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Conserved domains on  [gi|256818776|ref|NP_001028419|]
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cilia- and flagella-associated protein 44 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
222-593 2.26e-26

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 113.85  E-value: 2.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  222 VDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFWEMAftfTGlKLQGS 301
Cdd:COG2319    84 VAFSPDGRLLASAS--ADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA---TG-KLLRT 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  302 LgrfgKTSTSDIEGYAELPDGKVL-SGSEWGNLLLWE---GSLIKVelcRTGmkscHSGSINQIML--DEGEVITAGSDG 375
Cdd:COG2319   158 L----TGHSGAVTSVAFSPDGKLLaSGSDDGTVRLWDlatGKLLRT---LTG----HTGAVRSVAFspDGKLLASGSADG 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  376 SVRIWDFETIDTADVIDDTGlleiEPINelhidkSVNlFSmikmnevGNNFWLA---QDANGAIWKLDlsfsniTQDPEC 452
Cdd:COG2319   227 TVRLWDLATGKLLRTLTGHS----GSVR------SVA-FS-------PDGRLLAsgsADGTVRLWDLA------TGELLR 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  453 LFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVSA--SQIVVGFQDGVVRV 530
Cdd:COG2319   283 TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFSPdgKTLASGSDDGTVRL 356

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256818776  531 LELFDPKGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVE 593
Cdd:COG2319   357 WDLATGELLRTLTG-----------------HTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1539-1817 6.84e-06

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 6.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1539 ELALQLREKRLDIEEA--------LVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREK----------QQR 1600
Cdd:TIGR02168  210 EKAERYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeieelQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1601 LNELLVVIPLKLHQIEymEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTI 1680
Cdd:TIGR02168  290 LYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1681 SKMEETVRELMiskfgrvidlEALQTLSVNTTLEELKIKKLRKELSNAK-ELRMWE---EKIAQVRWDLMMKTKEHTKKL 1756
Cdd:TIGR02168  368 EELESRLEELE----------EQLETLRSKVAQLELQIASLNNEIERLEaRLERLEdrrERLQQEIEELLKKLEEAELKE 437

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256818776  1757 HQMN--DLCLEKKKLDSRLNTLQNQQGNAFQGLRKA--DIVAKQKVTELVQTQLEKITALKEEIE 1817
Cdd:TIGR02168  438 LQAEleELEEELEELQEELERLEEALEELREELEEAeqALDAAERELAQLQARLDSLERLQENLE 502
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 903-1817 1.30e-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 pfam02463:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1161  Bit Score: 50.36  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776   903 IEDPKAYSIENARKKREHDKLMKKVEELKAHKREQIKILRNEFwKLLELNKELPAHMQFQRTDFNIDAKIHAEIHKKTSL 982
Cdd:pfam02463  158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL-KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776   983 KIEQVEKELAWEKQKHELGLKKLQDRFREPLEsdtivvyatQSDHQIASYRLVKPSKYSKLKRpSQSERRQSKMERLEKE 1062
Cdd:pfam02463  237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLA---------QVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLE 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1063 GPGKKESQRDTGGSISLQEESVLEKGKKfrprtlsEIMVENQIEKTKKLIQQAERAQfKILQRKKEWEELYKSKPDDDYE 1142
Cdd:pfam02463  307 RRKVDDEEKLKESEKEKKKAEKELKKEK-------EEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAK 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1143 DPKDVQAIKEAQtymGDFNLKTAPDYKIpehmrINAAKKEEELgyldtmaHGKKRYMNKCILSLRDLKLAVIEEIQCLVQ 1222
Cdd:pfam02463  379 KKLESERLSSAA---KLKEEELELKSEE-----EKEAQLLLEL-------ARQLEDLLKEEKKEELEILEEEEESIELKQ 443

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1223 ELKNIQSsipaskhmpipqvpqiypeevperrfqyDEETLLRFQRKQKKRQDKSSSKQSGTGSGGSAGGGLVGFLKLSSG 1302
Cdd:pfam02463  444 GKLTEEK----------------------------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1303 KEGDLTTRDSLSRSSKASALLELPKPVEFEKAEPSDAELEimkrdEVKHLYMQQFLCNRINELTVTFDAELHLLRHQKLK 1382
Cdd:pfam02463  496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG-----VAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1383 LDTKMKLSDLHHLTLFQEMLLLKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQEKALYAGFQA 1462
Cdd:pfam02463  571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRK 650

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1463 ALGENNKFANFLMKVLKKKIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGS----------EDDVFDDSICPTN 1532
Cdd:pfam02463  651 GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeelkklklEAEELLADRVQEA 730

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1533 CDVSLFELALQLREKRLDIEEAL--VEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNELLVVIPL 1610
Cdd:pfam02463  731 QDKINEELKLLKQKIDEEEEEEEksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1611 KLHQIEYMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKEcRERRKLLIREKREMAKTISKMEETVREL 1690
Cdd:pfam02463  811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE-EITKEELLQELLLKEEELEEQKLKDELE 889

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1691 MISKFGRVIDLEALQTLSVNTTLEELKIKKLRKELSNAKELRMWEEKIAQ---VRWDLMMKTKEHTKKLHQMNDLCLEKK 1767
Cdd:pfam02463  890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEElllEEADEKEKEENNKEEEEERNKRLLLAK 969

                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|
gi 256818776  1768 KLDSRLNTLQnqqgnAFQGLRKaDIVAKQKVTELVQTQLEKITALKEEIE 1817
Cdd:pfam02463  970 EELGKVNLMA-----IEEFEEK-EERYNKDELEKERLEEEKKKLIRAIIE 1013
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 793-873 1.27e-03

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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 42.71  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  793 NPIRNITFSNDQTMMFCGMTNGAIRVYVLSENDPFLVSLQHYwhfnvhdnnyGSIKSITSSFDDQYLLTAGEDGNIFVFD 872
Cdd:cd00200    10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHT----------GPVRDVAASADGTYLASGSSDKTIRLWD 79


