|
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 755553365 222 VDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFWEMAftfTGlKLQGS 301
Cdd:COG2319 84 VAFSPDGRLLASAS--ADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA---TG-KLLRT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 302 LgrfgKTSTSDIEGYAELPDGKVL-SGSEWGNLLLWE---GSLIKVelcRTGmkscHSGSINQIML--DEGEVITAGSDG 375
Cdd:COG2319 158 L----TGHSGAVTSVAFSPDGKLLaSGSDDGTVRLWDlatGKLLRT---LTG----HTGAVRSVAFspDGKLLASGSADG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 376 SVRIWDFETIDTADVIDDTGlleiEPINelhidkSVNlFSmikmnevGNNFWLA---QDANGAIWKLDlsfsniTQDPEC 452
Cdd:COG2319 227 TVRLWDLATGKLLRTLTGHS----GSVR------SVA-FS-------PDGRLLAsgsADGTVRLWDLA------TGELLR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 453 LFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVSA--SQIVVGFQDGVVRV 530
Cdd:COG2319 283 TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFSPdgKTLASGSDDGTVRL 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755553365 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 755553365 320 PDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSDGSVRIWDFETIDTADVIddTGl 396
Cdd:cd00200 19 PDGKLLaTGSGDGTIKVWDLETGELLRTLKG----HTGPVRDVAAsaDGTYLASGSSDKTIRLWDLETGECVRTL--TG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 397 lEIEPINELHIDKsvnlfsmikmnevgNNFWLA---QDANGAIWKLDlsfsnitqDPECLFSF--HSGPIAALAVSPLTY 471
Cdd:cd00200 92 -HTSYVSSVAFSP--------------DGRILSsssRDKTIKVWDVE--------TGKCLTTLrgHTDWVNSVAFSPDGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 472 LMATTAMDCSVRVYDFSSKNPL-VHMKFKQGGTSLIWAPRSvsvsaSQIVVGFQDGVVRVLELfdpkgltvyagrkkipd 550
Cdd:cd00200 149 FVASSSQDGTIKLWDLRTGKCVaTLTGHTGEVNSVAFSPDG-----EKLLSSSSDGTIKLWDL----------------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755553365 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 755553365 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 755553365 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 755553365 1539 ELALQLREKRLDIEEA--------LVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREK----------QQR 1600
Cdd:TIGR02168 210 EKAERYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeieelQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1601 LNELLVVIPLKLHQIEymEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTI 1680
Cdd:TIGR02168 290 LYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1681 SKMEETVRELMiskfgrvidlEALQTLSVNTTLEELKIKKLRKELSNAK-ELRMWE---EKIAQVRWDLMMKTKEHTKKL 1756
Cdd:TIGR02168 368 EELESRLEELE----------EQLETLRSKVAQLELQIASLNNEIERLEaRLERLEdrrERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755553365 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 755553365 1543 QLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEayqrEKQQRLNELLVVIpLKLHQIEYMEF-- 1620
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE----AQKEELAELLRAL-YRLGRQPPLALll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1621 -GEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETV--RELMISKFGR 1697
Cdd:COG4942 127 sPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKaeRQKLLARLEK 206
|
170 180 190
....*....|....*....|....*....|....*
gi 755553365 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 755553365 903 IEDPKAYSIENARKKREHDKLMKKVEELKAHKREQIKILRNEFwKLLELNKELPAHMQFQRTDFNIDAKIHAEIHKKTSL 982
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL-KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 983 KIEQVEKELAWEKQKHELGLKKLQDRFREPLEsdtivvyatQSDHQIASYRLVKPSKYSKLKRpSQSERRQSKMERLEKE 1062
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLA---------QVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1063 GPGKKESQRDTGGSISLQEESVLEKGKKfrprtlsEIMVENQIEKTKKLIQQAERAQfKILQRKKEWEELYKSKPDDDYE 1142
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEK-------EEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1143 DPKDVQAIKEAQtymGDFNLKTAPDYKIpehmrINAAKKEEELgyldtmaHGKKRYMNKCILSLRDLKLAVIEEIQCLVQ 1222
