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Conserved domains on  [gi|1952711695|ref|XP_013977985|]
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protein Atg16l2 isoform X1 [Canis lupus familiaris]

Protein Classification

WD repeat ATG16 family protein( domain architecture ID 12095058)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
326-605 1.38e-53

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: 185.23  E-value: 1.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 326 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 405
Cdd:cd00200     4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 406 EAQSKETLSGHTDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTI-SVLSYCNDVV--CGDHVIISGHNDQKIRF 482
Cdd:cd00200    82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLrGHTDWVNSVAfsPDGTFVASSSQDGTIKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 483 WDSRVPCCTQVIPV-QGRVTSLNLSHDQLHLLSCSRDDTLKIIDLRVSNIRQVFRADGFRCGSdwtkAVFSPDRSYALAG 561
Cdd:cd00200   162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1952711695 562 SWDGALYIWDVDTGKLEGSLRGpHCTAVNAVAWCYSGSHVHSGS 605
Cdd:cd00200   238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGS 280
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
26-202 4.65e-49

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: 168.96  E-value: 4.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  26 LFLELVPAYNCLLEKAELLARISEKLQPKPNDVTPATLQGPWEEESgPDSDLVPSSSTLRVKWQEEEEGLRLVCGEMAYQ 105
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKAS-PQSASIQSLEQLLAQLREELAELYRSRGELAQR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 106 VVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEARD 185
Cdd:pfam08614  80 LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRE 159
                         170
                  ....*....|....*..
gi 1952711695 186 LLERLVQRKARAAAERN 202
Cdd:pfam08614 160 LVERWMKRKGQEAEAMN 176
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
326-605 1.38e-53

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: 185.23  E-value: 1.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 326 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 405
Cdd:cd00200     4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 406 EAQSKETLSGHTDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTI-SVLSYCNDVV--CGDHVIISGHNDQKIRF 482
Cdd:cd00200    82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLrGHTDWVNSVAfsPDGTFVASSSQDGTIKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 483 WDSRVPCCTQVIPV-QGRVTSLNLSHDQLHLLSCSRDDTLKIIDLRVSNIRQVFRADGFRCGSdwtkAVFSPDRSYALAG 561
Cdd:cd00200   162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1952711695 562 SWDGALYIWDVDTGKLEGSLRGpHCTAVNAVAWCYSGSHVHSGS 605
Cdd:cd00200   238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGS 280
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
26-202 4.65e-49

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: 168.96  E-value: 4.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  26 LFLELVPAYNCLLEKAELLARISEKLQPKPNDVTPATLQGPWEEESgPDSDLVPSSSTLRVKWQEEEEGLRLVCGEMAYQ 105
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKAS-PQSASIQSLEQLLAQLREELAELYRSRGELAQR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 106 VVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEARD 185
Cdd:pfam08614  80 LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRE 159
                         170
                  ....*....|....*..
gi 1952711695 186 LLERLVQRKARAAAERN 202
Cdd:pfam08614 160 LVERWMKRKGQEAEAMN 176
WD40 COG2319
WD40 repeat [General function prediction only];
321-606 6.87e-47

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 170.48  E-value: 6.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 321 SQVLDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQ 400
Cdd:COG2319   110 GLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVR 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 401 LWKVGEAQSKETLSGHTDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------ISVLSYCNDvvcgDHVIIS 473
Cdd:COG2319   188 LWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTltghsgsVRSVAFSPD----GRLLAS 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 474 GHNDQKIRFWDSRVPCCTQVIPVQ-GRVTSLNLSHDQLHLLSCSRDDTLKIIDLRVSNIRQVFRADGFRCGSdwtkAVFS 552
Cdd:COG2319   264 GSADGTVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS----VAFS 339
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1952711695 553 PDRSYALAGSWDGALYIWDVDTGKLEGSLRGpHCTAVNAVAWCYSGSHVHSGSR 606
Cdd:COG2319   340 PDGKTLASGSDDGTVRLWDLATGELLRTLTG-HTGAVTSVAFSPDGRTLASGSA 392
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
115-205 3.60e-21

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: 88.39  E-value: 3.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 115 ALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEARDLLERLVQRK 194
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80
                          90
                  ....*....|.
gi 1952711695 195 ARAAAERNLRN 205
Cdd:cd22887    81 QQEADKMNEAN 91
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
105-226 1.98e-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: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 105 QVVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEAR 184
Cdd:COG1196   240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1952711695 185 DL---LERLVQRKARAAAERNLRNERYEKAKQARMSLELKAAAQR 226
Cdd:COG1196   320 ELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
9-206 6.07e-08

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: 56.22  E-value: 6.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695    9 KRHIVRQLRQRDRTQKALFLELVPAYNCLLEKAELLARISEKLQPKPNDVtpATLQGPWEEESGPDSDLVPSSSTLRVKW 88
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL--ESLEAELEELEAELEELESRLEELEEQL 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695   89 QEEEEGLRlvcgEMAYQVVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQ-----TRQVDAQRALNVAQRAAYE 163
Cdd:TIGR02168  382 ETLRSKVA----QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkelQAELEELEEELEELQEELE 457
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1952711695  164 ALRGRARLQEAALRRLEEEARDLLERLVQRKARAAAERNLRNE 206
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
320-359 1.76e-07

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 47.69  E-value: 1.76e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1952711695  320 PSQVLDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWN 359
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
321-359 1.02e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 1.02e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1952711695 321 SQVLDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWN 359
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
331-529 6.06e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 49.31  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 331 LSEVNAVC---FGPNSSLLATGGADRLIHLWN----VVGGRLEANQTLEGAGGS-ITSVDFDPS-GSQVLAATYNQAAQL 401
Cdd:PLN00181  480 LNSSNLVCaigFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICWNSYiKSQVASSNFEGVVQV 559
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 402 WKVGEAQSKETLSGHTDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTISVLSycnDVVC------GDHVIISG 474
Cdd:PLN00181  560 WDVARSQLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpseSGRSLAFG 636
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952711695 475 HNDQKIRFWDSR---VPCCTQVipVQGRVTSLNLSHDQLHLLSCSRDDTLKIIDLRVS 529
Cdd:PLN00181  637 SADHKVYYYDLRnpkLPLCTMI--GHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMS 692
PRK14475 PRK14475
F0F1 ATP synthase subunit B; Provisional
106-224 1.84e-05

