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Conserved domains on  [gi|755553370|ref|XP_006522030|]
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cilia- and flagella-associated protein 44 isoform X4 [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];
141-309 1.13e-14

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 78.03  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  141 TQDPECLFSF--HSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVSA--SQIVVG 216
Cdd:COG2319   149 LATGKLLRTLtgHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFSPdgKLLASG 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  217 FQDGVVRVLELFDPKGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVEkEYKPIGFF 296
Cdd:COG2319   223 SADGTVRLWDLATGKLLRTLTG-----------------HSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGELLRTL 284

                         170
                  ....*....|....
gi 755553370  297 NTP-GPICQLMWSP 309
Cdd:COG2319   285 TGHsGGVNSVAFSP 298
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1233-1511 1.34e-05

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1233 ELALQLREKRLDIEEA--------LVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREK----------QQR 1294
Cdd:TIGR02168  210 EKAERYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeieelQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1295 LNELLVVIPLKLHQIEymEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTI 1374
Cdd:TIGR02168  290 LYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1375 SKMEETVRELMiskfgrvidlEALQTLSVNTTLEELKIKKLRKELSNAK-ELRMWE---EKIAQVRWDLMMKTKEHTKKL 1450
Cdd:TIGR02168  368 EELESRLEELE----------EQLETLRSKVAQLELQIASLNNEIERLEaRLERLEdrrERLQQEIEELLKKLEEAELKE 437

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755553370  1451 HQMN--DLCLEKKKLDSRLNTLQNQQGNAFQGLRKA--DIVAKQKVTELVQTQLEKITALKEEIE 1511
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 ...
 597-1511 8.03e-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: 47.66  E-value: 8.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   597 IEDPKAYSIENARKKREHDKLMKKVEELKAHKREQIKILRNEFwKLLELNKELPAHMQFQRTDFNIDAKIHAEIHKKTSL 676
Cdd:pfam02463  158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL-KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   677 KIEQVEKELAWEKQKHELGLKKLQDRFREPLEsdtivvyatQSDHQIASYRLVKPSKYSKLKRpSQSERRQSKMERLEKE 756
Cdd:pfam02463  237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLA---------QVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLE 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   757 GPGKKESQRDTGGSISLQEESVLEKGKKfrprtlsEIMVENQIEKTKKLIQQAERAQfKILQRKKEWEELYKSKPDDDYE 836
Cdd:pfam02463  307 RRKVDDEEKLKESEKEKKKAEKELKKEK-------EEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAK 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   837 DPKDVQAIKEAQtymGDFNLKTAPDYKIpehmrINAAKKEEELgyldtmaHGKKRYMNKCILSLRDLKLAVIEEIQCLVQ 916
Cdd:pfam02463  379 KKLESERLSSAA---KLKEEELELKSEE-----EKEAQLLLEL-------ARQLEDLLKEEKKEELEILEEEEESIELKQ 443

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   917 ELKNIQSsipaskhmpipqvpqiypeevperrfqyDEETLLRFQRKQKKRQDKSSSKQSGTGSGGSAGGGLVGFLKLSSG 996
Cdd:pfam02463  444 GKLTEEK----------------------------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   997 KEGDLTTRDSLSRSSKASALLELPKPVEFEKAEPSDAELEimkrdEVKHLYMQQFLCNRINELTVTFDAELHLLRHQKLK 1076
Cdd:pfam02463  496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG-----VAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1077 LDTKMKLSDLHHLTLFQEMLLLKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQEKALYAGFQA 1156
Cdd:pfam02463  571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRK 650

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1157 ALGENNKFANFLMKVLKKKIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGS----------EDDVFDDSICPTN 1226
Cdd:pfam02463  651 GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeelkklklEAEELLADRVQEA 730

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1227 CDVSLFELALQLREKRLDIEEAL--VEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNELLVVIPL 1304
Cdd:pfam02463  731 QDKINEELKLLKQKIDEEEEEEEksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1305 KLHQIEYMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKEcRERRKLLIREKREMAKTISKMEETVREL 1384
Cdd:pfam02463  811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE-EITKEELLQELLLKEEELEEQKLKDELE 889

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1385 MISKFGRVIDLEALQTLSVNTTLEELKIKKLRKELSNAKELRMWEEKIAQ---VRWDLMMKTKEHTKKLHQMNDLCLEKK 1461
Cdd:pfam02463  890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEElllEEADEKEKEENNKEEEEERNKRLLLAK 969

