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Conserved domains on  [gi|578821839|ref|XP_006718795|]
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protein Atg16l2 isoform X2 [Homo sapiens]

Protein Classification

WD repeat ATG16 family protein( domain architecture ID 12095058)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 310-598 1.49e-56

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: 192.16  E-value: 1.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 310 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 389
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 390 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 466
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 467 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 545
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578821839 546 SCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 598
Cdd:cd00200  238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 32-203 1.18e-55

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: 185.91  E-value: 1.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839   32 LFLELVPAYNHLLEKAELLDKFSKKLQPEPNSVTPTTHQGPWEESELDSDQVPSLVALRVKWQEEEEGLRLVCGEMAYQV 111
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  112 VEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL 191
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|..
gi 578821839  192 LERLVQRKARAA 203
Cdd:pfam08614 161 VERWMKRKGQEA 172
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 310-598 1.49e-56

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: 192.16  E-value: 1.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 310 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 389
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 390 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 466
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 467 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 545
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578821839 546 SCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 598
Cdd:cd00200  238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 32-203 1.18e-55

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: 185.91  E-value: 1.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839   32 LFLELVPAYNHLLEKAELLDKFSKKLQPEPNSVTPTTHQGPWEESELDSDQVPSLVALRVKWQEEEEGLRLVCGEMAYQV 111
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  112 VEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL 191
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|..
gi 578821839  192 LERLVQRKARAA 203
Cdd:pfam08614 161 VERWMKRKGQEA 172
WD40 COG2319
WD40 repeat [General function prediction only];
310-598 1.97e-51

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 182.03  E-value: 1.97e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 310 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 389
Cdd:COG2319  115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 390 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcgDHIIISGHNDQ 462
Cdd:COG2319  193 TGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTltghsgsVRSVAFSPD----GRLLASGSADG 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 463 KIRFWDSRGPHCTQVIPVQ-GRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcgSDWTKAV-FSPDRS 540
Cdd:COG2319  269 TVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH-----TGAVRSVaFSPDGK 343

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578821839 541 YALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 598
Cdd:COG2319  344 TLASGSDDGTVRLWDLATGELLRTLTG-HTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 120-203 1.86e-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: 88.78  E-value: 1.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 120 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 199
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80


                 ....
gi 578821839 200 ARAA 203
Cdd:cd22887   81 QQEA 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-231 5.21e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 5.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  92 KWQEEEEGLRLVcgEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALR 171
Cdd:COG1196  217 ELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 172 AHVGLREAALRRLQEEARDLLERLVQRKARAAAerNLRNERRERAKQARVSQELKKAAKR 231
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAE--LEEELEELEEELEELEEELEEAEEE 352
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 310-343 8.72e-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: 45.77  E-value: 8.72e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 578821839   310 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 343
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
310-343 1.76e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.64  E-value: 1.76e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 578821839  310 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 343
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 318-513 1.53e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 318 VNAVRFGPNSSLLATGGADRLIHLWN----VVGSRLEANQTLEGAGGS-ITSVDFDPS-GYQVLAATYNQAAQLWKVGEA 391
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICWNSYiKSQVASSNFEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 392 QSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSycnDVVC------GDHIIISGHNDQKI 464
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpseSGRSLAFGSADHKV 642

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578821839 465 RFWDSRGPH---CTQVipvqGRVTSLSLSH--DQLHLLSCSRDNTLKVIDLRVS 513
Cdd:PLN00181 643 YYYDLRNPKlplCTMI----GHSKTVSYVRfvDSSTLVSSSTDNTLKLWDLSMS 692
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-224 1.32e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839    94 QEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRah 173
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR-- 809

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578821839   174 vglreAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQE 224
Cdd:TIGR02168  810 -----AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
PTZ00121 PTZ00121
MAEBL; Provisional
 94-291 5.06e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839   94 QEEEEGLRlvcGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVA-QLREA----RAQQAQQVEEWRAQNAVQRAAYE 168
Cdd:PTZ00121 1237 KDAEEAKK---AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdELKKAeekkKADEAKKAEEKKKADEAKKKAEE 1313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  169 ALRAHvglreaALRRLQEEARDLLERLvQRKARAA--AERNLRNERRERAKQARVSQELKKAAK-RTVSISEGPDTLGDG 245
Cdd:PTZ00121 1314 AKKAD------EAKKKAEEAKKKADAA-KKKAEEAkkAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKADAAKKK 1386