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184697 [Multi-domain]  Cd Length: 167  Bit Score: 45.32  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 106 VVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRAlnVAQRAAYEALRGrarlQEAALRRLEEEARD 185
Cdd:PRK14475   25 LIALKVLPKALAGALDAYAAKIQAELDEAQRLREEAQALLADVKAERE--EAERQAAAMLAA----AKADARRMEAEAKE 98
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1952711695 186 LLERLVQRKARAAaernlrnERYEKAKQARMSLELKAAA 224
Cdd:PRK14475   99 KLEEQIKRRAEMA-------ERKIAQAEAQAAADVKAAA 130
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
326-605 1.38e-53

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: 185.23  E-value: 1.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 326 VLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVG 405
Cdd:cd00200     4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 406 EAQSKETLSGHTDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTI-SVLSYCNDVV--CGDHVIISGHNDQKIRF 482
Cdd:cd00200    82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLrGHTDWVNSVAfsPDGTFVASSSQDGTIKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 483 WDSRVPCCTQVIPV-QGRVTSLNLSHDQLHLLSCSRDDTLKIIDLRVSNIRQVFRADGFRCGSdwtkAVFSPDRSYALAG 561
Cdd:cd00200   162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1952711695 562 SWDGALYIWDVDTGKLEGSLRGpHCTAVNAVAWCYSGSHVHSGS 605
Cdd:cd00200   238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGS 280
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
26-202 4.65e-49

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: 168.96  E-value: 4.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  26 LFLELVPAYNCLLEKAELLARISEKLQPKPNDVTPATLQGPWEEESgPDSDLVPSSSTLRVKWQEEEEGLRLVCGEMAYQ 105
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKAS-PQSASIQSLEQLLAQLREELAELYRSRGELAQR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 106 VVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEARD 185
Cdd:pfam08614  80 LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENRE 159
                         170
                  ....*....|....*..
gi 1952711695 186 LLERLVQRKARAAAERN 202
Cdd:pfam08614 160 LVERWMKRKGQEAEAMN 176
WD40 COG2319
WD40 repeat [General function prediction only];
321-606 6.87e-47

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 170.48  E-value: 6.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 321 SQVLDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQ 400
Cdd:COG2319   110 GLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVR 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 401 LWKVGEAQSKETLSGHTDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------ISVLSYCNDvvcgDHVIIS 473
Cdd:COG2319   188 LWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTltghsgsVRSVAFSPD----GRLLAS 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 474 GHNDQKIRFWDSRVPCCTQVIPVQ-GRVTSLNLSHDQLHLLSCSRDDTLKIIDLRVSNIRQVFRADGFRCGSdwtkAVFS 552
Cdd:COG2319   264 GSADGTVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS----VAFS 339
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1952711695 553 PDRSYALAGSWDGALYIWDVDTGKLEGSLRGpHCTAVNAVAWCYSGSHVHSGSR 606
Cdd:COG2319   340 PDGKTLASGSDDGTVRLWDLATGELLRTLTG-HTGAVTSVAFSPDGRTLASGSA 392
WD40 COG2319
WD40 repeat [General function prediction only];
315-609 3.30e-43

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 160.08  E-value: 3.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 315 VAAQPPSQVLDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEAnqTLEGAGGSITSVDFDPSGSQVLAAT 394
Cdd:COG2319    62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLR--TLTGHTGAVRSVAFSPDGKTLASGS 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 395 YNQAAQLWKVGEAQSKETLSGHTDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------ISVLSYCNDvvcg 467
Cdd:COG2319   140 ADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTltghtgaVRSVAFSPD---- 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 468 DHVIISGHNDQKIRFWDSRVPCCTQVIPV-QGRVTSLNLSHDQLHLLSCSRDDTLKIIDLRVSNIRQVFRADgfrcgSDW 546
Cdd:COG2319   216 GKLLASGSADGTVRLWDLATGKLLRTLTGhSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH-----SGG 290
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952711695 547 TKAV-FSPDRSYALAGSWDGALYIWDVDTGKLEGSLRGpHCTAVNAVAWCYSGSHVHSGSRG----LW 609
Cdd:COG2319   291 VNSVaFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKTLASGSDDgtvrLW 357
WD40 COG2319
WD40 repeat [General function prediction only];
322-574 3.88e-39

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 148.91  E-value: 3.88e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 322 QVLDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQL 401
Cdd:COG2319   153 KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLL--RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRL 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 402 WKVGEAQSKETLSGHTDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTisvLSYCNDVVCG------DHVIISGH 475
Cdd:COG2319   231 WDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT---LTGHSGGVNSvafspdGKLLASGS 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 476 NDQKIRFWDSRVPCCTQVIPV-QGRVTSLNLSHDQLHLLSCSRDDTLKIIDLRVSNIRQVFRAdgfrcGSDWTKAV-FSP 553
Cdd:COG2319   308 DDGTVRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTG-----HTGAVTSVaFSP 382
                         250       260
                  ....*....|....*....|.
gi 1952711695 554 DRSYALAGSWDGALYIWDVDT 574
Cdd:COG2319   383 DGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
322-523 5.35e-32

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 125.53  E-value: 5.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 322 QVLDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEanQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQL 401
Cdd:cd00200    84 ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL--TTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKL 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 402 WKVGEAQSKETLSGHTDKVTAAKFKLTRHQAVTGSRDRTVKEWDLgraYCSRTISVLSYCNDVVCG------DHVIISGH 475
Cdd:cd00200   162 WDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL---STGKCLGTLRGHENGVNSvafspdGYLLASGS 238
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1952711695 476 NDQKIRFWDSRVPCCTQVIP-VQGRVTSLNLSHDQLHLLSCSRDDTLKI 523
Cdd:cd00200   239 EDGTIRVWDLRTGECVQTLSgHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
339-609 1.97e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 111.93  E-value: 1.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 339 FGPNSSLLATGGADRLIHLWNVVGGRLEAnqTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVGEAQSKETLSGHTD 418
Cdd:COG2319     2 LSADGAALAAASADLALALLAAALGALLL--LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 419 KVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTISVL-SYCNDVVC--GDHVIISGHNDQKIRFWDSRVPCCTQVIP 495
Cdd:COG2319    80 AVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHtGAVRSVAFspDGKTLASGSADGTVRLWDLATGKLLRTLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 496 V-QGRVTSLNLSHDQLHLLSCSRDDTLKIIDLRVSNIRQVFRADgfrcgSDWTKAV-FSPDRSYALAGSWDGALYIWDVD 573
Cdd:COG2319   160 GhSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH-----TGAVRSVaFSPDGKLLASGSADGTVRLWDLA 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1952711695 574 TGKLEGSLRGpHCTAVNAVAWCYSGSHVHSGSRG----LW 609
Cdd:COG2319   235 TGKLLRTLTG-HSGSVRSVAFSPDGRLLASGSADgtvrLW 273
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
319-484 2.36e-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: 109.35  E-value: 2.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 319 PPSQVLDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLeaNQTLEGAGGSITSVDFDPSGSQVLAATYNQA 398
Cdd:cd00200   123 ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC--VATLTGHTGEVNSVAFSPDGEKLLSSSSDGT 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 399 AQLWKVGEAQSKETLSGHTDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTISVLSycNDVVC-----GDHVIIS 473
Cdd:cd00200   201 IKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHT--NSVTSlawspDGKRLAS 278
                         170
                  ....*....|.
gi 1952711695 474 GHNDQKIRFWD 484
Cdd:cd00200   279 GSADGTIRIWD 289
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
115-205 3.60e-21

