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Conserved domains on  [gi|767968965|ref|XP_011543635|]
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protein Atg16l2 isoform X5 [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 ...
 225-513 1.26e-55

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: 187.93  E-value: 1.26e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 304
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 305 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 381
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 382 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 460
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767968965 461 SCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 513
Cdd:cd00200  238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 1-97 1.13e-28

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: 111.56  E-value: 1.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    1 MAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQE 80
Cdd:pfam08614  76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEK 155

                          90
                  ....*....|....*..
gi 767968965   81 EARDLLERLVQRKARAA 97
Cdd:pfam08614 156 ENRELVERWMKRKGQEA 172
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 15-189 3.77e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    15 LESELQQRQSRLAALEARVAQLREARA---QQAQQVE----EWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLE 87
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEdlrAELEEVDkefaETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    88 RLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKRTVSISEGPDTLGDGMRERRETL--------ALAPEPEPLEKE 159
Cdd:TIGR02169  421 ELADLNAAIAGIEAKINELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQELYDLKEEYdrvekelsKLQRELAEAEAQ 498

                          170       180       190
                   ....*....|....*....|....*....|
gi 767968965   160 AcEKWKRPFRSASATSLTLSHCVDVVKGLL 189
Cdd:TIGR02169  499 A-RASEERVRGGRAVEEVLKASIQGVHGTV 527
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 225-513 1.26e-55

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: 187.93  E-value: 1.26e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 304
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 305 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 381
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 382 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 460
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767968965 461 SCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 513
Cdd:cd00200  238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
225-513 1.20e-50

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.18  E-value: 1.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 304
Cdd:COG2319  115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 305 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcgDHIIISGHNDQ 377
Cdd:COG2319  193 TGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTltghsgsVRSVAFSPD----GRLLASGSADG 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 378 KIRFWDSRGPHCTQVIPVQ-GRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSY 456
Cdd:COG2319  269 TVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS----VAFSPDGKT 344

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767968965 457 ALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 513
Cdd:COG2319  345 LASGSDDGTVRLWDLATGELLRTLTG-HTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 1-97 1.13e-28

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: 111.56  E-value: 1.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    1 MAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQE 80
Cdd:pfam08614  76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEK 155

                          90
                  ....*....|....*..
gi 767968965   81 EARDLLERLVQRKARAA 97
Cdd:pfam08614 156 ENRELVERWMKRKGQEA 172
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 14-97 4.14e-22

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: 90.32  E-value: 4.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  14 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 93
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80


                 ....
gi 767968965  94 ARAA 97
Cdd:cd22887   81 QQEA 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 10-125 1.30e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  10 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERL 89
Cdd:COG1196  239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767968965  90 VQRKARAAAerNLRNERRERAKQARVSQELKKAAKR 125
Cdd:COG1196  319 EELEEELAE--LEEELEELEEELEELEEELEEAEEE 352
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 225-258 1.27e-06

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: 45.00  E-value: 1.27e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767968965   225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 258
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
225-258 3.31e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.87  E-value: 3.31e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767968965  225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 258
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 233-428 1.22e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 233 VNAVRFGPNSSLLATGGADRLIHLWN----VVGSRLEANQTLEGAGGS-ITSVDFDPS-GYQVLAATYNQAAQLWKVGEA 306
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICWNSYiKSQVASSNFEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 307 QSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSycnDVVC------GDHIIISGHNDQKI 379
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpseSGRSLAFGSADHKV 642

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767968965 380 RFWDSRGPH---CTQVipvqGRVTSLSLSH--DQLHLLSCSRDNTLKVIDLRVS 428
Cdd:PLN00181 643 YYYDLRNPKlplCTMI----GHSKTVSYVRfvDSSTLVSSSTDNTLKLWDLSMS 692
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 15-189 3.77e-05

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: 46.60  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    15 LESELQQRQSRLAALEARVAQLREARA---QQAQQVE----EWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLE 87
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEdlrAELEEVDkefaETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    88 RLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKRTVSISEGPDTLGDGMRERRETL--------ALAPEPEPLEKE 159
Cdd:TIGR02169  421 ELADLNAAIAGIEAKINELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQELYDLKEEYdrvekelsKLQRELAEAEAQ 498

