|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
113-484 |
2.10e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 113.85 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 113 VDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFWEMAftfTGlKLQGS 192
Cdd:COG2319 84 VAFSPDGRLLASAS--ADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA---TG-KLLRT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 193 LgrfgKTSTSDIEGYAELPDGKVL-SGSEWGNLLLWE---GSLIKVelcRTGmkscHSGSINQIML--DEGEVITAGSDG 266
Cdd:COG2319 158 L----TGHSGAVTSVAFSPDGKLLaSGSDDGTVRLWDlatGKLLRT---LTG----HTGAVRSVAFspDGKLLASGSADG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 267 SVRIWDFETIDTADVIDDTGlleiEPINelhidkSVNlFSmikmnevGNNFWLA---QDANGAIWKLDlsfsniTQDPEC 343
Cdd:COG2319 227 TVRLWDLATGKLLRTLTGHS----GSVR------SVA-FS-------PDGRLLAsgsADGTVRLWDLA------TGELLR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 344 LFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVSA--SQIVVGFQDGVVRV 421
Cdd:COG2319 283 TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFSPdgKTLASGSDDGTVRL 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568994982 422 LELFDPKGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVE 484
Cdd:COG2319 357 WDLATGELLRTLTG-----------------HTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
211-506 |
1.24e-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: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 211 PDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSDGSVRIWDFETIDTADVIddTGl 287
Cdd:cd00200 19 PDGKLLaTGSGDGTIKVWDLETGELLRTLKG----HTGPVRDVAAsaDGTYLASGSSDKTIRLWDLETGECVRTL--TG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 288 lEIEPINELHIDKsvnlfsmikmnevgNNFWLA---QDANGAIWKLDlsfsnitqDPECLFSF--HSGPIAALAVSPLTY 362
Cdd:cd00200 92 -HTSYVSSVAFSP--------------DGRILSsssRDKTIKVWDVE--------TGKCLTTLrgHTDWVNSVAFSPDGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 363 LMATTAMDCSVRVYDFSSKNPL-VHMKFKQGGTSLIWAPRSvsvsaSQIVVGFQDGVVRVLELfdpkgltvyagrkkipd 441
Cdd:cd00200 149 FVASSSQDGTIKLWDLRTGKCVaTLTGHTGEVNSVAFSPDG-----EKLLSSSSDGTIKLWDL----------------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568994982 442 AELHLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFDVEKEYKPIGFFNTPGPICQLMWSP 506
Cdd:cd00200 207 STGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSP 271
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
445-482 |
1.77e-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: 1.77e-06
10 20 30
....*....|....*....|....*....|....*...
gi 568994982 445 HLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 482
Cdd:smart00320 3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
446-482 |
2.77e-06 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 45.41 E-value: 2.77e-06
10 20 30
....*....|....*....|....*....|....*..
gi 568994982 446 LKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 482
Cdd:pfam00400 3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1437-1705 |
6.11e-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: 51.22 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1437 EKRLDIEEALVEEKKI-VDNLKKE------YDTISKK-----VKVVATNLNAAEEALEAYQRE------KQQRLNELLVV 1498
Cdd:TIGR02169 183 EENIERLDLIIDEKRQqLERLRRErekaerYQALLKEkreyeGYELLKEKEALERQKEAIERQlasleeELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1499 IPLKLHQIEymefgEVPEDLsgtlvfsNHSLDRL-QERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEET 1577
Cdd:TIGR02169 263 LEKRLEEIE-----QLLEEL-------NKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1578 VRELM--ISKFGRVIDLEALQTLSVNTTLEELKIK--KLRKEL-SNAKELRMWEEKIAQVRWDLMMKTKEHTKKLHQMND 1652
Cdd:TIGR02169 331 IDKLLaeIEELEREIEEERKRRDKLTEEYAELKEEleDLRAELeEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568994982 1653 LCLEKKKLDSRLNTLqnqqgnafqglrKADI-VAKQKVTELVQTQLEKITALKE 1705
Cdd:TIGR02169 411 LQEELQRLSEELADL------------NAAIaGIEAKINELEEEKEDKALEIKK 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1434-1621 |
1.24e-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: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1434 QLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEayqrEKQQRLNELLVVIpLKLHQIEYMEF-- 1511
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE----AQKEELAELLRAL-YRLGRQPPLALll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1512 -GEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETV--RELMISKFGR 1588
Cdd:COG4942 127 sPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKaeRQKLLARLEK 206
|
170 180 190
....*....|....*....|....*....|....*
gi 568994982 1589 VIDLEA--LQTLSVNTTLEELKIKKLRKELSNAKE 1621
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 ... |
794-1708 |
1.46e-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: 49.97 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 794 IEDPKAYSIENARKKREHDKLMKKVEELKAHKREQIKILRNEFwKLLELNKELPAHMQFQRTDFNIDAKIHAEIHKKTSL 873
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL-KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 874 KIEQVEKELAWEKQKHELGLKKLQDRFREPLEsdtivvyatQSDHQIASYRLVKPSKYSKLKRpSQSERRQSKMERLEKE 953
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLA---------QVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 954 GPGKKESQRDTGGSISLQEESVLEKGKKfrprtlsEIMVENQIEKTKKLIQQAERAQfKILQRKKEWEELYKSKPDDDYE 1033