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: 88.39  E-value: 3.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 115 ALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEARDLLERLVQRK 194
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80
                          90
                  ....*....|.
gi 1952711695 195 ARAAAERNLRN 205
Cdd:cd22887    81 QQEADKMNEAN 91
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
105-226 1.98e-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: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 105 QVVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEAR 184
Cdd:COG1196   240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1952711695 185 DL---LERLVQRKARAAAERNLRNERYEKAKQARMSLELKAAAQR 226
Cdd:COG1196   320 ELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
84-226 9.25e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 9.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  84 LRVKWQEEEEGLRlvcgEMAYQVVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQV---DAQRALNVAQRA 160
Cdd:COG1196   237 LEAELEELEAELE----ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELarlEQDIARLEERRR 312
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952711695 161 AYEALRGRARLQEAALRRLEEEARDLLERLVQRKARAAAERNLRNERYEKAKQARMSLELKAAAQR 226
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
108-226 1.95e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 108 AKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEARDLL 187
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1952711695 188 ERLVQRKARAAAERNLRNERYEKAKQARMSLELKAAAQR 226
Cdd:COG1196   463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
104-225 3.18e-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: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 104 YQVVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEE- 182
Cdd:COG1196   225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDi 304
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1952711695 183 --ARDLLERLVQRKARAAAERNLRNERYEKAKQARMSLELKAAAQ 225
Cdd:COG1196   305 arLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
9-206 6.07e-08

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: 56.22  E-value: 6.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695    9 KRHIVRQLRQRDRTQKALFLELVPAYNCLLEKAELLARISEKLQPKPNDVtpATLQGPWEEESGPDSDLVPSSSTLRVKW 88
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL--ESLEAELEELEAELEELESRLEELEEQL 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695   89 QEEEEGLRlvcgEMAYQVVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQ-----TRQVDAQRALNVAQRAAYE 163
Cdd:TIGR02168  382 ETLRSKVA----QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkelQAELEELEEELEELQEELE 457
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1952711695  164 ALRGRARLQEAALRRLEEEARDLLERLVQRKARAAAERNLRNE 206
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
320-359 1.76e-07

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 47.69  E-value: 1.76e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1952711695  320 PSQVLDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWN 359
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
321-359 1.02e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 1.02e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1952711695 321 SQVLDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWN 359
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
110-226 1.32e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 110 SAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAAL----RRLEEEARD 185
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELaeaeEALLEAEAE 373
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1952711695 186 LLERLVQRKARAAAERNLRNERYEKAKQARMSLELKAAAQR 226
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
102-249 3.37e-06

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: 49.76  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 102 MAYQVVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEE 181
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952711695 182 EARDLLERLVQRKAR-----AAAERNLRNERYEKAKQARMSLELKAAAQRTVSISESPNTIGDGIREEGKTLA 249
Cdd:COG4942    91 EIAELRAELEAQKEElaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
331-529 6.06e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 49.31  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 331 LSEVNAVC---FGPNSSLLATGGADRLIHLWN----VVGGRLEANQTLEGAGGS-ITSVDFDPS-GSQVLAATYNQAAQL 401
Cdd:PLN00181  480 LNSSNLVCaigFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICWNSYiKSQVASSNFEGVVQV 559
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 402 WKVGEAQSKETLSGHTDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTISVLSycnDVVC------GDHVIISG 474
Cdd:PLN00181  560 WDVARSQLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpseSGRSLAFG 636
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952711695 475 HNDQKIRFWDSR---VPCCTQVipVQGRVTSLNLSHDQLHLLSCSRDDTLKIIDLRVS 529
Cdd:PLN00181  637 SADHKVYYYDLRnpkLPLCTMI--GHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMS 692
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
105-220 7.69e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 7.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  105 QVVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRAL-------NVAQRAAYEALRGR---ARLQEA 174
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEleelesrLEELEEQLETLRSKvaqLELQIA 396
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1952711695  175 ALRRLEEEARDLLERLVQRKARAAAERNLRNERYEKAKQARMSLEL 220
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
68-222 1.08e-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: 48.90  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695   68 EEESGPDSDLVPSSSTLRVKWQEEEEGLRLVCGEMAYQVVAKSAALGALESTLEQRQ-------STLAALQARVAELREE 140
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkalrEALDELRAELTLLNEE 818
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  141 QARQT-RQVDAQRALNVAQRAAYEALRGRARLQE---------AALRRLEEEARDLLERLVQRKARAAAERNLRNERYEK 210
Cdd:TIGR02168  819 AANLReRLESLERRIAATERRLEDLEEQIEELSEdieslaaeiEELEELIEELESELEALLNERASLEEALALLRSELEE 898
                          170
                   ....*....|..
gi 1952711695  211 AKQARMSLELKA 222
Cdd:TIGR02168  899 LSEELRELESKR 910
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
131-249 1.49e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 47.95  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 131 QARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQ-EAALRRLEEEARDLLERLVQ--RKARAAAERNLRNER 207
Cdd:COG2268   222 EAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEaEAAYEIAEANAEREVQRQLEiaEREREIELQEKEAER 301
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1952711695 208 YEKAKQArmSLELKAAAQRTVSISESpNTIGDGIREEGKTLA 249
Cdd:COG2268   302 EEAELEA--DVRKPAEAEKQAAEAEA-EAEAEAIRAKGLAEA 340
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
127-227 1.54e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  127 LAALQARVAELREE---QARQTRQVDAQRALNVAQRAAYEALRGRARLQ------EAALRRLEEEARDL------LERLV 191
Cdd:COG4913    612 LAALEAELAELEEElaeAEERLEALEAELDALQERREALQRLAEYSWDEidvasaEREIAELEAELERLdassddLAALE 691
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1952711695  192 QRKARAAAERNLRNERYEKAKQARMSLELKAAAQRT 227
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
115-226 1.80e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 115 ALESTLEQRQstlaaLQARVAELREEQARQTR------QVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEARDLLE 188
Cdd:COG1196   217 ELKEELKELE-----AELLLLKLRELEAELEEleaeleELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1952711695 189 RLVQRKARAAAERNLRNER--YEKAKQARMSLELKAAAQR 226
Cdd:COG1196   292 ELLAELARLEQDIARLEERrrELEERLEELEEELAELEEE 331
PRK14475 PRK14475
F0F1 ATP synthase subunit B; Provisional
106-224 1.84e-05