                          170       180       190
                   ....*....|....*....|....*....|
gi 767968965   160 AcEKWKRPFRSASATSLTLSHCVDVVKGLL 189
Cdd:TIGR02169  499 A-RASEERVRGGRAVEEVLKASIQGVHGTV 527
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 10-118 1.57e-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: 44.66  E-value: 1.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    10 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRahvglreAALRRLQEEARDLLERL 89
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR-------AELTLLNEEAANLRERL 826

                           90       100
                   ....*....|....*....|....*....
gi 767968965    90 VQRKARAAAERNLRNERRERAKQARVSQE 118
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIE 855
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
7-163 2.60e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   7 EKGAALGTLESELQ-------QRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQ 79
Cdd:PRK02224 360 ELREEAAELESELEeareaveDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  80 ---EEARDLLE------------------RLVQRKARAA--AERNLRNERRERAKQARVSQ--ELKKAAKRTVSISEGPD 134
Cdd:PRK02224 440 ervEEAEALLEagkcpecgqpvegsphveTIEEDRERVEelEAELEDLEEEVEEVEERLERaeDLVEAEDRIERLEERRE 519

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767968965 135 TLGDGMRERRETLA--------LAPEPEPLEKEACEK 163
Cdd:PRK02224 520 DLEELIAERRETIEekreraeeLRERAAELEAEAEEK 556
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 225-513 1.26e-55

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: 187.93  E-value: 1.26e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 304
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 305 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 381
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 382 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 460
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767968965 461 SCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 513
Cdd:cd00200  238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
225-513 1.20e-50

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.18  E-value: 1.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 304
Cdd:COG2319  115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 305 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcgDHIIISGHNDQ 377
Cdd:COG2319  193 TGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTltghsgsVRSVAFSPD----GRLLASGSADG 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 378 KIRFWDSRGPHCTQVIPVQ-GRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSY 456
Cdd:COG2319  269 TVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS----VAFSPDGKT 344

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767968965 457 ALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 513
Cdd:COG2319  345 LASGSDDGTVRLWDLATGELLRTLTG-HTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
WD40 COG2319
WD40 repeat [General function prediction only];
214-512 1.62e-47

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 169.71  E-value: 1.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 214 VAARLPTRAQDVLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEAnqTLEGAGGSITSVDFDPSGYQVLAAT 293
Cdd:COG2319   62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLR--TLTGHTGAVRSVAFSPDGKTLASGS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 294 YNQAAQLWKVGEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcg 366
Cdd:COG2319  140 ADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTltghtgaVRSVAFSPD---- 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 367 DHIIISGHNDQKIRFWDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcgSDW 445
Cdd:COG2319  216 GKLLASGSADGTVRLWDLATGKLLRTLTGhSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH-----SGG 290

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767968965 446 TKAV-FSPDRSYALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLW 512
Cdd:COG2319  291 VNSVaFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKTLASGSDDGTVRLW 357
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 268-513 2.13e-40

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: 147.48  E-value: 2.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 268 QTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVGEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGR 347
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 348 AYCSRTINvlSYCNDVVCGD-----HIIISGHNDQKIRFWDSRGPHCTQVIP-VQGRVTSLSLSHDQLHLLSCSRDNTLK 421
Cdd:cd00200   83 GECVRTLT--GHTSYVSSVAfspdgRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAFSPDGTFVASSSQDGTIK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 422 VIDLRVSNIRQVFraDGFKcgsDWTKAV-FSPDRSYALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHM 500
Cdd:cd00200  161 LWDLRTGKCVATL--TGHT---GEVNSVaFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRG-HENGVNSVAFSPDGYLL 234

                        250
                 ....*....|...
gi 767968965 501 VSVDQGRKVVLWQ 513
Cdd:cd00200  235 ASGSEDGTIRVWD 247
WD40 COG2319
WD40 repeat [General function prediction only];
214-512 2.61e-39

