALVSQELKKAAKRT 260
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEE 425
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
143-232 1.27e-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: 47.84  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 143 SAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQ 222
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                         90
                 ....*....|
gi 568951451 223 LVQRKARAAA 232
Cdd:COG4942   99 LEAQKEELAE 108
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
138-300 1.68e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEAR 217
Cdd:COG4372   95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 218 DLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISEIPNTLEDGTKEETVALAPAALPEFSESETCEK 297
Cdd:COG4372  175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254

                 ...
gi 568951451 298 WKR 300
Cdd:COG4372  255 VIL 257
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
42-272 1.94e-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: 47.74  E-value: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451    42 KRHIVRQLRHRDRTQKALFLELVPAYNHLLEKAELLAKFSEKLKSepkdaISTRHEDWREEVsgtgpdqvsspASLRVKW 121
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE-----LKEELESLEAEL-----------EELEAEL 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   122 QQEKkglqlvcgemayqvvkksAALDTLQSQLEERQDRLEALQAcvvQLQEARAQQSR------QLEERQAENAAQREAY 195
Cdd:TIGR02168  368 EELE------------------SRLEELEEQLETLRSKVAQLEL---QIASLNNEIERlearleRLEDRRERLQQEIEEL 426
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568951451   196 ETLLQQAvhQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVS--QELKKAAKRTVSISEIPNTLED 272
Cdd:TIGR02168  427 LKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAaeRELAQLQARLDSLERLQENLEG 503
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
144-246 1.99e-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: 47.07  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 144 AALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQL 223
Cdd:COG4942  150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
                         90       100
                 ....*....|....*....|...
gi 568951451 224 VQRKARAAAERNLRNERRERANQ 246
Cdd:COG4942  230 ARLEAEAAAAAERTPAAGFAALK 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
47-230 2.24e-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: 47.74  E-value: 2.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451    47 RQLRHRDRTQKALFLELVPAYNHLLEKAELLAKFSEKLKS--EPKDAISTRHEDWREEVSgtgpdqvsspaSLRVKWQQE 124
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEleAQIEQLKEELKALREALD-----------ELRAELTLL 815
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   125 KKG---LQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEE-------RQAENAAQREA 194
Cdd:TIGR02168  816 NEEaanLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALLRSE 895
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 568951451   195 YETL---LQQAVHQEAALRRLQEEARDLLEQLVQRKARA 230
Cdd:TIGR02168  896 LEELseeLRELESKRSELRRELEELREKLAQLELRLEGL 934
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
139-309 2.41e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.13  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 139 VVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQavhQEAALRRLQEEARD 218
Cdd:COG3883  117 FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE---QEALLAQLSAEEAA 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 219 LLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISEIPNTLEDGTKEETVALAPAALPEFSESETCEKW 298
Cdd:COG3883  194 AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
                        170
                 ....*....|.
gi 568951451 299 KRPFRSASATS 309
Cdd:COG3883  274 AGAAAASAAGG 284
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
146-279 5.48e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 5.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 146 LDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQ 225
Cdd:COG4372   82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568951451 226 RKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISEIPNTLEDGTKEETV 279
Cdd:COG4372  162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
120-272 7.67e-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: 7.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   120 KWQQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLL 199
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568951451   200 QQAVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQAlvSQELKKAAKRTVSISEIPNTLED 272
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL--ESELEALLNERASLEEALALLRS 894
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
145-264 7.87e-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: 45.14  E-value: 7.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 145 ALDTLQSQLEERQDRLEALQacvvqlqearaQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLV 224
Cdd:COG4942  137 RLQYLKYLAPARREQAEELR-----------ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE 205
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568951451 225 QRKARAAAERNLRNERRERANQAL--VSQELKKAAKRTVSIS 264
Cdd:COG4942  206 KELAELAAELAELQQEAEELEALIarLEAEAAAAAERTPAAG 247
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
138-231 8.48e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 8.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEER-QAENAAQREAYETLLQQAvHQEAALRRLQEEA 216
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEERFAAA-LGDAVERELRENL 771
                          90
                  ....*....|....*
gi 568951451  217 RDLLEQLVQRKARAA 231
Cdd:COG4913   772 EERIDALRARLNRAE 786
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
120-232 9.61e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 9.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 120 KWQQEKKGLqlvcgEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQsRQLEERQAEnaAQREAYETLL 199
Cdd:COG4717  113 ELREELEKL-----EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEEL-EELEAELAE--LQEELEELLE 184
                         90       100       110
                 ....*....|....*....|....*....|...
gi 568951451 200 QQAVHQEAALRRLQEEARDLLEQLVQRKARAAA 232
Cdd:COG4717  185 QLSLATEEELQDLAEELEELQQRLAELEEELEE 217
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
122-232 1.05e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 45.71  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  122 QQEKKGLQLVC---GEmayqvVKKSAALDTLQSQLEE------RQDRLEALQAcvvQLQEARaqqsrQLEERQAENAAQR 192
Cdd:COG3096   472 RQFEKAYELVCkiaGE-----VERSQAWQTARELLRRyrsqqaLAQRLQQLRA---QLAELE-----QRLRQQQNAERLL 538
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568951451  193 EAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRKARAAA 232
Cdd:COG3096   539 EEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVE 578
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
146-232 1.15e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 146 LDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQ----REAYETLLQQAVHQEAALRRLQEEARDLLE 221
Cdd:COG4717  148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELEE 227
                         90
                 ....*....|.
gi 568951451 222 QLVQRKARAAA 232
Cdd:COG4717  228 ELEQLENELEA 238
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
146-280 1.15e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 146 LDTLQSQLEERQDRLEALQAcvvQLQEARAQQSR----------QLEERQAENAAQREAYETLLQQAVHQEAALRRLQEE 215
Cdd:COG4372   47 LEQLREELEQAREELEQLEE---ELEQARSELEQleeeleelneQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568951451 216 ARDLLEQLVQRKARAAAERNLRNERRERANQAlvSQELKKAAKRTVSISEIPNTLEDGTKEETVA 280
Cdd:COG4372  124 RQDLEQQRKQLEAQIAELQSEIAEREEELKEL--EEQLESLQEELAALEQELQALSEAEAEQALD 186
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
445-478 1.20e-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: 39.60  E-value: 1.20e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568951451   445 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 478
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
445-478 1.20e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 1.20e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568951451  445 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 478
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
138-257 1.37e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEER---QAENAAQREAYETLL-----QQAVHQEAAL 209
Cdd:COG3883   45 ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraLYRSGGSVSYLDVLLgsesfSDFLDRLSAL 124
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568951451 210 RRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAA 257
Cdd:COG3883  125 SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
141-227 1.56e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 42.18  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  141 KKSAALDTLQSQLEERQDRLEALQAcvvQLQEARAQQSRQLEERQAENAAQREAYETLLQQAvhQEAALRRLQEEARDLL 220
Cdd:pfam03938  30 KRQAELEAKQKELQKLYEELQKDGA---LLEEEREEKEQELQKKEQELQQLQQKAQQELQKK--QQELLQPIQDKINKAI 104