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184697 [Multi-domain]  Cd Length: 167  Bit Score: 45.32  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 106 VVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRAlnVAQRAAYEALRGrarlQEAALRRLEEEARD 185
Cdd:PRK14475   25 LIALKVLPKALAGALDAYAAKIQAELDEAQRLREEAQALLADVKAERE--EAERQAAAMLAA----AKADARRMEAEAKE 98
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1952711695 186 LLERLVQRKARAAaernlrnERYEKAKQARMSLELKAAA 224
Cdd:PRK14475   99 KLEEQIKRRAEMA-------ERKIAQAEAQAAADVKAAA 130
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
111-224 1.90e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.46  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 111 AALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAA---------YEALRGRARLQEAALRRLEE 181
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYEALQKEIESLKRRISDLED 110
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1952711695 182 EARDLLERLVQRKARAAAERNLRNERYEKAKQARMSLELKAAA 224
Cdd:COG1579   111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
101-226 4.45e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 101 EMAYQVVAKSAALGALESTLEQRQSTLAALQARVAELREeqaRQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLE 180
Cdd:COG4717   122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1952711695 181 EEARDLLERLVQRKARAAAERNLRNERYEKAKQARMSLELKAAAQR 226
Cdd:COG4717   199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
121-259 4.68e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 46.87  E-value: 4.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  121 EQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEardlLERLvqRKARAAAE 200
Cdd:PRK11448   138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQ----LEQL--QEKAAETS 211
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952711695  201 RNLRNERYEKAKQARMSLELKAAAQRTVsISESPNTIG-----------DGIR-EEGKTLALmAEPVSPKS 259
Cdd:PRK11448   212 QERKQKRKEITDQAAKRLELSEEETRIL-IDQQLRKAGweadsktlrfsKGARpEKGRNLAI-AEWPTGKT 280
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
120-256 5.13e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.02  E-value: 5.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 120 LEQRQSTLAALQARV-AELREEQARQTRQVDAQRAL---------NVAQRAAYEALRGRARLQEAALRRLEEEaRDLLER 189
Cdd:COG2268   228 LEQEREIETARIAEAeAELAKKKAEERREAETARAEaeaayeiaeANAEREVQRQLEIAEREREIELQEKEAE-REEAEL 306
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952711695 190 LVQRKARAAAERnLRNERYEKAKQARMSLELKAAAQRTVSISESPNTIGDGIREEG------KTLALMAEPVS 256
Cdd:COG2268   307 EADVRKPAEAEK-QAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMlieklpEIAEAAAKPLE 378
PTZ00421 PTZ00421
coronin; Provisional
315-445 5.25e-05

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 46.04  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 315 VAAQPP---SQVLDVLDahlsevnaVCFGP-NSSLLATGGADRLIHLWNVVGGRLEANQT-----LEGAGGSITSVDFDP 385
Cdd:PTZ00421   64 LASNPPillGQEGPIID--------VAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhLQGHTKKVGIVSFHP 135
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952711695 386 SGSQVLA-ATYNQAAQLWKVGEAQSKETLSGHTDKVTAAKFKLTRHQAVTGSRDRTVKEWD 445
Cdd:PTZ00421  136 SAMNVLAsAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
105-206 6.59e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 6.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  105 QVVAKSAALGALESTLEQRQSTLAALQARVAELREEQAR-QTRQVDAQRALNVAQRAAYEALRGRArLQEAALRRLEEEA 183
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElQDRLEAAEDLARLELRALLEERFAAA-LGDAVERELRENL 771
                           90       100
                   ....*....|....*....|....
gi 1952711695  184 RDLLERLVQRKARAAAE-RNLRNE 206
Cdd:COG4913    772 EERIDALRARLNRAEEElERAMRA 795
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
105-226 6.88e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 6.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  105 QVVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDA----------------QRALNVAQRAAYEALRGR 168
Cdd:COG4913    282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEleaqirgnggdrleqlEREIERLERELEERERRR 361
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952711695  169 ARLQEAaLRRLEEEARDLLERLVQRKARAAAERNLRNERYEKAKQARMSLELKAAAQR 226
Cdd:COG4913    362 ARLEAL-LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
PRK11637 PRK11637
AmiB activator; Provisional
108-174 8.76e-05

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 45.45  E-value: 8.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952711695 108 AKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQralnvAQRAAYEALRGRARLQEA 174
Cdd:PRK11637  216 ERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKAR-----AEREAREAARVRDKQKQA 277
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
412-445 9.31e-05