                  .
gi 256818776  873 I 873
Cdd:cd00200    80 L 80
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
222-593 2.26e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 113.85  E-value: 2.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  222 VDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFWEMAftfTGlKLQGS 301
Cdd:COG2319    84 VAFSPDGRLLASAS--ADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA---TG-KLLRT 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  302 LgrfgKTSTSDIEGYAELPDGKVL-SGSEWGNLLLWE---GSLIKVelcRTGmkscHSGSINQIML--DEGEVITAGSDG 375
Cdd:COG2319   158 L----TGHSGAVTSVAFSPDGKLLaSGSDDGTVRLWDlatGKLLRT---LTG----HTGAVRSVAFspDGKLLASGSADG 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  376 SVRIWDFETIDTADVIDDTGlleiEPINelhidkSVNlFSmikmnevGNNFWLA---QDANGAIWKLDlsfsniTQDPEC 452
Cdd:COG2319   227 TVRLWDLATGKLLRTLTGHS----GSVR------SVA-FS-------PDGRLLAsgsADGTVRLWDLA------TGELLR 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  453 LFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVSA--SQIVVGFQDGVVRV 530
Cdd:COG2319   283 TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFSPdgKTLASGSDDGTVRL 356

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256818776  531 LELFDPKGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVE 593
Cdd:COG2319   357 WDLATGELLRTLTG-----------------HTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 320-615 1.33e-20

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: 94.32  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  320 PDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSDGSVRIWDFETIDTADVIddTGl 396
Cdd:cd00200    19 PDGKLLaTGSGDGTIKVWDLETGELLRTLKG----HTGPVRDVAAsaDGTYLASGSSDKTIRLWDLETGECVRTL--TG- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  397 lEIEPINELHIDKsvnlfsmikmnevgNNFWLA---QDANGAIWKLDlsfsnitqDPECLFSF--HSGPIAALAVSPLTY 471
Cdd:cd00200    92 -HTSYVSSVAFSP--------------DGRILSsssRDKTIKVWDVE--------TGKCLTTLrgHTDWVNSVAFSPDGT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  472 LMATTAMDCSVRVYDFSSKNPL-VHMKFKQGGTSLIWAPRSvsvsaSQIVVGFQDGVVRVLELfdpkgltvyagrkkipd 550
Cdd:cd00200   149 FVASSSQDGTIKLWDLRTGKCVaTLTGHTGEVNSVAFSPDG-----EKLLSSSSDGTIKLWDL----------------- 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256818776  551 AELHLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFDVEKEYKPIGFFNTPGPICQLMWSP 615
Cdd:cd00200   207 STGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSP 271
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 554-591 1.88e-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: 46.15  E-value: 1.88e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 256818776    554 HLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 591
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
555-591 2.94e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 2.94e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 256818776   555 LKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 591
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1539-1817 6.84e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 6.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1539 ELALQLREKRLDIEEA--------LVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREK----------QQR 1600
Cdd:TIGR02168  210 EKAERYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeieelQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1601 LNELLVVIPLKLHQIEymEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTI 1680
Cdd:TIGR02168  290 LYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1681 SKMEETVRELMiskfgrvidlEALQTLSVNTTLEELKIKKLRKELSNAK-ELRMWE---EKIAQVRWDLMMKTKEHTKKL 1756
Cdd:TIGR02168  368 EELESRLEELE----------EQLETLRSKVAQLELQIASLNNEIERLEaRLERLEdrrERLQQEIEELLKKLEEAELKE 437

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256818776  1757 HQMN--DLCLEKKKLDSRLNTLQNQQGNAFQGLRKA--DIVAKQKVTELVQTQLEKITALKEEIE 1817
Cdd:TIGR02168  438 LQAEleELEEELEELQEELERLEEALEELREELEEAeqALDAAERELAQLQARLDSLERLQENLE 502
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1543-1730 1.21e-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: 49.76  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1543 QLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEayqrEKQQRLNELLVVIpLKLHQIEYMEF-- 1620
Cdd:COG4942    52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE----AQKEELAELLRAL-YRLGRQPPLALll 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1621 -GEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETV--RELMISKFGR 1697
Cdd:COG4942   127 sPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKaeRQKLLARLEK 206

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 256818776 1698 VIDLEA--LQTLSVNTTLEELKIKKLRKELSNAKE 1730
Cdd:COG4942   207 ELAELAaeLAELQQEAEELEALIARLEAEAAAAAE 241
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 903-1817 1.30e-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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 50.36  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776   903 IEDPKAYSIENARKKREHDKLMKKVEELKAHKREQIKILRNEFwKLLELNKELPAHMQFQRTDFNIDAKIHAEIHKKTSL 982
Cdd:pfam02463  158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL-KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776   983 KIEQVEKELAWEKQKHELGLKKLQDRFREPLEsdtivvyatQSDHQIASYRLVKPSKYSKLKRpSQSERRQSKMERLEKE 1062
Cdd:pfam02463  237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLA---------QVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLE 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1063 GPGKKESQRDTGGSISLQEESVLEKGKKfrprtlsEIMVENQIEKTKKLIQQAERAQfKILQRKKEWEELYKSKPDDDYE 1142
Cdd:pfam02463  307 RRKVDDEEKLKESEKEKKKAEKELKKEK-------EEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAK 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1143 DPKDVQAIKEAQtymGDFNLKTAPDYKIpehmrINAAKKEEELgyldtmaHGKKRYMNKCILSLRDLKLAVIEEIQCLVQ 1222
Cdd:pfam02463  379 KKLESERLSSAA---KLKEEELELKSEE-----EKEAQLLLEL-------ARQLEDLLKEEKKEELEILEEEEESIELKQ 443

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1223 ELKNIQSsipaskhmpipqvpqiypeevperrfqyDEETLLRFQRKQKKRQDKSSSKQSGTGSGGSAGGGLVGFLKLSSG 1302
Cdd:pfam02463  444 GKLTEEK----------------------------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1303 KEGDLTTRDSLSRSSKASALLELPKPVEFEKAEPSDAELEimkrdEVKHLYMQQFLCNRINELTVTFDAELHLLRHQKLK 1382
Cdd:pfam02463  496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG-----VAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1383 LDTKMKLSDLHHLTLFQEMLLLKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQEKALYAGFQA 1462
Cdd:pfam02463  571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRK 650