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 147.37  E-value: 2.61e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 214 VAARLPTRAQDVLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEAnqTLEGAGGSITSVDFDPSGYQVLAAT 293
Cdd:COG2319   20 LLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLA--TLLGHTAAVLSVAFSPDGRLLASAS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 294 YNQAAQLWKVGEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcg 366
Cdd:COG2319   98 ADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTltghsgaVTSVAFSPD---- 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 367 DHIIISGHNDQKIRFWDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcgSDW 445
Cdd:COG2319  174 GKLLASGSDDGTVRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGH-----SGS 248

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767968965 446 TKAV-FSPDRSYALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLW 512
Cdd:COG2319  249 VRSVaFSPDGRLLASGSADGTVRLWDLATGELLRTLTG-HSGGVNSVAFSPDGKLLASGSDDGTVRLW 315
WD40 COG2319
WD40 repeat [General function prediction only];
225-473 7.06e-38

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 143.51  E-value: 7.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 304
Cdd:COG2319  157 TLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLL--RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 305 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTinvLSYCNDVVCG------DHIIISGHNDQK 378
Cdd:COG2319  235 TGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT---LTGHSGGVNSvafspdGKLLASGSDDGT 311

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 379 IRFWDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRAdgfkcGSDWTKAV-FSPDRSY 456
Cdd:COG2319  312 VRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTG-----HTGAVTSVaFSPDGRT 386

                        250
                 ....*....|....*..
gi 767968965 457 ALAGSCDGALYIWDVDT 473
Cdd:COG2319  387 LASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
237-513 2.98e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 121.94  E-value: 2.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 237 RFGPNSSLLATGGADRLIHLWNVVGSRLEAnqTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVGEAQSKETLSGHK 316
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLL--LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 317 DKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVL-SYCNDVVC--GDHIIISGHNDQKIRFWDSRGPHCTQVI 393
Cdd:COG2319   79 AAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHtGAVRSVAFspDGKTLASGSADGTVRLWDLATGKLLRTL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 394 PV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcgSDWTKAV-FSPDRSYALAGSCDGALYIWDV 471
Cdd:COG2319  159 TGhSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH-----TGAVRSVaFSPDGKLLASGSADGTVRLWDL 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 767968965 472 DTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 513
Cdd:COG2319  234 ATGKLLRTLTG-HSGSVRSVAFSPDGRLLASGSADGTVRLWD 274
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 1-97 1.13e-28

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: 111.56  E-value: 1.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    1 MAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQE 80
Cdd:pfam08614  76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEK 155

                          90
                  ....*....|....*..
gi 767968965   81 EARDLLERLVQRKARAA 97
Cdd:pfam08614 156 ENRELVERWMKRKGQEA 172
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 14-97 4.14e-22

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: 90.32  E-value: 4.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  14 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 93
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80


                 ....
gi 767968965  94 ARAA 97
Cdd:cd22887   81 QQEA 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 10-125 1.30e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  10 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERL 89
Cdd:COG1196  239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767968965  90 VQRKARAAAerNLRNERRERAKQARVSQELKKAAKR 125
Cdd:COG1196  319 EELEEELAE--LEEELEELEEELEELEEELEEAEEE 352
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
10-131 5.50e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 5.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   10 AALGTLESELQQRQSRLAALEARVAQLREARAQQ-AQQVEEWRAQNAV----------QRAAYEALRAHVGLR----EAA 74
Cdd:COG4913   302 AELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERlereleererRRARLEALLAALGLPlpasAEE 381

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767968965   75 LRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQAR--VSQELKKAAKRTVSISE 131
Cdd:COG4913   382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELreLEAEIASLERRKSNIPA 440
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-150 9.25e-07

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: 9.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   4 QVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEAR 83
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767968965  84 DLLERLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKRTVSISEGPDTLGDGMRERRETLALA 150
Cdd:COG1196  411 ALLERLERLEEELEELEEALAELEEEEEEEE--EALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 225-258 1.27e-06

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: 45.00  E-value: 1.27e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767968965   225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 258
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
225-258 3.31e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.87  E-value: 3.31e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767968965  225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 258
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
4-127 3.52e-06

