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Conserved domains on  [gi|755523167|ref|XP_011240218|]
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protein Atg16l2 isoform X6 [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
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 59-231 7.87e-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: 7.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167   59 LFLELVPAYNHLLEKAELLAKFSEKLKSEPKDAISTRHEDwREEVSGTGPDQVSSPASLRVKWQQEKKGLQLVCGEMAYQ 138
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSS-KLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  139 VVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARD 218
Cdd:pfam08614  80 LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRE 159

                         170
                  ....*....|...
gi 755523167  219 LLEQLVQRKARAA 231
Cdd:pfam08614 160 LVERWMKRKGQEA 172
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 359-560 3.82e-41

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: 150.95  E-value: 3.82e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 438
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 439 ETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 515
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755523167 516 WDSRGPHCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLR 560
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS 207
 
Name Accession Description Interval E-value
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 59-231 7.87e-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: 7.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167   59 LFLELVPAYNHLLEKAELLAKFSEKLKSEPKDAISTRHEDwREEVSGTGPDQVSSPASLRVKWQQEKKGLQLVCGEMAYQ 138
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSS-KLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  139 VVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARD 218
Cdd:pfam08614  80 LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRE 159

                         170
                  ....*....|...
gi 755523167  219 LLEQLVQRKARAA 231
Cdd:pfam08614 160 LVERWMKRKGQEA 172
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 359-560 3.82e-41

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: 150.95  E-value: 3.82e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 438
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 439 ETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 515
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755523167 516 WDSRGPHCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLR 560
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS 207
WD40 COG2319
WD40 repeat [General function prediction only];
359-560 1.44e-37

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 143.90  E-value: 1.44e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 438
Cdd:COG2319  199 TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLL--RTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 439 ETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVLSYCNDVVC---GDHIIISGHNDQKIRF 515
Cdd:COG2319  277 TGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAfspDGKTLASGSDDGTVRL 356

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755523167 516 WDSRGPHCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLR 560
Cdd:COG2319  357 WDLATGELLRTLTGhTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 148-231 3.11e-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: 3.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 148 TLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRK 227
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80


                 ....
gi 755523167 228 ARAA 231
Cdd:cd22887   81 QQEA 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 122-286 1.82e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 122 QQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQ 201
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 202 AVHQEAALRRLQEEARDL---LEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISEIPNTLEDGTKEET 278
Cdd:COG1196  395 AAELAAQLEELEEAEEALlerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474


                 ....*...
gi 755523167 279 VALAPAAL 286
Cdd:COG1196  475 LEAALAEL 482
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 147-562 2.60e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 53.94  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 147 DTLQSQ-LEERQDRLEALQAcVVQLQEARAQQSRQLE------ERQAENAAQREAYETLLQQAVHQeaALRR---LQEEA 216
Cdd:PLN00181 261 ELLQSEfINEPRENLEEREA-AMELRDRIEEQELLLEflfliqQRKQEAADKLQDTISLLSSDIDQ--VVKRqlvLQQKG 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 217 RDLLEQLVQRK-----ARAAAERNLRNERRERANQALVS------------------------QELKKAAKRTVSISE-I 266
Cdd:PLN00181 338 SDVRSFLASRKrirqgAETLAAEEENDDNSSKLDDTLEStllessrlmrnlkklesvyfatryRQIKAAAAAEKPLARyY 417

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 267 PNTLEDGTKEETVALA-PAALPEFSESETCEK-WKRPFrsasatsltlsrcvdvVKGL---LDFKKRRghsvggapeqry 341
Cdd:PLN00181 418 SALSENGRSSEKSSMSnPAKPPDFYINDSRQGgWIDPF----------------LEGLckyLSFSKLR------------ 469

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 342 qsipvcVSAQIpsQAQDVLDAHlSEVNAVCFGPNSSLLATGGADRLIHLWN----VVGGRLEANQTLEGAGGS-ITSVDF 416
Cdd:PLN00181 470 ------VKADL--KQGDLLNSS-NLVCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICW 540

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 417 DPS-GSQVLAATYNQAAQLWKVGETQSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSyc 494
Cdd:PLN00181 541 NSYiKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA-- 618

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755523167 495 nDVVC------GDHIIISGHNDQKIRFWDSRGPHCIQVIPVQGRVTSLHLSY-DQLHLLSCSRDNTLKVIDLRIS 562
Cdd:PLN00181 619 -NICCvqfpseSGRSLAFGSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFvDSSTLVSSSTDNTLKLWDLSMS 692
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 359-392 3.56e-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: 46.92  E-value: 3.56e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 755523167   359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWN 392
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 39-253 7.53e-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: 7.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167    39 AVWKRHIVRQLRHRDRTQKALflelvPAYNHLLEKAELLAKFSEKLKSEPKDAISTRHEDWRE---EVSGTGPDQVSSPA 115
Cdd:TIGR02168  228 ALLVLRLEELREELEELQEEL-----KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLEQ 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167   116 SLRVKwQQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEA---RAQQSRQLEERQAENAAQR 192
Cdd:TIGR02168  303 QKQIL-RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEleeLEAELEELESRLEELEEQL 381

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755523167   193 EAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVSQEL 253
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
WD40 pfam00400
WD domain, G-beta repeat;
359-392 1.09e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 1.09e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 755523167  359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWN 392
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 370-478 6.08e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 42.57  E-value: 6.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 370 VCFGP-NSSLLATGGADRLIHLWNVVGGRLEANQT-----LEGAGGSITSVDFDPSGSQVLA-ATYNQAAQLWKVGETQS 442
Cdd:PTZ00421  81 VAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhLQGHTKKVGIVSFHPSAMNVLAsAGADMVVNVWDVERGKA 160

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755523167 443 KETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 478
Cdd:PTZ00421 161 VEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
 
Name Accession Description Interval E-value
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 59-231 7.87e-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: 7.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167   59 LFLELVPAYNHLLEKAELLAKFSEKLKSEPKDAISTRHEDwREEVSGTGPDQVSSPASLRVKWQQEKKGLQLVCGEMAYQ 138
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSS-KLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  139 VVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARD 218
Cdd:pfam08614  80 LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRE 159

                         170
                  ....*....|...
gi 755523167  219 LLEQLVQRKARAA 231
Cdd:pfam08614 160 LVERWMKRKGQEA 172
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 359-560 3.82e-41

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: 150.95  E-value: 3.82e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 438
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 439 ETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 515
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755523167 516 WDSRGPHCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLR 560
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS 207
WD40 COG2319
WD40 repeat [General function prediction only];
359-560 1.44e-37

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 143.90  E-value: 1.44e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 438
Cdd:COG2319  199 TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLL--RTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 439 ETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVLSYCNDVVC---GDHIIISGHNDQKIRF 515
Cdd:COG2319  277 TGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAfspDGKTLASGSDDGTVRL 356

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755523167 516 WDSRGPHCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLR 560
Cdd:COG2319  357 WDLATGELLRTLTGhTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
354-570 1.31e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 141.20  E-value: 1.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 354 SQAQDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQ 433
Cdd:COG2319  110 GLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVR 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 434 LWKVGETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcgDHIIIS 506
Cdd:COG2319  188 LWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTltghsgsVRSVAFSPD----GRLLAS 263

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755523167 507 GHNDQKIRFWDSRGPHCIQVIPVQ-GRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRA 570
Cdd:COG2319  264 GSADGTVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG 328
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 359-556 1.34e-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: 135.54  E-value: 1.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 438
Cdd:cd00200   88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL--TTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLR 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 439 ETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLgraYCSRTINVLSYCNDVVCG------DHIIISGHNDQK 512
Cdd:cd00200  166 TGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL---STGKCLGTLRGHENGVNSvafspdGYLLASGSEDGT 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 755523167 513 IRFWDSRGPHCIQVIP-VQGRVTSLHLSYDQLHLLSCSRDNTLKV 556
Cdd:cd00200  243 IRVWDLRTGECVQTLSgHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
359-570 3.09e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 134.65  E-value: 3.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 438
Cdd:COG2319  157 TLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLL--RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 439 ETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTinvLSYCNDVVCG------DHIIISGHNDQK 512
Cdd:COG2319  235 TGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT---LTGHSGGVNSvafspdGKLLASGSDDGT 311

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755523167 513 IRFWDSRGPHCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRA 570
Cdd:COG2319  312 VRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTG 370
WD40 COG2319
WD40 repeat [General function prediction only];
348-572 1.48e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 129.65  E-value: 1.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 348 VSAQIPSQAQDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEAnqTLEGAGGSITSVDFDPSGSQVLAAT 427
Cdd:COG2319   62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLR--TLTGHTGAVRSVAFSPDGKTLASGS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 428 YNQAAQLWKVGETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcg 500
Cdd:COG2319  140 ADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTltghtgaVRSVAFSPD---- 215

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755523167 501 DHIIISGHNDQKIRFWDSRGPHCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRADG 572
Cdd:COG2319  216 GKLLASGSADGTVRLWDLATGKLLRTLTGhSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 402-600 1.22e-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: 110.12  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 402 QTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVGETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGR 481
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 482 AYCSRTINvlSYCNDVVCGD-----HIIISGHNDQKIRFWDSRGPHCIQVIP-VQGRVTSLHLSYDQLHLLSCSRDNTLK 555
Cdd:cd00200   83 GECVRTLT--GHTSYVSSVAfspdgRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAFSPDGTFVASSSQDGTIK 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 556 VIDLRISNIRQVFRA------------DGFK---CSSDWTKAVFRLFKRRPVHLGCEHRE 600
Cdd:cd00200  161 LWDLRTGKCVATLTGhtgevnsvafspDGEKllsSSSDGTIKLWDLSTGKCLGTLRGHEN 220
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 355-517 2.84e-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: 108.96  E-value: 2.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 355 QAQDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLeaNQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQL 434
Cdd:cd00200  126 KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC--VATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKL 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 435 WKVGETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDVvcgdHIIISG 507
Cdd:cd00200  204 WDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTlsghtnsVTSLAWSPDG----KRLASG 279