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1463 ALGENNKFANFLMKVLKKKIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGS----------EDDVFDDSICPTN 1532
Cdd:pfam02463  651 GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeelkklklEAEELLADRVQEA 730

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1533 CDVSLFELALQLREKRLDIEEAL--VEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNELLVVIPL 1610
Cdd:pfam02463  731 QDKINEELKLLKQKIDEEEEEEEksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1611 KLHQIEYMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKEcRERRKLLIREKREMAKTISKMEETVREL 1690
Cdd:pfam02463  811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE-EITKEELLQELLLKEEELEEQKLKDELE 889

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1691 MISKFGRVIDLEALQTLSVNTTLEELKIKKLRKELSNAKELRMWEEKIAQ---VRWDLMMKTKEHTKKLHQMNDLCLEKK 1767
Cdd:pfam02463  890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEElllEEADEKEKEENNKEEEEERNKRLLLAK 969

                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|
gi 256818776  1768 KLDSRLNTLQnqqgnAFQGLRKaDIVAKQKVTELVQTQLEKITALKEEIE 1817
Cdd:pfam02463  970 EELGKVNLMA-----IEEFEEK-EERYNKDELEKERLEEEKKKLIRAIIE 1013
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1404-1604 3.66e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1404 LKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQ---EKALYAGFQAALGE-------NNKFANF 1473
Cdd:COG3883    25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGEraralyrSGGSVSY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1474 LMKVLKkkikrakkkevegdadedeeseesseeesslesdedaSGSEDDVFDDsicptncdvslFELALQLREKRLDIEE 1553
Cdd:COG3883   105 LDVLLG-------------------------------------SESFSDFLDR-----------LSALSKIADADADLLE 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 256818776 1554 ALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNEL 1604
Cdd:COG3883   137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 793-873 1.27e-03

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: 42.71  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  793 NPIRNITFSNDQTMMFCGMTNGAIRVYVLSENDPFLVSLQHYwhfnvhdnnyGSIKSITSSFDDQYLLTAGEDGNIFVFD 872
Cdd:cd00200    10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHT----------GPVRDVAASADGTYLASGSSDKTIRLWD 79


                  .
gi 256818776  873 I 873
Cdd:cd00200    80 L 80
PTZ00121 PTZ00121
MAEBL; Provisional
 912-1216 1.38e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  912 ENARKKREHDKLMKKVEELK-----AHKREQIKILRNEFWKLLELNK--ELPAHMQFQRTDfniDAKIHAEIHKKTSL-K 983
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKkkadeAKKAAEAKKKADEAKKAEEAKKadEAKKAEEAKKAD---EAKKAEEKKKADELkK 1553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  984 IEQVEKelAWEKQKHELGLKKLQDRFREPLESDTIvvyatqsdHQIASYRLVKPSK-YSKLKRPSQSERRQSKMERLEKE 1062
Cdd:PTZ00121 1554 AEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEA--------KKAEEARIEEVMKlYEEEKKMKAEEAKKAEEAKIKAE 1623

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1063 GPGKKESQRDTGGSISLQEESVLEKGKKFR-PRTLSEIMVENQIEKTKKLIQQAERAQFKILQRKKEWEELYKSKpdddy 1141
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA----- 1698

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1142 EDPKDVQAIKEAQTYmgdfNLKTAPDYKIPEHMR---INAAKKEEE------------LGYLDTMAHGKKRYMNKCiLSL 1206
Cdd:PTZ00121 1699 EEAKKAEELKKKEAE----EKKKAEELKKAEEENkikAEEAKKEAEedkkkaeeakkdEEEKKKIAHLKKEEEKKA-EEI 1773

                         330
                  ....*....|
gi 256818776 1207 RDLKLAVIEE 1216
Cdd:PTZ00121 1774 RKEKEAVIEE 1783
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 1537-1741 1.43e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 42.74  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1537 LFELALQLREKR--LDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQ---REKQQRLNELLvviplk 1611
Cdd:cd22656    96 ILELIDDLADATddEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQtalETLEKALKDLL------ 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1612 lhqieymefgevpEDLSGTLVfsNHSLDRLQERIVQLQEENAKqqKLNKECRERRKLLIREKREMAK------TISKMEE 1685
Cdd:cd22656   170 -------------TDEGGAIA--RKEIKDLQKELEKLNEEYAA--KLKAKIDELKALIADDEAKLAAalrliaDLTAADT 232

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 256818776 1686 TVRELmISKFGRVID-LEALQTL--SVNTTLEELKiKKLRKELSNAKELRMWEEKIAQV 1741
Cdd:cd22656   233 DLDNL-LALIGPAIPaLEKLQGAwqAIATDLDSLK-DLLEDDISKIPAAILAKLELEKA 289
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1536-1745 1.83e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1536 SLFELALQLRE-----KRLDIEEaLVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEE------ALEAYQREKQQRLNEL 1604
Cdd:PRK03918  497 KLKELAEQLKEleeklKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAEL 575

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1605 LvviplklHQIEYMEFGEVPEDLSG------------TLVFSNHSLDRLQERIVQLQEE----NAKQQKLNKECRERRKL 1668
Cdd:PRK03918  576 L-------KELEELGFESVEELEERlkelepfyneylELKDAEKELEREEKELKKLEEEldkaFEELAETEKRLEELRKE 648