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578821839  246 MRERRETLALAPEPEPLEKEAcEKWKRPFSFKKRRGHSIGGAPEQR 291
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKA-DELKKAAAAKKKADEAKKKAEEKK 1431
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 310-598 1.49e-56

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: 192.16  E-value: 1.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 310 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 389
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 390 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 466
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 467 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 545
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578821839 546 SCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 598
Cdd:cd00200  238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 32-203 1.18e-55

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: 185.91  E-value: 1.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839   32 LFLELVPAYNHLLEKAELLDKFSKKLQPEPNSVTPTTHQGPWEESELDSDQVPSLVALRVKWQEEEEGLRLVCGEMAYQV 111
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  112 VEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL 191
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|..
gi 578821839  192 LERLVQRKARAA 203
Cdd:pfam08614 161 VERWMKRKGQEA 172
WD40 COG2319
WD40 repeat [General function prediction only];
310-598 1.97e-51

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 182.03  E-value: 1.97e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 310 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 389
Cdd:COG2319  115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 390 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcgDHIIISGHNDQ 462
Cdd:COG2319  193 TGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTltghsgsVRSVAFSPD----GRLLASGSADG 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 463 KIRFWDSRGPHCTQVIPVQ-GRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcgSDWTKAV-FSPDRS 540
Cdd:COG2319  269 TVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH-----TGAVRSVaFSPDGK 343

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578821839 541 YALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 598
Cdd:COG2319  344 TLASGSDDGTVRLWDLATGELLRTLTG-HTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
WD40 COG2319
WD40 repeat [General function prediction only];
299-597 2.46e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 173.56  E-value: 2.46e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 299 VAARLPTRAQDVLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEAnqTLEGAGGSITSVDFDPSGYQVLAAT 378
Cdd:COG2319   62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLR--TLTGHTGAVRSVAFSPDGKTLASGS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 379 YNQAAQLWKVGEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcg 451
Cdd:COG2319  140 ADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTltghtgaVRSVAFSPD---- 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 452 DHIIISGHNDQKIRFWDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcgSDW 530
Cdd:COG2319  216 GKLLASGSADGTVRLWDLATGKLLRTLTGhSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH-----SGG 290

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578821839 531 TKAV-FSPDRSYALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLW 597
Cdd:COG2319  291 VNSVaFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKTLASGSDDGTVRLW 357
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 353-598 2.83e-41

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 150.95  E-value: 2.83e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 353 QTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVGEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGR 432
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 433 AYCSRTINvlSYCNDVVCGD-----HIIISGHNDQKIRFWDSRGPHCTQVIP-VQGRVTSLSLSHDQLHLLSCSRDNTLK 506
Cdd:cd00200   83 GECVRTLT--GHTSYVSSVAfspdgRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAFSPDGTFVASSSQDGTIK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 507 VIDLRVSNIRQVFraDGFKcgsDWTKAV-FSPDRSYALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHM 585
Cdd:cd00200  161 LWDLRTGKCVATL--TGHT---GEVNSVaFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRG-HENGVNSVAFSPDGYLL 234

                        250
                 ....*....|...
gi 578821839 586 VSVDQGRKVVLWQ 598
Cdd:cd00200  235 ASGSEDGTIRVWD 247
WD40 COG2319
WD40 repeat [General function prediction only];
299-597 4.23e-40

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 150.83  E-value: 4.23e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 299 VAARLPTRAQDVLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEAnqTLEGAGGSITSVDFDPSGYQVLAAT 378
Cdd:COG2319   20 LLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLA--TLLGHTAAVLSVAFSPDGRLLASAS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 379 YNQAAQLWKVGEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcg 451
Cdd:COG2319   98 ADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTltghsgaVTSVAFSPD---- 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 452 DHIIISGHNDQKIRFWDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcgSDW 530
Cdd:COG2319  174 GKLLASGSDDGTVRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGH-----SGS 248

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578821839 531 TKAV-FSPDRSYALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLW 597
Cdd:COG2319  249 VRSVaFSPDGRLLASGSADGTVRLWDLATGELLRTLTG-HSGGVNSVAFSPDGKLLASGSDDGTVRLW 315
WD40 COG2319
WD40 repeat [General function prediction only];
310-558 1.50e-38