                        170
                 ....*....|
gi 755523167 508 HNDQKIRFWD 517
Cdd:cd00200  280 SADGTIRIWD 289
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 148-231 3.11e-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: 3.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 148 TLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRK 227
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80


                 ....
gi 755523167 228 ARAA 231
Cdd:cd22887   81 QQEA 84
WD40 COG2319
WD40 repeat [General function prediction only];
372-570 4.40e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 80.73  E-value: 4.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 372 FGPNSSLLATGGADRLIHLWNVVGGRLEAnqTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVGETQSKETLSGHKD 451
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLL--LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 452 KVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVL-SYCNDVVC--GDHIIISGHNDQKIRFWDSRGPHCIQVIP 528
Cdd:COG2319   80 AVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHtGAVRSVAFspDGKTLASGSADGTVRLWDLATGKLLRTLT 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 755523167 529 V-QGRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRA 570
Cdd:COG2319  160 GhSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG 202
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 122-286 1.82e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 122 QQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQ 201
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 202 AVHQEAALRRLQEEARDL---LEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISEIPNTLEDGTKEET 278
Cdd:COG1196  395 AAELAAQLEELEEAEEALlerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474


                 ....*...
gi 755523167 279 VALAPAAL 286
Cdd:COG1196  475 LEAALAEL 482
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 120-260 3.16e-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: 3.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 120 KWQQEKKGLQLVcgEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLL 199
Cdd:COG1196  217 ELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755523167 200 QQAVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRT 260
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
120-265 2.06e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  120 KWQQEKKGLQLVCGEMAYQVVKK-----SAALDTLQSQLEERQDRLEALQACVVQLQEARAQQS-----------RQLEE 183
Cdd:COG4913   273 ELEYLRAALRLWFAQRRLELLEAeleelRAELARLEAELERLEARLDALREELDELEAQIRGNGgdrleqlereiERLER 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  184 RQAENAAQREAYETLLQQ----AVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQAL--VSQELKKAA 257
Cdd:COG4913   353 ELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELreLEAEIASLE 432


                  ....*...
gi 755523167  258 KRTVSISE 265
Cdd:COG4913   433 RRKSNIPA 440
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 147-562 2.60e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 53.94  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 147 DTLQSQ-LEERQDRLEALQAcVVQLQEARAQQSRQLE------ERQAENAAQREAYETLLQQAVHQeaALRR---LQEEA 216
Cdd:PLN00181 261 ELLQSEfINEPRENLEEREA-AMELRDRIEEQELLLEflfliqQRKQEAADKLQDTISLLSSDIDQ--VVKRqlvLQQKG 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 217 RDLLEQLVQRK-----ARAAAERNLRNERRERANQALVS------------------------QELKKAAKRTVSISE-I 266
Cdd:PLN00181 338 SDVRSFLASRKrirqgAETLAAEEENDDNSSKLDDTLEStllessrlmrnlkklesvyfatryRQIKAAAAAEKPLARyY 417

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 267 PNTLEDGTKEETVALA-PAALPEFSESETCEK-WKRPFrsasatsltlsrcvdvVKGL---LDFKKRRghsvggapeqry 341
Cdd:PLN00181 418 SALSENGRSSEKSSMSnPAKPPDFYINDSRQGgWIDPF----------------LEGLckyLSFSKLR------------ 469

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 342 qsipvcVSAQIpsQAQDVLDAHlSEVNAVCFGPNSSLLATGGADRLIHLWN----VVGGRLEANQTLEGAGGS-ITSVDF 416
Cdd:PLN00181 470 ------VKADL--KQGDLLNSS-NLVCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICW 540

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 417 DPS-GSQVLAATYNQAAQLWKVGETQSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSyc 494
Cdd:PLN00181 541 NSYiKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA-- 618

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755523167 495 nDVVC------GDHIIISGHNDQKIRFWDSRGPHCIQVIPVQGRVTSLHLSY-DQLHLLSCSRDNTLKVIDLRIS 562
Cdd:PLN00181 619 -NICCvqfpseSGRSLAFGSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFvDSSTLVSSSTDNTLKLWDLSMS 692
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 359-392 3.56e-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: 46.92  E-value: 3.56e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 755523167   359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWN 392
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 141-285 3.85e-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: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 141 KKSAALDTLQSQLEERQDRLE----ALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEA 216
Cdd:COG1196  400 AQLEELEEAEEALLERLERLEeeleELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755523167 217 RDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISEIpntLEDGTKEETVALAPAA 285
Cdd:COG1196  480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL---IGVEAAYEAALEAALA 545
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 39-253 7.53e-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: 7.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167    39 AVWKRHIVRQLRHRDRTQKALflelvPAYNHLLEKAELLAKFSEKLKSEPKDAISTRHEDWRE---EVSGTGPDQVSSPA 115
Cdd:TIGR02168  228 ALLVLRLEELREELEELQEEL-----KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLEQ 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167   116 SLRVKwQQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEA---RAQQSRQLEERQAENAAQR 192
Cdd:TIGR02168  303 QKQIL-RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEleeLEAELEELESRLEELEEQL 381

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755523167   193 EAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVSQEL 253
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
WD40 pfam00400
WD domain, G-beta repeat;
359-392 1.09e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 1.09e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 755523167  359 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWN 392
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 138-252 1.98e-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: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEAR 217
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755523167 218 DLLEQLVQRKARAAAERNLRNERRERANQALVSQE 252
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 138-260 4.13e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARA---QQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQE 214
Cdd:COG1196  268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755523167 215 EARDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRT 260
Cdd:COG1196  348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 149-260 6.72e-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: 6.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 149 LQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRKA 228
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                         90       100       110
                 ....*....|....*....|....*....|..
gi 755523167 229 RAAAERNLRNERRERANQALVSQELKKAAKRT 260
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEE 425
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 139-309 9.76e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 9.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 139 VVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQavhQEAALRRLQEEARD 218
Cdd:COG3883  117 FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE---QEALLAQLSAEEAA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 219 LLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISEIPNTLEDGTKEETVALAPAALPEFSESETCEKW 298
Cdd:COG3883  194 AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273

                        170
                 ....*....|.
gi 755523167 299 KRPFRSASATS 309
Cdd:COG3883  274 AGAAAASAAGG 284
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 143-232 1.04e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 143 SAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQ 222
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90
                 ....*....|
gi 755523167 223 LVQRKARAAA 232
Cdd:COG4942   99 LEAQKEELAE 108
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
138-300 1.31e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEAR 217
Cdd:COG4372   95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 218 DLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISEIPNTLEDGTKEETVALAPAALPEFSESETCEK 297
Cdd:COG4372  175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254


                 ...
gi 755523167 298 WKR 300
Cdd:COG4372  255 VIL 257
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 144-246 1.65e-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: 47.45  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 144 AALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQL 223
Cdd:COG4942  150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229

                         90       100
                 ....*....|....*....|...
gi 755523167 224 VQRKARAAAERNLRNERRERANQ 246
Cdd:COG4942  230 ARLEAEAAAAAERTPAAGFAALK 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 42-272 1.76e-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: 48.13  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167    42 KRHIVRQLRHRDRTQKALFLELVPAYNHLLEKAELLAKFSEKLKSepkdaISTRHEDWREEVsgtgpdqvsspASLRVKW 121
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE-----LKEELESLEAEL-----------EELEAEL 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167   122 QQEKkglqlvcgemayqvvkksAALDTLQSQLEERQDRLEALQAcvvQLQEARAQQSR------QLEERQAENAAQREAY 195
Cdd:TIGR02168  368 EELE------------------SRLEELEEQLETLRSKVAQLEL---QIASLNNEIERlearleRLEDRRERLQQEIEEL 426

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755523167   196 ETLLQQAvhQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVS--QELKKAAKRTVSISEIPNTLED 272
Cdd:TIGR02168  427 LKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAaeRELAQLQARLDSLERLQENLEG 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-230 2.14e-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: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167    47 RQLRHRDRTQKALFLELVPAYNHLLEKAELLAKFSEKLKS--EPKDAISTRHEDWREEVSgtgpdqvsspaSLRVKWQQE 124
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEleAQIEQLKEELKALREALD-----------ELRAELTLL 815

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167   125 KKG---LQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEE-------RQAENAAQREA 194
Cdd:TIGR02168  816 NEEaanLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALLRSE 895

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 755523167   195 YETL---LQQAVHQEAALRRLQEEARDLLEQLVQRKARA 230
Cdd:TIGR02168  896 LEELseeLRELESKRSELRRELEELREKLAQLELRLEGL 934
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
146-279 4.10e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 146 LDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQ 225
Cdd:COG4372   82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755523167 226 RKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISEIPNTLEDGTKEETV 279
Cdd:COG4372  162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 138-257 4.76e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEER---QAENAAQREAYETLL-----QQAVHQEAAL 209
Cdd:COG3883   45 ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraLYRSGGSVSYLDVLLgsesfSDFLDRLSAL 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 755523167 210 RRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAA 257
Cdd:COG3883  125 SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 145-264 6.59e-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: 45.53  E-value: 6.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 145 ALDTLQSQLEERQDRLEALQacvvqlqearaQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLV 224
Cdd:COG4942  137 RLQYLKYLAPARREQAEELR-----------ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE 205

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755523167 225 QRKARAAAERNLRNERRERANQAL--VSQELKKAAKRTVSIS 264
Cdd:COG4942  206 KELAELAAELAELQQEAEELEALIarLEAEAAAAAERTPAAG 247
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
146-280 7.63e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 7.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 146 LDTLQSQLEERQDRLEALQAcvvQLQEARAQQSR----------QLEERQAENAAQREAYETLLQQAVHQEAALRRLQEE 215
Cdd:COG4372   47 LEQLREELEQAREELEQLEE---ELEQARSELEQleeeleelneQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755523167 216 ARDLLEQLVQRKARAAAERNLRNERRERANQAlvSQELKKAAKRTVSISEIPNTLEDGTKEETVA 280
Cdd:COG4372  124 RQDLEQQRKQLEAQIAELQSEIAEREEELKEL--EEQLESLQEELAALEQELQALSEAEAEQALD 186
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 120-232 7.71e-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: 7.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167   120 KWQQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLL 199
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823