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1669 LirekREMAKTISKME-ETVRELMISKFGRVIDLEAlQTLSVNTTLEELK--IKKLRKELSNAKELRMWEEKIAQVRWDL 1745
Cdd:PRK03918  649 L----EELEKKYSEEEyEELREEYLELSRELAGLRA-ELEELEKRREEIKktLEKLKEELEEREKAKKELEKLEKALERV 723
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
222-593 2.26e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 113.85  E-value: 2.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  222 VDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFWEMAftfTGlKLQGS 301
Cdd:COG2319    84 VAFSPDGRLLASAS--ADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA---TG-KLLRT 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  302 LgrfgKTSTSDIEGYAELPDGKVL-SGSEWGNLLLWE---GSLIKVelcRTGmkscHSGSINQIML--DEGEVITAGSDG 375
Cdd:COG2319   158 L----TGHSGAVTSVAFSPDGKLLaSGSDDGTVRLWDlatGKLLRT---LTG----HTGAVRSVAFspDGKLLASGSADG 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  376 SVRIWDFETIDTADVIDDTGlleiEPINelhidkSVNlFSmikmnevGNNFWLA---QDANGAIWKLDlsfsniTQDPEC 452
Cdd:COG2319   227 TVRLWDLATGKLLRTLTGHS----GSVR------SVA-FS-------PDGRLLAsgsADGTVRLWDLA------TGELLR 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  453 LFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVSA--SQIVVGFQDGVVRV 530
Cdd:COG2319   283 TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFSPdgKTLASGSDDGTVRL 356

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256818776  531 LELFDPKGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVE 593
Cdd:COG2319   357 WDLATGELLRTLTG-----------------HTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
239-615 3.86e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.22  E-value: 3.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  239 DYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFWEMAftftglklQGSLGRFGKTSTSDIEGYAE 318
Cdd:COG2319    57 DLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA--------TGLLLRTLTGHTGAVRSVAF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  319 LPDGK-VLSGSEWGNLLLWE---GSLIKVelcrtgmKSCHSGSINQIML--DEGEVITAGSDGSVRIWDFETIDTADVID 392
Cdd:COG2319   129 SPDGKtLASGSADGTVRLWDlatGKLLRT-------LTGHSGAVTSVAFspDGKLLASGSDDGTVRLWDLATGKLLRTLT 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  393 DTGlleiEPINELHidksvnlFSmikmnevGNNFWLA---QDANGAIWKLDlsfsniTQDPECLFSFHSGPIAALAVSPL 469
Cdd:COG2319   202 GHT----GAVRSVA-------FS-------PDGKLLAsgsADGTVRLWDLA------TGKLLRTLTGHSGSVRSVAFSPD 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  470 TYLMATTAMDCSVRVYDFSSKNPLvhmKFKQGGTSLIWaprSVSVSA--SQIVVGFQDGVVRVLELfdpkgltvyagrkk 547
Cdd:COG2319   258 GRLLASGSADGTVRLWDLATGELL---RTLTGHSGGVN---SVAFSPdgKLLASGSDDGTVRLWDL-------------- 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256818776  548 ipdAELHLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFDVEKEYKPIGFFNTPGPICQLMWSP 615
Cdd:COG2319   318 ---ATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSP 382
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 320-615 1.33e-20

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: 94.32  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  320 PDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSDGSVRIWDFETIDTADVIddTGl 396
Cdd:cd00200    19 PDGKLLaTGSGDGTIKVWDLETGELLRTLKG----HTGPVRDVAAsaDGTYLASGSSDKTIRLWDLETGECVRTL--TG- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  397 lEIEPINELHIDKsvnlfsmikmnevgNNFWLA---QDANGAIWKLDlsfsnitqDPECLFSF--HSGPIAALAVSPLTY 471
Cdd:cd00200    92 -HTSYVSSVAFSP--------------DGRILSsssRDKTIKVWDVE--------TGKCLTTLrgHTDWVNSVAFSPDGT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  472 LMATTAMDCSVRVYDFSSKNPL-VHMKFKQGGTSLIWAPRSvsvsaSQIVVGFQDGVVRVLELfdpkgltvyagrkkipd 550
Cdd:cd00200   149 FVASSSQDGTIKLWDLRTGKCVaTLTGHTGEVNSVAFSPDG-----EKLLSSSSDGTIKLWDL----------------- 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256818776  551 AELHLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFDVEKEYKPIGFFNTPGPICQLMWSP 615
Cdd:cd00200   207 STGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSP 271
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 222-591 5.01e-20

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: 92.40  E-value: 5.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  222 VDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFW-----EMAFTFTGl 296
Cdd:cd00200    15 VAFSPDGKLLATGS--GDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWdletgECVRTLTG- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  297 klqgslgrfgktSTSDIEGYAELPDGKVLSGSEW-GNLLLWEgsLIKVELCRTGmkSCHSGSINQI-MLDEGEVITAGS- 373
Cdd:cd00200    92 ------------HTSYVSSVAFSPDGRILSSSSRdKTIKVWD--VETGKCLTTL--RGHTDWVNSVaFSPDGTFVASSSq 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  374 DGSVRIWDFETIdtadviddtglleiepinelhidksvnlfsmikmnevgnnfwlaqdangaiwkldlsfsnitqdpECL 453
Cdd:cd00200   156 DGTIKLWDLRTG-----------------------------------------------------------------KCV 170

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  454 --FSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKFKQGG-TSLIWAP-RSVSVSASQivvgfqDGVVR 529
Cdd:cd00200   171 atLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGvNSVAFSPdGYLLASGSE------DGTIR 244

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256818776  530 VlelFDpkgltVYAGRkkipdaelhLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 591
Cdd:cd00200   245 V---WD-----LRTGE---------CVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
239-615 1.71e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 89.97  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  239 DYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFWEMAftftglklQGSLGRFGKTSTSDIEGYAE 318
Cdd:COG2319    15 DLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAA--------AGALLATLLGHTAAVLSVAF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  319 LPDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSDGSVRIWDfetidtadviddtg 395
Cdd:COG2319    87 SPDGRLLaSASADGTVRLWDLATGLLLRTLTG----HTGAVRSVAFspDGKTLASGSADGTVRLWD-------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  396 lleiepinelhidksvnlfsmikmnevgnnfwlaqdangaiwkldlsfsniTQDPECLFSF--HSGPIAALAVSPLTYLM 473
Cdd:COG2319   149 ---------------------------------------------------LATGKLLRTLtgHSGAVTSVAFSPDGKLL 177