                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|
gi 755553370  1462 KLDSRLNTLQnqqgnAFQGLRKaDIVAKQKVTELVQTQLEKITALKEEIE 1511
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 ...
 487-567 1.04e-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: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  487 NPIRNITFSNDQTMMFCGMTNGAIRVYVLSENDPFLVSLQHYwhfnvhdnnyGSIKSITSSFDDQYLLTAGEDGNIFVFD 566
Cdd:cd00200    10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHT----------GPVRDVAASADGTYLASGSSDKTIRLWD 79


                  .
gi 755553370  567 I 567
Cdd:cd00200    80 L 80
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
141-309 1.13e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 78.03  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  141 TQDPECLFSF--HSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVSA--SQIVVG 216
Cdd:COG2319   149 LATGKLLRTLtgHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFSPdgKLLASG 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  217 FQDGVVRVLELFDPKGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVEkEYKPIGFF 296
Cdd:COG2319   223 SADGTVRLWDLATGKLLRTLTG-----------------HSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGELLRTL 284

                         170
                  ....*....|....
gi 755553370  297 NTP-GPICQLMWSP 309
Cdd:COG2319   285 TGHsGGVNSVAFSP 298
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 141-309 2.21e-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: 72.37  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  141 TQDPECLFSF--HSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPL-VHMKFKQGGTSLIWAPRSvsvsaSQIVVGF 217
Cdd:cd00200   122 VETGKCLTTLrgHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVaTLTGHTGEVNSVAFSPDG-----EKLLSSS 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  218 QDGVVRVLELfdpkgltvyagrkkipdAELHLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFDVEKEYKPIGFFN 297
Cdd:cd00200   197 SDGTIKLWDL-----------------STGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSG 259

                         170
                  ....*....|..
gi 755553370  298 TPGPICQLMWSP 309
Cdd:cd00200   260 HTNSVTSLAWSP 271
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 248-285 1.57e-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: 1.57e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 755553370    248 HLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 285
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
249-285 2.45e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 2.45e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 755553370   249 LKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 285
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1233-1511 1.34e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1233 ELALQLREKRLDIEEA--------LVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREK----------QQR 1294
Cdd:TIGR02168  210 EKAERYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeieelQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1295 LNELLVVIPLKLHQIEymEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTI 1374
Cdd:TIGR02168  290 LYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1375 SKMEETVRELMiskfgrvidlEALQTLSVNTTLEELKIKKLRKELSNAK-ELRMWE---EKIAQVRWDLMMKTKEHTKKL 1450
Cdd:TIGR02168  368 EELESRLEELE----------EQLETLRSKVAQLELQIASLNNEIERLEaRLERLEdrrERLQQEIEELLKKLEEAELKE 437

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755553370  1451 HQMN--DLCLEKKKLDSRLNTLQNQQGNAFQGLRKA--DIVAKQKVTELVQTQLEKITALKEEIE 1511
Cdd:TIGR02168  438 LQAEleELEEELEELQEELERLEEALEELREELEEAeqALDAAERELAQLQARLDSLERLQENLE 502
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1237-1424 1.74e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1237 QLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEayqrEKQQRLNELLVVIpLKLHQIEYMEF-- 1314
Cdd:COG4942    52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE----AQKEELAELLRAL-YRLGRQPPLALll 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1315 -GEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETV--RELMISKFGR 1391
Cdd:COG4942   127 sPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKaeRQKLLARLEK 206

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 755553370 1392 VIDLEA--LQTLSVNTTLEELKIKKLRKELSNAKE 1424
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 ...
 597-1511 8.03e-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: 47.66  E-value: 8.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   597 IEDPKAYSIENARKKREHDKLMKKVEELKAHKREQIKILRNEFwKLLELNKELPAHMQFQRTDFNIDAKIHAEIHKKTSL 676
Cdd:pfam02463  158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL-KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   677 KIEQVEKELAWEKQKHELGLKKLQDRFREPLEsdtivvyatQSDHQIASYRLVKPSKYSKLKRpSQSERRQSKMERLEKE 756
Cdd:pfam02463  237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLA---------QVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLE 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   757 GPGKKESQRDTGGSISLQEESVLEKGKKfrprtlsEIMVENQIEKTKKLIQQAERAQfKILQRKKEWEELYKSKPDDDYE 836
Cdd:pfam02463  307 RRKVDDEEKLKESEKEKKKAEKELKKEK-------EEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAK 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   837 DPKDVQAIKEAQtymGDFNLKTAPDYKIpehmrINAAKKEEELgyldtmaHGKKRYMNKCILSLRDLKLAVIEEIQCLVQ 916
Cdd:pfam02463  379 KKLESERLSSAA---KLKEEELELKSEE-----EKEAQLLLEL-------ARQLEDLLKEEKKEELEILEEEEESIELKQ 443