                           90       100       110
                   ....*....|....*....|....*....|...
gi 755523167   200 QQAVHQEAALRRLQEEARDLLEQLVQRKARAAA 232
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIES 856
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
138-231 9.21e-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: 9.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEER-QAENAAQREAYETLLQQAvHQEAALRRLQEEA 216
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEERFAAA-LGDAVERELRENL 771

                          90
                  ....*....|....*
gi 755523167  217 RDLLEQLVQRKARAA 231
Cdd:COG4913   772 EERIDALRARLNRAE 786
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
120-232 1.01e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 120 KWQQEKKGLqlvcgEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQsRQLEERQAEnaAQREAYETLL 199
Cdd:COG4717  113 ELREELEKL-----EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEEL-EELEAELAE--LQEELEELLE 184

                         90       100       110
                 ....*....|....*....|....*....|...
gi 755523167 200 QQAVHQEAALRRLQEEARDLLEQLVQRKARAAA 232
Cdd:COG4717  185 QLSLATEEELQDLAEELEELQQRLAELEEELEE 217
WD40 pfam00400
WD domain, G-beta repeat;
445-478 1.05e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 1.05e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 755523167  445 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 478
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 445-478 1.07e-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: 39.99  E-value: 1.07e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 755523167   445 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 478
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 141-227 1.13e-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: 42.56  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  141 KKSAALDTLQSQLEERQDRLEALQAcvvQLQEARAQQSRQLEERQAENAAQREAYETLLQQAvhQEAALRRLQEEARDLL 220
Cdd:pfam03938  30 KRQAELEAKQKELQKLYEELQKDGA---LLEEEREEKEQELQKKEQELQQLQQKAQQELQKK--QQELLQPIQDKINKAI 104


                  ....*..
gi 755523167  221 EQLVQRK 227
Cdd:pfam03938 105 KEVAKEK 111
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
146-232 1.27e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 146 LDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQ----REAYETLLQQAVHQEAALRRLQEEARDLLE 221
Cdd:COG4717  148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELEE 227

                         90
                 ....*....|.
gi 755523167 222 QLVQRKARAAA 232
Cdd:COG4717  228 ELEQLENELEA 238
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 122-232 1.29e-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: 45.33  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  122 QQEKKGLQLVC---GEmayqvVKKSAALDTLQSQLEerqdRLEALQACVVQLQEARAQQS--RQLEERQAENAAQREAYE 196
Cdd:COG3096   472 RQFEKAYELVCkiaGE-----VERSQAWQTARELLR----RYRSQQALAQRLQQLRAQLAelEQRLRQQQNAERLLEEFC 542

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 755523167  197 TLLQQAVHQEAALRRLQEEARDLLEQLVQRKARAAA 232
Cdd:COG3096   543 QRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVE 578
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
146-228 1.63e-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: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  146 LDTLQSQLEERQDRLEALQACVVQLQEARAQQsRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQ 225
Cdd:COG4913   663 VASAEREIAELEAELERLDASSDDLAALEEQL-EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741


                  ...
gi 755523167  226 RKA 228
Cdd:COG4913   742 LAR 744
PRK11281 PRK11281
mechanosensitive channel MscK;
93-229 2.50e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167   93 STRHEDWREEVSGTGPDQVSSPASLRVKWQQEkkgLQLVCGEMAYQvvKKSAA-----LDTLQSQLEERQDRLEALQACV 167
Cdd:PRK11281  169 SQRLQQIRNLLKGGKVGGKALRPSQRVLLQAE---QALLNAQNDLQ--RKSLEgntqlQDLLQKQRDYLTARIQRLEHQL 243

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755523167  168 VQLQEARAQQSRQLEERQAENA-AQREAYETLLQQAVHQEAAL-RRLQE---EARDLLEQLVQRKAR 229
Cdd:PRK11281  244 QLLQEAINSKRLTLSEKTVQEAqSQDEAARIQANPLVAQELEInLQLSQrllKATEKLNTLTQQNLR 310
TrbJ_Ti TIGR02780
P-type conjugative transfer protein TrbJ; The TrbJ protein is found in the trb locus of ...
 133-220 3.15e-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: 42.81  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  133 GEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVvqlqEARAQQSRQLEERQAENAAQREAYETLLQQavhQEAALRRL 212
Cdd:TIGR02780 152 GLQTGNLAEDNATLDQLQSLSQSASGQLQALQAGN----QLAAQQSKQLQKLRALLAAQIQAQSTYMAS---EQAREDVT 224


                  ....*...
gi 755523167  213 QEEARDLL 220
Cdd:TIGR02780 225 QQQRRQFL 232
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
143-226 5.17e-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: 5.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  143 SAALDTLQSQLEERQDRLEALQACVVQLQEARA---QQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDL 219
Cdd:COG4913   684 SDDLAALEEQLEELEAELEELEEELDELKGEIGrleKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763