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 39.99  E-value: 9.31e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1952711695  412 TLSGHTDKVTAAKFKLTRHQAVTGSRDRTVKEWD 445
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
110-219 1.14e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  110 SAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALnvaQRAAYEALRGRARLQEAALR-RLEEEARDLLE 188
Cdd:COG4913    684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE---LDELQDRLEAAEDLARLELRaLLEERFAAALG 760
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1952711695  189 RLVQRKARAAAERNLRNERyEKAKQARMSLE 219
Cdd:COG4913    761 DAVERELRENLEERIDALR-ARLNRAEEELE 790
WD40 pfam00400
WD domain, G-beta repeat;
412-445 1.16e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 1.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1952711695 412 TLSGHTDKVTAAKFKLTRHQAVTGSRDRTVKEWD 445
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
111-201 1.17e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 111 AALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRAlnvAQRAAYEALRGRARLQEAALRRLEEEARDlLERL 190
Cdd:COG4942   153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEE-LEAL 228
                          90
                  ....*....|.
gi 1952711695 191 VQRKARAAAER 201
Cdd:COG4942   229 IARLEAEAAAA 239
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
105-264 1.20e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 105 QVVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQ--------------------------------R 152
Cdd:COG4942    63 RIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqpplalllspedfldavrrlqylK 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 153 ALNVAQRAAYEALRGRARLQEAALRRLEEEARDLLERLVQRKARAAAERNLRNERyeKAKQARMSLELKAAAQRTVSISE 232
Cdd:COG4942   143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER--QKLLARLEKELAELAAELAELQQ 220
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1952711695 233 SPNTIGDGIREEGKTLALMAEPVSPKSEAGEK 264
Cdd:COG4942   221 EAEELEALIARLEAEAAAAAERTPAAGFAALK 252
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
108-226 1.39e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 108 AKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQE--AALRRLEEEARD 185
Cdd:COG4717    78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElpERLEELEERLEE 157
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1952711695 186 LLERLVQRKARAAAERNLRNERYEKAKQ--ARMSLELKAAAQR 226
Cdd:COG4717   158 LRELEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEE 200
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
113-226 1.71e-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: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  113 LGALESTLEQRQSTLAALQARVAELREEQarqtRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEARDLLERLVQ 192
Cdd:COG4913    663 VASAEREIAELEAELERLDASSDDLAALE----EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1952711695  193 RKARAAAERNLR-NERYEKAKQARMSLELKAAAQR 226
Cdd:COG4913    739 AEDLARLELRALlEERFAAALGDAVERELRENLEE 773
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
115-264 1.83e-04

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: 44.56  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 115 ALESTLEQRQSTLAALQARVAELR-----------EEQARQtRQVDAQRA------LNVAQRAAYEALRGRA-RLQEAAL 176
Cdd:pfam15709 323 ALLEKREQEKASRDRLRAERAEMRrleverkrreqEEQRRL-QQEQLERAekmreeLELEQQRRFEEIRLRKqRLEEERQ 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 177 RRLEEEARD-LLERLVQRKARAAAE---RNLRN----------ERYEKAKQARMSLELKAAaqrtvsisespntigdgir 242
Cdd:pfam15709 402 RQEEEERKQrLQLQAAQERARQQQEefrRKLQElqrkkqqeeaERAEAEKQRQKELEMQLA------------------- 462
                         170       180
                  ....*....|....*....|....*..
gi 1952711695 243 EEGKTLALMAEP-----VSPKSEAGEK 264
Cdd:pfam15709 463 EEQKRLMEMAEEerleyQRQKQEAEEK 489
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
105-272 2.40e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 105 QVVAKSAALGALESTLEQRQSTLAALQARVAELREEQAR---QTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEE 181
Cdd:COG4372    88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDleqQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 182 EARDLLERLVQRKARAAAERNLR--NERYEKAKQARMSLELKAAAQRTVSISESPNTIGDGIREEGKTLALMAEPVSPKS 259
Cdd:COG4372   168 ALEQELQALSEAEAEQALDELLKeaNRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
                         170
                  ....*....|...
gi 1952711695 260 EAGEKWLRTFRSA 272
Cdd:COG4372   248 KEELLEEVILKEI 260
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
105-224 2.76e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  105 QVVAKSAALGALESTLEQRQSTLAAL-----QARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRL 179
Cdd:COG4913    256 PIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1952711695  180 EEEARDLLERLVQRKARAAAERNLRNERYEK-AKQARMSLELKAAA 224
Cdd:COG4913    336 GGDRLEQLEREIERLERELEERERRRARLEAlLAALGLPLPASAEE 381
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
113-212 3.65e-04

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


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 41.15  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 113 LGALESTLEQRQS---TLAALQARVAELREEQARQTRQV-DAQRALNVAQrAAYEALRGRARLQEAALRRLEEEARDLLE 188
Cdd:pfam11559  44 LQQRDRDLEFRESlneTIRTLEAEIERLQSKIERLKTQLeDLERELALLQ-AKERQLEKKLKTLEQKLKNEKEELQRLKN 122
                          90       100
                  ....*....|....*....|....
gi 1952711695 189 RLVQRKARAAAERNLRNERYEKAK 212
Cdd:pfam11559 123 ALQQIKTQFAHEVKKRDREIEKLK 146
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-214 3.73e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 3.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  111 AALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEARDLLERL 190
Cdd:COG4913    345 REIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
                           90       100
                   ....*....|....*....|....
gi 1952711695  191 VQRKARAAAERNLRNERYEKAKQA 214
Cdd:COG4913    425 EAEIASLERRKSNIPARLLALRDA 448
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
105-225 4.16e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 105 QVVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRalnvaqRAAYEALRGRARLQEAALRRLEEEAR 184
Cdd:COG3206   271 QLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASL------EAELEALQAREASLQAQLAQLEARLA 344
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1952711695 185 DLLERLVQRkARAAAERNLRNERYEKAKQARMSLELKAAAQ 225
Cdd:COG3206   345 ELPELEAEL-RRLEREVEVARELYESLLQRLEEARLAEALT 384
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
122-225 4.59e-04

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: 42.91  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 122 QRQSTLAALQARVAELRE--EQARQTRQVDAQRALNVAQRAAYEALRGRA---RLQEAALRRLEEE--ARDLLERlvQRK 194
Cdd:TIGR02794  58 QKKPAAKKEQERQKKLEQqaEEAEKQRAAEQARQKELEQRAAAEKAAKQAeqaAKQAEEKQKQAEEakAKQAAEA--KAK 135
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1952711695 195 ARAAAERNLRNeryEKAKQARMSLELKAAAQ 225
Cdd:TIGR02794 136 AEAEAERKAKE---EAAKQAEEEAKAKAAAE 163
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
105-232 6.01e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 6.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  105 QVVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRA-LNVAQ-RAAYEALRG-RARLQEA--ALRRL 179
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeIDVASaEREIAELEAeLERLDASsdDLAAL 690
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1952711695  180 EEEardlLERLVQRKARAAAERNLRNERYEK--AKQARMSLELKAAAQRTVSISE 232
Cdd:COG4913    691 EEQ----LEELEAELEELEEELDELKGEIGRleKELEQAEEELDELQDRLEAAED 741
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
120-201 6.14e-04