                  ....*..
gi 568951451  221 EQLVQRK 227
Cdd:pfam03938 105 KEVAKEK 111
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
146-228 1.57e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  146 LDTLQSQLEERQDRLEALQACVVQLQEARAQQsRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQ 225
Cdd:COG4913   663 VASAEREIAELEAELERLDASSDDLAALEEQL-EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741

                  ...
gi 568951451  226 RKA 228
Cdd:COG4913   742 LAR 744
PRK11281 PRK11281
mechanosensitive channel MscK;
93-229 3.21e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 43.75  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   93 STRHEDWREEVSGTGPDQVSSPASLRVKWQQEkkgLQLVCGEMAYQvvKKSAA-----LDTLQSQLEERQDRLEALQACV 167
Cdd:PRK11281  169 SQRLQQIRNLLKGGKVGGKALRPSQRVLLQAE---QALLNAQNDLQ--RKSLEgntqlQDLLQKQRDYLTARIQRLEHQL 243
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568951451  168 VQLQEARAQQSRQLEERQAENA-AQREAYETLLQQAVHQEAAL-RRLQE---EARDLLEQLVQRKAR 229
Cdd:PRK11281  244 QLLQEAINSKRLTLSEKTVQEAqSQDEAARIQANPLVAQELEInLQLSQrllKATEKLNTLTQQNLR 310
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
143-226 4.80e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  143 SAALDTLQSQLEERQDRLEALQACVVQLQEARA---QQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDL 219
Cdd:COG4913   684 SDDLAALEEQLEELEAELEELEEELDELKGEIGrleKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763

                  ....*..
gi 568951451  220 LEQLVQR 226
Cdd:COG4913   764 ERELREN 770
TrbJ_Ti TIGR02780
P-type conjugative transfer protein TrbJ; The TrbJ protein is found in the trb locus of ...
133-220 6.10e-04

P-type conjugative transfer protein TrbJ; The TrbJ protein is found in the trb locus of Agrobacterium Ti plasmids where it is involved in the type IV secretion system for plasmid conjugative transfer. TrbJ is a homolog of the F-type TraE protein (which is believed to be an inner membrane pore-forming protein, TIGR02761) as well as the vir system VirB5 protein.