                  ....*..
gi 755523167  220 LEQLVQR 226
Cdd:COG4913   764 ERELREN 770
PTZ00421 PTZ00421
coronin; Provisional
 370-478 6.08e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 42.57  E-value: 6.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 370 VCFGP-NSSLLATGGADRLIHLWNVVGGRLEANQT-----LEGAGGSITSVDFDPSGSQVLA-ATYNQAAQLWKVGETQS 442
Cdd:PTZ00421  81 VAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhLQGHTKKVGIVSFHPSAMNVLAsAGADMVVNVWDVERGKA 160

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755523167 443 KETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 478
Cdd:PTZ00421 161 VEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
143-228 6.61e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 6.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 143 SAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQRE-------AYETLLQQAVHQEAALRRLQEE 215
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEeleelneQLQAAQAELAQAQEELESLQEE 109

                         90
                 ....*....|...
gi 755523167 216 ARDLLEQLVQRKA 228
Cdd:COG4372  110 AEELQEELEELQK 122
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
138-226 6.65e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 138 QVVKKSAALDTLQSQLEERQDRLealqacvvqLQEARAQQsRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEE-- 215
Cdd:COG3206  292 DVIALRAQIAALRAQLQQEAQRI---------LASLEAEL-EALQAREASLQAQLAQLEARLAELPELEAELRRLEREve 361

                         90
                 ....*....|..
gi 755523167 216 -ARDLLEQLVQR 226
Cdd:COG3206  362 vARELYESLLQR 373
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 138-245 8.63e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 8.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 138 QVVKKSAALDTLQSQLEERQDRLEALQAcvvQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEAR 217
Cdd:COG3883  144 ELEAKKAELEAKLAELEALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220

                         90       100
                 ....*....|....*....|....*...
gi 755523167 218 DLLEQLVQRKARAAAERNLRNERRERAN 245
Cdd:COG3883  221 AAAAAAAAAAAAAAAAAAAAAAAASAAG 248
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
110-291 9.64e-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: 9.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  110 QVSSPASLRVKWQQEKKGLQLVCGEMAYqvvkksAALDTLQSQLEERQDRLEALQAcvvQLQEARAQQsRQLEERQAENA 189
Cdd:COG4913   582 QVKGNGTRHEKDDRRRIRSRYVLGFDNR------AKLAALEAELAELEEELAEAEE---RLEALEAEL-DALQERREALQ 651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  190 AQREAYETLLQQAVHQEaALRRLQEEARDL------LEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTvSI 263
Cdd:COG4913   652 RLAEYSWDEIDVASAER-EIAELEAELERLdassddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-EL 729

                         170       180
                  ....*....|....*....|....*...
gi 755523167  264 SEIPNTLEDGTKEETVALAPAALPEFSE 291
Cdd:COG4913   730 DELQDRLEAAEDLARLELRALLEERFAA 757
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 68-227 1.58e-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: 41.70  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167    68 NHLLEKAE----LLAKFSEKLKSEPKDAISTRHEDWREEVSgtgpdqvsspASLRVK-WQQEKKGL--QLVCGEMAYQVV 140
Cdd:pfam01576  446 SSLLNEAEgkniKLSKDVSSLESQLQDTQELLQEETRQKLN----------LSTRLRqLEDERNSLqeQLEEEEEAKRNV 515

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167   141 KKSaaLDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLlqqavhqEAALRRLQEEARDLL 220
Cdd:pfam01576  516 ERQ--LSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-------EKTKNRLQQELDDLL 586


                   ....*..
gi 755523167   221 EQLVQRK 227
Cdd:pfam01576  587 VDLDHQR 593
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 138-247 1.67e-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: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 138 QVVKKSAALDTLQSQLEERQDRLEALQAcvvQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEAR 217
Cdd:COG3883  137 ELKADKAELEAKKAELEAKLAELEALKA---ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213

                         90       100       110
                 ....*....|....*....|....*....|
gi 755523167 218 DLLEQLVQRKARAAAERNLRNERRERANQA 247
Cdd:COG3883  214 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 122-259 1.70e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 122 QQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEA--LQACVVQLQEARAQQSRQLEERQAENAAQREAYETLL 199
Cdd:PRK09510  68 QQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKerLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755523167 200 ---QQAVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERAN---QALVSQELKKAAKR 259
Cdd:PRK09510 148 kaeAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAaeaKKKAEAEAKKKAAA 213
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 138-218 1.74e-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: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 138 QVVKKSAALDTLQSQLEERQDRLEALQAcvvQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEAR 217
Cdd:COG4942  161 ELAALRAELEAERAELEALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237


                 .
gi 755523167 218 D 218
Cdd:COG4942  238 A 238
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
146-232 1.84e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 40.19  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 146 LDTLQSQLEERQDRleALQAcvvqLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQ 225
Cdd:COG1842   60 LEELEAEAEKWEEK--ARLA----LEKGREDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKA 133