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 40.22  E-value: 6.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 120 LEQRQSTLAALQARVAELREEQARQTRQVD--------AQRALNVAQRAAyEALRGRAR------LQEAALR--RLEEEA 183
Cdd:COG3599    29 LDEVAEDYERLIRENKELKEKLEELEEELEeyreleetLQKTLVVAQETA-EEVKENAEkeaeliIKEAELEaeKIIEEA 107
                          90
                  ....*....|....*...
gi 1952711695 184 RDLLERLVQRKARAAAER 201
Cdd:COG3599   108 QEKARKIVREIEELKRQR 125
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
74-229 8.60e-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: 42.63  E-value: 8.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695   74 DSDLVPSsstLRVKWQEEEEgLRLVCGEMAYQVVAK----SAALGALESTLEQRQSTLAALQARVAEL-------REEQA 142
Cdd:COG3096    982 NSDLNEK---LRARLEQAEE-ARREAREQLRQAQAQysqyNQVLASLKSSRDAKQQTLQELEQELEELgvqadaeAEERA 1057
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  143 RQTR-QVDAQRALNVAQRAAYEALRGRARLQ----EAALRRLEEEARDLLERLVQRKARAAAERNL-RNERYEKAKQARM 216
Cdd:COG3096   1058 RIRRdELHEELSQNRSRRSQLEKQLTRCEAEmdslQKRLRKAERDYKQEREQVVQAKAGWCAVLRLaRDNDVERRLHRRE 1137
                          170
                   ....*....|...
gi 1952711695  217 SLELKAAAQRTVS 229
Cdd:COG3096   1138 LAYLSADELRSMS 1150
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
121-226 8.72e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 8.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 121 EQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQ-----RAAYEALR---GRARLQEAALRRLEEEARDLLERLVQ 192
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEereedERILEYLKekaEREEEREAEREEIEEEKEREIARLRA 191
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1952711695 193 RKARAAAER----NLRNERYEKAKQARMSLELKAAAQR 226
Cdd:pfam13868 192 QQEKAQDEKaerdELRAKLYQEEQERKERQKEREEAEK 229
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
115-257 8.95e-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: 8.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 115 ALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRAlnvAQRAAYEALRGRARLQEAALRRLEEEARDLLERLvqrk 194
Cdd:COG3883   140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA---EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA---- 212
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952711695 195 ARAAAERNLRNERYEKAKQARMSLELKAAAQRTVSISESPNTIGDGIREEGKTLALMAEPVSP 257
Cdd:COG3883   213 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAG 275
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
120-226 8.96e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 8.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 120 LEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALR-----------GRARLQEAALRRLEEEA---RD 185
Cdd:pfam13868 161 LKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRaklyqeeqerkERQKEREEAEKKARQRQelqQA 240
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1952711695 186 LLERLVQRKARAAAERNLRNERYEKAKQARMSLELKAAAQR 226
Cdd:pfam13868 241 REEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEA 281
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
115-217 9.85e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 9.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  115 ALESTLEQRQsTLAALQARVAELRE--EQARQTRQVDAQRALNVAQRaayealrgRARLQEAALRRLEEEardlLERLVQ 192
Cdd:COG4913    243 ALEDAREQIE-LLEPIRELAERYAAarERLAELEYLRAALRLWFAQR--------RLELLEAELEELRAE----LARLEA 309
                           90       100
                   ....*....|....*....|....*
gi 1952711695  193 RKARAAAERNLRNERYEKAKQARMS 217
Cdd:COG4913    310 ELERLEARLDALREELDELEAQIRG 334
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
121-226 9.86e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 9.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 121 EQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQR--AAYEALRGRARLQEAALRRLEEEARDLLERLVQRKA--- 195
Cdd:pfam13868  51 EERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRqeEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQlre 130
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1952711695 196 ---RAAAER--------------NLRNERYEKAKQARMslELKAAAQR 226
Cdd:pfam13868 131 eidEFNEEQaewkelekeeereeDERILEYLKEKAERE--EEREAERE 176
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
111-243 9.87e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 9.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 111 AALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEaaLRRLEEEARDLLERL 190
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE--LEALEAELAELPERL 148
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1952711695 191 VQRKARAAAERNLRnERYEKAKQARMSLELKAAAQRTVSISESPNTIGDGIRE 243
Cdd:COG4717   149 EELEERLEELRELE-EELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
87-226 1.14e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.72  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  87 KWQEEEEGLRLVCGEMAYQVVAKSAALGALESTLEQRQSTLAALQArvaelrEEQARQTRQVDAQralnvaQRAAYEAlr 166
Cdd:PRK09510  118 KQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKA------AAEAKKKAEAEAA------KKAAAEA-- 183
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 167 gRARLQEAALRRLEEEARDLLERLVQRKARAAAERnlRNERYEKAKQARMSLELKAAAQR 226
Cdd:PRK09510  184 -KKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKK--KAAAEAKAAAAKAAAEAKAAAEK 240
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
136-216 1.23e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 39.64  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 136 ELREEQARQTRQVDAQRALNVAQRAAYEALRG---RARLQEAALRRLEEEA-------RDLLERLVQ------RKARAAA 199
Cdd:pfam05672  35 LEKEEEERLRKEELRRRAEEERARREEEARRLeeeRRREEEERQRKAEEEAeereqreQEEQERLQKqkeeaeAKAREEA 114
                          90
                  ....*....|....*....
gi 1952711695 200 ERNL--RNERYEKAKQARM 216
Cdd:pfam05672 115 ERQRqeREKIMQQEEQERL 133
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
117-226 1.31e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 117 ESTLEQRQSTLAALQARVAELREEQARQTRQV-----------DAQRALNVAQRAAYEAlrgRARLQEAALRRLEEEARD 185
Cdd:PRK09510  109 ERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKaaaaakakaeaEAKRAAAAAKKAAAEA---KKKAEAEAAKKAAAEAKK 185
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1952711695 186 LLERLVQRKARAAAERNLRNERYEKAKQ---ARMSLELKAAAQR 226
Cdd:PRK09510  186 KAEAEAAAKAAAEAKKKAEAEAKKKAAAeakKKAAAEAKAAAAK 229
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
113-276 1.35e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 113 LGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEARDLLERLVQ 192
Cdd:COG3883   121 LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 193 RKARAAAERNLRNERYEKAKQARMSLELKAAAQRTVSISESPNTIGDGIREEGKTLALMAEPVSPKSEAGEKWLRTFRSA 272
Cdd:COG3883   201 LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAAS 280