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   917 ELKNIQSsipaskhmpipqvpqiypeevperrfqyDEETLLRFQRKQKKRQDKSSSKQSGTGSGGSAGGGLVGFLKLSSG 996
Cdd:pfam02463  444 GKLTEEK----------------------------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   997 KEGDLTTRDSLSRSSKASALLELPKPVEFEKAEPSDAELEimkrdEVKHLYMQQFLCNRINELTVTFDAELHLLRHQKLK 1076
Cdd:pfam02463  496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG-----VAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1077 LDTKMKLSDLHHLTLFQEMLLLKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQEKALYAGFQA 1156
Cdd:pfam02463  571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRK 650

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1157 ALGENNKFANFLMKVLKKKIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGS----------EDDVFDDSICPTN 1226
Cdd:pfam02463  651 GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeelkklklEAEELLADRVQEA 730

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1227 CDVSLFELALQLREKRLDIEEAL--VEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNELLVVIPL 1304
Cdd:pfam02463  731 QDKINEELKLLKQKIDEEEEEEEksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1305 KLHQIEYMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKEcRERRKLLIREKREMAKTISKMEETVREL 1384
Cdd:pfam02463  811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE-EITKEELLQELLLKEEELEEQKLKDELE 889

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1385 MISKFGRVIDLEALQTLSVNTTLEELKIKKLRKELSNAKELRMWEEKIAQ---VRWDLMMKTKEHTKKLHQMNDLCLEKK 1461
Cdd:pfam02463  890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEElllEEADEKEKEENNKEEEEERNKRLLLAK 969

                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|
gi 755553370  1462 KLDSRLNTLQnqqgnAFQGLRKaDIVAKQKVTELVQTQLEKITALKEEIE 1511
Cdd:pfam02463  970 EELGKVNLMA-----IEEFEEK-EERYNKDELEKERLEEEKKKLIRAIIE 1013
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1098-1298 2.19e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1098 LKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQ---EKALYAGFQAALGE-------NNKFANF 1167
Cdd:COG3883    25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGEraralyrSGGSVSY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1168 LMKVLKkkikrakkkevegdadedeeseesseeesslesdedaSGSEDDVFDDsicptncdvslFELALQLREKRLDIEE 1247
Cdd:COG3883   105 LDVLLG-------------------------------------SESFSDFLDR-----------LSALSKIADADADLLE 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755553370 1248 ALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNEL 1298
Cdd:COG3883   137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 487-567 1.04e-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: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  487 NPIRNITFSNDQTMMFCGMTNGAIRVYVLSENDPFLVSLQHYwhfnvhdnnyGSIKSITSSFDDQYLLTAGEDGNIFVFD 566
Cdd:cd00200    10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHT----------GPVRDVAASADGTYLASGSSDKTIRLWD 79


                  .
gi 755553370  567 I 567
Cdd:cd00200    80 L 80
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 1244-1435 1.51e-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: 42.36  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1244 DIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQ---REKQQRLNELLvviplklhqieymefgevpED 1320
Cdd:cd22656   111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQtalETLEKALKDLL-------------------TD 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1321 LSGTLVfsNHSLDRLQERIVQLQEENAKqqKLNKECRERRKLLIREKREMAK------TISKMEETVRELmISKFGRVID 1394
Cdd:cd22656   172 EGGAIA--RKEIKDLQKELEKLNEEYAA--KLKAKIDELKALIADDEAKLAAalrliaDLTAADTDLDNL-LALIGPAIP 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 755553370 1395 -LEALQTL--SVNTTLEELKiKKLRKELSNAKELRMWEEKIAQV 1435
Cdd:cd22656   247 aLEKLQGAwqAIATDLDSLK-DLLEDDISKIPAAILAKLELEKA 289
PTZ00121 PTZ00121
MAEBL; Provisional
 606-910 1.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  606 ENARKKREHDKLMKKVEELK-----AHKREQIKILRNEFWKLLELNK--ELPAHMQFQRTDfniDAKIHAEIHKKTSL-K 677
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKkkadeAKKAAEAKKKADEAKKAEEAKKadEAKKAEEAKKAD---EAKKAEEKKKADELkK 1553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  678 IEQVEKelAWEKQKHELGLKKLQDRFREPLESDTIvvyatqsdHQIASYRLVKPSK-YSKLKRPSQSERRQSKMERLEKE 756
Cdd:PTZ00121 1554 AEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEA--------KKAEEARIEEVMKlYEEEKKMKAEEAKKAEEAKIKAE 1623

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  757 GPGKKESQRDTGGSISLQEESVLEKGKKFR-PRTLSEIMVENQIEKTKKLIQQAERAQFKILQRKKEWEELYKSKpdddy 835
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA----- 1698