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEK-------EEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1034 DPKDVQAIKEAQtymGDFNLKTAPDYKIpehmrINAAKKEEELgyldtmaHGKKRYMNKCILSLRDLKLAVIEEIQCLVQ 1113
Cdd:pfam02463 379 KKLESERLSSAA---KLKEEELELKSEE-----EKEAQLLLEL-------ARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1114 ELKNIQSsipaskhmpipqvpqiypeevperrfqyDEETLLRFQRKQKKRQDKSSSKQSGTGSGGSAGGGLVGFLKLSSG 1193
Cdd:pfam02463 444 GKLTEEK----------------------------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1194 KEGDLTTRDSLSRSSKASALLELPKPVEFEKAEPSDAELEimkrdEVKHLYMQQFLCNRINELTVTFDAELHLLRHQKLK 1273
Cdd:pfam02463 496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG-----VAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1274 LDTKMKLSDLHHLTLFQEMLLLKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQEKALYAGFQA 1353
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRK 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1354 ALGENNKFANFLMKVLKKKIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGS----------EDDVFDDSICPTN 1423
Cdd:pfam02463 651 GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeelkklklEAEELLADRVQEA 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1424 CDVSLFELALQLREKRLDIEEAL--VEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNELLVVIPL 1501
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1502 KLHQIEYMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKEcRERRKLLIREKREMAKTISKMEETVREL 1581
Cdd:pfam02463 811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE-EITKEELLQELLLKEEELEEQKLKDELE 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1582 MISKFGRVIDLEALQTLSVNTTLEELKIKKLRKELSNAKELRMWEEKIAQ---VRWDLMMKTKEHTKKLHQMNDLCLEKK 1658
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEElllEEADEKEKEENNKEEEEERNKRLLLAK 969
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 568994982 1659 KLDSRLNTLQnqqgnAFQGLRKaDIVAKQKVTELVQTQLEKITALKEEIE 1708
Cdd:pfam02463 970 EELGKVNLMA-----IEEFEEK-EERYNKDELEKERLEEEKKKLIRAIIE 1013
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1295-1495 |
1.74e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1295 LKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQ---EKALYAGFQAALGE-------NNKFANF 1364
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGEraralyrSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1365 LMKVLKkkikrakkkevegdadedeeseesseeesslesdedaSGSEDDVFDDsicptncdvslFELALQLREKRLDIEE 1444
Cdd:COG3883 105 LDVLLG-------------------------------------SESFSDFLDR-----------LSALSKIADADADLLE 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568994982 1445 ALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNEL 1495
Cdd:COG3883 137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
786-1021 |
3.52e-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: 45.50 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 786 ESEAAPE-DIEDPKAYSIENARKKREHDKLMKKVEeLKAHKREQIKILRNEFWKLLELNKELpAHMQFQRTDFNidAKIH 864
Cdd:pfam17380 320 EAEKARQaEMDRQAAIYAEQERMAMERERELERIR-QEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKN--ERVR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 865 AEIHKKTSLKIEQVEKELAWEKQKHEL-GLKKLQDRFREplesDTIVVYATQSDHQIASYRLVKPSKYSKLKRPSQSE-- 941
Cdd:pfam17380 396 QELEAARKVKILEEERQRKIQQQKVEMeQIRAEQEEARQ----REVRRLEEERAREMERVRLEEQERQQQVERLRQQEee 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 942 RRQSKMErLEKEGPGKKESQRdtggsislQEESVLEKGKKFRPRTLSE-----IMVENQIEKTKKLIQQAERAQFKILQR 1016
Cdd:pfam17380 472 RKRKKLE-LEKEKRDRKRAEE--------QRRKILEKELEERKQAMIEeerkrKLLEKEMEERQKAIYEEERRREAEEER 542
|
....*
gi 568994982 1017 KKEWE 1021
Cdd:pfam17380 543 RKQQE 547
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
803-1107 |
7.57e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 803 ENARKKREHDKLMKKVEELK-----AHKREQIKILRNEFWKLLELNK--ELPAHMQFQRTDfniDAKIHAEIHKKTSL-K 874
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKkkadeAKKAAEAKKKADEAKKAEEAKKadEAKKAEEAKKAD---EAKKAEEKKKADELkK 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 875 IEQVEKelAWEKQKHELGLKKLQDRFREPLESDTIvvyatqsdHQIASYRLVKPSK-YSKLKRPSQSERRQSKMERLEKE 953
Cdd:PTZ00121 1554 AEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEA--------KKAEEARIEEVMKlYEEEKKMKAEEAKKAEEAKIKAE 1623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 954 GPGKKESQRDTGGSISLQEESVLEKGKKFR-PRTLSEIMVENQIEKTKKLIQQAERAQFKILQRKKEWEELYKSKpdddy 1032
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA----- 1698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1033 EDPKDVQAIKEAQTYmgdfNLKTAPDYKIPEHMR---INAAKKEEE------------LGYLDTMAHGKKRYMNKCiLSL 1097
Cdd:PTZ00121 1699 EEAKKAEELKKKEAE----EKKKAEELKKAEEENkikAEEAKKEAEedkkkaeeakkdEEEKKKIAHLKKEEEKKA-EEI 1773
|
330
....*....|
gi 568994982 1098 RDLKLAVIEE 1107
Cdd:PTZ00121 1774 RKEKEAVIEE 1783
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
684-764 |
1.19e-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: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 684 NPIRNITFSNDQTMMFCGMTNGAIRVYVLSENDPFLVSLQHYwhfnvhdnnyGSIKSITSSFDDQYLLTAGEDGNIFVFD 763
Cdd:cd00200 10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHT----------GPVRDVAASADGTYLASGSSDKTIRLWD 79
|
.