                  ....
gi 1952711695 273 SATS 276
Cdd:COG3883   281 AAGG 284
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
111-228 1.42e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 111 AALGALESTLEQRQSTLAALQARVAElrEEQARQTRQVDAQRAlnvAQRAAYEALRGRARLQEAALRRL---EEEARDLL 187
Cdd:pfam13868 187 ARLRAQQEKAQDEKAERDELRAKLYQ--EEQERKERQKEREEA---EKKARQRQELQQAREEQIELKERrlaEEAEREEE 261
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1952711695 188 ERLVQRKARAAAErnlRNERYEKAKQARMSLELKAAAQRTV 228
Cdd:pfam13868 262 EFERMLRKQAEDE---EIEQEEAEKRRMKRLEHRRELEKQI 299
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
83-226 1.61e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  83 TLRVKWQEEEEGLRLVCGEMAYQVVAKSAALGALEsTLEQRqstLAALQARVaELREEQARQTRQVDAQR--ALNVAQRA 160
Cdd:COG4717   351 ELLREAEELEEELQLEELEQEIAALLAEAGVEDEE-ELRAA---LEQAEEYQ-ELKEELEELEEQLEELLgeLEELLEAL 425
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952711695 161 AYEALRGRARLQEAALRRLEEEARDLLERLvqRKARAAAERNLRNERYEKAKQARMSL--ELKAAAQR 226
Cdd:COG4717   426 DEEELEEELEELEEELEELEEELEELREEL--AELEAELEQLEEDGELAELLQELEELkaELRELAEE 491
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
76-225 1.70e-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: 41.86  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695   76 DLVPSSSTLRVKWQEEEEGLRLVCGEMAYQ--VVAKSAALGALESTLEQRQSTLAALQARVAElREEQARQTRQ------ 147
Cdd:COG3096    317 ELSARESDLEQDYQAASDHLNLVQTALRQQekIERYQEDLEELTERLEEQEEVVEEAAEQLAE-AEARLEAAEEevdslk 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  148 ---VDAQRALNVAQRAAYEALRGRARLQEAalRRLEEEARDLLERLVQRKARAAAERNLRNERYEKAKQaRMSLELKAAA 224
Cdd:COG3096    396 sqlADYQQALDVQQTRAIQYQQAVQALEKA--RALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQ-KLSVADAARR 472

                   .
gi 1952711695  225 Q 225
Cdd:COG3096    473 Q 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
115-274 2.02e-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: 41.58  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  115 ALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEardlLERLVQRK 194
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ----KQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  195 ARAAAERNLRNERYEKAKQARmsLELKAAAQRTVSISESPNTIGDGIREEGKTLALMAEPVSPKSEAGEKWLRTFRSASA 274
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKL--DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
84-232 2.07e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  84 LRVKWQEEEEGLRLVCGEMayQVVAKSAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYE 163
Cdd:COG4717   400 LKEELEELEEQLEELLGEL--EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQE 477
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 164 ALRGRARLQEAALRRLE--------EEARDLLERLVQRKARAAAERNLR---NERYEKAKQA-RMSLELKAAAQRTVSIS 231
Cdd:COG4717   478 LEELKAELRELAEEWAAlklalellEEAREEYREERLPPVLERASEYFSrltDGRYRLIRIDeDLSLKVDTEDGRTRPVE 557

                  .
gi 1952711695 232 E 232
Cdd:COG4717   558 E 558
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
115-219 2.12e-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: 41.31  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  115 ALESTLEQRQSTLAALQARVAELR--------EEQARQTRQVDAQRALNVAQRAAYEALRGRARLQE------AALRRLE 180
Cdd:pfam01576  212 KLEGESTDLQEQIAELQAQIAELRaqlakkeeELQAALARLEEETAQKNNALKKIRELEAQISELQEdleserAARNKAE 291
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1952711695  181 EEARDLLERLVQRKAR-------AAAERNLRNERYEKAKQARMSLE 219
Cdd:pfam01576  292 KQRRDLGEELEALKTEledtldtTAAQQELRSKREQEVTELKKALE 337
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
121-227 2.53e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.36  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 121 EQRQstlAALQARVAELREEQARqtrqvdAQRALNVAQRAAYEALRGRARLQEAAlRRLEEEARDLLE---RLVQRKARA 197
Cdd:pfam20492   5 EREK---QELEERLKQYEEETKK------AQEELEESEETAEELEEERRQAEEEA-ERLEQKRQEAEEekeRLEESAEME 74
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1952711695 198 AAER-NLRNERYEK-AKQARMSLELKAAAQRT 227
Cdd:pfam20492  75 AEEKeQLEAELAEAqEEIARLEEEVERKEEEA 106
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
110-226 2.79e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 110 SAALGALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQEAALR---------RLE 180
Cdd:COG3206   218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdviALR 297
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1952711695 181 EEARDLLERLVQRKARAAAErnLRNErYEKAKQARMSLELKAAAQR 226
Cdd:COG3206   298 AQIAALRAQLQQEAQRILAS--LEAE-LEALQAREASLQAQLAQLE 340
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
111-276 3.23e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 111 AALGALESTL---EQRQSTLAALQARVAELREEQARQTRQvdaqralnvaqraaYEALRGRARLQEAALRRLEEEARDLL 187
Cdd:PRK02224  234 ETRDEADEVLeehEERREELETLEAEIEDLRETIAETERE--------------REELAEEVRDLRERLEELEEERDDLL 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 188 ERLVQRKARAAAERNLRNERYEKAKQARMSLElkaaaQRTVSISESPNTIgDGIREEGKTLALMAEPVSPKSEAGEKWLR 267
Cdd:PRK02224  300 AEAGLDDADAEAVEARREELEDRDEELRDRLE-----ECRVAAQAHNEEA-ESLREDADDLEERAEELREEAAELESELE 373

                  ....*....
gi 1952711695 268 TFRSASATS 276
Cdd:PRK02224  374 EAREAVEDR 382
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
115-215 3.94e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 115 ALESTLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRA-----RLQE-----AALRRLE---- 180
Cdd:PRK02224  520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVaelnsKLAElkeriESLERIRtlla 599
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1952711695 181 --EEARDLLERLVQRKArAAAERNlrNERYEKAKQAR 215
Cdd:PRK02224  600 aiADAEDEIERLREKRE-ALAELN--DERRERLAEKR 633
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
141-219 4.36e-03

High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259802 [Multi-domain]  Cd Length: 266  Bit Score: 39.42  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 141 QARQtrqvDAQRALNVAQRAAYEALrGRARlQEAAlrRLEEEARDLLERLVQRkARAAAER--NLRNErYEKAKQA---R 215
Cdd:cd03404   181 AARQ----DKERLINEAQAYANEVI-PRAR-GEAA--RIIQEAEAYKAEVVAR-AEGDAARflALLAE-YRKAPEVtreR 250