Cdd:pfam02463 379 KKLESERLSSAA---KLKEEELELKSEE-----EKEAQLLLEL-------ARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1223 ELKNIQSsipaskhmpipqvpqiypeevperrfqyDEETLLRFQRKQKKRQDKSSSKQSGTGSGGSAGGGLVGFLKLSSG 1302
Cdd:pfam02463 444 GKLTEEK----------------------------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1303 KEGDLTTRDSLSRSSKASALLELPKPVEFEKAEPSDAELEimkrdEVKHLYMQQFLCNRINELTVTFDAELHLLRHQKLK 1382
Cdd:pfam02463 496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG-----VAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1383 LDTKMKLSDLHHLTLFQEMLLLKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQEKALYAGFQA 1462
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRK 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1463 ALGENNKFANFLMKVLKKKIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGS----------EDDVFDDSICPTN 1532
Cdd:pfam02463 651 GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeelkklklEAEELLADRVQEA 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1533 CDVSLFELALQLREKRLDIEEAL--VEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNELLVVIPL 1610
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1611 KLHQIEYMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKEcRERRKLLIREKREMAKTISKMEETVREL 1690
Cdd:pfam02463 811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE-EITKEELLQELLLKEEELEEQKLKDELE 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1691 MISKFGRVIDLEALQTLSVNTTLEELKIKKLRKELSNAKELRMWEEKIAQ---VRWDLMMKTKEHTKKLHQMNDLCLEKK 1767
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEElllEEADEKEKEENNKEEEEERNKRLLLAK 969
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 755553365 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 755553365 1404 LKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQ---EKALYAGFQAALGE-------NNKFANF 1473
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGEraralyrSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1474 LMKVLKkkikrakkkevegdadedeeseesseeesslesdedaSGSEDDVFDDsicptncdvslFELALQLREKRLDIEE 1553
Cdd:COG3883 105 LDVLLG-------------------------------------SESFSDFLDR-----------LSALSKIADADADLLE 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 755553365 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 755553365 793 NPIRNITFSNDQTMMFCGMTNGAIRVYVLSENDPFLVSLQHYwhfnvhdnnyGSIKSITSSFDDQYLLTAGEDGNIFVFD 872
Cdd:cd00200 10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHT----------GPVRDVAASADGTYLASGSSDKTIRLWD 79
|
.
gi 755553365 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 755553365 912 ENARKKREHDKLMKKVEELK-----AHKREQIKILRNEFWKLLELNK--ELPAHMQFQRTDfniDAKIHAEIHKKTSL-K 983
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKkkadeAKKAAEAKKKADEAKKAEEAKKadEAKKAEEAKKAD---EAKKAEEKKKADELkK 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 984 IEQVEKelAWEKQKHELGLKKLQDRFREPLESDTIvvyatqsdHQIASYRLVKPSK-YSKLKRPSQSERRQSKMERLEKE 1062
Cdd:PTZ00121 1554 AEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEA--------KKAEEARIEEVMKlYEEEKKMKAEEAKKAEEAKIKAE 1623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1063 GPGKKESQRDTGGSISLQEESVLEKGKKFR-PRTLSEIMVENQIEKTKKLIQQAERAQFKILQRKKEWEELYKSKpdddy 1141
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA----- 1698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1142 EDPKDVQAIKEAQTYmgdfNLKTAPDYKIPEHMR---INAAKKEEE------------LGYLDTMAHGKKRYMNKCiLSL 1206
Cdd:PTZ00121 1699 EEAKKAEELKKKEAE----EKKKAEELKKAEEENkikAEEAKKEAEedkkkaeeakkdEEEKKKIAHLKKEEEKKA-EEI 1773
|
330
....*....|
gi 755553365 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 755553365 1537 LFELALQLREKR--LDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQ---REKQQRLNELLvviplk 1611