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 48.89  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   4 QVVEKGAALGTLESElqQRQSRLAALEARVAQLrEARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQ---- 79
Cdd:COG1566   65 DRVKKGQVLARLDPT--DLQAALAQAEAQLAAA-EAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQalyk 141

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767968965  80 ---------EEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTV 127
Cdd:COG1566  142 kgavsqqelDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAAL 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 14-123 8.88e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 8.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  14 TLESELQQRQSRLAAL-----EARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL--- 85
Cdd:COG1196  217 ELKEELKELEAELLLLklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELlae 296

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767968965  86 LERLVQRKARAAAERNLRNERRERAKQARVSQELKKAA 123
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 233-428 1.22e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 233 VNAVRFGPNSSLLATGGADRLIHLWN----VVGSRLEANQTLEGAGGS-ITSVDFDPS-GYQVLAATYNQAAQLWKVGEA 306
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICWNSYiKSQVASSNFEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 307 QSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSycnDVVC------GDHIIISGHNDQKI 379
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpseSGRSLAFGSADHKV 642

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767968965 380 RFWDSRGPH---CTQVipvqGRVTSLSLSH--DQLHLLSCSRDNTLKVIDLRVS 428
Cdd:PLN00181 643 YYYDLRNPKlplCTMI----GHSKTVSYVRfvDSSTLVSSSTDNTLKLWDLSMS 692
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 4-90 1.26e-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: 47.25  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   4 QVVEKGAALGTLESELQQrqsrlAALEARVAQLREARAQ------QAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRR 77
Cdd:COG0845   43 DRVKKGQVLARLDPPDLQ-----AALAQAQAQLAAAQAQlelakaELERYKALLKKGAVSQQELDQAKAALDQAQAALAA 117

                         90
                 ....*....|....*.
gi 767968965  78 LQ---EEARDLLERLV 90
Cdd:COG0845  118 AQaalEQARANLAYTT 133
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-123 1.35e-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: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   3 YQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEE- 81
Cdd:COG1196  225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDi 304

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767968965  82 --ARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAA 123
Cdd:COG1196  305 arLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 15-98 1.42e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  15 LESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKA 94
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104


                 ....
gi 767968965  95 RAAA 98
Cdd:COG4942  105 ELAE 108
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
12-159 1.45e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  12 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQ 91
Cdd:COG4372   82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767968965  92 RKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKE 159
Cdd:COG4372  162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 15-118 2.53e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  15 LESELQQRQSRlaaLEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKA 94
Cdd:COG1196  310 RRRELEERLEE---LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                         90       100
                 ....*....|....*....|....
gi 767968965  95 RAAAERNLRNERRERAKQARVSQE 118
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEE 410
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 15-189 3.77e-05

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: 46.60  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    15 LESELQQRQSRLAALEARVAQLREARA---QQAQQVE----EWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLE 87
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEdlrAELEEVDkefaETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    88 RLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKRTVSISEGPDTLGDGMRERRETL--------ALAPEPEPLEKE 159
Cdd:TIGR02169  421 ELADLNAAIAGIEAKINELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQELYDLKEEYdrvekelsKLQRELAEAEAQ 498

                          170       180       190
                   ....*....|....*....|....*....|
gi 767968965   160 AcEKWKRPFRSASATSLTLSHCVDVVKGLL 189
Cdd:TIGR02169  499 A-RASEERVRGGRAVEEVLKASIQGVHGTV 527
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 10-125 6.74e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 6.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  10 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLER- 88
Cdd:COG1196  316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAa 395

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767968965  89 --LVQRKARAAAERNLRNERRERAKQARVSQELKKAAKR 125
Cdd:COG1196  396 aeLAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
14-98 8.59e-05

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 43.66  E-value: 8.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  14 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQR- 92
Cdd:COG1842   95 ELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKi 174


                 ....*....
gi 767968965  93 ---KARAAA 98
Cdd:COG1842  175 eemEARAEA 183
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
10-131 1.18e-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: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  10 AALGTLESELQQRQSRLAALEARVAQLREARAQ---------QAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQE 80
Cdd:COG3206  219 QQLSELESQLAEARAELAEAEARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA 298