                 ....*..
gi 755523167 226 RKARAAA 232
Cdd:COG1842  134 KKDTLKA 140
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 138-259 1.96e-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: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQ-QSRQLEERQAENAAQREAYEtllQQAVHQEAALRRLQEEA 216
Cdd:TIGR02794  72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAaKQAEEKQKQAEEAKAKQAAE---AKAKAEAEAERKAKEEA 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 755523167  217 RDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKR 259
Cdd:TIGR02794 149 AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA 191
dsDNA_bind pfam01984
Double-stranded DNA-binding domain; This domain is believed to bind double-stranded DNA of 20 ...
 156-225 2.02e-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: 2.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755523167  156 RQDRLEALQacvvQLQEARAQQSRQLEERQAENAAQREAyetLLQQAVHQEAA--LRRLQ----EEARDLLEQLVQ 225
Cdd:pfam01984   2 RRARLAELQ----KQQGGGGGSGGAQEQAQEEQEEQKQA---ILRQILTPEARerLSRIRlvkpERAEAVENQLIQ 70
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
138-232 2.22e-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: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQleeRQAENAAQREAYEtlLQQAvhqeAALRRLQEEAR 217
Cdd:COG2268  238 RIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQ---RQLEIAEREREIE--LQEK----EAEREEAELEA 308

                         90
                 ....*....|....*
gi 755523167 218 DLLEQLVQRKARAAA 232
Cdd:COG2268  309 DVRKPAEAEKQAAEA 323
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 138-231 2.35e-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: 40.48  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  138 QVVKKSAALDTL-QSQLEERQDRLEAlqacvvQLQEARAQQSR------QLEERQAENAAQREAYETLLQQAVHQEAALR 210
Cdd:pfam00529  40 DRVKAGDVLFQLdPTDYQAALDSAEA------QLAKAQAQVARlqaeldRLQALESELAISRQDYDGATAQLRAAQAAVK 113

                          90       100
                  ....*....|....*....|.
gi 755523167  211 RLQEEARDLLEQLVQRKARAA 231
Cdd:pfam00529 114 AAQAQLAQAQIDLARRRVLAP 134
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 171-231 2.44e-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: 2.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755523167 171 QEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRKARAA 231
Cdd:cd22265    9 QEYEEEISKLEAERRALEEEENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKEDEELA 69
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 133-259 2.58e-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: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 133 GEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRL 212
Cdd:COG1196  651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 755523167 213 QEEARDLLEQLVQrkARAAAERNLRNERRERANQALVSQELKKAAKR 259
Cdd:COG1196  731 EAEREELLEELLE--EEELLEEEALEELPEPPDLEELERELERLERE 775
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 144-258 2.82e-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: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167   144 AALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQ---EEARDLL 220
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErqlEELEAQL 325

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 755523167   221 EQLVQRK--ARAAAERNLRNERRERANQALVSQELKKAAK 258
Cdd:TIGR02168  326 EELESKLdeLAEELAELEEKLEELKEELESLEAELEELEA 365
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
143-261 2.92e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  143 SAALDTLQSQLEERQDRLEALQAC---------VVQLQEARAQQSRQLEERQAENA------AQREAYETLLQQAVHQEA 207
Cdd:COG4913   630 EERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAELERLDASSDdlaaleEQLEELEAELEELEEELD 709

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 755523167  208 ALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTV 261
Cdd:COG4913   710 ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 122-277 3.50e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 122 QQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEER----------------- 184
Cdd:COG4942   47 KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqpplalll 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 185 QAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKA---AKRTV 261
Cdd:COG4942  127 SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQkllARLEK 206

                        170
                 ....*....|....*.
gi 755523167 262 SISEIPNTLEDGTKEE 277
Cdd:COG4942  207 ELAELAAELAELQQEA 222
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 522-558 3.69e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.37  E-value: 3.69e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 755523167   522 HCIQVIPV-QGRVTSLHLSYDQLHLLSCSRDNTLKVID 558
Cdd:smart00320   3 ELLKTLKGhTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 79-232 4.03e-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: 39.93  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167   79 KFSEKLKSEPKDAIS-TRHEDWREEVSGTGPDQvsspaSLRVKWQQEKKGLQLVCGEMAYQ----VVKKSAALDTLQSQL 153
Cdd:pfam15709 290 QVSIDGRSSPTQTFVvTGNMESEEERSEEDPSK-----ALLEKREQEKASRDRLRAERAEMrrleVERKRREQEEQRRLQ 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  154 EERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYET---LLQQAVHQEAalRRLQEEARDLLEQLVQRKARA 230
Cdd:pfam15709 365 QEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERkqrLQLQAAQERA--RQQQEEFRRKLQELQRKKQQE 442


                  ..
gi 755523167  231 AA 232
Cdd:pfam15709 443 EA 444
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 118-215 4.47e-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: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  118 RVKWQQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYET 197
Cdd:COG3096   527 RLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLA 606

                          90
                  ....*....|....*...
gi 755523167  198 LlqqavhqEAALRRLQEE 215
Cdd:COG3096   607 A-------QDALERLREQ 617
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
143-266 4.58e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 4.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 143 SAALDTLQSQLEERQDRLEALQACVVQLQEARAQ---------QSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQ 213
Cdd:COG3206  218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALR 297

