|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
234-599 |
2.95e-24 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 107.30 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 234 VNFNYSGTLLASVGSnpDYTLTIWNWKEEQPILRTKAFSQEVFKVTFNPDNEEQLTTSGSGHIKFWEMAftfTGLKLQGS 313
Cdd:COG2319 84 VAFSPDGRLLASASA--DGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA---TGKLLRTL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 314 LGRFGKTTTTDIegymeLPDGKVL-SGSEWGNMLLWE---GGLIKVelCRGtskscHNGPINQIML--DEGEVITVGSDG 387
Cdd:COG2319 159 TGHSGAVTSVAF-----SPDGKLLaSGSDDGTVRLWDlatGKLLRT--LTG-----HTGAVRSVAFspDGKLLASGSADG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 388 CVRIWDFETidtadiidetGlleiEPINELQVDKNVNL---FSmtkmsetGNNFWLA---QDANGAIWKLDlsfsniTQD 461
Cdd:COG2319 227 TVRLWDLAT----------G----KLLRTLTGHSGSVRsvaFS-------PDGRLLAsgsADGTVRLWDLA------TGE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 462 PECLFSFHSGAVEAVAVSPLTYLMATTALDCSVRIYDFASKTLLTQMKFKQGG-TALVWVPrmvnfTGAEIIVGFEDGVV 540
Cdd:COG2319 280 LLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAvRSVAFSP-----DGKTLASGSDDGTV 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622909265 541 RVLELYDPKGLTIFVGrkkisdadirlkqvfkpHTARVTALAYERDGEILATGSKDQTV 599
Cdd:COG2319 355 RLWDLATGELLRTLTG-----------------HTGAVTSVAFSPDGRTLASGSADGTV 396
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
234-599 |
1.22e-21 |
|
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: 97.02 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 234 VNFNYSGTLLASVGSnpDYTLTIWNWKEEQPILRTKAFSQEVFKVTFNPDNEEQLTTSGSGHIKFW-----EMAFTFTGL 308
Cdd:cd00200 15 VAFSPDGKLLATGSG--DGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWdletgECVRTLTGH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 309 KLQGSLGRFgkttttdiegymeLPDGKVLSGSEW-GNMLLWEggLIKVELCrgTSKSCHNGPINQI-MLDEGEVITVGS- 385
Cdd:cd00200 93 TSYVSSVAF-------------SPDGRILSSSSRdKTIKVWD--VETGKCL--TTLRGHTDWVNSVaFSPDGTFVASSSq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 386 DGCVRIWDFETIdtadiidetglleiepinelqvdknvnlfsmtkmsetgnnfwlaqdangaiwkldlsfsnitqdpECL 465
Cdd:cd00200 156 DGTIKLWDLRTG-----------------------------------------------------------------KCV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 466 --FSFHSGAVEAVAVSPLTYLMATTALDCSVRIYDFASKTLLTQMKFKQGG-TALVWvprmvNFTGAEIIVGFEDGVVRV 542
Cdd:cd00200 171 atLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGvNSVAF-----SPDGYLLASGSEDGTIRV 245
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622909265 543 lelYDpkgltifvGRKKisdadiRLKQVFKPHTARVTALAYERDGEILATGSKDQTV 599
Cdd:cd00200 246 ---WD--------LRTG------ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1276-1557 |
4.56e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1276 LTLQLREKRLDIEEALVEekkvVDNLKKEYDTLSKKVKIVATNLNAAEEALEAYQREKQQRLNELLVVIpLKLHQIeyvv 1355
Cdd:COG1196 216 RELKEELKELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE-LELEEA---- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1356 fgeipsdlsgtlvfsNHALRRLQERIRELQEENSKQQKLNKEWRERRKQLIREKREMTKTIHKMEETVRQLmiskfgrvv 1435
Cdd:COG1196 287 ---------------QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL--------- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1436 NLEALQTLSVNTTLEELKIRKLRKELANAKEMKMWEEKIAQMRWELMMKTKEHTRKLYQMNDLCIEKKKLDSRLNTLQNQ 1515
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622909265 1516 QGNAFQSLREADVVAREEVTELIQLQAERISALKEEIALLRR 1557
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1271-1558 |
1.17e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1271 VALFELTLQLREKRLDIEEA---LVEEKKVVDNLKKEYDTLSKKVKIVATNLNAAEEALEAYQREKQQrLNELLVVIPLK 1347