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  836 EDPKDVQAIKEAQTYmgdfNLKTAPDYKIPEHMR---INAAKKEEE------------LGYLDTMAHGKKRYMNKCiLSL 900
Cdd:PTZ00121 1699 EEAKKAEELKKKEAE----EKKKAEELKKAEEENkikAEEAKKEAEedkkkaeeakkdEEEKKKIAHLKKEEEKKA-EEI 1773

                         330
                  ....*....|
gi 755553370  901 RDLKLAVIEE 910
Cdd:PTZ00121 1774 RKEKEAVIEE 1783
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1233-1477 3.47e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1233 ELALQLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEA----------LEAYQREKQQRLNELlvvi 1302
Cdd:PRK02224  488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERaeelreraaeLEAEAEEKREAAAEA---- 563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1303 plklhQIEYMEFGEVPEDLSGTLVFSNHSLDRLqERIVQLQEENAkqqklnkECRERRKLLiREKREmakTISKMEETVR 1382
Cdd:PRK02224  564 -----EEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIA-------DAEDEIERL-REKRE---ALAELNDERR 626

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1383 ELMISKFGRVIDLEAlqtlsvntTLEELKIKKLRKELSNAKE-LRMWEEKIAQV---RWDLMMKTKEHTKKLHQMNDLCL 1458
Cdd:PRK02224  627 ERLAEKRERKRELEA--------EFDEARIEEAREDKERAEEyLEQVEEKLDELreeRDDLQAEIGAVENELEELEELRE 698

                         250
                  ....*....|....*....
gi 755553370 1459 EKKKLDSRLNTLQNQQGNA 1477
Cdd:PRK02224  699 RREALENRVEALEALYDEA 717
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
141-309 1.13e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 78.03  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  141 TQDPECLFSF--HSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVSA--SQIVVG 216
Cdd:COG2319   149 LATGKLLRTLtgHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFSPdgKLLASG 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  217 FQDGVVRVLELFDPKGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVEkEYKPIGFF 296
Cdd:COG2319   223 SADGTVRLWDLATGKLLRTLTG-----------------HSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGELLRTL 284

                         170
                  ....*....|....
gi 755553370  297 NTP-GPICQLMWSP 309
Cdd:COG2319   285 TGHsGGVNSVAFSP 298
WD40 COG2319
WD40 repeat [General function prediction only];
130-287 2.61e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.87  E-value: 2.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  130 IWKLDlsfsniTQDPECLFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVS 209
Cdd:COG2319   272 LWDLA------TGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFS 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  210 A--SQIVVGFQDGVVRVLELFDPKGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVE 287
Cdd:COG2319   340 PdgKTLASGSDDGTVRLWDLATGELLRTLTG-----------------HTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 141-309 2.21e-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: 72.37  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  141 TQDPECLFSF--HSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPL-VHMKFKQGGTSLIWAPRSvsvsaSQIVVGF 217
Cdd:cd00200   122 VETGKCLTTLrgHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVaTLTGHTGEVNSVAFSPDG-----EKLLSSS 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  218 QDGVVRVLELfdpkgltvyagrkkipdAELHLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFDVEKEYKPIGFFN 297
Cdd:cd00200   197 SDGTIKLWDL-----------------STGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSG 259

                         170
                  ....*....|..
gi 755553370  298 TPGPICQLMWSP 309
Cdd:cd00200   260 HTNSVTSLAWSP 271
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 151-309 7.15e-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: 7.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  151 HSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLvhmKFKQGGTSLIWAPRSVSVSaSQIVVGFQDGVVRVLELFDP 230
Cdd:cd00200     8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL---RTLKGHTGPVRDVAASADG-TYLASGSSDKTIRLWDLETG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  231 KGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVEKeYKPIGFFNT-PGPICQLMWSP 309
Cdd:cd00200    84 ECVRTLTG-----------------HTSYVSSVAFSPDGRILSSSSRDKTIKVWDVET-GKCLTTLRGhTDWVNSVAFSP 145
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 123-309 1.80e-12

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: 69.67  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  123 AQDANGAIWKLDlsfsniTQDPECLFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMK-FKQGGTSLIW 201
Cdd:cd00200    28 SGDGTIKVWDLE------TGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTgHTSYVSSVAF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  202 APrsvsvsASQIVVG-FQDGVVRVLELFDPKgltvyagrkkipdaelhLKYVFKPHTDEVTALAYERDGDILATGSEDKT 280
Cdd:cd00200   102 SP------DGRILSSsSRDKTIKVWDVETGK-----------------CLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 755553370  281 VFFFDVEKEyKPIGFFNTP-GPICQLMWSP 309
Cdd:cd00200   159 IKLWDLRTG-KCVATLTGHtGEVNSVAFSP 187
WD40 COG2319
WD40 repeat [General function prediction only];
121-287 3.58e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 54.53  E-value: 3.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  121 WLAQDANGAIWKLDLSFSNITQDPECLFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMkfkQGGTSLI 200
Cdd:COG2319     5 DGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATL---LGHTAAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  201 WApRSVSVSASQIVVGFQDGVVRVLELFDPKGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKT 280
Cdd:COG2319    82 LS-VAFSPDGRLLASASADGTVRLWDLATGLLLRTLTG-----------------HTGAVRSVAFSPDGKTLASGSADGT 143