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767968965  81 EARDLLERLVQRKARAAAeRNLRNERRERAKQARVSQELKKAAKRTVSISE 131
Cdd:COG3206  299 QIAALRAQLQQEAQRILA-SLEAELEALQAREASLQAQLAQLEARLAELPE 348
PTZ00421 PTZ00421
coronin; Provisional
 236-344 1.21e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.50  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965 236 VRFGP-NSSLLATGGADRLIHLWNVVGSRLEANQT-----LEGAGGSITSVDFDPSGYQVLA-ATYNQAAQLWKVGEAQS 308
Cdd:PTZ00421  81 VAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhLQGHTKKVGIVSFHPSAMNVLAsAGADMVVNVWDVERGKA 160

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767968965 309 KETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 344
Cdd:PTZ00421 161 VEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 311-344 1.40e-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: 39.22  E-value: 1.40e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767968965   311 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 344
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
311-344 1.54e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 1.54e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767968965  311 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 344
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 10-118 1.57e-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: 44.66  E-value: 1.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    10 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRahvglreAALRRLQEEARDLLERL 89
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR-------AELTLLNEEAANLRERL 826

                           90       100
                   ....*....|....*....|....*....
gi 767968965    90 VQRKARAAAERNLRNERRERAKQARVSQE 118
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIE 855
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
4-125 2.46e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   4 QVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEwraQNAVQRAAYEALRAHVGLREAALRRLQEEAR 83
Cdd:COG4717  126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE---LAELQEELEELLEQLSLATEEELQDLAEELE 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767968965  84 DLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKR 125
Cdd:COG4717  203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
23-125 2.49e-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: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   23 QSRLAALEARVAQLREARAQ---QAQQVEEWRAQNAVQRAAYEALRAH------VGLREAALRRLQEEARDL------LE 87
Cdd:COG4913   609 RAKLAALEAELAELEEELAEaeeRLEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLdassddLA 688

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767968965   88 RLVQR--KARAAAERNLRNERRERAKQARVSQELKKAAKR 125
Cdd:COG4913   689 ALEEQleELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
7-163 2.60e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   7 EKGAALGTLESELQ-------QRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQ 79
Cdd:PRK02224 360 ELREEAAELESELEeareaveDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  80 ---EEARDLLE------------------RLVQRKARAA--AERNLRNERRERAKQARVSQ--ELKKAAKRTVSISEGPD 134
Cdd:PRK02224 440 ervEEAEALLEagkcpecgqpvegsphveTIEEDRERVEelEAELEDLEEEVEEVEERLERaeDLVEAEDRIERLEERRE 519

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767968965 135 TLGDGMRERRETLA--------LAPEPEPLEKEACEK 163
Cdd:PRK02224 520 DLEELIAERRETIEekreraeeLRERAAELEAEAEEK 556
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
12-94 3.69e-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: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   12 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHvGLREAALRRLQEEARDLLERLVQ 91
Cdd:COG4913   663 VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL-EKELEQAEEELDELQDRLEAAED 741


                  ...
gi 767968965   92 RKA 94
Cdd:COG4913   742 LAR 744
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 10-98 4.59e-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: 4.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  10 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL---L 86
Cdd:COG4942  150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELealI 229

                         90
                 ....*....|..
gi 767968965  87 ERLVQRKARAAA 98
Cdd:COG4942  230 ARLEAEAAAAAE 241
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-89 7.32e-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: 42.35  E-value: 7.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965     7 EKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLL 86
Cdd:TIGR02168  863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942


                   ...
gi 767968965    87 ERL 89
Cdd:TIGR02168  943 ERL 945
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 4-127 7.84e-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: 41.67  E-value: 7.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   4 QVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEW-RAQNAVQRAAYEALRAHVGLREAALRRLQ--- 79
Cdd:COG4942   63 RIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlRALYRLGRQPPLALLLSPEDFLDAVRRLQylk 142

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767968965  80 ----------EEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTV 127
Cdd:COG4942  143 ylaparreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 396-424 8.25e-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: 36.91  E-value: 8.25e-04
                           10        20
                   ....*....|....*....|....*....
gi 767968965   396 QGRVTSLSLSHDQLHLLSCSRDNTLKVID 424
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
4-98 1.02e-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: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    4 QVVEKGAALGTLES------ELQQRQSRLAALEARVAQLREAR---AQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAA 74
Cdd:COG4913   642 ALQERREALQRLAEyswdeiDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721