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  474 ATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVSA--SQIVVGFQDGVVRVLELFDPKGLTVYAGrkkipda 551
Cdd:COG2319   178 ASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFSPdgKLLASGSADGTVRLWDLATGKLLRTLTG------- 244

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256818776  552 elhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVEkEYKPIGFFNTP-GPICQLMWSP 615
Cdd:COG2319   245 ----------HSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGELLRTLTGHsGGVNSVAFSP 298
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 137-486 6.49e-15

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: 77.38  E-value: 6.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  137 LQLLDSNTLLYVAG--NQMVLLDFKDKTQIYLQSSSGQGIGAIGVHPKKTYFAVAekGSFPKIIIYEYPSLKPYRILRdG 214
Cdd:cd00200    15 VAFSPDGKLLATGSgdGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASG--SSDKTIRLWDLETGECVRTLT-G 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  215 AEKAYAYVDFNNEGNLLasVGCHPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNdeQLTTSGS--GHIKFWEMAft 292
Cdd:cd00200    92 HTSYVSSVAFSPDGRIL--SSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDG--TFVASSSqdGTIKLWDLR-- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  293 ftglklQGSLGRFGKTSTSDIEGYAELPDG-KVLSGSEWGNLLLWEgslikvelCRTGMKSC----HSGSINQIMLDE-G 366
Cdd:cd00200   166 ------TGKCVATLTGHTGEVNSVAFSPDGeKLLSSSSDGTIKLWD--------LSTGKCLGtlrgHENGVNSVAFSPdG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  367 EVITAGS-DGSVRIWDFETidtadviddtglleiepinelhidksvnlfsmikmnevgnnfwlaqdangaiwkldlsfsn 445
Cdd:cd00200   232 YLLASGSeDGTIRVWDLRT------------------------------------------------------------- 250

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 256818776  446 itqdPECLFSF--HSGPIAALAVSPLTYLMATTAMDCSVRVYD 486
Cdd:cd00200   251 ----GECVQTLsgHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
141-384 9.43e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 78.41  E-value: 9.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  141 DSNTLLYVAGNQMV-LLDFKDKTQIYLQSSSGQGIGAIGVHPKKTYFAVAekGSFPKIIIYEYPSLKPYRILRDGAEKAY 219
Cdd:COG2319   131 DGKTLASGSADGTVrLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASG--SDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  220 AyVDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNdEQL-TTSGSGHIKFWEMAFTFTGLKL 298
Cdd:COG2319   209 S-VAFSPDGKLLASGS--ADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDG-RLLaSGSADGTVRLWDLATGELLRTL 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  299 QGSLGRFGKTSTSdiegyaelPDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSDG 375
Cdd:COG2319   285 TGHSGGVNSVAFS--------PDGKLLaSGSDDGTVRLWDLATGKLLRTLTG----HTGAVRSVAFspDGKTLASGSDDG 352


                  ....*....
gi 256818776  376 SVRIWDFET 384
Cdd:COG2319   353 TVRLWDLAT 361
WD40 COG2319
WD40 repeat [General function prediction only];
141-384 8.32e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 75.72  E-value: 8.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  141 DSNTLLYVAGNQMVLL-DFKDKTQIYLQSSSGQGIGAIGVHPKKTYFAVaekGSFPK-IIIYEYPSLKPYRILRDGAEKA 218
Cdd:COG2319   173 DGKLLASGSDDGTVRLwDLATGKLLRTLTGHTGAVRSVAFSPDGKLLAS---GSADGtVRLWDLATGKLLRTLTGHSGSV 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  219 YAyVDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDnDEQL-TTSGSGHIKFWEMAftfTGLK 297
Cdd:COG2319   250 RS-VAFSPDGRLLASGS--ADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPD-GKLLaSGSDDGTVRLWDLA---TGKL 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  298 LQGSLGrfgktSTSDIEGYAELPDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSD 374
Cdd:COG2319   323 LRTLTG-----HTGAVRSVAFSPDGKTLaSGSDDGTVRLWDLATGELLRTLTG----HTGAVTSVAFspDGRTLASGSAD 393

                         250
                  ....*....|
gi 256818776  375 GSVRIWDFET 384
Cdd:COG2319   394 GTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 457-615 8.78e-13

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: 70.83  E-value: 8.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  457 HSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLvhmKFKQGGTSLIWAPRSVSVSaSQIVVGFQDGVVRVLELFDP 536
Cdd:cd00200     8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL---RTLKGHTGPVRDVAASADG-TYLASGSSDKTIRLWDLETG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  537 KGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVEKeYKPIGFFNT-PGPICQLMWSP 615
Cdd:cd00200    84 ECVRTLTG-----------------HTSYVSSVAFSPDGRILSSSSRDKTIKVWDVET-GKCLTTLRGhTDWVNSVAFSP 145
WD40 COG2319
WD40 repeat [General function prediction only];
427-593 4.40e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 54.53  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  427 WLAQDANGAIWKLDLSFSNITQDPECLFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMkfkQGGTSLI 506
Cdd:COG2319     5 DGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATL---LGHTAAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  507 WApRSVSVSASQIVVGFQDGVVRVLELFDPKGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKT 586
Cdd:COG2319    82 LS-VAFSPDGRLLASASADGTVRLWDLATGLLLRTLTG-----------------HTGAVRSVAFSPDGKTLASGSADGT 143


                  ....*..
gi 256818776  587 VFFFDVE 593
Cdd:COG2319   144 VRLWDLA 150
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 554-591 1.88e-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: 46.15  E-value: 1.88e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 256818776    554 HLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 591
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
555-591 2.94e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 2.94e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 256818776   555 LKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 591
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1539-1817 6.84e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 6.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1539 ELALQLREKRLDIEEA--------LVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREK----------QQR 1600
Cdd:TIGR02168  210 EKAERYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeieelQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1601 LNELLVVIPLKLHQIEymEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTI 1680
Cdd:TIGR02168  290 LYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1681 SKMEETVRELMiskfgrvidlEALQTLSVNTTLEELKIKKLRKELSNAK-ELRMWE---EKIAQVRWDLMMKTKEHTKKL 1756
Cdd:TIGR02168  368 EELESRLEELE----------EQLETLRSKVAQLELQIASLNNEIERLEaRLERLEdrrERLQQEIEELLKKLEEAELKE 437