gi 568994982 764 I 764
Cdd:cd00200 80 L 80
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1428-1632 |
1.36e-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: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1428 LFELALQLREKR--LDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQ---REKQQRLNELLvviplk 1502
Cdd:cd22656 96 ILELIDDLADATddEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQtalETLEKALKDLL------ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1503 lhqieymefgevpEDLSGTLVfsNHSLDRLQERIVQLQEENAKqqKLNKECRERRKLLIREKREMAK------TISKMEE 1576
Cdd:cd22656 170 -------------TDEGGAIA--RKEIKDLQKELEKLNEEYAA--KLKAKIDELKALIADDEAKLAAalrliaDLTAADT 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568994982 1577 TVRELmISKFGRVID-LEALQTL--SVNTTLEELKiKKLRKELSNAKELRMWEEKIAQV 1632
Cdd:cd22656 233 DLDNL-LALIGPAIPaLEKLQGAwqAIATDLDSLK-DLLEDDISKIPAAILAKLELEKA 289
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1427-1636 |
1.64e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1427 SLFELALQLRE-----KRLDIEEaLVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEE------ALEAYQREKQQRLNEL 1495
Cdd:PRK03918 497 KLKELAEQLKEleeklKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAEL 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1496 LvviplklHQIEYMEFGEVPEDLSG------------TLVFSNHSLDRLQERIVQLQEE----NAKQQKLNKECRERRKL 1559
Cdd:PRK03918 576 L-------KELEELGFESVEELEERlkelepfyneylELKDAEKELEREEKELKKLEEEldkaFEELAETEKRLEELRKE 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1560 LirekREMAKTISKME-ETVRELMISKFGRVIDLEAlQTLSVNTTLEELK--IKKLRKELSNAKELRMWEEKIAQVRWDL 1636
Cdd:PRK03918 649 L----EELEKKYSEEEyEELREEYLELSRELAGLRA-ELEELEKRREEIKktLEKLKEELEEREKAKKELEKLEKALERV 723
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
113-484 |
2.10e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 113.85 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 113 VDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFWEMAftfTGlKLQGS 192
Cdd:COG2319 84 VAFSPDGRLLASAS--ADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA---TG-KLLRT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 193 LgrfgKTSTSDIEGYAELPDGKVL-SGSEWGNLLLWE---GSLIKVelcRTGmkscHSGSINQIML--DEGEVITAGSDG 266
Cdd:COG2319 158 L----TGHSGAVTSVAFSPDGKLLaSGSDDGTVRLWDlatGKLLRT---LTG----HTGAVRSVAFspDGKLLASGSADG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 267 SVRIWDFETIDTADVIDDTGlleiEPINelhidkSVNlFSmikmnevGNNFWLA---QDANGAIWKLDlsfsniTQDPEC 343
Cdd:COG2319 227 TVRLWDLATGKLLRTLTGHS----GSVR------SVA-FS-------PDGRLLAsgsADGTVRLWDLA------TGELLR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 344 LFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVSA--SQIVVGFQDGVVRV 421
Cdd:COG2319 283 TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFSPdgKTLASGSDDGTVRL 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568994982 422 LELFDPKGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVE 484
Cdd:COG2319 357 WDLATGELLRTLTG-----------------HTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
130-506 |
3.59e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.22 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 130 DYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFWEMAftftglklQGSLGRFGKTSTSDIEGYAE 209
Cdd:COG2319 57 DLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA--------TGLLLRTLTGHTGAVRSVAF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 210 LPDGK-VLSGSEWGNLLLWE---GSLIKVelcrtgmKSCHSGSINQIML--DEGEVITAGSDGSVRIWDFETIDTADVID 283
Cdd:COG2319 129 SPDGKtLASGSADGTVRLWDlatGKLLRT-------LTGHSGAVTSVAFspDGKLLASGSDDGTVRLWDLATGKLLRTLT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 284 DTGlleiEPINELHidksvnlFSmikmnevGNNFWLA---QDANGAIWKLDlsfsniTQDPECLFSFHSGPIAALAVSPL 360
Cdd:COG2319 202 GHT----GAVRSVA-------FS-------PDGKLLAsgsADGTVRLWDLA------TGKLLRTLTGHSGSVRSVAFSPD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 361 TYLMATTAMDCSVRVYDFSSKNPLvhmKFKQGGTSLIWaprSVSVSA--SQIVVGFQDGVVRVLELfdpkgltvyagrkk 438
Cdd:COG2319 258 GRLLASGSADGTVRLWDLATGELL---RTLTGHSGGVN---SVAFSPdgKLLASGSDDGTVRLWDL-------------- 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568994982 439 ipdAELHLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFDVEKEYKPIGFFNTPGPICQLMWSP 506
Cdd:COG2319 318 ---ATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSP 382
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
211-506 |
1.24e-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: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 211 PDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSDGSVRIWDFETIDTADVIddTGl 287
Cdd:cd00200 19 PDGKLLaTGSGDGTIKVWDLETGELLRTLKG----HTGPVRDVAAsaDGTYLASGSSDKTIRLWDLETGECVRTL--TG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 288 lEIEPINELHIDKsvnlfsmikmnevgNNFWLA---QDANGAIWKLDlsfsnitqDPECLFSF--HSGPIAALAVSPLTY 362
Cdd:cd00200 92 -HTSYVSSVAFSP--------------DGRILSsssRDKTIKVWDVE--------TGKCLTTLrgHTDWVNSVAFSPDGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 363 LMATTAMDCSVRVYDFSSKNPL-VHMKFKQGGTSLIWAPRSvsvsaSQIVVGFQDGVVRVLELfdpkgltvyagrkkipd 441