                  ....
gi 1952711695 216 MSLE 219
Cdd:cd03404   251 LYLE 254
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
113-219 4.47e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 113 LGALESTLEQRQSTLAALQARVAELREEQARQ-------TRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEARD 185
Cdd:COG4372    47 LEQLREELEQAREELEQLEEELEQARSELEQLeeeleelNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1952711695 186 LLERLVQRKARAAAERNLRNERYEKAKQARMSLE 219
Cdd:COG4372   127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
105-219 4.78e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 39.21  E-value: 4.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 105 QVVAKSAALGALESTLEQRQSTLAALQARVAELREEQA---RQTRQV--------DAQRALNVAQRAAYEALRgRARLQE 173
Cdd:pfam12795  86 RLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSearQRLQQIrnrlngpaPPGEPLSEAQRWALQAEL-AALKAQ 164
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1952711695 174 AALRRLEEEARDLLERLVQrkaraaAERNLRNERYEKAKQARMSLE 219
Cdd:pfam12795 165 IDMLEQELLSNNNRQDLLK------ARRDLLTLRIQRLEQQLQALQ 204
COG4223 COG4223
Uncharacterized conserved protein [Function unknown];
113-199 4.89e-03

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443367 [Multi-domain]  Cd Length: 259  Bit Score: 39.26  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 113 LGALESTLEQRQSTLAALQARVAELREEQ------ARQTRQVDAQRALNVAQRAAYEALRGRArlQEAALRRLEEEARDL 186
Cdd:COG4223     2 IAALEAAVAELPAQLTALEQRLAALEAAPaaaaatAALEARLAALRAALAAAREAVAAAAAAA--LEARLAALEAKAAAP 79
                          90
                  ....*....|...
gi 1952711695 187 LERLVQRKARAAA 199
Cdd:COG4223    80 EAEAAAAARAAAL 92
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
120-257 6.14e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.47  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 120 LEQRQSTLAAL-QARVAELREEQARQTRQVD---------AQRALNVAQRAAYEALRGRARLQEAALRRLEEEArdllER 189
Cdd:COG2268   179 LEDENNYLDALgRRKIAEIIRDARIAEAEAEreteiaiaqANREAEEAELEQEREIETARIAEAEAELAKKKAE----ER 254
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952711695 190 LVQRKARAAAERNLRNERYEKAKQARMSLELkAAAQRTVSISEspntigdgIREEGKTLALMAEPVSP 257
Cdd:COG2268   255 REAETARAEAEAAYEIAEANAEREVQRQLEI-AEREREIELQE--------KEAEREEAELEADVRKP 313
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
110-253 6.25e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 110 SAALGALESTLEQRQSTLAALQARVAELREEQarQTRQVDAQRALNVAQRAAYEALRGRARLQEAALRRLEEEARDLLER 189
Cdd:COG3206   174 RKALEFLEEQLPELRKELEEAEAALEEFRQKN--GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952711695 190 LVQRKARAAAE---RNLRNERYE-KAKQARMSLELKAAAQRTVSISESPNTIGDGIREEGKTLALMAE 253
Cdd:COG3206   252 GPDALPELLQSpviQQLRAQLAElEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
119-223 6.59e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.13  E-value: 6.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695 119 TLEQRQSTLAALQARVAELREEQARQTRQVDAQRALNVAQRAAYEALRGRARLQE----AALRRLEEEARD---LLERLV 191
Cdd:pfam13868 128 LREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKereiARLRAQQEKAQDekaERDELR 207
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1952711695 192 QRKARAAAERNLR-NERYEKAKQARMSLELKAA 223
Cdd:pfam13868 208 AKLYQEEQERKERqKEREEAEKKARQRQELQQA 240
mukB PRK04863
chromosome partition protein MukB;
92-226 7.08e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 7.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695   92 EEGLRLVC---GEMAYQVvAKSAALGALESTLEQRQstLAA-LQARVAELREEQARQTRQVDAQRALNVAQRAAyealrG 167
Cdd:PRK04863   476 EQAYQLVRkiaGEVSRSE-AWDVARELLRRLREQRH--LAEqLQQLRMRLSELEQRLRQQQRAERLLAEFCKRL-----G 547
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952711695  168 RARLQEAALRRLEEEARDLLERLVQRKARAAAER--------NLRNERYEKAKQARMSLELKAAAQR 226
Cdd:PRK04863   548 KNLDDEDELEQLQEELEARLESLSESVSEARERRmalrqqleQLQARIQRLAARAPAWLAAQDALAR 614
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
111-226 8.78e-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: 39.55  E-value: 8.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  111 AALGALE---STLEQRQSTLAALQARVAELREEQARQTRQVDaqrALN-VAQRAAYEAlrgrarLQEAAlrRLEEEARDL 186
Cdd:COG3096    917 KALAQLEplvAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIF---ALSeVVQRRPHFS------YEDAV--GLLGENSDL 985
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952711695  187 LERLVQRKARAAAERNLRNE-------RYEKAKQARMSL---------ELKAAAQR 226
Cdd:COG3096    986 NEKLRARLEQAEEARREAREqlrqaqaQYSQYNQVLASLkssrdakqqTLQELEQE 1041
mukB PRK04863
chromosome partition protein MukB;
74-229 9.06e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 9.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695   74 DSDLVPSsstLRVKwQEEEEGLRLVCGEMAYQVVAK----SAALGALESTLEQRQSTLAALQARVAEL-------REEQA 142
Cdd:PRK04863   983 NSDLNEK---LRQR-LEQAEQERTRAREQLRQAQAQlaqyNQVLASLKSSYDAKRQMLQELKQELQDLgvpadsgAEERA 1058
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952711695  143 RQTR-QVDAQRALNVAQRAAYEALRGR--ARLQEAA--LRRLEEEARDLLERLVQRKAR-AAAERNLRNERYEKAKQARM 216
Cdd:PRK04863  1059 RARRdELHARLSANRSRRNQLEKQLTFceAEMDNLTkkLRKLERDYHEMREQVVNAKAGwCAVLRLVKDNGVERRLHRRE 1138
                          170
                   ....*....|...
gi 1952711695  217 SLELKAAAQRTVS 229
Cdd:PRK04863  1139 LAYLSADELRSMS 1151
 
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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