Cdd:cd22656 96 ILELIDDLADATddEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQtalETLEKALKDLL------ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1612 lhqieymefgevpEDLSGTLVfsNHSLDRLQERIVQLQEENAKqqKLNKECRERRKLLIREKREMAK------TISKMEE 1685
Cdd:cd22656 170 -------------TDEGGAIA--RKEIKDLQKELEKLNEEYAA--KLKAKIDELKALIADDEAKLAAalrliaDLTAADT 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 755553365 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 755553365 1536 SLFELALQLRE-----KRLDIEEaLVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEE------ALEAYQREKQQRLNEL 1604
Cdd:PRK03918 497 KLKELAEQLKEleeklKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAEL 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1605 LvviplklHQIEYMEFGEVPEDLSG------------TLVFSNHSLDRLQERIVQLQEE----NAKQQKLNKECRERRKL 1668
Cdd:PRK03918 576 L-------KELEELGFESVEELEERlkelepfyneylELKDAEKELEREEKELKKLEEEldkaFEELAETEKRLEELRKE 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 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 755553365 222 VDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFWEMAftfTGlKLQGS 301
Cdd:COG2319 84 VAFSPDGRLLASAS--ADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA---TG-KLLRT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 302 LgrfgKTSTSDIEGYAELPDGKVL-SGSEWGNLLLWE---GSLIKVelcRTGmkscHSGSINQIML--DEGEVITAGSDG 375
Cdd:COG2319 158 L----TGHSGAVTSVAFSPDGKLLaSGSDDGTVRLWDlatGKLLRT---LTG----HTGAVRSVAFspDGKLLASGSADG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 376 SVRIWDFETIDTADVIDDTGlleiEPINelhidkSVNlFSmikmnevGNNFWLA---QDANGAIWKLDlsfsniTQDPEC 452
Cdd:COG2319 227 TVRLWDLATGKLLRTLTGHS----GSVR------SVA-FS-------PDGRLLAsgsADGTVRLWDLA------TGELLR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 453 LFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVSA--SQIVVGFQDGVVRV 530
Cdd:COG2319 283 TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFSPdgKTLASGSDDGTVRL 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755553365 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 755553365 239 DYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFWEMAftftglklQGSLGRFGKTSTSDIEGYAE 318
Cdd:COG2319 57 DLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA--------TGLLLRTLTGHTGAVRSVAF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 319 LPDGK-VLSGSEWGNLLLWE---GSLIKVelcrtgmKSCHSGSINQIML--DEGEVITAGSDGSVRIWDFETIDTADVID 392
Cdd:COG2319 129 SPDGKtLASGSADGTVRLWDlatGKLLRT-------LTGHSGAVTSVAFspDGKLLASGSDDGTVRLWDLATGKLLRTLT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 393 DTGlleiEPINELHidksvnlFSmikmnevGNNFWLA---QDANGAIWKLDlsfsniTQDPECLFSFHSGPIAALAVSPL 469
Cdd:COG2319 202 GHT----GAVRSVA-------FS-------PDGKLLAsgsADGTVRLWDLA------TGKLLRTLTGHSGSVRSVAFSPD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 470 TYLMATTAMDCSVRVYDFSSKNPLvhmKFKQGGTSLIWaprSVSVSA--SQIVVGFQDGVVRVLELfdpkgltvyagrkk 547
Cdd:COG2319 258 GRLLASGSADGTVRLWDLATGELL---RTLTGHSGGVN---SVAFSPdgKLLASGSDDGTVRLWDL-------------- 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755553365 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 755553365 320 PDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSDGSVRIWDFETIDTADVIddTGl 396
Cdd:cd00200 19 PDGKLLaTGSGDGTIKVWDLETGELLRTLKG----HTGPVRDVAAsaDGTYLASGSSDKTIRLWDLETGECVRTL--TG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 397 lEIEPINELHIDKsvnlfsmikmnevgNNFWLA---QDANGAIWKLDlsfsnitqDPECLFSF--HSGPIAALAVSPLTY 471
Cdd:cd00200 92 -HTSYVSSVAFSP--------------DGRILSsssRDKTIKVWDVE--------TGKCLTTLrgHTDWVNSVAFSPDGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 472 LMATTAMDCSVRVYDFSSKNPL-VHMKFKQGGTSLIWAPRSvsvsaSQIVVGFQDGVVRVLELfdpkgltvyagrkkipd 550
Cdd:cd00200 149 FVASSSQDGTIKLWDLRTGKCVaTLTGHTGEVNSVAFSPDG-----EKLLSSSSDGTIKLWDL----------------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755553365 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 755553365 222 VDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFW-----EMAFTFTGl 296