Pssm-ID: 131827 [Multi-domain]  Cd Length: 246  Bit Score: 42.04  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  133 GEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVvqlqEARAQQSRQLEERQAENAAQREAYETLLQQavhQEAALRRL 212
Cdd:TIGR02780 152 GLQTGNLAEDNATLDQLQSLSQSASGQLQALQAGN----QLAAQQSKQLQKLRALLAAQIQAQSTYMAS---EQAREDVT 224

                  ....*...
gi 568951451  213 QEEARDLL 220
Cdd:TIGR02780 225 QQQRRQFL 232
PTZ00421 PTZ00421
coronin; Provisional
370-478 6.36e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 42.57  E-value: 6.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 370 VCFGP-NSSLLATGGADRLIHLWNVVGGRLEANQT-----LEGAGGSITSVDFDPSGSQVLA-ATYNQAAQLWKVGETQS 442
Cdd:PTZ00421  81 VAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhLQGHTKKVGIVSFHPSAMNVLAsAGADMVVNVWDVERGKA 160
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568951451 443 KETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 478
Cdd:PTZ00421 161 VEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
143-228 8.99e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 8.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 143 SAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQRE-------AYETLLQQAVHQEAALRRLQEE 215
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEeleelneQLQAAQAELAQAQEELESLQEE 109
                         90
                 ....*....|...
gi 568951451 216 ARDLLEQLVQRKA 228
Cdd:COG4372  110 AEELQEELEELQK 122
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
110-291 9.50e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 9.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  110 QVSSPASLRVKWQQEKKGLQLVCGEMAYqvvkksAALDTLQSQLEERQDRLEALQAcvvQLQEARAQQsRQLEERQAENA 189
Cdd:COG4913   582 QVKGNGTRHEKDDRRRIRSRYVLGFDNR------AKLAALEAELAELEEELAEAEE---RLEALEAEL-DALQERREALQ 651
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  190 AQREAYETLLQQAVHQEaALRRLQEEARDL------LEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTvSI 263
Cdd:COG4913   652 RLAEYSWDEIDVASAER-EIAELEAELERLdassddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-EL 729
                         170       180
                  ....*....|....*....|....*...
gi 568951451  264 SEIPNTLEDGTKEETVALAPAALPEFSE 291
Cdd:COG4913   730 DELQDRLEAAEDLARLELRALLEERFAA 757
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
138-226 1.09e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 138 QVVKKSAALDTLQSQLEERQDRLealqacvvqLQEARAQQsRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEE-- 215
Cdd:COG3206  292 DVIALRAQIAALRAQLQQEAQRI---------LASLEAEL-EALQAREASLQAQLAQLEARLAELPELEAELRRLEREve 361
                         90
                 ....*....|..
gi 568951451 216 -ARDLLEQLVQR 226
Cdd:COG3206  362 vARELYESLLQR 373
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
68-227 1.25e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451    68 NHLLEKAE----LLAKFSEKLKSEPKDAISTRHEDWREEVSgtgpdqvsspASLRVK-WQQEKKGL--QLVCGEMAYQVV 140
Cdd:pfam01576  446 SSLLNEAEgkniKLSKDVSSLESQLQDTQELLQEETRQKLN----------LSTRLRqLEDERNSLqeQLEEEEEAKRNV 515
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   141 KKSaaLDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLlqqavhqEAALRRLQEEARDLL 220
Cdd:pfam01576  516 ERQ--LSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-------EKTKNRLQQELDDLL 586

                   ....*..
gi 568951451   221 EQLVQRK 227
Cdd:pfam01576  587 VDLDHQR 593
dsDNA_bind pfam01984
Double-stranded DNA-binding domain; This domain is believed to bind double-stranded DNA of 20 ...
156-225 1.68e-03

Double-stranded DNA-binding domain; This domain is believed to bind double-stranded DNA of 20 bases length.