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256818776  1757 HQMN--DLCLEKKKLDSRLNTLQNQQGNAFQGLRKA--DIVAKQKVTELVQTQLEKITALKEEIE 1817
Cdd:TIGR02168  438 LQAEleELEEELEELQEELERLEEALEELREELEEAeqALDAAERELAQLQARLDSLERLQENLE 502
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1546-1814 8.57e-06

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: 50.84  E-value: 8.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1546 EKRLDIEEALVEEKKI-VDNLKKE------YDTISKK-----VKVVATNLNAAEEALEAYQRE------KQQRLNELLVV 1607
Cdd:TIGR02169  183 EENIERLDLIIDEKRQqLERLRRErekaerYQALLKEkreyeGYELLKEKEALERQKEAIERQlasleeELEKLTEEISE 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1608 IPLKLHQIEymefgEVPEDLsgtlvfsNHSLDRL-QERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEET 1686
Cdd:TIGR02169  263 LEKRLEEIE-----QLLEEL-------NKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1687 VRELM--ISKFGRVIDLEALQTLSVNTTLEELKIK--KLRKEL-SNAKELRMWEEKIAQVRWDLMMKTKEHTKKLHQMND 1761
Cdd:TIGR02169  331 IDKLLaeIEELEREIEEERKRRDKLTEEYAELKEEleDLRAELeEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 256818776  1762 LCLEKKKLDSRLNTLqnqqgnafqglrKADI-VAKQKVTELVQTQLEKITALKE 1814
Cdd:TIGR02169  411 LQEELQRLSEELADL------------NAAIaGIEAKINELEEEKEDKALEIKK 452
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1543-1730 1.21e-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: 49.76  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1543 QLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEayqrEKQQRLNELLVVIpLKLHQIEYMEF-- 1620
Cdd:COG4942    52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE----AQKEELAELLRAL-YRLGRQPPLALll 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1621 -GEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETV--RELMISKFGR 1697
Cdd:COG4942   127 sPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKaeRQKLLARLEK 206

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 256818776 1698 VIDLEA--LQTLSVNTTLEELKIKKLRKELSNAKE 1730
Cdd:COG4942   207 ELAELAaeLAELQQEAEELEALIARLEAEAAAAAE 241
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 903-1817 1.30e-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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 50.36  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776   903 IEDPKAYSIENARKKREHDKLMKKVEELKAHKREQIKILRNEFwKLLELNKELPAHMQFQRTDFNIDAKIHAEIHKKTSL 982
Cdd:pfam02463  158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL-KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776   983 KIEQVEKELAWEKQKHELGLKKLQDRFREPLEsdtivvyatQSDHQIASYRLVKPSKYSKLKRpSQSERRQSKMERLEKE 1062
Cdd:pfam02463  237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLA---------QVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLE 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1063 GPGKKESQRDTGGSISLQEESVLEKGKKfrprtlsEIMVENQIEKTKKLIQQAERAQfKILQRKKEWEELYKSKPDDDYE 1142
Cdd:pfam02463  307 RRKVDDEEKLKESEKEKKKAEKELKKEK-------EEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAK 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1143 DPKDVQAIKEAQtymGDFNLKTAPDYKIpehmrINAAKKEEELgyldtmaHGKKRYMNKCILSLRDLKLAVIEEIQCLVQ 1222
Cdd:pfam02463  379 KKLESERLSSAA---KLKEEELELKSEE-----EKEAQLLLEL-------ARQLEDLLKEEKKEELEILEEEEESIELKQ 443

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1223 ELKNIQSsipaskhmpipqvpqiypeevperrfqyDEETLLRFQRKQKKRQDKSSSKQSGTGSGGSAGGGLVGFLKLSSG 1302
Cdd:pfam02463  444 GKLTEEK----------------------------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1303 KEGDLTTRDSLSRSSKASALLELPKPVEFEKAEPSDAELEimkrdEVKHLYMQQFLCNRINELTVTFDAELHLLRHQKLK 1382
Cdd:pfam02463  496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG-----VAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1383 LDTKMKLSDLHHLTLFQEMLLLKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQEKALYAGFQA 1462
Cdd:pfam02463  571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRK 650

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1463 ALGENNKFANFLMKVLKKKIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGS----------EDDVFDDSICPTN 1532
Cdd:pfam02463  651 GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeelkklklEAEELLADRVQEA 730

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1533 CDVSLFELALQLREKRLDIEEAL--VEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNELLVVIPL 1610
Cdd:pfam02463  731 QDKINEELKLLKQKIDEEEEEEEksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1611 KLHQIEYMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKEcRERRKLLIREKREMAKTISKMEETVREL 1690
Cdd:pfam02463  811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE-EITKEELLQELLLKEEELEEQKLKDELE 889

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1691 MISKFGRVIDLEALQTLSVNTTLEELKIKKLRKELSNAKELRMWEEKIAQ---VRWDLMMKTKEHTKKLHQMNDLCLEKK 1767
Cdd:pfam02463  890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEElllEEADEKEKEENNKEEEEERNKRLLLAK 969

                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|
gi 256818776  1768 KLDSRLNTLQnqqgnAFQGLRKaDIVAKQKVTELVQTQLEKITALKEEIE 1817
Cdd:pfam02463  970 EELGKVNLMA-----IEEFEEK-EERYNKDELEKERLEEEKKKLIRAIIE 1013
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 555-618 1.68e-05