Cdd:cd00200 15 VAFSPDGKLLATGS--GDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWdletgECVRTLTG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 297 klqgslgrfgktSTSDIEGYAELPDGKVLSGSEW-GNLLLWEgsLIKVELCRTGmkSCHSGSINQI-MLDEGEVITAGS- 373
Cdd:cd00200 92 ------------HTSYVSSVAFSPDGRILSSSSRdKTIKVWD--VETGKCLTTL--RGHTDWVNSVaFSPDGTFVASSSq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 374 DGSVRIWDFETIdtadviddtglleiepinelhidksvnlfsmikmnevgnnfwlaqdangaiwkldlsfsnitqdpECL 453
Cdd:cd00200 156 DGTIKLWDLRTG-----------------------------------------------------------------KCV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 454 --FSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKFKQGG-TSLIWAP-RSVSVSASQivvgfqDGVVR 529
Cdd:cd00200 171 atLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGvNSVAFSPdGYLLASGSE------DGTIR 244
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755553365 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 755553365 239 DYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFWEMAftftglklQGSLGRFGKTSTSDIEGYAE 318
Cdd:COG2319 15 DLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAA--------AGALLATLLGHTAAVLSVAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 319 LPDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSDGSVRIWDfetidtadviddtg 395
Cdd:COG2319 87 SPDGRLLaSASADGTVRLWDLATGLLLRTLTG----HTGAVRSVAFspDGKTLASGSADGTVRLWD-------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 396 lleiepinelhidksvnlfsmikmnevgnnfwlaqdangaiwkldlsfsniTQDPECLFSF--HSGPIAALAVSPLTYLM 473
Cdd:COG2319 149 ---------------------------------------------------LATGKLLRTLtgHSGAVTSVAFSPDGKLL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 474 ATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVSA--SQIVVGFQDGVVRVLELFDPKGLTVYAGrkkipda 551
Cdd:COG2319 178 ASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFSPdgKLLASGSADGTVRLWDLATGKLLRTLTG------- 244
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755553365 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 755553365 137 LQLLDSNTLLYVAG--NQMVLLDFKDKTQIYLQSSSGQGIGAIGVHPKKTYFAVAekGSFPKIIIYEYPSLKPYRILRdG 214
Cdd:cd00200 15 VAFSPDGKLLATGSgdGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASG--SSDKTIRLWDLETGECVRTLT-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 215 AEKAYAYVDFNNEGNLLasVGCHPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNdeQLTTSGS--GHIKFWEMAft 292
Cdd:cd00200 92 HTSYVSSVAFSPDGRIL--SSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDG--TFVASSSqdGTIKLWDLR-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 293 ftglklQGSLGRFGKTSTSDIEGYAELPDG-KVLSGSEWGNLLLWEgslikvelCRTGMKSC----HSGSINQIMLDE-G 366
Cdd:cd00200 166 ------TGKCVATLTGHTGEVNSVAFSPDGeKLLSSSSDGTIKLWD--------LSTGKCLGtlrgHENGVNSVAFSPdG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 367 EVITAGS-DGSVRIWDFETidtadviddtglleiepinelhidksvnlfsmikmnevgnnfwlaqdangaiwkldlsfsn 445
Cdd:cd00200 232 YLLASGSeDGTIRVWDLRT------------------------------------------------------------- 250
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 755553365 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 755553365 141 DSNTLLYVAGNQMV-LLDFKDKTQIYLQSSSGQGIGAIGVHPKKTYFAVAekGSFPKIIIYEYPSLKPYRILRDGAEKAY 219
Cdd:COG2319 131 DGKTLASGSADGTVrLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASG--SDDGTVRLWDLATGKLLRTLTGHTGAVR 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 220 AyVDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNdEQL-TTSGSGHIKFWEMAFTFTGLKL 298
Cdd:COG2319 209 S-VAFSPDGKLLASGS--ADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDG-RLLaSGSADGTVRLWDLATGELLRTL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 299 QGSLGRFGKTSTSdiegyaelPDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSDG 375
Cdd:COG2319 285 TGHSGGVNSVAFS--------PDGKLLaSGSDDGTVRLWDLATGKLLRTLTG----HTGAVRSVAFspDGKTLASGSDDG 352
|
....*....