                          90       100
                  ....*....|....*....|....
gi 767968965   75 LRRLQEEARDLLERLVQRKARAAA 98
Cdd:COG4913   722 LEQAEEELDELQDRLEAAEDLARL 745
PTZ00121 PTZ00121
MAEBL; Provisional
 17-162 1.07e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   17 SELQQRQSRLAALEARVA-QLREA----RAQQAQQVEEWRAQNAVQRAAYEALRAHvglreaALRRLQEEARDLLERLvQ 91
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKAdELKKAeekkKADEAKKAEEKKKADEAKKKAEEAKKAD------EAKKKAEEAKKKADAA-K 1335

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767968965   92 RKARAA--AERNLRNERRERAKQARVSQELKKAAK-RTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACE 162
Cdd:PTZ00121 1336 KKAEEAkkAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE 1409
PTZ00121 PTZ00121
MAEBL; Provisional
 16-166 1.10e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   16 ESELQQRQSRLAALEARVAQLREA-----RAQQAQQVEEWRaQNAVQRAAYEALRAHVGLREAALR----RLQEEARDLL 86
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAeeakkDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAAIKaeeaRKADELKKAE 1287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   87 ERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACEKWKR 166
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
PRK12704 PRK12704
phosphodiesterase; Provisional
 15-89 1.18e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767968965  15 LESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERL 89
Cdd:PRK12704  73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 4-84 1.41e-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: 40.76  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    4 QVVEKGAALGTLESELQQrqsrlAALEARVAQLREARAQ------QAQQVEEWRAQNAV-------QRAAYEALRAHVGL 70
Cdd:TIGR01730  46 QKVKKGQVLARLDDDDYQ-----LALQAALAQLAAAEAQlelaqrSFERAERLVKRNAVsqadlddAKAAVEAAQADLEA 120

                          90
                  ....*....|....
gi 767968965   71 REAALRRLQEEARD 84
Cdd:TIGR01730 121 AKASLASAQLNLRY 134
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
7-125 1.46e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   7 EKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQR--AAYEALRAHVGLREAALRRLQEEARD 84
Cdd:COG4717   78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEE 157

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767968965  85 LLERLVQRKARAAAERNLRNERRERAKQ--ARVSQELKKAAKR 125
Cdd:COG4717  158 LRELEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEE 200
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
14-92 1.53e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  14 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAhvglrEAALRRLQEE------ARDLLE 87
Cdd:COG4717  429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL-----KAELRELAEEwaalklALELLE 503


                 ....*
gi 767968965  88 RLVQR 92
Cdd:COG4717  504 EAREE 508
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 473-512 1.76e-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: 36.14  E-value: 1.76e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 767968965   473 TGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLW 512
Cdd:smart00320   1 SGELLKTLKG-HTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
10-89 1.82e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  10 AALGTLESELQQRQSRLAALEARVAQLR-------------EARAQQAQQVEEWRAQNAVQRAAYEALRAHvglREAALR 76
Cdd:COG4717  439 EELEELEEELEELREELAELEAELEQLEedgelaellqeleELKAELRELAEEWAALKLALELLEEAREEY---REERLP 515

                         90
                 ....*....|...
gi 767968965  77 RLQEEARDLLERL 89
Cdd:COG4717  516 PVLERASEYFSRL 528
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 18-139 1.94e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  18 ELQQRQSRL----AALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 93
Cdd:COG3883  137 ELKADKAELeakkAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767968965  94 ARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDG 139
Cdd:COG3883  217 AAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSA 262
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
18-163 2.07e-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: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   18 ELQQRQSRLAALEARVAQLREARAQQAqqVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERL----VQRK 93
Cdd:COG4913   263 RYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgngGDRL 340