                  ....*..
gi 755553370  281 VFFFDVE 287
Cdd:COG2319   144 VRLWDLA 150
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 248-285 1.57e-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: 1.57e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 755553370    248 HLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 285
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
249-285 2.45e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 2.45e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 755553370   249 LKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 285
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1233-1511 1.34e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1233 ELALQLREKRLDIEEA--------LVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREK----------QQR 1294
Cdd:TIGR02168  210 EKAERYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeieelQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1295 LNELLVVIPLKLHQIEymEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTI 1374
Cdd:TIGR02168  290 LYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1375 SKMEETVRELMiskfgrvidlEALQTLSVNTTLEELKIKKLRKELSNAK-ELRMWE---EKIAQVRWDLMMKTKEHTKKL 1450
Cdd:TIGR02168  368 EELESRLEELE----------EQLETLRSKVAQLELQIASLNNEIERLEaRLERLEdrrERLQQEIEELLKKLEEAELKE 437

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755553370  1451 HQMN--DLCLEKKKLDSRLNTLQNQQGNAFQGLRKA--DIVAKQKVTELVQTQLEKITALKEEIE 1511
Cdd:TIGR02168  438 LQAEleELEEELEELQEELERLEEALEELREELEEAeqALDAAERELAQLQARLDSLERLQENLE 502
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 249-312 1.38e-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: 1.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755553370  249 LKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFDVEKEYKPIGFFNTPGPICQLMWSPASH 312
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGT 64
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1240-1508 1.65e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1240 EKRLDIEEALVEEKKI-VDNLKKE------YDTISKK-----VKVVATNLNAAEEALEAYQRE------KQQRLNELLVV 1301
Cdd:TIGR02169  183 EENIERLDLIIDEKRQqLERLRRErekaerYQALLKEkreyeGYELLKEKEALERQKEAIERQlasleeELEKLTEEISE 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1302 IPLKLHQIEymefgEVPEDLsgtlvfsNHSLDRL-QERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEET 1380
Cdd:TIGR02169  263 LEKRLEEIE-----QLLEEL-------NKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1381 VRELM--ISKFGRVIDLEALQTLSVNTTLEELKIK--KLRKEL-SNAKELRMWEEKIAQVRWDLMMKTKEHTKKLHQMND 1455
Cdd:TIGR02169  331 IDKLLaeIEELEREIEEERKRRDKLTEEYAELKEEleDLRAELeEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 755553370  1456 LCLEKKKLDSRLNTLqnqqgnafqglrKADI-VAKQKVTELVQTQLEKITALKE 1508
Cdd:TIGR02169  411 LQEELQRLSEELADL------------NAAIaGIEAKINELEEEKEDKALEIKK 452
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1237-1424 1.74e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1237 QLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEayqrEKQQRLNELLVVIpLKLHQIEYMEF-- 1314
Cdd:COG4942    52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE----AQKEELAELLRAL-YRLGRQPPLALll 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1315 -GEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETV--RELMISKFGR 1391
Cdd:COG4942   127 sPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKaeRQKLLARLEK 206