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELsrqISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1348 LHQIEYVVfgeipSDLSGTLVFSNHALRRLQERIRELQEENSKQQklnkewrERRKQLIREKREMTKTIHKMEETVRQLm 1427
Cdd:TIGR02168 784 IEELEAQI-----EQLKEELKALREALDELRAELTLLNEEAANLR-------ERLESLERRIAATERRLEDLEEQIEEL- 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1428 iskfgrvvnLEALQTLSVNTTLEELKIRKLRKELANA-KEMKMWEEKIAQMRWE---LMMKTKEHTRKLYQMNDLCIEKK 1503
Cdd:TIGR02168 851 ---------SEDIESLAAEIEELEELIEELESELEALlNERASLEEALALLRSEleeLSEELRELESKRSELRRELEELR 921
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622909265 1504 ----KLDSRLNTLQNQQGNAFQSLREADVVAREEVTELIQLQAERISALKEEIALLRRK 1558
Cdd:TIGR02168 922 eklaQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
566-603 |
4.28e-05 |
|
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: 41.91 E-value: 4.28e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1622909265 566 RLKQVFKPHTARVTALAYERDGEILATGSKDQTVFFFE 603
Cdd:smart00320 3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
566-603 |
1.17e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 40.79 E-value: 1.17e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1622909265 566 RLKQVFKPHTARVTALAYERDGEILATGSKDQTVFFFE 603
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
642-1558 |
1.99e-04 |
|
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: 46.12 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 642 IEDPKAYSIENARRKREHDKLMKEVEEIKAQKREQIKALRTEFcKLLEMNEELPTHMQFKRTDFDVDSKIRAEmhrrtaf 721
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL-KLKEQAKKALEYYQLKEKLELEEEYLLYL------- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 722 KIQQVEKElaWEKEKHELGLKKLKnrfrdplesdtivvhailsdhKISSYRLVQPSKYSKFKRTSQSERKPSKLDRFEKE 801
Cdd:pfam02463 230 DYLKLNEE--RIDLLQELLRDEQE---------------------EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 802 GTGRKDSQRDAGGSIAIQEESIIEKGKkfRPKTLSEIMVENQIEKTRKLILKAERAQ--LKIQQRKKEWEELYKSKPGDD 879
Cdd:pfam02463 287 ELKLLAKEEEELKSELLKLERRKVDDE--EKLKESEKEKKKAEKELKKEKEEIEELEkeLKELEIKREAEEEEEEELEKL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 880 YE-DPKDLQAIKEAQVYMGDFNLKTAPDYKIPEHMRINAAKKEEELGHLDSlvhgNKRYMNKCILSLRDLKVAVVEEIQC 958
Cdd:pfam02463 365 QEkLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELAR----QLEDLLKEEKKEELEILEEEEESIE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 959 LVQELKNIQST-LHVSKHIpipQIPQIHPEEVPEKRFQYDEETLLNFKQQHMKSD-DEKSPGVEQTGSGGPGGGFLKLSS 1036
Cdd:pfam02463 441 LKQGKLTEEKEeLEKQELK---LLKDELELKKSEDLLKETQLVKLQEQLELLLSRqKLEERSQKESKARSGLKVLLALIK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1037 GKDGDLTTRDSMSRSSKASTLSLDIPKYMEFEKAEPTDVELEIMKRDEIKHVYMQQYLVNRVKELIVTFDAELRLLRHQK 1116
Cdd:pfam02463 518 DGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1117 LKLDTQMKLSDLHHVTLFQEI----LLLKNFEKQENILQERVNSLDKEEQYMQWKINETLKEMEEKKNEITKLQEQEKAL 1192
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDdkraKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1193 YAGFQTAIGENNKFANFLMKVLKKKIKRVKKKEVEGDADEDEESEESSEEESSLESDEDESESEDEVFDDSICPTNCDVA 1272
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1273 LFELTLQLREKRLDIEEALvEEKKVVDNLKKEYDTLSKKVKIVATNLNAAEEALEAYQREKQQRLNELLVVIPLKLHQIE 1352
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKEL-AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1353 YvvfgeipsdLSGTLVFSNHALRRLQERIRELQEENSKQQKLNKEWRERRKQLIREKREMTKTIHKMEETVRQlmiskfg 1432
Cdd:pfam02463 837 E---------LALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKK------- 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1433 rvvnlEALQTLSVNTTLEELKIRKLRKELANAKEMKMWEEkiaqmrWELMMKTKEHTRKLYQMNDLCIEKKKLDSRLNTL 1512