Cdd:cd00200 149 FVASSSQDGTIKLWDLRTGKCVaTLTGHTGEVNSVAFSPDG-----EKLLSSSSDGTIKLWDL----------------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568994982 442 AELHLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFDVEKEYKPIGFFNTPGPICQLMWSP 506
Cdd:cd00200 207 STGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSP 271
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
113-482 |
4.68e-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: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 113 VDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFW-----EMAFTFTGl 187
Cdd:cd00200 15 VAFSPDGKLLATGS--GDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWdletgECVRTLTG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 188 klqgslgrfgktSTSDIEGYAELPDGKVLSGSEW-GNLLLWEgsLIKVELCRTGmkSCHSGSINQI-MLDEGEVITAGS- 264
Cdd:cd00200 92 ------------HTSYVSSVAFSPDGRILSSSSRdKTIKVWD--VETGKCLTTL--RGHTDWVNSVaFSPDGTFVASSSq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 265 DGSVRIWDFETIdtadviddtglleiepinelhidksvnlfsmikmnevgnnfwlaqdangaiwkldlsfsnitqdpECL 344
Cdd:cd00200 156 DGTIKLWDLRTG-----------------------------------------------------------------KCV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 345 --FSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMKFKQGG-TSLIWAP-RSVSVSASQivvgfqDGVVR 420
Cdd:cd00200 171 atLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGvNSVAFSPdGYLLASGSE------DGTIR 244
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568994982 421 VlelFDpkgltVYAGRkkipdaelhLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 482
Cdd:cd00200 245 V---WD-----LRTGE---------CVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
130-506 |
1.59e-18 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 89.97 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 130 DYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNDEQLTTSGSGHIKFWEMAftftglklQGSLGRFGKTSTSDIEGYAE 209
Cdd:COG2319 15 DLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAA--------AGALLATLLGHTAAVLSVAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 210 LPDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSDGSVRIWDfetidtadviddtg 286
Cdd:COG2319 87 SPDGRLLaSASADGTVRLWDLATGLLLRTLTG----HTGAVRSVAFspDGKTLASGSADGTVRLWD-------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 287 lleiepinelhidksvnlfsmikmnevgnnfwlaqdangaiwkldlsfsniTQDPECLFSF--HSGPIAALAVSPLTYLM 364
Cdd:COG2319 149 ---------------------------------------------------LATGKLLRTLtgHSGAVTSVAFSPDGKLL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 365 ATTAMDCSVRVYDFSSKNPLVHMKfkqGGTSLIWaprSVSVSA--SQIVVGFQDGVVRVLELFDPKGLTVYAGrkkipda 442
Cdd:COG2319 178 ASGSDDGTVRLWDLATGKLLRTLT---GHTGAVR---SVAFSPdgKLLASGSADGTVRLWDLATGKLLRTLTG------- 244
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568994982 443 elhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVEkEYKPIGFFNTP-GPICQLMWSP 506
Cdd:COG2319 245 ----------HSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGELLRTLTGHsGGVNSVAFSP 298
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
28-377 |
6.06e-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: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 28 LQLLDSNTLLYVAG--NQMVLLDFKDKTQIYLQSSSGQGIGAIGVHPKKTYFAVAekGSFPKIIIYEYPSLKPYRILRdG 105
Cdd:cd00200 15 VAFSPDGKLLATGSgdGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASG--SSDKTIRLWDLETGECVRTLT-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 106 AEKAYAYVDFNNEGNLLasVGCHPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNdeQLTTSGS--GHIKFWEMAft 183
Cdd:cd00200 92 HTSYVSSVAFSPDGRIL--SSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDG--TFVASSSqdGTIKLWDLR-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 184 ftglklQGSLGRFGKTSTSDIEGYAELPDG-KVLSGSEWGNLLLWEgslikvelCRTGMKSC----HSGSINQIMLDE-G 257
Cdd:cd00200 166 ------TGKCVATLTGHTGEVNSVAFSPDGeKLLSSSSDGTIKLWD--------LSTGKCLGtlrgHENGVNSVAFSPdG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 258 EVITAGS-DGSVRIWDFETidtadviddtglleiepinelhidksvnlfsmikmnevgnnfwlaqdangaiwkldlsfsn 336
Cdd:cd00200 232 YLLASGSeDGTIRVWDLRT------------------------------------------------------------- 250
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 568994982 337 itqdPECLFSF--HSGPIAALAVSPLTYLMATTAMDCSVRVYD 377
Cdd:cd00200 251 ----GECVQTLsgHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
32-275 |
8.78e-15 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 78.41 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 32 DSNTLLYVAGNQMV-LLDFKDKTQIYLQSSSGQGIGAIGVHPKKTYFAVAekGSFPKIIIYEYPSLKPYRILRDGAEKAY 110
Cdd:COG2319 131 DGKTLASGSADGTVrLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASG--SDDGTVRLWDLATGKLLRTLTGHTGAVR 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 111 AyVDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDNdEQL-TTSGSGHIKFWEMAFTFTGLKL 189
Cdd:COG2319 209 S-VAFSPDGKLLASGS--ADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDG-RLLaSGSADGTVRLWDLATGELLRTL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 190 QGSLGRFGKTSTSdiegyaelPDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSDG 266
Cdd:COG2319 285 TGHSGGVNSVAFS--------PDGKLLaSGSDDGTVRLWDLATGKLLRTLTG----HTGAVRSVAFspDGKTLASGSDDG 352
|
....*....