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: 48.87  E-value: 1.68e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256818776  555 LKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFDVEKEYKPIGFFNTPGPICQLMWSPASH 618
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGT 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1540-1817 1.70e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1540 LALQLREKRLDIEEALVEEKKI---VDNLKKEYDTISKKVKVVATNLNAAEEALEAyQREKQQRLNELLvviplKLHQIE 1616
Cdd:COG1196   216 RELKEELKELEAELLLLKLRELeaeLEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELEL-----EEAQAE 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1617 YMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETVRELMISKFG 1696
Cdd:COG1196   290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1697 RVIDLEALQTLSVNTTLEEL-KIKKLRKELSNAKELRMWEEKIAQVRWDLMMKTKEHTKKLHQMNDLCLEKKKLDSRLNT 1775
Cdd:COG1196   370 AEAELAEAEEELEELAEELLeALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 256818776 1776 LQNQQGNAFQGLRKAdIVAKQKVTELVQTQLEKITALKEEIE 1817
Cdd:COG1196   450 EEAELEEEEEALLEL-LAELLEEAALLEAALAELLEELAEAA 490
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1404-1604 3.66e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1404 LKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQ---EKALYAGFQAALGE-------NNKFANF 1473
Cdd:COG3883    25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGEraralyrSGGSVSY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1474 LMKVLKkkikrakkkevegdadedeeseesseeesslesdedaSGSEDDVFDDsicptncdvslFELALQLREKRLDIEE 1553
Cdd:COG3883   105 LDVLLG-------------------------------------SESFSDFLDR-----------LSALSKIADADADLLE 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 256818776 1554 ALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNEL 1604
Cdd:COG3883   137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 895-1130 4.70e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.11  E-value: 4.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776   895 ESEAAPE-DIEDPKAYSIENARKKREHDKLMKKVEeLKAHKREQIKILRNEFWKLLELNKELpAHMQFQRTDFNidAKIH 973
Cdd:pfam17380  320 EAEKARQaEMDRQAAIYAEQERMAMERERELERIR-QEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKN--ERVR 395

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776   974 AEIHKKTSLKIEQVEKELAWEKQKHEL-GLKKLQDRFREplesDTIVVYATQSDHQIASYRLVKPSKYSKLKRPSQSE-- 1050
Cdd:pfam17380  396 QELEAARKVKILEEERQRKIQQQKVEMeQIRAEQEEARQ----REVRRLEEERAREMERVRLEEQERQQQVERLRQQEee 471

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1051 RRQSKMErLEKEGPGKKESQRdtggsislQEESVLEKGKKFRPRTLSE-----IMVENQIEKTKKLIQQAERAQFKILQR 1125
Cdd:pfam17380  472 RKRKKLE-LEKEKRDRKRAEE--------QRRKILEKELEERKQAMIEeerkrKLLEKEMEERQKAIYEEERRREAEEER 542


                   ....*
gi 256818776  1126 KKEWE 1130
Cdd:pfam17380  543 RKQQE 547
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1543-1742 5.55e-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: 5.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1543 QLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQRE---KQQRLNELLVVIPLKLHQIEYME 1619
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanLRERLESLERRIAATERRLEDLE 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1620 fgEVPEDLSGTLVFSNHSL-------DRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETVRELM- 1691
Cdd:TIGR02168  845 --EQIEELSEDIESLAAEIeeleeliEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRe 922

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1692 -ISKFGRVID------LEALQTLSV--NTTLEELKIKKLRKELSNAKelrmWEEKIAQVR 1742
Cdd:TIGR02168  923 kLAQLELRLEglevriDNLQERLSEeySLTLEEAEALENKIEDDEEE----ARRRLKRLE 978
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1536-1817 7.25e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 7.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1536 SLFELALQLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAyQREKQQRLNELLVVIPLKLHQI 1615
Cdd:COG4372    14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ-ARSELEQLEEELEELNEQLQAA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1616 EymefgEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETVRELMISKF 1695
Cdd:COG4372    93 Q-----AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1696 GRVIDLEALQTLSVNTTLEEL-------KIKKLRKELSNAKELRMWEEKIAQVRWDLMMKTKEHTKKLHQMNDLCLEKKK 1768
Cdd:COG4372   168 ALEQELQALSEAEAEQALDELlkeanrnAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 256818776 1769 LDSRLNTLQNQQGNAFQGLRKADIVAKQKVTELVQTQLEKITALKEEIE 1817
Cdd:COG4372   248 KEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK 296
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 793-873 1.27e-03

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: 42.71  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  793 NPIRNITFSNDQTMMFCGMTNGAIRVYVLSENDPFLVSLQHYwhfnvhdnnyGSIKSITSSFDDQYLLTAGEDGNIFVFD 872
Cdd:cd00200    10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHT----------GPVRDVAASADGTYLASGSSDKTIRLWD 79


                  .
gi 256818776  873 I 873
Cdd:cd00200    80 L 80
PTZ00121 PTZ00121
MAEBL; Provisional
 912-1216 1.38e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  912 ENARKKREHDKLMKKVEELK-----AHKREQIKILRNEFWKLLELNK--ELPAHMQFQRTDfniDAKIHAEIHKKTSL-K 983
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKkkadeAKKAAEAKKKADEAKKAEEAKKadEAKKAEEAKKAD---EAKKAEEKKKADELkK 1553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  984 IEQVEKelAWEKQKHELGLKKLQDRFREPLESDTIvvyatqsdHQIASYRLVKPSK-YSKLKRPSQSERRQSKMERLEKE 1062
Cdd:PTZ00121 1554 AEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEA--------KKAEEARIEEVMKlYEEEKKMKAEEAKKAEEAKIKAE 1623

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1063 GPGKKESQRDTGGSISLQEESVLEKGKKFR-PRTLSEIMVENQIEKTKKLIQQAERAQFKILQRKKEWEELYKSKpdddy 1141
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA----- 1698

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1142 EDPKDVQAIKEAQTYmgdfNLKTAPDYKIPEHMR---INAAKKEEE------------LGYLDTMAHGKKRYMNKCiLSL 1206
Cdd:PTZ00121 1699 EEAKKAEELKKKEAE----EKKKAEELKKAEEENkikAEEAKKEAEedkkkaeeakkdEEEKKKIAHLKKEEEKKA-EEI 1773