gi 755553365 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 755553365 141 DSNTLLYVAGNQMVLL-DFKDKTQIYLQSSSGQGIGAIGVHPKKTYFAVaekGSFPK-IIIYEYPSLKPYRILRDGAEKA 218
Cdd:COG2319 173 DGKLLASGSDDGTVRLwDLATGKLLRTLTGHTGAVRSVAFSPDGKLLAS---GSADGtVRLWDLATGKLLRTLTGHSGSV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 219 YAyVDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDnDEQL-TTSGSGHIKFWEMAftfTGLK 297
Cdd:COG2319 250 RS-VAFSPDGRLLASGS--ADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPD-GKLLaSGSDDGTVRLWDLA---TGKL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 298 LQGSLGrfgktSTSDIEGYAELPDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSD 374
Cdd:COG2319 323 LRTLTG-----HTGAVRSVAFSPDGKTLaSGSDDGTVRLWDLATGELLRTLTG----HTGAVTSVAFspDGRTLASGSAD 393
|
250
....*....|
gi 755553365 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 755553365 457 HSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLvhmKFKQGGTSLIWAPRSVSVSaSQIVVGFQDGVVRVLELFDP 536
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL---RTLKGHTGPVRDVAASADG-TYLASGSSDKTIRLWDLETG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 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 755553365 427 WLAQDANGAIWKLDLSFSNITQDPECLFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMkfkQGGTSLI 506
Cdd:COG2319 5 DGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATL---LGHTAAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 507 WApRSVSVSASQIVVGFQDGVVRVLELFDPKGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKT 586
Cdd:COG2319 82 LS-VAFSPDGRLLASASADGTVRLWDLATGLLLRTLTG-----------------HTGAVRSVAFSPDGKTLASGSADGT 143
|
....*..
gi 755553365 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 755553365 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 755553365 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 755553365 1539 ELALQLREKRLDIEEA--------LVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREK----------QQR 1600
Cdd:TIGR02168 210 EKAERYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeieelQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1601 LNELLVVIPLKLHQIEymEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTI 1680
Cdd:TIGR02168 290 LYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1681 SKMEETVRELMiskfgrvidlEALQTLSVNTTLEELKIKKLRKELSNAK-ELRMWE---EKIAQVRWDLMMKTKEHTKKL 1756
Cdd:TIGR02168 368 EELESRLEELE----------EQLETLRSKVAQLELQIASLNNEIERLEaRLERLEdrrERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755553365 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 755553365 1546 EKRLDIEEALVEEKKI-VDNLKKE------YDTISKK-----VKVVATNLNAAEEALEAYQRE------KQQRLNELLVV 1607
Cdd:TIGR02169 183 EENIERLDLIIDEKRQqLERLRRErekaerYQALLKEkreyeGYELLKEKEALERQKEAIERQlasleeELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1608 IPLKLHQIEymefgEVPEDLsgtlvfsNHSLDRL-QERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEET 1686
Cdd:TIGR02169 263 LEKRLEEIE-----QLLEEL-------NKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1687 VRELM--ISKFGRVIDLEALQTLSVNTTLEELKIK--KLRKEL-SNAKELRMWEEKIAQVRWDLMMKTKEHTKKLHQMND 1761
Cdd:TIGR02169 331 IDKLLaeIEELEREIEEERKRRDKLTEEYAELKEEleDLRAELeEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 755553365 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 755553365 1543 QLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEayqrEKQQRLNELLVVIpLKLHQIEYMEF-- 1620
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE----AQKEELAELLRAL-YRLGRQPPLALll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1621 -GEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETV--RELMISKFGR 1697