gi 568994982 267 SVRIWDFET 275
Cdd:COG2319 353 TVRLWDLAT 361
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
32-275 |
7.75e-14 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 75.72 E-value: 7.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 32 DSNTLLYVAGNQMVLL-DFKDKTQIYLQSSSGQGIGAIGVHPKKTYFAVaekGSFPK-IIIYEYPSLKPYRILRDGAEKA 109
Cdd:COG2319 173 DGKLLASGSDDGTVRLwDLATGKLLRTLTGHTGAVRSVAFSPDGKLLAS---GSADGtVRLWDLATGKLLRTLTGHSGSV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 110 YAyVDFNNEGNLLASVGchPDYTITIWGWKEEQPILRTKAFSQDVFKVTFNPDnDEQL-TTSGSGHIKFWEMAftfTGLK 188
Cdd:COG2319 250 RS-VAFSPDGRLLASGS--ADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPD-GKLLaSGSDDGTVRLWDLA---TGKL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 189 LQGSLGrfgktSTSDIEGYAELPDGKVL-SGSEWGNLLLWEGSLIKVELCRTGmkscHSGSINQIML--DEGEVITAGSD 265
Cdd:COG2319 323 LRTLTG-----HTGAVRSVAFSPDGKTLaSGSDDGTVRLWDLATGELLRTLTG----HTGAVTSVAFspDGRTLASGSAD 393
|
250
....*....|
gi 568994982 266 GSVRIWDFET 275
Cdd:COG2319 394 GTVRLWDLAT 403
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
348-506 |
8.20e-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: 8.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 348 HSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLvhmKFKQGGTSLIWAPRSVSVSaSQIVVGFQDGVVRVLELFDP 427
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL---RTLKGHTGPVRDVAASADG-TYLASGSSDKTIRLWDLETG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 428 KGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKTVFFFDVEKeYKPIGFFNT-PGPICQLMWSP 506
Cdd:cd00200 84 ECVRTLTG-----------------HTSYVSSVAFSPDGRILSSSSRDKTIKVWDVET-GKCLTTLRGhTDWVNSVAFSP 145
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
318-484 |
4.11e-07 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 54.53 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 318 WLAQDANGAIWKLDLSFSNITQDPECLFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYDFSSKNPLVHMkfkQGGTSLI 397
Cdd:COG2319 5 DGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATL---LGHTAAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 398 WApRSVSVSASQIVVGFQDGVVRVLELFDPKGLTVYAGrkkipdaelhlkyvfkpHTDEVTALAYERDGDILATGSEDKT 477
Cdd:COG2319 82 LS-VAFSPDGRLLASASADGTVRLWDLATGLLLRTLTG-----------------HTGAVRSVAFSPDGKTLASGSADGT 143
|
....*..
gi 568994982 478 VFFFDVE 484
Cdd:COG2319 144 VRLWDLA 150
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
445-482 |
1.77e-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: 1.77e-06
10 20 30
....*....|....*....|....*....|....*...
gi 568994982 445 HLKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 482
Cdd:smart00320 3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
446-482 |
2.77e-06 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 45.41 E-value: 2.77e-06
10 20 30
....*....|....*....|....*....|....*..
gi 568994982 446 LKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFD 482
Cdd:pfam00400 3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1437-1705 |
6.11e-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: 51.22 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1437 EKRLDIEEALVEEKKI-VDNLKKE------YDTISKK-----VKVVATNLNAAEEALEAYQRE------KQQRLNELLVV 1498
Cdd:TIGR02169 183 EENIERLDLIIDEKRQqLERLRRErekaerYQALLKEkreyeGYELLKEKEALERQKEAIERQlasleeELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1499 IPLKLHQIEymefgEVPEDLsgtlvfsNHSLDRL-QERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEET 1577
Cdd:TIGR02169 263 LEKRLEEIE-----QLLEEL-------NKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1578 VRELM--ISKFGRVIDLEALQTLSVNTTLEELKIK--KLRKEL-SNAKELRMWEEKIAQVRWDLMMKTKEHTKKLHQMND 1652
Cdd:TIGR02169 331 IDKLLaeIEELEREIEEERKRRDKLTEEYAELKEEleDLRAELeEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568994982 1653 LCLEKKKLDSRLNTLqnqqgnafqglrKADI-VAKQKVTELVQTQLEKITALKE 1705
Cdd:TIGR02169 411 LQEELQRLSEELADL------------NAAIaGIEAKINELEEEKEDKALEIKK 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1430-1708 |
6.39e-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: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1430 ELALQLREKRLDIEEA--------LVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREK----------QQR 1491
Cdd:TIGR02168 210 EKAERYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeieelQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1492 LNELLVVIPLKLHQIEymEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTI 1571
Cdd:TIGR02168 290 LYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1572 SKMEETVRELMiskfgrvidlEALQTLSVNTTLEELKIKKLRKELSNAK-ELRMWE---EKIAQVRWDLMMKTKEHTKKL 1647
Cdd:TIGR02168 368 EELESRLEELE----------EQLETLRSKVAQLELQIASLNNEIERLEaRLERLEdrrERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568994982 1648 HQMN--DLCLEKKKLDSRLNTLQNQQGNAFQGLRKA--DIVAKQKVTELVQTQLEKITALKEEIE 1708