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   94 ARAAAernlrNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACEK 163
Cdd:COG4913   341 EQLER-----EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
PRK09039 PRK09039
peptidoglycan -binding protein;
4-84 2.09e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.33  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   4 QVVEKGAALGTLESELQQRQS-------RLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALR 76
Cdd:PRK09039  82 SVANLRASLSAAEAERSRLQAllaelagAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD 161


                 ....*...
gi 767968965  77 rlQEEARD 84
Cdd:PRK09039 162 --ASEKRD 167
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 12-98 2.42e-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: 39.52  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  12 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHV-GLREAALRRLQEEARDLLERLV 90
Cdd:COG1579  105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELeAEREELAAKIPPELLALYERIR 184


                 ....*...
gi 767968965  91 QRKARAAA 98
Cdd:COG1579  185 KRKNGLAV 192
WD40 pfam00400
WD domain, G-beta repeat;
396-424 3.01e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 3.01e-03
                          10        20
                  ....*....|....*....|....*....
gi 767968965  396 QGRVTSLSLSHDQLHLLSCSRDNTLKVID 424
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
12-94 3.41e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 3.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  12 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQnavqraaYEALRAHVGLREAALRRLQEEARDLLERLVQ 91
Cdd:COG4372   47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ-------LQAAQAELAQAQEELESLQEEAEELQEELEE 119


                 ...
gi 767968965  92 RKA 94
Cdd:COG4372  120 LQK 122
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-125 4.15e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   7 EKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLL 86
Cdd:COG1196  662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767968965  87 ERlvqrkARAAAERNLRNERRERAKQARVSQELKKAAKR 125
Cdd:COG1196  742 LE-----EEELLEEEALEELPEPPDLEELERELERLERE 775
PTZ00121 PTZ00121
MAEBL; Provisional
 6-166 4.60e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    6 VEKGAALGTLESELQQRQSRLAALEARVAQLReaRAQQAQQVEEWRAQNAVQRAAYEALRAHvGLREAALRRLQEEARdl 85
Cdd:PTZ00121 1187 VRKAEELRKAEDARKAEAARKAEEERKAEEAR--KAEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEAR-- 1261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   86 LERLVQRKARAAAERNLRNERRERAKQARVSQELKKA-AKRTVsisegpDTLGDGMRERRETLALAPEPEPLEKEACEKW 164
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAeEKKKA------DEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335


                  ..
gi 767968965  165 KR 166
Cdd:PTZ00121 1336 KK 1337
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 10-126 5.36e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  10 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRA----HVGLREAALRRLQEEARDL 85
Cdd:COG1196  442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEaeadYEGFLEGVKAALLLAGLRG 521

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767968965  86 LERLVQ-------------RKARAAAERNLRNERRERAKQARVSQELKKAAKRT 126
Cdd:COG1196  522 LAGAVAvligveaayeaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
14-166 5.38e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 5.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965  14 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEaRDLLERLVQRK 93
Cdd:PRK02224 520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER-IESLERIRTLL 598

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767968965  94 ARAAAernlrnerrerAKQARVSQELKKAAKRTVSiSEGPDTLGDgMRERRETLALAPEPEPLEkEACEKWKR 166
Cdd:PRK02224 599 AAIAD-----------AEDEIERLREKREALAELN-DERRERLAE-KRERKRELEAEFDEARIE-EAREDKER 657
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 24-125 7.42e-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: 39.17  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965   24 SRLAALEARVAQLREARAQQAQqveewrAQNAvqraayEALRAHVGLREAALRRlQEEARDLLERLVQRKAR--AAAERN 101
Cdd:COG3096   489 ERSQAWQTARELLRRYRSQQAL------AQRL------QQLRAQLAELEQRLRQ-QQNAERLLEEFCQRIGQqlDAAEEL 555

                          90       100
                  ....*....|....*....|....
gi 767968965  102 LRNERRERAKQARVSQELKKAAKR 125
Cdd:COG3096   556 EELLAELEAQLEELEEQAAEAVEQ 579
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 1-80 8.82e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 34.93  E-value: 8.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968965    1 MAYQVVEKgaalgtLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVglrEAALRRLQE 80
Cdd:pfam06005   1 MSLELLEQ------LETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERI---RGLLGKLDE 71
 
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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