Cdd:COG4942 127 sPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKaeRQKLLARLEK 206
|
170 180 190
....*....|....*....|....*....|....*
gi 755553365 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 755553365 903 IEDPKAYSIENARKKREHDKLMKKVEELKAHKREQIKILRNEFwKLLELNKELPAHMQFQRTDFNIDAKIHAEIHKKTSL 982
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL-KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 983 KIEQVEKELAWEKQKHELGLKKLQDRFREPLEsdtivvyatQSDHQIASYRLVKPSKYSKLKRpSQSERRQSKMERLEKE 1062
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLA---------QVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1063 GPGKKESQRDTGGSISLQEESVLEKGKKfrprtlsEIMVENQIEKTKKLIQQAERAQfKILQRKKEWEELYKSKPDDDYE 1142
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEK-------EEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1143 DPKDVQAIKEAQtymGDFNLKTAPDYKIpehmrINAAKKEEELgyldtmaHGKKRYMNKCILSLRDLKLAVIEEIQCLVQ 1222
Cdd:pfam02463 379 KKLESERLSSAA---KLKEEELELKSEE-----EKEAQLLLEL-------ARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1223 ELKNIQSsipaskhmpipqvpqiypeevperrfqyDEETLLRFQRKQKKRQDKSSSKQSGTGSGGSAGGGLVGFLKLSSG 1302
Cdd:pfam02463 444 GKLTEEK----------------------------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1303 KEGDLTTRDSLSRSSKASALLELPKPVEFEKAEPSDAELEimkrdEVKHLYMQQFLCNRINELTVTFDAELHLLRHQKLK 1382
Cdd:pfam02463 496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG-----VAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1383 LDTKMKLSDLHHLTLFQEMLLLKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQEKALYAGFQA 1462
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRK 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1463 ALGENNKFANFLMKVLKKKIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGS----------EDDVFDDSICPTN 1532
Cdd:pfam02463 651 GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeelkklklEAEELLADRVQEA 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1533 CDVSLFELALQLREKRLDIEEAL--VEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNELLVVIPL 1610
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1611 KLHQIEYMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKEcRERRKLLIREKREMAKTISKMEETVREL 1690
Cdd:pfam02463 811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE-EITKEELLQELLLKEEELEEQKLKDELE 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1691 MISKFGRVIDLEALQTLSVNTTLEELKIKKLRKELSNAKELRMWEEKIAQ---VRWDLMMKTKEHTKKLHQMNDLCLEKK 1767
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEElllEEADEKEKEENNKEEEEERNKRLLLAK 969
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 755553365 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 755553365 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 755553365 1540 LALQLREKRLDIEEALVEEKKI---VDNLKKEYDTISKKVKVVATNLNAAEEALEAyQREKQQRLNELLvviplKLHQIE 1616
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELeaeLEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELEL-----EEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1617 YMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETVRELMISKFG 1696
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1697 RVIDLEALQTLSVNTTLEEL-KIKKLRKELSNAKELRMWEEKIAQVRWDLMMKTKEHTKKLHQMNDLCLEKKKLDSRLNT 1775
Cdd:COG1196 370 AEAELAEAEEELEELAEELLeALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755553365 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 755553365 1404 LKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQ---EKALYAGFQAALGE-------NNKFANF 1473
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGEraralyrSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1474 LMKVLKkkikrakkkevegdadedeeseesseeesslesdedaSGSEDDVFDDsicptncdvslFELALQLREKRLDIEE 1553