Cdd:TIGR02168 438 LQAEleELEEELEELQEELERLEEALEELREELEEAeqALDAAERELAQLQARLDSLERLQENLE 502
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1434-1621 |
1.24e-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: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1434 QLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEayqrEKQQRLNELLVVIpLKLHQIEYMEF-- 1511
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE----AQKEELAELLRAL-YRLGRQPPLALll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1512 -GEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETV--RELMISKFGR 1588
Cdd:COG4942 127 sPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKaeRQKLLARLEK 206
|
170 180 190
....*....|....*....|....*....|....*
gi 568994982 1589 VIDLEA--LQTLSVNTTLEELKIKKLRKELSNAKE 1621
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 ... |
794-1708 |
1.46e-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: 49.97 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 794 IEDPKAYSIENARKKREHDKLMKKVEELKAHKREQIKILRNEFwKLLELNKELPAHMQFQRTDFNIDAKIHAEIHKKTSL 873
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL-KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 874 KIEQVEKELAWEKQKHELGLKKLQDRFREPLEsdtivvyatQSDHQIASYRLVKPSKYSKLKRpSQSERRQSKMERLEKE 953
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLA---------QVLKENKEEEKEKKLQEEELKL-LAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 954 GPGKKESQRDTGGSISLQEESVLEKGKKfrprtlsEIMVENQIEKTKKLIQQAERAQfKILQRKKEWEELYKSKPDDDYE 1033
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEK-------EEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1034 DPKDVQAIKEAQtymGDFNLKTAPDYKIpehmrINAAKKEEELgyldtmaHGKKRYMNKCILSLRDLKLAVIEEIQCLVQ 1113
Cdd:pfam02463 379 KKLESERLSSAA---KLKEEELELKSEE-----EKEAQLLLEL-------ARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1114 ELKNIQSsipaskhmpipqvpqiypeevperrfqyDEETLLRFQRKQKKRQDKSSSKQSGTGSGGSAGGGLVGFLKLSSG 1193
Cdd:pfam02463 444 GKLTEEK----------------------------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1194 KEGDLTTRDSLSRSSKASALLELPKPVEFEKAEPSDAELEimkrdEVKHLYMQQFLCNRINELTVTFDAELHLLRHQKLK 1273
Cdd:pfam02463 496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG-----VAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1274 LDTKMKLSDLHHLTLFQEMLLLKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQEKALYAGFQA 1353
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRK 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1354 ALGENNKFANFLMKVLKKKIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGS----------EDDVFDDSICPTN 1423
Cdd:pfam02463 651 GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeelkklklEAEELLADRVQEA 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1424 CDVSLFELALQLREKRLDIEEAL--VEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNELLVVIPL 1501
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1502 KLHQIEYMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKEcRERRKLLIREKREMAKTISKMEETVREL 1581
Cdd:pfam02463 811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE-EITKEELLQELLLKEEELEEQKLKDELE 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1582 MISKFGRVIDLEALQTLSVNTTLEELKIKKLRKELSNAKELRMWEEKIAQ---VRWDLMMKTKEHTKKLHQMNDLCLEKK 1658
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEElllEEADEKEKEENNKEEEEERNKRLLLAK 969
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 568994982 1659 KLDSRLNTLQnqqgnAFQGLRKaDIVAKQKVTELVQTQLEKITALKEEIE 1708
Cdd:pfam02463 970 EELGKVNLMA-----IEEFEEK-EERYNKDELEKERLEEEKKKLIRAIIE 1013
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1431-1708 |
1.54e-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: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1431 LALQLREKRLDIEEALVEEKKI---VDNLKKEYDTISKKVKVVATNLNAAEEALEAyQREKQQRLNELLvviplKLHQIE 1507
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELeaeLEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELEL-----EEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1508 YMEFGEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETVRELMISKFG 1587
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1588 RVIDLEALQTLSVNTTLEEL-KIKKLRKELSNAKELRMWEEKIAQVRWDLMMKTKEHTKKLHQMNDLCLEKKKLDSRLNT 1666
Cdd:COG1196 370 AEAELAEAEEELEELAEELLeALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568994982 1667 LQNQQGNAFQGLRKAdIVAKQKVTELVQTQLEKITALKEEIE 1708
Cdd:COG1196 450 EEAELEEEEEALLEL-LAELLEEAALLEAALAELLEELAEAA 490
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
446-509 |
1.57e-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: 1.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568994982 446 LKYVFKPHTDEVTALAYERDGDILATGSEDKTVFFFDVEKEYKPIGFFNTPGPICQLMWSPASH 509
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGT 64
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1295-1495 |