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 755553370 1392 VIDLEA--LQTLSVNTTLEELKIKKLRKELSNAKE 1424
Cdd:COG4942   207 ELAELAaeLAELQQEAEELEALIARLEAEAAAAAE 241
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1234-1511 2.40e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1234 LALQLREKRLDIEEALVEEKKI---VDNLKKEYDTISKKVKVVATNLNAAEEALEAyQREKQQRLNELLvviplKLHQIE 1310
Cdd:COG1196   216 RELKEELKELEAELLLLKLRELeaeLEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELEL-----EEAQAE 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1311 YMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETVRELMISKFG 1390
Cdd:COG1196   290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1391 RVIDLEALQTLSVNTTLEEL-KIKKLRKELSNAKELRMWEEKIAQVRWDLMMKTKEHTKKLHQMNDLCLEKKKLDSRLNT 1469
Cdd:COG1196   370 AEAELAEAEEELEELAEELLeALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 755553370 1470 LQNQQGNAFQGLRKAdIVAKQKVTELVQTQLEKITALKEEIE 1511
Cdd:COG1196   450 EEAELEEEEEALLEL-LAELLEEAALLEAALAELLEELAEAA 490
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 597-1511 8.03e-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: 47.66  E-value: 8.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   597 IEDPKAYSIENARKKREHDKLMKKVEELKAHKREQIKILRNEFwKLLELNKELPAHMQFQRTDFNIDAKIHAEIHKKTSL 676
Cdd:pfam02463  158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL-KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   677 KIEQVEKELAWEKQKHELGLKKLQDRFREPLEsdtivvyatQSDHQIASYRLVKPSKYSKLKRpSQSERRQSKMERLEKE 756
Cdd:pfam02463  237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLA---------QVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLE 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   757 GPGKKESQRDTGGSISLQEESVLEKGKKfrprtlsEIMVENQIEKTKKLIQQAERAQfKILQRKKEWEELYKSKPDDDYE 836
Cdd:pfam02463  307 RRKVDDEEKLKESEKEKKKAEKELKKEK-------EEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAK 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   837 DPKDVQAIKEAQtymGDFNLKTAPDYKIpehmrINAAKKEEELgyldtmaHGKKRYMNKCILSLRDLKLAVIEEIQCLVQ 916
Cdd:pfam02463  379 KKLESERLSSAA---KLKEEELELKSEE-----EKEAQLLLEL-------ARQLEDLLKEEKKEELEILEEEEESIELKQ 443

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   917 ELKNIQSsipaskhmpipqvpqiypeevperrfqyDEETLLRFQRKQKKRQDKSSSKQSGTGSGGSAGGGLVGFLKLSSG 996
Cdd:pfam02463  444 GKLTEEK----------------------------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   997 KEGDLTTRDSLSRSSKASALLELPKPVEFEKAEPSDAELEimkrdEVKHLYMQQFLCNRINELTVTFDAELHLLRHQKLK 1076
Cdd:pfam02463  496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG-----VAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1077 LDTKMKLSDLHHLTLFQEMLLLKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQEKALYAGFQA 1156
Cdd:pfam02463  571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRK 650

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1157 ALGENNKFANFLMKVLKKKIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGS----------EDDVFDDSICPTN 1226
Cdd:pfam02463  651 GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeelkklklEAEELLADRVQEA 730

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1227 CDVSLFELALQLREKRLDIEEAL--VEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNELLVVIPL 1304
Cdd:pfam02463  731 QDKINEELKLLKQKIDEEEEEEEksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1305 KLHQIEYMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKEcRERRKLLIREKREMAKTISKMEETVREL 1384
Cdd:pfam02463  811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE-EITKEELLQELLLKEEELEEQKLKDELE 889

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1385 MISKFGRVIDLEALQTLSVNTTLEELKIKKLRKELSNAKELRMWEEKIAQ---VRWDLMMKTKEHTKKLHQMNDLCLEKK 1461
Cdd:pfam02463  890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEElllEEADEKEKEENNKEEEEERNKRLLLAK 969

                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|
gi 755553370  1462 KLDSRLNTLQnqqgnAFQGLRKaDIVAKQKVTELVQTQLEKITALKEEIE 1511
Cdd:pfam02463  970 EELGKVNLMA-----IEEFEEK-EERYNKDELEKERLEEEKKKLIRAIIE 1013
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1098-1298 2.19e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1098 LKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQ---EKALYAGFQAALGE-------NNKFANF 1167
Cdd:COG3883    25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGEraralyrSGGSVSY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1168 LMKVLKkkikrakkkevegdadedeeseesseeesslesdedaSGSEDDVFDDsicptncdvslFELALQLREKRLDIEE 1247
Cdd:COG3883   105 LDVLLG-------------------------------------SESFSDFLDR-----------LSALSKIADADADLLE 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755553370 1248 ALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNEL 1298
Cdd:COG3883   137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1237-1436 8.76e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 8.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1237 QLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQRE---KQQRLNELLVVIPLKLHQIEYME 1313
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanLRERLESLERRIAATERRLEDLE 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1314 fgEVPEDLSGTLVFSNHSL-------DRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETVRELM- 1385
Cdd:TIGR02168  845 --EQIEELSEDIESLAAEIeeleeliEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRe 922

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1386 -ISKFGRVID------LEALQTLSV--NTTLEELKIKKLRKELSNAKelrmWEEKIAQVR 1436
Cdd:TIGR02168  923 kLAQLELRLEglevriDNLQERLSEeySLTLEEAEALENKIEDDEEE----ARRRLKRLE 978
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 487-567 1.04e-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: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  487 NPIRNITFSNDQTMMFCGMTNGAIRVYVLSENDPFLVSLQHYwhfnvhdnnyGSIKSITSSFDDQYLLTAGEDGNIFVFD 566
Cdd:cd00200    10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHT----------GPVRDVAASADGTYLASGSSDKTIRLWD 79