Cdd:pfam02463 901 -----ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEE------EPEELLLEEADEKEKEENNKEEEEERNKRLLLAK 969
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 1622909265 1513 Q---NQQGNAFQSLREADVVAREEVTELIQLQAERISALKEEIALLRRK 1558
Cdd:pfam02463 970 EelgKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1275-1553 |
2.24e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1275 ELTLQLREKRLDIEEALVEEKKVVDNLKKEYDTLSKKVKI-----VATNLNAAEEALEAYQREKQQRLNELLVVIPLKLH 1349
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELiklkeLAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1350 QIEyvvfGEIpsdlsgtlvfsnhalRRLQERIRELQEENSKQQKLNKEWR---ERRKQLIREKREMT-KTIHKMEETVRQ 1425
Cdd:PRK03918 536 KLK----GEI---------------KSLKKELEKLEELKKKLAELEKKLDeleEELAELLKELEELGfESVEELEERLKE 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1426 L--MISKFGRVVN----LEALQTL--SVNTTLEEL---------KIRKLRKELaNAKEMKMWEEKIAQMRWELMMKTKEH 1488
Cdd:PRK03918 597 LepFYNEYLELKDaekeLEREEKElkKLEEELDKAfeelaetekRLEELRKEL-EELEKKYSEEEYEELREEYLELSREL 675
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622909265 1489 TRKLYQMNDLCIEKKKLDSRLNTLQNQQGNAFQSLREADVV--AREEVTELIqlqaERISALKEEIA 1553
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLekALERVEELR----EKVKKYKALLK 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
643-955 |
7.64e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 643 EDPKAYSIENARRKREHDKLMKEVEEIKAQkrEQIKALRTEFCKLLEMNEELPTHMQFKRTDFDVDSKIRAEMHRRTAFK 722
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKAD--EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 723 IQQVEKELAWEKEKHELGLKKLKNRFRDPLESDTIVVHAILSDHKISSYRLVQPSKYSKFKRTSQSERKPSKLDRFEKEG 802
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 803 TGRKDSQRDAGGSIAIQEESiiEKGKKfrpktlseimvENQIEKTRKLILKAERAQLKIQQRKKEWEELYKSkpgDDYED 882
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEE--DEKKA-----------AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA---EEENK 1729
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622909265 883 PKDLQAIKEAQvymgdfnlktaPDYKIPEHMRINAAKKEEelghldslVHGNKRYMNKCILSLRDLKVAVVEE 955
Cdd:PTZ00121 1730 IKAEEAKKEAE-----------EDKKKAEEAKKDEEEKKK--------IAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
234-599 |
2.95e-24 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 107.30 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 234 VNFNYSGTLLASVGSnpDYTLTIWNWKEEQPILRTKAFSQEVFKVTFNPDNEEQLTTSGSGHIKFWEMAftfTGLKLQGS 313
Cdd:COG2319 84 VAFSPDGRLLASASA--DGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA---TGKLLRTL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 314 LGRFGKTTTTDIegymeLPDGKVL-SGSEWGNMLLWE---GGLIKVelCRGtskscHNGPINQIML--DEGEVITVGSDG 387
Cdd:COG2319 159 TGHSGAVTSVAF-----SPDGKLLaSGSDDGTVRLWDlatGKLLRT--LTG-----HTGAVRSVAFspDGKLLASGSADG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 388 CVRIWDFETidtadiidetGlleiEPINELQVDKNVNL---FSmtkmsetGNNFWLA---QDANGAIWKLDlsfsniTQD 461
Cdd:COG2319 227 TVRLWDLAT----------G----KLLRTLTGHSGSVRsvaFS-------PDGRLLAsgsADGTVRLWDLA------TGE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 462 PECLFSFHSGAVEAVAVSPLTYLMATTALDCSVRIYDFASKTLLTQMKFKQGG-TALVWVPrmvnfTGAEIIVGFEDGVV 540
Cdd:COG2319 280 LLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAvRSVAFSP-----DGKTLASGSDDGTV 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622909265 541 RVLELYDPKGLTIFVGrkkisdadirlkqvfkpHTARVTALAYERDGEILATGSKDQTV 599
Cdd:COG2319 355 RLWDLATGELLRTLTG-----------------HTGAVTSVAFSPDGRTLASGSADGTV 396
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
234-599 |
1.22e-21 |
|