                         330
                  ....*....|
gi 256818776 1207 RDLKLAVIEE 1216
Cdd:PTZ00121 1774 RKEKEAVIEE 1783
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 1537-1741 1.43e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 42.74  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1537 LFELALQLREKR--LDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQ---REKQQRLNELLvviplk 1611
Cdd:cd22656    96 ILELIDDLADATddEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQtalETLEKALKDLL------ 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1612 lhqieymefgevpEDLSGTLVfsNHSLDRLQERIVQLQEENAKqqKLNKECRERRKLLIREKREMAK------TISKMEE 1685
Cdd:cd22656   170 -------------TDEGGAIA--RKEIKDLQKELEKLNEEYAA--KLKAKIDELKALIADDEAKLAAalrliaDLTAADT 232

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 256818776 1686 TVRELmISKFGRVID-LEALQTL--SVNTTLEELKiKKLRKELSNAKELRMWEEKIAQV 1741
Cdd:cd22656   233 DLDNL-LALIGPAIPaLEKLQGAwqAIATDLDSLK-DLLEDDISKIPAAILAKLELEKA 289
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1536-1745 1.83e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1536 SLFELALQLRE-----KRLDIEEaLVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEE------ALEAYQREKQQRLNEL 1604
Cdd:PRK03918  497 KLKELAEQLKEleeklKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAEL 575

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1605 LvviplklHQIEYMEFGEVPEDLSG------------TLVFSNHSLDRLQERIVQLQEE----NAKQQKLNKECRERRKL 1668
Cdd:PRK03918  576 L-------KELEELGFESVEELEERlkelepfyneylELKDAEKELEREEKELKKLEEEldkaFEELAETEKRLEELRKE 648

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1669 LirekREMAKTISKME-ETVRELMISKFGRVIDLEAlQTLSVNTTLEELK--IKKLRKELSNAKELRMWEEKIAQVRWDL 1745
Cdd:PRK03918  649 L----EELEKKYSEEEyEELREEYLELSRELAGLRA-ELEELEKRREEIKktLEKLKEELEEREKAKKELEKLEKALERV 723
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 447-486 2.55e-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: 37.29  E-value: 2.55e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 256818776    447 TQDPECLFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYD 486
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1404-1690 2.58e-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: 42.74  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1404 LKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEE---KKNEITKLQDQEKALYAGFQAALGENNKFANFLMKVLKK 1480
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1481 KIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGSEDDVfddsicptncDVSLFELALQLREKRLDIEEALVEEKK 1560
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL----------AAEIEELEELIEELESELEALLNERAS 884

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  1561 I---VDNLKKEYDTISKKVKVVATNLNAAE-------EALEAYQREKQ---QRLNELLVVIPlKLHQIEYMEFGEVPEDL 1627
Cdd:TIGR02168  885 LeeaLALLRSELEELSEELRELESKRSELRreleelrEKLAQLELRLEgleVRIDNLQERLS-EEYSLTLEEAEALENKI 963

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256818776  1628 SGTLVFSNHSLDRLQERIVQLQEENakqqkLN-----KECRERRKLLIREKREMAKTISKMEETVREL 1690
Cdd:TIGR02168  964 EDDEEEARRRLKRLENKIKELGPVN-----LAaieeyEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1539-1783 2.94e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1539 ELALQLREKRLDIEEALVEEKKIVDNLKKEYDTISKKV----------KVVATNLNAAEEALEAYQREKQQRLNELlvvi 1608
Cdd:PRK02224  488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIaerretieekRERAEELRERAAELEAEAEEKREAAAEA---- 563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1609 plklhQIEYMEFGEVPEDLSGTLVFSNHSLDRLqERIVQLQEENAkqqklnkECRERRKLLiREKREmakTISKMEETVR 1688
Cdd:PRK02224  564 -----EEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIA-------DAEDEIERL-REKRE---ALAELNDERR 626

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1689 ELMISKFGRVIDLEAlqtlsvntTLEELKIKKLRKELSNAKE-LRMWEEKIAQV---RWDLMMKTKEHTKKLHQMNDLCL 1764
Cdd:PRK02224  627 ERLAEKRERKRELEA--------EFDEARIEEAREDKERAEEyLEQVEEKLDELreeRDDLQAEIGAVENELEELEELRE 698

                         250
                  ....*....|....*....
gi 256818776 1765 EKKKLDSRLNTLQNQQGNA 1783
Cdd:PRK02224  699 RREALENRVEALEALYDEA 717
WD40 pfam00400
WD domain, G-beta repeat;
451-486 6.47e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 6.47e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 256818776   451 ECLFSF--HSGPIAALAVSPLTYLMATTAMDCSVRVYD 486
Cdd:pfam00400    2 KLLKTLegHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00121 PTZ00121
MAEBL; Provisional
 895-1154 9.44e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 9.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  895 ESEAAPEDIEDPKAYSIENARKKREHDKLmKKVEELK----AHKREQIKilRNEFWKLLELNK-ELPAHMQFQRTDFNID 969
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADEL-KKAEELKkaeeKKKAEEAK--KAEEDKNMALRKaEEAKKAEEARIEEVMK 1599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776  970 AKIHAEIHKKTSLKIEQVEKELAWEKQKHELGLKKLQDRFREPLESdtivvyaTQSDHQIASYRLVKPSKYSKLKRPSQS 1049
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE-------KKKAEELKKAEEENKIKAAEEAKKAEE 1672

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256818776 1050 ERRQSKMERLEKEGPGKKESQRDtggsislQEESVLEKGKKFRPRTlseimvENQIEKTKKLIQQAERAQFKILQRKKEW 1129
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALK-------KEAEEAKKAEELKKKE------AEEKKKAEELKKAEEENKIKAEEAKKEA 1739

                         250       260
                  ....*....|....*....|....*...
gi 256818776 1130 EElYKSKPDD---DYEDPKDVQAIKEAQ 1154
Cdd:PTZ00121 1740 EE-DKKKAEEakkDEEEKKKIAHLKKEE 1766
 
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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