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 146.59  E-value: 1.50e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 310 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 389
Cdd:COG2319  157 TLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLL--RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 390 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTinvLSYCNDVVCG------DHIIISGHNDQK 463
Cdd:COG2319  235 TGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT---LTGHSGGVNSvafspdGKLLASGSDDGT 311

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 464 IRFWDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRAdgfkcGSDWTKAV-FSPDRSY 541
Cdd:COG2319  312 VRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTG-----HTGAVTSVaFSPDGRT 386

                        250
                 ....*....|....*..
gi 578821839 542 ALAGSCDGALYIWDVDT 558
Cdd:COG2319  387 LASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
322-598 6.12e-31

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 125.02  E-value: 6.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 322 RFGPNSSLLATGGADRLIHLWNVVGSRLEAnqTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVGEAQSKETLSGHK 401
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLL--LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 402 DKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVL-SYCNDVVC--GDHIIISGHNDQKIRFWDSRGPHCTQVI 478
Cdd:COG2319   79 AAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHtGAVRSVAFspDGKTLASGSADGTVRLWDLATGKLLRTL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 479 PV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcgSDWTKAV-FSPDRSYALAGSCDGALYIWDV 556
Cdd:COG2319  159 TGhSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH-----TGAVRSVaFSPDGKLLASGSADGTVRLWDL 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 578821839 557 DTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 598
Cdd:COG2319  234 ATGKLLRTLTG-HSGSVRSVAFSPDGRLLASGSADGTVRLWD 274
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 120-203 1.86e-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: 88.78  E-value: 1.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 120 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 199
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80


                 ....
gi 578821839 200 ARAA 203
Cdd:cd22887   81 QQEA 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-231 5.21e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 5.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  92 KWQEEEEGLRLVcgEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALR 171
Cdd:COG1196  217 ELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 172 AHVGLREAALRRLQEEARDLLERLVQRKARAAAerNLRNERRERAKQARVSQELKKAAKR 231
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAE--LEEELEELEEELEELEEELEEAEEE 352
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 94-256 2.48e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  94 QEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAH 173
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 174 VGLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKRTVSISEGPDTLGDGMRERRETL 253
Cdd:COG1196  395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE--EALEEAAEEEAELEEEEEALLELLAELLEEA 472


                 ...
gi 578821839 254 ALA 256
Cdd:COG1196  473 ALL 475
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
92-237 4.54e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 4.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839   92 KWQEEEEGLRLVCGEMAYQVVEK-----GAALGTLESELQQRQSRLAALEARVAQLREARAQQ-AQQVEEWRAQNAV--- 162
Cdd:COG4913   273 ELEYLRAALRLWFAQRRLELLEAeleelRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERler 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  163 -------QRAAYEALRAHVGLR----EAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQAR--VSQELKKAA 229
Cdd:COG4913   353 eleererRRARLEALLAALGLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELreLEAEIASLE 432


                  ....*...
gi 578821839  230 KRTVSISE 237
Cdd:COG4913   433 RRKSNIPA 440
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 310-343 8.72e-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: 45.77  E-value: 8.72e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 578821839   310 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 343
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
310-343 1.76e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.64  E-value: 1.76e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 578821839  310 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 343
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
110-233 3.48e-06

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 49.28  E-value: 3.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 110 QVVEKGAALGTLESElqQRQSRLAALEARVAQLrEARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQ---- 185
Cdd:COG1566   65 DRVKKGQVLARLDPT--DLQAALAQAEAQLAAA-EAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQalyk 141

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578821839 186 ---------EEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTV 233
Cdd:COG1566  142 kgavsqqelDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAAL 198
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 110-196 1.24e-05

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 47.63  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 110 QVVEKGAALGTLESELQQrqsrlAALEARVAQLREARAQ------QAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRR 183
Cdd:COG0845   43 DRVKKGQVLARLDPPDLQ-----AALAQAQAQLAAAQAQlelakaELERYKALLKKGAVSQQELDQAKAALDQAQAALAA 117

                         90
                 ....*....|....*.
gi 578821839 184 LQ---EEARDLLERLV 196
Cdd:COG0845  118 AQaalEQARANLAYTT 133
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 318-513 1.53e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 318 VNAVRFGPNSSLLATGGADRLIHLWN----VVGSRLEANQTLEGAGGS-ITSVDFDPS-GYQVLAATYNQAAQLWKVGEA 391
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICWNSYiKSQVASSNFEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 392 QSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSycnDVVC------GDHIIISGHNDQKI 464
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpseSGRSLAFGSADHKV 642

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578821839 465 RFWDSRGPH---CTQVipvqGRVTSLSLSH--DQLHLLSCSRDNTLKVIDLRVS 513
Cdd:PLN00181 643 YYYDLRNPKlplCTMI----GHSKTVSYVRfvDSSTLVSSSTDNTLKLWDLSMS 692
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 121-204 2.06e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 121 LESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKA 200
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104


                 ....
gi 578821839 201 RAAA 204
Cdd:COG4942  105 ELAE 108
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
118-265 4.14e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 118 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQ 197
Cdd:COG4372   82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578821839 198 RKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKE 265
Cdd:COG4372  162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 74-224 4.15e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  74 EESELDSDQVPSLVALRVKWQEEEEGLRLVCGEMAYQVVEKGAALGTLESE-----------------LQQRQSRlaaLE 136
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAElarleqdiarleerrreLEERLEE---LE 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 137 ARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERA 216
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402


                 ....*...
gi 578821839 217 KQARVSQE 224
Cdd:COG1196  403 EELEEAEE 410
WD40 pfam00400
WD domain, G-beta repeat;
396-429 9.20e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.02  E-value: 9.20e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 578821839  396 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 429
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 396-429 1.04e-04

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 39.99  E-value: 1.04e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 578821839   396 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 429
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
120-204 1.11e-04

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 43.66  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 120 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQR- 198
Cdd:COG1842   95 ELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKi 174


                 ....*....
gi 578821839 199 ---KARAAA 204
Cdd:COG1842  175 eemEARAEA 183
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-224 1.32e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839    94 QEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRah 173
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR-- 809

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578821839   174 vglreAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQE 224
Cdd:TIGR02168  810 -----AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
116-237 1.46e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 116 AALGTLESELQQRQSRLAALEARVAQLREARAQ---------QAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQE 186
Cdd:COG3206  219 QQLSELESQLAEARAELAEAEARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA 298

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578821839 187 EARDLLERLVQRKARAAAeRNLRNERRERAKQARVSQELKKAAKRTVSISE 237
Cdd:COG3206  299 QIAALRAQLQQEAQRILA-SLEAELEALQAREASLQAQLAQLEARLAELPE 348
PTZ00421 PTZ00421
coronin; Provisional
 321-429 1.50e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.50  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 321 VRFGP-NSSLLATGGADRLIHLWNVVGSRLEANQT-----LEGAGGSITSVDFDPSGYQVLA-ATYNQAAQLWKVGEAQS 393
Cdd:PTZ00421  81 VAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhLQGHTKKVGIVSFHPSAMNVLAsAGADMVVNVWDVERGKA 160

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 578821839 394 KETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 429
Cdd:PTZ00421 161 VEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 121-254 1.81e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839   121 LESELQQRQSRLAALEARVAQLREARA---QQAQQVE----EWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLE 193
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEdlrAELEEVDkefaETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578821839   194 RLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKRTVSISEGPDTLGDGMRERRETLA 254
Cdd:TIGR02169  421 ELADLNAAIAGIEAKINELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
129-231 3.52e-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: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  129 QSRLAALEARVAQLREARAQ---QAQQVEEWRAQNAVQRAAYEALRAH------VGLREAALRRLQEEARDL------LE 193
Cdd:COG4913   609 RAKLAALEAELAELEEELAEaeeRLEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLdassddLA 688

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 578821839  194 RLVQR--KARAAAERNLRNERRERAKQARVSQELKKAAKR 231
Cdd:COG4913   689 ALEEQleELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-195 4.47e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 4.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839    94 QEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAH 173
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923

                           90       100
                   ....*....|....*....|..
gi 578821839   174 VGLREAALRRLQEEARDLLERL 195
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDNLQERL 945
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
86-204 4.74e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 4.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  86 LVALRVKWQEEEEGLRLVcgEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQA---QQVEEWRAQ--- 159
Cdd:COG4717  104 LEELEAELEELREELEKL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeleAELAELQEElee 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578821839 160 ----------NAVQRAA--YEALRAHVGLREAALRRLQEEARDLLERLVQRKARAAA 204
Cdd:COG4717  182 lleqlslateEELQDLAeeLEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
118-200 4.75e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 4.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  118 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHvGLREAALRRLQEEARDLLERLVQ 197
Cdd:COG4913   663 VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL-EKELEQAEEELDELQDRLEAAED 741