Pssm-ID: 460404  Cd Length: 106  Bit Score: 38.25  E-value: 1.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568951451  156 RQDRLEALQacvvQLQEARAQQSRQLEERQAENAAQREAyetLLQQAVHQEAA--LRRLQ----EEARDLLEQLVQ 225
Cdd:pfam01984   2 RRARLAELQ----KQQGGGGGSGGAQEQAQEEQEEQKQA---ILRQILTPEARerLSRIRlvkpERAEAVENQLIQ 70
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
171-231 1.85e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; RING finger protein 168 (RNF168) is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. Together with RNF8, RNF168 functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. This model corresponds to the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) domain of RNF168, which comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409018 [Multi-domain]  Cd Length: 73  Bit Score: 37.15  E-value: 1.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568951451 171 QEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRKARAA 231
Cdd:cd22265    9 QEYEEEISKLEAERRALEEEENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKEDEELA 69
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
138-245 1.98e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 138 QVVKKSAALDTLQSQLEERQDRLEALQAcvvQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEAR 217
Cdd:COG3883  144 ELEAKKAELEAKLAELEALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
                         90       100
                 ....*....|....*....|....*...
gi 568951451 218 DLLEQLVQRKARAAAERNLRNERRERAN 245
Cdd:COG3883  221 AAAAAAAAAAAAAAAAAAAAAAAASAAG 248
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
146-232 2.06e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.81  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 146 LDTLQSQLEERQDRleALQAcvvqLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQ 225
Cdd:COG1842   60 LEELEAEAEKWEEK--ARLA----LEKGREDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKA 133

                 ....*..
gi 568951451 226 RKARAAA 232
Cdd:COG1842  134 KKDTLKA 140
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
138-218 2.06e-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: 40.90  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 138 QVVKKSAALDTLQSQLEERQDRLEALQAcvvQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEAR 217
Cdd:COG4942  161 ELAALRAELEAERAELEALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237

                 .
gi 568951451 218 D 218
Cdd:COG4942  238 A 238
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
138-259 2.26e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.60  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQ-QSRQLEERQAENAAQREAYEtllQQAVHQEAALRRLQEEA 216
Cdd:TIGR02794  72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAaKQAEEKQKQAEEAKAKQAAE---AKAKAEAEAERKAKEEA 148
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568951451  217 RDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKR 259
Cdd:TIGR02794 149 AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA 191
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
133-259 2.31e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 133 GEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRL 212
Cdd:COG1196  651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568951451 213 QEEARDLLEQLVQrkARAAAERNLRNERRERANQALVSQELKKAAKR 259
Cdd:COG1196  731 EAEREELLEELLE--EEELLEEEALEELPEPPDLEELERELERLERE 775
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
122-259 2.32e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 122 QQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEA--LQACVVQLQEARAQQSRQLEERQAENAAQREAYETLL 199
Cdd:PRK09510  68 QQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKerLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568951451 200 ---QQAVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERAN---QALVSQELKKAAKR 259
Cdd:PRK09510 148 kaeAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAaeaKKKAEAEAKKKAAA 213
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
138-232 2.43e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.63  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQleeRQAENAAQREAYEtlLQQAvhqeAALRRLQEEAR 217
Cdd:COG2268  238 RIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQ---RQLEIAEREREIE--LQEK----EAEREEAELEA 308
                         90
                 ....*....|....*
gi 568951451 218 DLLEQLVQRKARAAA 232
Cdd:COG2268  309 DVRKPAEAEKQAAEA 323
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
143-261 2.67e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  143 SAALDTLQSQLEERQDRLEALQAC---------VVQLQEARAQQSRQLEERQAENA------AQREAYETLLQQAVHQEA 207
Cdd:COG4913   630 EERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAELERLDASSDdlaaleEQLEELEAELEELEEELD 709
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568951451  208 ALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTV 261
Cdd:COG4913   710 ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
79-232 2.74e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   79 KFSEKLKSEPKDAIS-TRHEDWREEVSGTGPDQvsspaSLRVKWQQEKKGLQLVCGEMAYQ----VVKKSAALDTLQSQL 153
Cdd:pfam15709 290 QVSIDGRSSPTQTFVvTGNMESEEERSEEDPSK-----ALLEKREQEKASRDRLRAERAEMrrleVERKRREQEEQRRLQ 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  154 EERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYET---LLQQAVHQEAalRRLQEEARDLLEQLVQRKARA 230
Cdd:pfam15709 365 QEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERkqrLQLQAAQERA--RQQQEEFRRKLQELQRKKQQE 442