                  .
gi 755553370  567 I 567
Cdd:cd00200    80 L 80
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 589-824 1.33e-03

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: 43.19  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   589 ESEAAPE-DIEDPKAYSIENARKKREHDKLMKKVEeLKAHKREQIKILRNEFWKLLELNKELpAHMQFQRTDFNidAKIH 667
Cdd:pfam17380  320 EAEKARQaEMDRQAAIYAEQERMAMERERELERIR-QEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKN--ERVR 395

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   668 AEIHKKTSLKIEQVEKELAWEKQKHEL-GLKKLQDRFREplesDTIVVYATQSDHQIASYRLVKPSKYSKLKRPSQSE-- 744
Cdd:pfam17380  396 QELEAARKVKILEEERQRKIQQQKVEMeQIRAEQEEARQ----REVRRLEEERAREMERVRLEEQERQQQVERLRQQEee 471

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370   745 RRQSKMErLEKEGPGKKESQRdtggsislQEESVLEKGKKFRPRTLSE-----IMVENQIEKTKKLIQQAERAQFKILQR 819
Cdd:pfam17380  472 RKRKKLE-LEKEKRDRKRAEE--------QRRKILEKELEERKQAMIEeerkrKLLEKEMEERQKAIYEEERRREAEEER 542


                   ....*
gi 755553370   820 KKEWE 824
Cdd:pfam17380  543 RKQQE 547
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 1244-1435 1.51e-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: 42.36  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1244 DIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQ---REKQQRLNELLvviplklhqieymefgevpED 1320
Cdd:cd22656   111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQtalETLEKALKDLL-------------------TD 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1321 LSGTLVfsNHSLDRLQERIVQLQEENAKqqKLNKECRERRKLLIREKREMAK------TISKMEETVRELmISKFGRVID 1394
Cdd:cd22656   172 EGGAIA--RKEIKDLQKELEKLNEEYAA--KLKAKIDELKALIADDEAKLAAalrliaDLTAADTDLDNL-LALIGPAIP 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 755553370 1395 -LEALQTL--SVNTTLEELKiKKLRKELSNAKELRMWEEKIAQV 1435
Cdd:cd22656   247 aLEKLQGAwqAIATDLDSLK-DLLEDDISKIPAAILAKLELEKA 289
PTZ00121 PTZ00121
MAEBL; Provisional
 606-910 1.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  606 ENARKKREHDKLMKKVEELK-----AHKREQIKILRNEFWKLLELNK--ELPAHMQFQRTDfniDAKIHAEIHKKTSL-K 677
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKkkadeAKKAAEAKKKADEAKKAEEAKKadEAKKAEEAKKAD---EAKKAEEKKKADELkK 1553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  678 IEQVEKelAWEKQKHELGLKKLQDRFREPLESDTIvvyatqsdHQIASYRLVKPSK-YSKLKRPSQSERRQSKMERLEKE 756
Cdd:PTZ00121 1554 AEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEA--------KKAEEARIEEVMKlYEEEKKMKAEEAKKAEEAKIKAE 1623

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  757 GPGKKESQRDTGGSISLQEESVLEKGKKFR-PRTLSEIMVENQIEKTKKLIQQAERAQFKILQRKKEWEELYKSKpdddy 835
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA----- 1698

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  836 EDPKDVQAIKEAQTYmgdfNLKTAPDYKIPEHMR---INAAKKEEE------------LGYLDTMAHGKKRYMNKCiLSL 900
Cdd:PTZ00121 1699 EEAKKAEELKKKEAE----EKKKAEELKKAEEENkikAEEAKKEAEedkkkaeeakkdEEEKKKIAHLKKEEEKKA-EEI 1773

                         330
                  ....*....|
gi 755553370  901 RDLKLAVIEE 910
Cdd:PTZ00121 1774 RKEKEAVIEE 1783
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 141-180 2.13e-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: 2.13e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 755553370    141 TQDPECLFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYD 180
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1230-1511 2.18e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1230 SLFELALQLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAyQREKQQRLNELLVVIPLKLHQI 1309
Cdd:COG4372    14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ-ARSELEQLEEELEELNEQLQAA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1310 EymefgEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETVRELMISKF 1389
Cdd:COG4372    93 Q-----AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1390 GRVIDLEALQTLSVNTTLEEL-------KIKKLRKELSNAKELRMWEEKIAQVRWDLMMKTKEHTKKLHQMNDLCLEKKK 1462
Cdd:COG4372   168 ALEQELQALSEAEAEQALDELlkeanrnAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 755553370 1463 LDSRLNTLQNQQGNAFQGLRKADIVAKQKVTELVQTQLEKITALKEEIE 1511
Cdd:COG4372   248 KEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK 296
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1233-1477 3.47e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1233 ELALQLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEA----------LEAYQREKQQRLNELlvvi 1302
Cdd:PRK02224  488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERaeelreraaeLEAEAEEKREAAAEA---- 563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1303 plklhQIEYMEFGEVPEDLSGTLVFSNHSLDRLqERIVQLQEENAkqqklnkECRERRKLLiREKREmakTISKMEETVR 1382
Cdd:PRK02224  564 -----EEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIA-------DAEDEIERL-REKRE---ALAELNDERR 626