                  ...
gi 578821839  198 RKA 200
Cdd:COG4913   742 LAR 744
PTZ00121 PTZ00121
MAEBL; Provisional
 94-291 5.06e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839   94 QEEEEGLRlvcGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVA-QLREA----RAQQAQQVEEWRAQNAVQRAAYE 168
Cdd:PTZ00121 1237 KDAEEAKK---AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdELKKAeekkKADEAKKAEEKKKADEAKKKAEE 1313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  169 ALRAHvglreaALRRLQEEARDLLERLvQRKARAA--AERNLRNERRERAKQARVSQELKKAAK-RTVSISEGPDTLGDG 245
Cdd:PTZ00121 1314 AKKAD------EAKKKAEEAKKKADAA-KKKAEEAkkAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKADAAKKK 1386

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578821839  246 MRERRETLALAPEPEPLEKEAcEKWKRPFSFKKRRGHSIGGAPEQR 291
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKA-DELKKAAAAKKKADEAKKKAEEKK 1431
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 116-204 6.07e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 6.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 116 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL---L 192
Cdd:COG4942  150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELealI 229

                         90
                 ....*....|..
gi 578821839 193 ERLVQRKARAAA 204
Cdd:COG4942  230 ARLEAEAAAAAE 241
PTZ00121 PTZ00121
MAEBL; Provisional
 122-278 6.16e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 6.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  122 ESELQQRQSRLAALEARVAQLREA-----RAQQAQQVEEWRaQNAVQRAAYEALRAHVGLREAALR----RLQEEARDLL 192
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAeeakkDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAAIKaeeaRKADELKKAE 1287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  193 ERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACEKWKR 272
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367


                  ....*.
gi 578821839  273 PFSFKK 278
Cdd:PTZ00121 1368 AAEKKK 1373
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
81-198 6.24e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 6.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  81 DQVPSLVALRVKWQEEEEGLRLVCGEMayQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQN 160
Cdd:COG4717  392 EQAEEYQELKEELEELEEQLEELLGEL--EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 578821839 161 AVQRAAYEALRAhvglrEAALRRLQEE------ARDLLERLVQR 198
Cdd:COG4717  470 ELAELLQELEEL-----KAELRELAEEwaalklALELLEEAREE 508
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 481-509 6.29e-04

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 37.68  E-value: 6.29e-04
                           10        20
                   ....*....|....*....|....*....
gi 578821839   481 QGRVTSLSLSHDQLHLLSCSRDNTLKVID 509
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 110-286 7.86e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 7.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839   110 QVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEAR 189
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839   190 DL---LERLVQRKARAAAERNLrnerrerAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEA 266
Cdd:TIGR02168  397 SLnneIERLEARLERLEDRRER-------LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469

                          170       180
                   ....*....|....*....|
gi 578821839   267 CEKWKRPFSFKKRRGHSIGG 286
Cdd:TIGR02168  470 LEEAEQALDAAERELAQLQA 489
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 110-281 8.17e-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: 42.06  E-value: 8.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 110 QVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEW-RAQNAVQRAAYEALRAHVGLREAALRRLQ--- 185
Cdd:COG4942   63 RIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlRALYRLGRQPPLALLLSPEDFLDAVRRLQylk 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 186 ----------EEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTV------SISEGPDTLGDGMRER 249
Cdd:COG4942  143 ylaparreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLlarlekELAELAAELAELQQEA 222

                        170       180       190
                 ....*....|....*....|....*....|....
gi 578821839 250 REtlaLAPEPEPLEKEACEKWKRPFS--FKKRRG 281
Cdd:COG4942  223 EE---LEALIARLEAEAAAAAERTPAagFAALKG 253
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 558-597 1.30e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 36.52  E-value: 1.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 578821839   558 TGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLW 597
Cdd:smart00320   1 SGELLKTLKG-HTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
110-204 1.32e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  110 QVVEKGAALGTLES------ELQQRQSRLAALEARVAQLREAR---AQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAA 180
Cdd:COG4913   642 ALQERREALQRLAEyswdeiDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721

                          90       100
                  ....*....|....*....|....
gi 578821839  181 LRRLQEEARDLLERLVQRKARAAA 204
Cdd:COG4913   722 LEQAEEELDELQDRLEAAEDLARL 745
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 110-190 1.33e-03