1.74e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1295 LKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEEKKNEITKLQDQ---EKALYAGFQAALGE-------NNKFANF 1364
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGEraralyrSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1365 LMKVLKkkikrakkkevegdadedeeseesseeesslesdedaSGSEDDVFDDsicptncdvslFELALQLREKRLDIEE 1444
Cdd:COG3883 105 LDVLLG-------------------------------------SESFSDFLDR-----------LSALSKIADADADLLE 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568994982 1445 ALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQREKQQRLNEL 1495
Cdd:COG3883 137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
786-1021 |
3.52e-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: 45.50 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 786 ESEAAPE-DIEDPKAYSIENARKKREHDKLMKKVEeLKAHKREQIKILRNEFWKLLELNKELpAHMQFQRTDFNidAKIH 864
Cdd:pfam17380 320 EAEKARQaEMDRQAAIYAEQERMAMERERELERIR-QEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKN--ERVR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 865 AEIHKKTSLKIEQVEKELAWEKQKHEL-GLKKLQDRFREplesDTIVVYATQSDHQIASYRLVKPSKYSKLKRPSQSE-- 941
Cdd:pfam17380 396 QELEAARKVKILEEERQRKIQQQKVEMeQIRAEQEEARQ----REVRRLEEERAREMERVRLEEQERQQQVERLRQQEee 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 942 RRQSKMErLEKEGPGKKESQRdtggsislQEESVLEKGKKFRPRTLSE-----IMVENQIEKTKKLIQQAERAQFKILQR 1016
Cdd:pfam17380 472 RKRKKLE-LEKEKRDRKRAEE--------QRRKILEKELEERKQAMIEeerkrKLLEKEMEERQKAIYEEERRREAEEER 542
|
....*
gi 568994982 1017 KKEWE 1021
Cdd:pfam17380 543 RKQQE 547
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1434-1633 |
5.10e-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: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1434 QLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQRE---KQQRLNELLVVIPLKLHQIEYME 1510
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanLRERLESLERRIAATERRLEDLE 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1511 fgEVPEDLSGTLVFSNHSL-------DRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETVRELM- 1582
Cdd:TIGR02168 845 --EQIEELSEDIESLAAEIeeleeliEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRe 922
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1583 -ISKFGRVID------LEALQTLSV--NTTLEELKIKKLRKELSNAKelrmWEEKIAQVR 1633
Cdd:TIGR02168 923 kLAQLELRLEglevriDNLQERLSEeySLTLEEAEALENKIEDDEEE----ARRRLKRLE 978
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1427-1708 |
6.33e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1427 SLFELALQLREKRLDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAyQREKQQRLNELLVVIPLKLHQI 1506
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ-ARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1507 EymefgEVPEDLSGTLVFSNHSLDRLQERIVQLQEENAKQQKLNKECRERRKLLIREKREMAKTISKMEETVRELMISKF 1586
Cdd:COG4372 93 Q-----AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1587 GRVIDLEALQTLSVNTTLEEL-------KIKKLRKELSNAKELRMWEEKIAQVRWDLMMKTKEHTKKLHQMNDLCLEKKK 1659
Cdd:COG4372 168 ALEQELQALSEAEAEQALDELlkeanrnAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568994982 1660 LDSRLNTLQNQQGNAFQGLRKADIVAKQKVTELVQTQLEKITALKEEIE 1708
Cdd:COG4372 248 KEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK 296
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
803-1107 |
7.57e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 803 ENARKKREHDKLMKKVEELK-----AHKREQIKILRNEFWKLLELNK--ELPAHMQFQRTDfniDAKIHAEIHKKTSL-K 874
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKkkadeAKKAAEAKKKADEAKKAEEAKKadEAKKAEEAKKAD---EAKKAEEKKKADELkK 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 875 IEQVEKelAWEKQKHELGLKKLQDRFREPLESDTIvvyatqsdHQIASYRLVKPSK-YSKLKRPSQSERRQSKMERLEKE 953
Cdd:PTZ00121 1554 AEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEA--------KKAEEARIEEVMKlYEEEKKMKAEEAKKAEEAKIKAE 1623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 954 GPGKKESQRDTGGSISLQEESVLEKGKKFR-PRTLSEIMVENQIEKTKKLIQQAERAQFKILQRKKEWEELYKSKpdddy 1032
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA----- 1698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1033 EDPKDVQAIKEAQTYmgdfNLKTAPDYKIPEHMR---INAAKKEEE------------LGYLDTMAHGKKRYMNKCiLSL 1097
Cdd:PTZ00121 1699 EEAKKAEELKKKEAE----EKKKAEELKKAEEENkikAEEAKKEAEedkkkaeeakkdEEEKKKIAHLKKEEEKKA-EEI 1773
|
330
....*....|
gi 568994982 1098 RDLKLAVIEE 1107
Cdd:PTZ00121 1774 RKEKEAVIEE 1783
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
684-764 |
1.19e-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: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 684 NPIRNITFSNDQTMMFCGMTNGAIRVYVLSENDPFLVSLQHYwhfnvhdnnyGSIKSITSSFDDQYLLTAGEDGNIFVFD 763
Cdd:cd00200 10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHT----------GPVRDVAASADGTYLASGSSDKTIRLWD 79
|
.