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1383 ELMISKFGRVIDLEAlqtlsvntTLEELKIKKLRKELSNAKE-LRMWEEKIAQV---RWDLMMKTKEHTKKLHQMNDLCL 1458
Cdd:PRK02224  627 ERLAEKRERKRELEA--------EFDEARIEEAREDKERAEEyLEQVEEKLDELreeRDDLQAEIGAVENELEELEELRE 698

                         250
                  ....*....|....*....
gi 755553370 1459 EKKKLDSRLNTLQNQQGNA 1477
Cdd:PRK02224  699 RREALENRVEALEALYDEA 717
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1098-1384 3.94e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 3.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1098 LKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEE---KKNEITKLQDQEKALYAGFQAALGENNKFANFLMKVLKK 1174
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1175 KIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGSEDDVfddsicptncDVSLFELALQLREKRLDIEEALVEEKK 1254
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL----------AAEIEELEELIEELESELEALLNERAS 884

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  1255 I---VDNLKKEYDTISKKVKVVATNLNAAE-------EALEAYQREKQ---QRLNELLVVIPlKLHQIEYMEFGEVPEDL 1321
Cdd:TIGR02168  885 LeeaLALLRSELEELSEELRELESKRSELRreleelrEKLAQLELRLEgleVRIDNLQERLS-EEYSLTLEEAEALENKI 963

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755553370  1322 SGTLVFSNHSLDRLQERIVQLQEENakqqkLN-----KECRERRKLLIREKREMAKTISKMEETVREL 1384
Cdd:TIGR02168  964 EDDEEEARRRLKRLENKIKELGPVN-----LAaieeyEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1230-1439 4.22e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1230 SLFELALQLRE-----KRLDIEEaLVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEE------ALEAYQREKQQRLNEL 1298
Cdd:PRK03918  497 KLKELAEQLKEleeklKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAEL 575

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1299 LvviplklHQIEYMEFGEVPEDLSG------------TLVFSNHSLDRLQERIVQLQEE----NAKQQKLNKECRERRKL 1362
Cdd:PRK03918  576 L-------KELEELGFESVEELEERlkelepfyneylELKDAEKELEREEKELKKLEEEldkaFEELAETEKRLEELRKE 648

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370 1363 LirekREMAKTISKME-ETVRELMISKFGRVIDLEAlQTLSVNTTLEELK--IKKLRKELSNAKELRMWEEKIAQVRWDL 1439
Cdd:PRK03918  649 L----EELEKKYSEEEyEELREEYLELSRELAGLRA-ELEELEKRREEIKktLEKLKEELEEREKAKKELEKLEKALERV 723
WD40 pfam00400
WD domain, G-beta repeat;
145-180 5.40e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 5.40e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 755553370   145 ECLFSF--HSGPIAALAVSPLTYLMATTAMDCSVRVYD 180
Cdd:pfam00400    2 KLLKTLegHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00121 PTZ00121
MAEBL; Provisional
 589-848 9.15e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 9.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  589 ESEAAPEDIEDPKAYSIENARKKREHDKLmKKVEELK----AHKREQIKilRNEFWKLLELNK-ELPAHMQFQRTDFNID 663
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADEL-KKAEELKkaeeKKKAEEAK--KAEEDKNMALRKaEEAKKAEEARIEEVMK 1599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  664 AKIHAEIHKKTSLKIEQVEKELAWEKQKHELGLKKLQDRFREPLESdtivvyaTQSDHQIASYRLVKPSKYSKLKRPSQS 743
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE-------KKKAEELKKAEEENKIKAAEEAKKAEE 1672

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553370  744 ERRQSKMERLEKEGPGKKESQRDtggsislQEESVLEKGKKFRPRTlseimvENQIEKTKKLIQQAERAQFKILQRKKEW 823
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALK-------KEAEEAKKAEELKKKE------AEEKKKAEELKKAEEENKIKAEEAKKEA 1739

                         250       260
                  ....*....|....*....|....*...
gi 755553370  824 EElYKSKPDD---DYEDPKDVQAIKEAQ 848
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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