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 41.15  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  110 QVVEKGAALGTLESELQQrqsrlAALEARVAQLREARAQ------QAQQVEEWRAQNAV-------QRAAYEALRAHVGL 176
Cdd:TIGR01730  46 QKVKKGQVLARLDDDDYQ-----LALQAALAQLAAAEAQlelaqrSFERAERLVKRNAVsqadlddAKAAVEAAQADLEA 120

                          90
                  ....*....|....
gi 578821839  177 REAALRRLQEEARD 190
Cdd:TIGR01730 121 AKASLASAQLNLRY 134
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 124-245 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 578821839 124 ELQQRQSRL----AALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 199
Cdd:COG3883  137 ELKADKAELeakkAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 578821839 200 ARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDG 245
Cdd:COG3883  217 AAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSA 262
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-231 1.49e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  95 EEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHV 174
Cdd:COG1196  641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578821839 175 GLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKR 231
Cdd:COG1196  721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE--RELERLERE 775
PRK12704 PRK12704
phosphodiesterase; Provisional
 121-195 1.68e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578821839 121 LESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERL 195
Cdd:PRK12704  73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
112-231 1.71e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 112 VEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNA----VQRAAYEALRAHVGLREAALRRLQEE 187
Cdd:COG4717  121 LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAelaeLQEELEELLEQLSLATEEELQDLAEE 200

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 578821839 188 ARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKR 231
Cdd:COG4717  201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
PRK09039 PRK09039
peptidoglycan -binding protein;
105-190 1.85e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 105 GEMAYQVVEKGAALGTLESELQQRQS-------RLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLR 177
Cdd:PRK09039  77 QDLQDSVANLRASLSAAEAERSRLQAllaelagAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAAL 156

                         90
                 ....*....|...
gi 578821839 178 EAALRrlQEEARD 190
Cdd:PRK09039 157 EAALD--ASEKRD 167
WD40 pfam00400
WD domain, G-beta repeat;
481-509 1.94e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 1.94e-03
                          10        20
                  ....*....|....*....|....*....
gi 578821839  481 QGRVTSLSLSHDQLHLLSCSRDNTLKVID 509
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 92-226 1.99e-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: 41.20  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839    92 KWQEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQ------------ 159
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerledrrerlq 420

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578821839   160 ---NAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQ--ARVSQELK 226
Cdd:TIGR02168  421 qeiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERelAQLQARLD 492
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
113-254 2.12e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 113 EKGAALGTLESELQQRQSRLAALEARVAQLREAR--AQQAQQVEEwRAQNAVQRAAYEalRAHVGLREAALRRLQEEARD 190
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEE-RREDLEELIAER--RETIEEKRERAEELRERAAE 548

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578821839 191 LLE-----RLVQRKARAAAERNLRNERRERAKQARVSQE---LKKAAKRTVSISEGPDTLGDgMRERRETLA 254
Cdd:PRK02224 549 LEAeaeekREAAAEAEEEAEEAREEVAELNSKLAELKERiesLERIRTLLAAIADAEDEIER-LREKREALA 619
PTZ00121 PTZ00121
MAEBL; Provisional
 112-279 2.59e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  112 VEKGAALGTLESELQQRQSRLAALEARVAQLReaRAQQAQQVEEWRAQNAVQRAAYEALRAHvGLREAALRRLQEEARdl 191
Cdd:PTZ00121 1187 VRKAEELRKAEDARKAEAARKAEEERKAEEAR--KAEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEAR-- 1261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  192 LERLVQRKARAAAERNLRNERRERAKQARVSQELKKA-AKRTVsisegpDTLGDGMRERRETLALAPEPEPLEKEACEKW 270
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAeEKKKA------DEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335


                  ....*....
gi 578821839  271 KRPFSFKKR 279
Cdd:PTZ00121 1336 KKAEEAKKA 1344
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
124-269 2.69e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  124 ELQQRQSRLAALEARVAQLREARAQQAqqVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERL----VQRK 199
Cdd:COG4913   263 RYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgngGDRL 340

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  200 ARAAAernlrNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACEK 269
Cdd:COG4913   341 EQLER-----EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
113-231 3.06e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 113 EKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQR--AAYEALRAHVGLREAALRRLQEEARD 190
Cdd:COG4717   78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEE 157