Cdd:COG3883 105 LDVLLG-------------------------------------SESFSDFLDR-----------LSALSKIADADADLLE 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 755553365 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 755553365 895 ESEAAPE-DIEDPKAYSIENARKKREHDKLMKKVEeLKAHKREQIKILRNEFWKLLELNKELpAHMQFQRTDFNidAKIH 973
Cdd:pfam17380 320 EAEKARQaEMDRQAAIYAEQERMAMERERELERIR-QEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKN--ERVR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 974 AEIHKKTSLKIEQVEKELAWEKQKHEL-GLKKLQDRFREplesDTIVVYATQSDHQIASYRLVKPSKYSKLKRPSQSE-- 1050
Cdd:pfam17380 396 QELEAARKVKILEEERQRKIQQQKVEMeQIRAEQEEARQ----REVRRLEEERAREMERVRLEEQERQQQVERLRQQEee 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1051 RRQSKMErLEKEGPGKKESQRdtggsislQEESVLEKGKKFRPRTLSE-----IMVENQIEKTKKLIQQAERAQFKILQR 1125
Cdd:pfam17380 472 RKRKKLE-LEKEKRDRKRAEE--------QRRKILEKELEERKQAMIEeerkrKLLEKEMEERQKAIYEEERRREAEEER 542
|
....*
gi 755553365 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 755553365 1543 QLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQRE---KQQRLNELLVVIPLKLHQIEYME 1619
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanLRERLESLERRIAATERRLEDLE 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1620 fgEVPEDLSGTLVFSNHSL-------DRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETVRELM- 1691
Cdd:TIGR02168 845 --EQIEELSEDIESLAAEIeeleeliEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRe 922
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 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 755553365 1536 SLFELALQLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAyQREKQQRLNELLVVIPLKLHQI 1615
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ-ARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1616 EymefgEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETVRELMISKF 1695
Cdd:COG4372 93 Q-----AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1696 GRVIDLEALQTLSVNTTLEEL-------KIKKLRKELSNAKELRMWEEKIAQVRWDLMMKTKEHTKKLHQMNDLCLEKKK 1768
Cdd:COG4372 168 ALEQELQALSEAEAEQALDELlkeanrnAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 755553365 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 755553365 793 NPIRNITFSNDQTMMFCGMTNGAIRVYVLSENDPFLVSLQHYwhfnvhdnnyGSIKSITSSFDDQYLLTAGEDGNIFVFD 872
Cdd:cd00200 10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHT----------GPVRDVAASADGTYLASGSSDKTIRLWD 79
|
.
gi 755553365 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 755553365 912 ENARKKREHDKLMKKVEELK-----AHKREQIKILRNEFWKLLELNK--ELPAHMQFQRTDfniDAKIHAEIHKKTSL-K 983
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKkkadeAKKAAEAKKKADEAKKAEEAKKadEAKKAEEAKKAD---EAKKAEEKKKADELkK 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 984 IEQVEKelAWEKQKHELGLKKLQDRFREPLESDTIvvyatqsdHQIASYRLVKPSK-YSKLKRPSQSERRQSKMERLEKE 1062
Cdd:PTZ00121 1554 AEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEA--------KKAEEARIEEVMKlYEEEKKMKAEEAKKAEEAKIKAE 1623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1063 GPGKKESQRDTGGSISLQEESVLEKGKKFR-PRTLSEIMVENQIEKTKKLIQQAERAQFKILQRKKEWEELYKSKpdddy 1141
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA----- 1698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1142 EDPKDVQAIKEAQTYmgdfNLKTAPDYKIPEHMR---INAAKKEEE------------LGYLDTMAHGKKRYMNKCiLSL 1206
Cdd:PTZ00121 1699 EEAKKAEELKKKEAE----EKKKAEELKKAEEENkikAEEAKKEAEedkkkaeeakkdEEEKKKIAHLKKEEEKKA-EEI 1773
|
330
....*....|
gi 755553365 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 755553365 1537 LFELALQLREKR--LDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQ---REKQQRLNELLvviplk 1611