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755523167 214 EEARDLLEQLVQRKARAAAERNLRNERRERANQALvSQELKKAAKRTVSISEI 266
Cdd:COG3206  298 AQIAALRAQLQQEAQRILASLEAELEALQAREASL-QAQLAQLEARLAELPEL 349
mukB PRK04863
chromosome partition protein MukB;
144-214 6.00e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 6.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755523167  144 AALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLlqqavhqEAALRRLQE 214
Cdd:PRK04863  554 DELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAA-------QDALARLRE 617
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
66-226 6.04e-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: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167   66 AYNHLLEKAELLAKFSEkLKSEPKDAISTRHE--DWREEVSG--TGPDQVSSPASLRVKWQQEKKGLQLVCGEMAYQVVK 141
Cdd:COG4913   639 ELDALQERREALQRLAE-YSWDEIDVASAEREiaELEAELERldASSDDLAALEEQLEELEAELEELEEELDELKGEIGR 717

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  142 KSAALDTLQSQLEERQDRLEALQacvvqlQEARAQQSRQLEERQAEnAAQREAYETLLQQAVHQEAALRRLQEEARDLLE 221
Cdd:COG4913   718 LEKELEQAEEELDELQDRLEAAE------DLARLELRALLEERFAA-ALGDAVERELRENLEERIDALRARLNRAEEELE 790


                  ....*
gi 755523167  222 QLVQR 226
Cdd:COG4913   791 RAMRA 795
WD40 pfam00400
WD domain, G-beta repeat;
530-558 6.06e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.01  E-value: 6.06e-03
                          10        20
                  ....*....|....*....|....*....
gi 755523167  530 QGRVTSLHLSYDQLHLLSCSRDNTLKVID 558
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 138-228 7.02e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.55  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  138 QVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQ-REAYETLLQQAVHQEAALRRLQEEA 216
Cdd:PRK11448  157 QLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETsQERKQKRKEITDQAAKRLELSEEET 236

                          90
                  ....*....|...
gi 755523167  217 RDLL-EQLvqRKA 228
Cdd:PRK11448  237 RILIdQQL--RKA 247
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 144-232 7.06e-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: 7.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 144 AALDTLQSQLEERQ----DRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALR-RLQEEARD 218
Cdd:COG1579   99 ESLKRRISDLEDEIlelmERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAaKIPPELLA 178

                         90
                 ....*....|....
gi 755523167 219 LLEQLVQRKARAAA 232
Cdd:COG1579  179 LYERIRKRKNGLAV 192
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
144-280 7.53e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 7.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 144 AALDTLQSQLEERQDRLEALQACVVQLQEARA--QQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLE 221
Cdd:COG4717  105 EELEAELEELREELEKLEKLLQLLPLYQELEAleAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755523167 222 QLvQRKARAAAERNLRNERRERANQALVSQELKKA----AKRTVSISEIPNTLEDGTKEETVA 280
Cdd:COG4717  185 QL-SLATEEELQDLAEELEELQQRLAELEEELEEAqeelEELEEELEQLENELEAAALEERLK 246
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
143-225 7.59e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 7.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 143 SAALDTLQSQLEERQDRLEALQACVVQLQEAR-----AQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEAR 217
Cdd:COG3206  174 RKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253


                 ....*...
gi 755523167 218 DLLEQLVQ 225
Cdd:COG3206  254 DALPELLQ 261
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 149-226 8.96e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 36.91  E-value: 8.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 149 LQSQLEE--RQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQavHQEAALRRLQEEARDLLEQLVQR 226
Cdd:PRK07353  58 LEAQYEQqlASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQASKEKARREIEQ--QKQAALAQLEQQVDALSRQILEK 135
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 144-232 9.00e-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: 9.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 144 AALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQL----------EERQAENAAQREaYETLLQQAVHQEAALRRLQ 213
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIeevearikkyEEQLGNVRNNKE-YEALQKEIESLKRRISDLE 109

                         90
                 ....*....|....*....
gi 755523167 214 EEARDLLEQLVQRKARAAA 232
Cdd:COG1579  110 DEILELMERIEELEEELAE 128
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
144-232 9.02e-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: 9.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167  144 AALDTLQSQ---LEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLL 220
Cdd:COG4913   225 EAADALVEHfddLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304

                          90
                  ....*....|..
gi 755523167  221 EQLVQRKARAAA 232
Cdd:COG4913   305 ARLEAELERLEA 316
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
144-265 9.49e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 9.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523167 144 AALDTLQSQLEERQDRLEALQACVVQLQEARAQQsRQLEERQAENAAQREAYETLLQqAVHQEAALRRLQEEARDLLEQL 223
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEELEELEEEL-EELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPERL 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755523167 224 VQRKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISE 265
Cdd:COG4717  149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
FliT pfam05400
Flagellar protein FliT; This family contains several bacterial flagellar FliT proteins. The ...
 167-231 9.65e-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: 9.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755523167  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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