gi 568994982 764 I 764
Cdd:cd00200 80 L 80
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1428-1632 |
1.36e-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: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1428 LFELALQLREKR--LDIEEALVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEEALEAYQ---REKQQRLNELLvviplk 1502
Cdd:cd22656 96 ILELIDDLADATddEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQtalETLEKALKDLL------ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1503 lhqieymefgevpEDLSGTLVfsNHSLDRLQERIVQLQEENAKqqKLNKECRERRKLLIREKREMAK------TISKMEE 1576
Cdd:cd22656 170 -------------TDEGGAIA--RKEIKDLQKELEKLNEEYAA--KLKAKIDELKALIADDEAKLAAalrliaDLTAADT 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568994982 1577 TVRELmISKFGRVID-LEALQTL--SVNTTLEELKiKKLRKELSNAKELRMWEEKIAQV 1632
Cdd:cd22656 233 DLDNL-LALIGPAIPaLEKLQGAwqAIATDLDSLK-DLLEDDISKIPAAILAKLELEKA 289
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1427-1636 |
1.64e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1427 SLFELALQLRE-----KRLDIEEaLVEEKKIVDNLKKEYDTISKKVKVVATNLNAAEE------ALEAYQREKQQRLNEL 1495
Cdd:PRK03918 497 KLKELAEQLKEleeklKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAEL 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1496 LvviplklHQIEYMEFGEVPEDLSG------------TLVFSNHSLDRLQERIVQLQEE----NAKQQKLNKECRERRKL 1559
Cdd:PRK03918 576 L-------KELEELGFESVEELEERlkelepfyneylELKDAEKELEREEKELKKLEEEldkaFEELAETEKRLEELRKE 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1560 LirekREMAKTISKME-ETVRELMISKFGRVIDLEAlQTLSVNTTLEELK--IKKLRKELSNAKELRMWEEKIAQVRWDL 1636
Cdd:PRK03918 649 L----EELEKKYSEEEyEELREEYLELSRELAGLRA-ELEELEKRREEIKktLEKLKEELEEREKAKKELEKLEKALERV 723
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1430-1674 |
1.85e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1430 ELALQLREKRLDIEEALVEEKKIVDNLKKEYDTISKKV----------KVVATNLNAAEEALEAYQREKQQRLNELlvvi 1499
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIaerretieekRERAEELRERAAELEAEAEEKREAAAEA---- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1500 plklhQIEYMEFGEVPEDLSGTLVFSNHSLDRLqERIVQLQEENAkqqklnkECRERRKLLiREKREmakTISKMEETVR 1579
Cdd:PRK02224 564 -----EEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIA-------DAEDEIERL-REKRE---ALAELNDERR 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1580 ELMISKFGRVIDLEAlqtlsvntTLEELKIKKLRKELSNAKE-LRMWEEKIAQV---RWDLMMKTKEHTKKLHQMNDLCL 1655
Cdd:PRK02224 627 ERLAEKRERKRELEA--------EFDEARIEEAREDKERAEEyLEQVEEKLDELreeRDDLQAEIGAVENELEELEELRE 698
|
250
....*....|....*....
gi 568994982 1656 EKKKLDSRLNTLQNQQGNA 1674
Cdd:PRK02224 699 RREALENRVEALEALYDEA 717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1295-1581 |
2.37e-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: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1295 LKNFEKQENILQERVNSLDKEEQDMQWKINETLKEMEE---KKNEITKLQDQEKALYAGFQAALGENNKFANFLMKVLKK 1371
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1372 KIKRAKKKEVEGDADEDEESEESSEEESSLESDEDASGSEDDVfddsicptncDVSLFELALQLREKRLDIEEALVEEKK 1451
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL----------AAEIEELEELIEELESELEALLNERAS 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1452 I---VDNLKKEYDTISKKVKVVATNLNAAE-------EALEAYQREKQ---QRLNELLVVIPlKLHQIEYMEFGEVPEDL 1518
Cdd:TIGR02168 885 LeeaLALLRSELEELSEELRELESKRSELRreleelrEKLAQLELRLEgleVRIDNLQERLS-EEYSLTLEEAEALENKI 963
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568994982 1519 SGTLVFSNHSLDRLQERIVQLQEENakqqkLN-----KECRERRKLLIREKREMAKTISKMEETVREL 1581
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKELGPVN-----LAaieeyEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
338-377 |
2.40e-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: 2.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 568994982 338 TQDPECLFSFHSGPIAALAVSPLTYLMATTAMDCSVRVYD 377
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
786-1045 |
5.42e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 786 ESEAAPEDIEDPKAYSIENARKKREHDKLmKKVEELK----AHKREQIKilRNEFWKLLELNK-ELPAHMQFQRTDFNID 860
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADEL-KKAEELKkaeeKKKAEEAK--KAEEDKNMALRKaEEAKKAEEARIEEVMK 1599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 861 AKIHAEIHKKTSLKIEQVEKELAWEKQKHELGLKKLQDRFREPLESdtivvyaTQSDHQIASYRLVKPSKYSKLKRPSQS 940
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE-------KKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 941 ERRQSKMERLEKEGPGKKESQRDtggsislQEESVLEKGKKFRPRTlseimvENQIEKTKKLIQQAERAQFKILQRKKEW 1020
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALK-------KEAEEAKKAEELKKKE------AEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
250 260
....*....|....*....|....*...
gi 568994982 1021 EElYKSKPDD---DYEDPKDVQAIKEAQ 1045
Cdd:PTZ00121 1740 EE-DKKKAEEakkDEEEKKKIAHLKKEE 1766
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
342-377 |
6.09e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.17 E-value: 6.09e-03
10 20 30
....*....|....*....|....*....|....*...
gi 568994982 342 ECLFSF--HSGPIAALAVSPLTYLMATTAMDCSVRVYD 377
Cdd:pfam00400 2 KLLKTLegHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1506-1649 |
9.11e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994982 1506 IEYMEFGEVPEDLSGTLVFSNHS---LDRLQERIVQLQEENAKQQKLNKECRERrkllIREKREmakTISKMEETVRELM 1582
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEereLTEEEEEIRRLEEQVERLEAEVEELEAE----LEEKDE---RIERLERELSEAR 454
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568994982 1583 ISKFGRVIDLEALQTLsvNTTLEELKiKKLRKELSNAKELRmweEKIAqvrwdlmmKTKEHTKKLHQ 1649
Cdd:COG2433 455 SEERREIRKDREISRL--DREIERLE-RELEEERERIEELK---RKLE--------RLKELWKLEHS 507
|
|
|