Cdd:cd22656 96 ILELIDDLADATddEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQtalETLEKALKDLL------ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1612 lhqieymefgevpEDLSGTLVfsNHSLDRLQERIVQLQEENAKqqKLNKECRERRKLLIREKREMAK------TISKMEE 1685
Cdd:cd22656 170 -------------TDEGGAIA--RKEIKDLQKELEKLNEEYAA--KLKAKIDELKALIADDEAKLAAalrliaDLTAADT 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 755553365 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 755553365 1536 SLFELALQLRE-----KRLDIEEaLVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEE------ALEAYQREKQQRLNEL 1604
Cdd:PRK03918 497 KLKELAEQLKEleeklKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAEL 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1605 LvviplklHQIEYMEFGEVPEDLSG------------TLVFSNHSLDRLQERIVQLQEE----NAKQQKLNKECRERRKL 1668
Cdd:PRK03918 576 L-------KELEELGFESVEELEERlkelepfyneylELKDAEKELEREEKELKKLEEEldkaFEELAETEKRLEELRKE 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 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 755553365 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 755553365 1404 LKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEE---KKNEITKLQDQEKALYAGFQAALGENNKFANFLMKVLKK 1480
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1481 KIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGSEDDVfddsicptncDVSLFELALQLREKRLDIEEALVEEKK 1560
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL----------AAEIEELEELIEELESELEALLNERAS 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1561 I---VDNLKKEYDTISKKVKVVATNLNAAE-------EALEAYQREKQ---QRLNELLVVIPlKLHQIEYMEFGEVPEDL 1627
Cdd:TIGR02168 885 LeeaLALLRSELEELSEELRELESKRSELRreleelrEKLAQLELRLEgleVRIDNLQERLS-EEYSLTLEEAEALENKI 963
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755553365 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 755553365 1539 ELALQLREKRLDIEEALVEEKKIVDNLKKEYDTISKKV----------KVVATNLNAAEEALEAYQREKQQRLNELlvvi 1608
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIaerretieekRERAEELRERAAELEAEAEEKREAAAEA---- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1609 plklhQIEYMEFGEVPEDLSGTLVFSNHSLDRLqERIVQLQEENAkqqklnkECRERRKLLiREKREmakTISKMEETVR 1688
Cdd:PRK02224 564 -----EEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIA-------DAEDEIERL-REKRE---ALAELNDERR 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1689 ELMISKFGRVIDLEAlqtlsvntTLEELKIKKLRKELSNAKE-LRMWEEKIAQV---RWDLMMKTKEHTKKLHQMNDLCL 1764
Cdd:PRK02224 627 ERLAEKRERKRELEA--------EFDEARIEEAREDKERAEEyLEQVEEKLDELreeRDDLQAEIGAVENELEELEELRE 698
|
250
....*....|....*....
gi 755553365 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 755553365 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 755553365 895 ESEAAPEDIEDPKAYSIENARKKREHDKLmKKVEELK----AHKREQIKilRNEFWKLLELNK-ELPAHMQFQRTDFNID 969
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADEL-KKAEELKkaeeKKKAEEAK--KAEEDKNMALRKaEEAKKAEEARIEEVMK 1599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 970 AKIHAEIHKKTSLKIEQVEKELAWEKQKHELGLKKLQDRFREPLESdtivvyaTQSDHQIASYRLVKPSKYSKLKRPSQS 1049
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE-------KKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553365 1050 ERRQSKMERLEKEGPGKKESQRDtggsislQEESVLEKGKKFRPRTlseimvENQIEKTKKLIQQAERAQFKILQRKKEW 1129
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALK-------KEAEEAKKAEELKKKE------AEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
250 260
....*....|....*....|....*...
gi 755553365 1130 EElYKSKPDD---DYEDPKDVQAIKEAQ 1154
Cdd:PTZ00121 1740 EE-DKKKAEEakkDEEEKKKIAHLKKEE 1766
|
|
|