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 578821839 191 LLERLVQRKARAAAERNLRNERRERAKQ--ARVSQELKKAAKR 231
Cdd:COG4717  158 LRELEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEE 200
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 15-201 4.08e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839    15 KRHIVRQLRLRDRTQKALFLELVPAYNHLLEKAELLDKFSKKLQPEpnsVTPTTHQGPWEESELDS-DQVPSLVALRVKW 93
Cdd:TIGR02169  207 REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE---LEKLTEEISELEKRLEEiEQLLEELNKKIKD 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839    94 QEEEEGLRLV--CGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALR 171
Cdd:TIGR02169  284 LGEEEQLRVKekIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363

                          170       180       190
                   ....*....|....*....|....*....|
gi 578821839   172 AHVGLREAALRRLQEEARDLLERLVQRKAR 201
Cdd:TIGR02169  364 EELEDLRAELEEVDKEFAETRDELKDYREK 393
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 118-204 4.25e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 4.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 118 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHV-GLREAALRRLQEEARDLLERLV 196
Cdd:COG1579  105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELeAEREELAAKIPPELLALYERIR 184


                 ....*...
gi 578821839 197 QRKARAAA 204
Cdd:COG1579  185 KRKNGLAV 192
mukB PRK04863
chromosome partition protein MukB;
2-201 5.43e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839    2 AGPGVPGAPAARWKRHIVRQLRlrdrTQKALFLELVPAYNHL--LEKA--------ELLDKFSKKLQpepnsvtptthQG 71
Cdd:PRK04863  485 IAGEVSRSEAWDVARELLRRLR----EQRHLAEQLQQLRMRLseLEQRlrqqqraeRLLAEFCKRLG-----------KN 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839   72 PWEESELDsdqvpslvALRVKWQEEEEGLRlvcgEMAYQVVEKGAALGTLESELQQRQSRLAALE-------ARVAQLRE 144
Cdd:PRK04863  550 LDDEDELE--------QLQEELEARLESLS----ESVSEARERRMALRQQLEQLQARIQRLAARApawlaaqDALARLRE 617

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578821839  145 ARAQQ---AQQVEEWRAQNAVQRAAYEALRAHVglrEAALRRLQEEARDL-------LERLVQRKAR 201
Cdd:PRK04863  618 QSGEEfedSQDVTEYMQQLLERERELTVERDEL---AARKQALDEEIERLsqpggseDPRLNALAER 681
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 106-231 7.14e-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: 7.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839  106 EMAYQVVEKGAAlgtleselqqRQSRLAALEARVAQLREARAQQAQqveewrAQNAvqraayEALRAHVGLREAALRRlQ 185
Cdd:COG3096   475 EKAYELVCKIAG----------EVERSQAWQTARELLRRYRSQQAL------AQRL------QQLRAQLAELEQRLRQ-Q 531

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 578821839  186 EEARDLLERLVQRKAR--AAAERNLRNERRERAKQARVSQELKKAAKR 231
Cdd:COG3096   532 QNAERLLEEFCQRIGQqlDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
FliJ pfam02050
Flagellar FliJ protein;
86-190 9.45e-03

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 36.49  E-value: 9.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839   86 LVALRVKWQEEEEGLRLVCGEMA-YQVVEKGAALGTLESELQQRQSRLAalearvaQLREARAQQAQQVEEWRAQNAVQR 164
Cdd:pfam02050   7 LAEAQRELQQAEEKLEELQQYRAeYQQQLSGAGQGISAAELRNYQAFIS-------QLDEAIAQQQQELAQAEAQVEKAR 79

                          90       100
                  ....*....|....*....|....*.
gi 578821839  165 AAYEALRahvgLREAALRRLQEEARD 190
Cdd:pfam02050  80 EEWQEAR----QERKSLEKLREREKK 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-232 9.45e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 9.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 116 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRA----HVGLREAALRRLQEEARDL 191
Cdd:COG1196  442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEaeadYEGFLEGVKAALLLAGLRG 521

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578821839 192 LERLVQ-------------RKARAAAERNLRNERRERAKQARVSQELKKAAKRT 232
Cdd:COG1196  522 LAGAVAvligveaayeaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
118-200 9.55e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 9.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821839 118 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQnavqraaYEALRAHVGLREAALRRLQEEARDLLERLVQ 197
Cdd:COG4372   47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ-------LQAAQAELAQAQEELESLQEEAEELQEELEE 119


                 ...
gi 578821839 198 RKA 200
Cdd:COG4372  120 LQK 122
 
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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