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: 97.02 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 234 VNFNYSGTLLASVGSnpDYTLTIWNWKEEQPILRTKAFSQEVFKVTFNPDNEEQLTTSGSGHIKFW-----EMAFTFTGL 308
Cdd:cd00200 15 VAFSPDGKLLATGSG--DGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWdletgECVRTLTGH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 309 KLQGSLGRFgkttttdiegymeLPDGKVLSGSEW-GNMLLWEggLIKVELCrgTSKSCHNGPINQI-MLDEGEVITVGS- 385
Cdd:cd00200 93 TSYVSSVAF-------------SPDGRILSSSSRdKTIKVWD--VETGKCL--TTLRGHTDWVNSVaFSPDGTFVASSSq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 386 DGCVRIWDFETIdtadiidetglleiepinelqvdknvnlfsmtkmsetgnnfwlaqdangaiwkldlsfsnitqdpECL 465
Cdd:cd00200 156 DGTIKLWDLRTG-----------------------------------------------------------------KCV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 466 --FSFHSGAVEAVAVSPLTYLMATTALDCSVRIYDFASKTLLTQMKFKQGG-TALVWvprmvNFTGAEIIVGFEDGVVRV 542
Cdd:cd00200 171 atLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGvNSVAF-----SPDGYLLASGSEDGTIRV 245
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622909265 543 lelYDpkgltifvGRKKisdadiRLKQVFKPHTARVTALAYERDGEILATGSKDQTV 599
Cdd:cd00200 246 ---WD--------LRTG------ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
238-627 |
1.42e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 99.22 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 238 YSGTLLASVGSNPDYTLTIWNWKEEQPILRTKAFSQEVFKVTFNPDNEEQLTTSGSGHIKFWEMAftfTGLKLQGSLGRF 317
Cdd:COG2319 44 ASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA---TGLLLRTLTGHT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 318 GKTTTTDIEgymelPDGK-VLSGSEWGNMLLWE---GGLIKVelcrgtsKSCHNGPINQIML--DEGEVITVGSDGCVRI 391
Cdd:COG2319 121 GAVRSVAFS-----PDGKtLASGSADGTVRLWDlatGKLLRT-------LTGHSGAVTSVAFspDGKLLASGSDDGTVRL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 392 WDFETidtadiidetGlleiEPINELQVDKNVnLFSMTkMSETGNnfWLA---QDANGAIWKLDlsfsniTQDPECLFSF 468
Cdd:COG2319 189 WDLAT----------G----KLLRTLTGHTGA-VRSVA-FSPDGK--LLAsgsADGTVRLWDLA------TGKLLRTLTG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 469 HSGAVEAVAVSPLTYLMATTALDCSVRIYDFASKTLLTQMKFKQGG-TALVWVPrmvnfTGAEIIVGFEDGVVRVLELyd 547
Cdd:COG2319 245 HSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGvNSVAFSP-----DGKLLASGSDDGTVRLWDL-- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 548 pkgltifvgrkkisdADIRLKQVFKPHTARVTALAYERDGEILATGSKDQTVFFFEVERDYKPIGYINTPGPVCQLMWSP 627
Cdd:COG2319 318 ---------------ATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSP 382
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
209-498 |
2.78e-19 |
|
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: 90.09 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 209 IIIYEYPSLRPYRILRdGTEKGYAYVNFNYSGTLLASVGSnpDYTLTIWNWKEEQPILRTKAFSQEVFKVTFNPDNEEQL 288
Cdd:cd00200 33 IKVWDLETGELLRTLK-GHTGPVRDVAASADGTYLASGSS--DKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 289 TTSGSGHIKFWEMA-----FTFTGLKLQGSLGRFgkttttdiegymeLPDGKVLSGSEW-GNMLLWEGGLIKvelCRGTS 362
Cdd:cd00200 110 SSSRDKTIKVWDVEtgkclTTLRGHTDWVNSVAF-------------SPDGTFVASSSQdGTIKLWDLRTGK---CVATL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 363 KScHNGPINQIML--DEGEVITVGSDGCVRIWDFETIDTadiideTGLLEI--EPINELQVDKNVNLFSmtkmsetgnnf 438
Cdd:cd00200 174 TG-HTGEVNSVAFspDGEKLLSSSSDGTIKLWDLSTGKC------LGTLRGheNGVNSVAFSPDGYLLA----------- 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622909265 439 wlAQDANGAI--WKLDlsfsnitqDPECLFSF--HSGAVEAVAVSPLTYLMATTALDCSVRIYD 498
Cdd:cd00200 236 --SGSEDGTIrvWDLR--------TGECVQTLsgHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
332-627 |
8.09e-19 |
|