                  ..
gi 568951451  231 AA 232
Cdd:pfam15709 443 EA 444
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
144-258 2.90e-03

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: 40.81  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   144 AALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQ---EEARDLL 220
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErqlEELEAQL 325
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 568951451   221 EQLVQRK--ARAAAERNLRNERRERANQALVSQELKKAAK 258
Cdd:TIGR02168  326 EELESKLdeLAEELAELEEKLEELKEELESLEAELEELEA 365
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
138-231 3.17e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 40.10  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  138 QVVKKSAALDTL-QSQLEERQDRLEAlqacvvQLQEARAQQSR------QLEERQAENAAQREAYETLLQQAVHQEAALR 210
Cdd:pfam00529  40 DRVKAGDVLFQLdPTDYQAALDSAEA------QLAKAQAQVARlqaeldRLQALESELAISRQDYDGATAQLRAAQAAVK 113
                          90       100
                  ....*....|....*....|.
gi 568951451  211 RLQEEARDLLEQLVQRKARAA 231
Cdd:pfam00529 114 AAQAQLAQAQIDLARRRVLAP 134
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
138-247 3.70e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 138 QVVKKSAALDTLQSQLEERQDRLEALQAcvvQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEAR 217
Cdd:COG3883  137 ELKADKAELEAKKAELEAKLAELEALKA---ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
                         90       100       110
                 ....*....|....*....|....*....|
gi 568951451 218 DLLEQLVQRKARAAAERNLRNERRERANQA 247
Cdd:COG3883  214 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
122-277 4.17e-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: 39.75  E-value: 4.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 122 QQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEER----------------- 184
Cdd:COG4942   47 KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqpplalll 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 185 QAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKA---AKRTV 261
Cdd:COG4942  127 SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQkllARLEK 206
                        170
                 ....*....|....*.
gi 568951451 262 SISEIPNTLEDGTKEE 277
Cdd:COG4942  207 ELAELAAELAELQQEA 222
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
118-215 4.22e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.32  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  118 RVKWQQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYET 197
Cdd:COG3096   527 RLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLA 606
                          90
                  ....*....|....*...
gi 568951451  198 LlqqavhqEAALRRLQEE 215
Cdd:COG3096   607 A-------QDALERLREQ 617
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
522-558 4.31e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.37  E-value: 4.31e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568951451   522 HCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVID 558
Cdd:smart00320   3 ELLKTLKGhTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
66-226 5.51e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451   66 AYNHLLEKAELLAKFSEkLKSEPKDAISTRHE--DWREEVSG--TGPDQVSSPASLRVKWQQEKKGLQLVCGEMAYQVVK 141
Cdd:COG4913   639 ELDALQERREALQRLAE-YSWDEIDVASAEREiaELEAELERldASSDDLAALEEQLEELEAELEELEEELDELKGEIGR 717
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  142 KSAALDTLQSQLEERQDRLEALQacvvqlQEARAQQSRQLEERQAEnAAQREAYETLLQQAVHQEAALRRLQEEARDLLE 221
Cdd:COG4913   718 LEKELEQAEEELDELQDRLEAAE------DLARLELRALLEERFAA-ALGDAVERELRENLEERIDALRARLNRAEEELE 790

                  ....*
gi 568951451  222 QLVQR 226
Cdd:COG4913   791 RAMRA 795
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
144-232 5.96e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 144 AALDTLQSQLEERQ----DRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALR-RLQEEARD 218
Cdd:COG1579   99 ESLKRRISDLEDEIlelmERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAaKIPPELLA 178
                         90
                 ....*....|....
gi 568951451 219 LLEQLVQRKARAAA 232
Cdd:COG1579  179 LYERIRKRKNGLAV 192
mukB PRK04863
chromosome partition protein MukB;
144-214 5.96e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 5.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568951451  144 AALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLlqqavhqEAALRRLQE 214
Cdd:PRK04863  554 DELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAA-------QDALARLRE 617
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
143-266 5.98e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 5.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 143 SAALDTLQSQLEERQDRLEALQACVVQLQEARAQ---------QSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQ 213
Cdd:COG3206  218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALR 297
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568951451 214 EEARDLLEQLVQRKARAAAERNLRNERRERANQALvSQELKKAAKRTVSISEI 266
Cdd:COG3206  298 AQIAALRAQLQQEAQRILASLEAELEALQAREASL-QAQLAQLEARLAELPEL 349
WD40 pfam00400
WD domain, G-beta repeat;
530-558 6.81e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 34.63  E-value: 6.81e-03
                          10        20
                  ....*....|....*....|....*....
gi 568951451  530 QGRVTSLHLSYDQLHLLSCSRDNTLKVID 558
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
144-232 7.00e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 7.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 144 AALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQL----------EERQAENAAQREaYETLLQQAVHQEAALRRLQ 213
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIeevearikkyEEQLGNVRNNKE-YEALQKEIESLKRRISDLE 109
                         90
                 ....*....|....*....
gi 568951451 214 EEARDLLEQLVQRKARAAA 232
Cdd:COG1579  110 DEILELMERIEELEEELAE 128
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
138-228 7.09e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.55  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQ-REAYETLLQQAVHQEAALRRLQEEA 216
Cdd:PRK11448  157 QLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETsQERKQKRKEITDQAAKRLELSEEET 236
                          90
                  ....*....|...
gi 568951451  217 RDLL-EQLvqRKA 228
Cdd:PRK11448  237 RILIdQQL--RKA 247
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
141-280 7.16e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 7.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 141 KKSAALDTLQSQLEERQDRLEALQACVVQLQE-----ARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEE 215
Cdd:COG4717   85 EKEEEYAELQEELEELEEELEELEAELEELREeleklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 216 ARDLLEQLVQRKARAAAERNLRNERRER-------------ANQALVSQELKKA----AKRTVSISEIPNTLEDGTKEET 278
Cdd:COG4717  165 LEELEAELAELQEELEELLEQLSLATEEelqdlaeeleelqQRLAELEEELEEAqeelEELEEELEQLENELEAAALEER 244

                 ..
gi 568951451 279 VA 280
Cdd:COG4717  245 LK 246
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
141-228 7.59e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.75  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  141 KKSAALDTLQSQLEERQDRLEALQAcvVQLQEARAQQSRQLEERQAENAAQ--REAYETLLQQAVHQEAALRRLQEEARD 218
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELRA--KLYQEEQERKERQKEREEAEKKARqrQELQQAREEQIELKERRLAEEAEREEE 261
                          90
                  ....*....|
gi 568951451  219 LLEQLVQRKA 228
Cdd:pfam13868 262 EFERMLRKQA 271
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
144-232 8.44e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 8.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451  144 AALDTLQSQ---LEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLL 220
Cdd:COG4913   225 EAADALVEHfddLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
                          90
                  ....*....|..
gi 568951451  221 EQLVQRKARAAA 232
Cdd:COG4913   305 ARLEAELERLEA 316
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
144-265 8.95e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 8.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 144 AALDTLQSQLEERQDRLEALQACVVQLQEARAQQsRQLEERQAENAAQREAYETLLQqAVHQEAALRRLQEEARDLLEQL 223
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEELEELEEEL-EELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPERL 148
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568951451 224 VQRKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISE 265
Cdd:COG4717  149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
PRK12704 PRK12704
phosphodiesterase; Provisional
138-232 9.78e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 9.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951451 138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEaraqqsrQLEERQAEnaaqreaYETLLQQavhQEAALRRL----Q 213
Cdd:PRK12704  90 RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQ-------ELEKKEEE-------LEELIEE---QLQELERIsgltA 152
                         90
                 ....*....|....*....
gi 568951451 214 EEARDLLEQLVQRKARAAA 232
Cdd:PRK12704 153 EEAKEILLEKVEEEARHEA 171
FliT pfam05400
Flagellar protein FliT; This family contains several bacterial flagellar FliT proteins. The ...
167-231 9.83e-03

Flagellar protein FliT; This family contains several bacterial flagellar FliT proteins. The flagellar proteins FlgN and FliT have been proposed to act as substrate specific export chaperones, facilitating incorporation of the enterobacterial hook-associated axial proteins (HAPs) FlgK/FlgL and FliD into the growing flagellum. In Salmonella typhimurium flgN and fliT mutants, the export of target HAPs is reduced, concomitant with loss of unincorporated flagellin into the surrounding medium.


Pssm-ID: 461640  Cd Length: 86  Bit Score: 35.77  E-value: 9.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568951451  167 VVQLQEARAQQSRQLEERQAE---NAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLV-----QRKARAA 231
Cdd:pfam05400  13 LVALEAERQQLVERLRELEPEaplSDAERAEKRELLRRILENDAEIRALLQPRLDELQKLLgqarrQRKANNA 85
 
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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