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: 88.55 E-value: 8.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 332 PDGKVL-SGSEWGNMLLW--EGGLIKVELCrGtskscHNGPINQIML--DEGEVITVGSDGCVRIWDFETIdtadiidet 406
Cdd:cd00200 19 PDGKLLaTGSGDGTIKVWdlETGELLRTLK-G-----HTGPVRDVAAsaDGTYLASGSSDKTIRLWDLETG--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 407 glleiEPINELQVDKNvNLFSMTKMSetgNNFWLA---QDANGAIWKLDlsfsnitqDPECLFSF--HSGAVEAVAVSPL 481
Cdd:cd00200 84 -----ECVRTLTGHTS-YVSSVAFSP---DGRILSsssRDKTIKVWDVE--------TGKCLTTLrgHTDWVNSVAFSPD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 482 TYLMATTALDCSVRIYDFASKTLLTQMKFKQGG-TALVWVPrmvnfTGAEIIVGFEDGVVRVLELYDPKgltifvgrkki 560
Cdd:cd00200 147 GTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEvNSVAFSP-----DGEKLLSSSSDGTIKLWDLSTGK----------- 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622909265 561 sdadirLKQVFKPHTARVTALAYERDGEILATGSKDQTVFFFEVERDYKPIGYINTPGPVCQLMWSP 627
Cdd:cd00200 211 ------CLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSP 271
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
239-627 |
1.25e-14 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 78.03 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 239 SGTLLASVGSNPDYTLTIWNWKEEQPILRTKAFSQEVFKVTFNPDNEEQLTTSGSGHIKFWEMAFTFTGLKLQGSLGRfg 318
Cdd:COG2319 3 SADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 319 kttttdIEGYMELPDGKVL-SGSEWGNMLLW--EGGLIKVELcrgtskSCHNGPINQIML--DEGEVITVGSDGCVRIWD 393
Cdd:COG2319 81 ------VLSVAFSPDGRLLaSASADGTVRLWdlATGLLLRTL------TGHTGAVRSVAFspDGKTLASGSADGTVRLWD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 394 fetidtadiidetglleiepinelqvdknvnlfsmtkmsetgnnfwlaqdangaiwkldlsfsniTQDPECLFSF--HSG 471
Cdd:COG2319 149 -----------------------------------------------------------------LATGKLLRTLtgHSG 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 472 AVEAVAVSPLTYLMATTALDCSVRIYDFASKTLLTQMKfkqGGTALVWVprmVNFT--GAEIIVGFEDGVVRVLELYDPK 549
Cdd:COG2319 164 AVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVRS---VAFSpdGKLLASGSADGTVRLWDLATGK 237
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622909265 550 GLTIFVGrkkisdadirlkqvfkpHTARVTALAYERDGEILATGSKDQTVFFFEVErDYKPIGYINTP-GPVCQLMWSP 627
Cdd:COG2319 238 LLRTLTG-----------------HSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGELLRTLTGHsGGVNSVAFSP 298
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
158-393 |
1.02e-11 |
|
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: 67.36 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 158 IYIAG--NQLIFLNLKTKEQIylRSSSGEGIGVIGVHPHKTYFIVAekGSFPD--IIIYEYPSLRPYRILRdGTEKGYAY 233
Cdd:cd00200 66 LASGSsdKTIRLWDLETGECV--RTLTGHTSYVSSVAFSPDGRILS--SSSRDktIKVWDVETGKCLTTLR-GHTDWVNS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 234 VNFNYSGTLLASVGSnpDYTLTIWNWKEEQPILRTKAFSQEVFKVTFNPDNEEQLTTSGSGHIKFWEMAFTFTGLKLQGS 313
Cdd:cd00200 141 VAFSPDGTFVASSSQ--DGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 314 LGRFgktTTTDIegymeLPDGK-VLSGSEWGNMLLWegglikvELCRGTSKSC---HNGPINQIML--DEGEVITVGSDG 387
Cdd:cd00200 219 ENGV---NSVAF-----SPDGYlLASGSEDGTIRVW-------DLRTGECVQTlsgHTNSVTSLAWspDGKRLASGSADG 283
|
....*.
gi 1622909265 388 CVRIWD 393
Cdd:cd00200 284 TIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
234-396 |
2.31e-11 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 67.63 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 234 VNFNYSGTLLASVGSnpDYTLTIWNWKEEQPILRTKAFSQEVFKVTFNPDNEeQL-TTSGSGHIKFWEMAftfTGLKLQG 312
Cdd:COG2319 252 VAFSPDGRLLASGSA--DGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGK-LLaSGSDDGTVRLWDLA---TGKLLRT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 313 SLGRFGKTTTTDIegymeLPDGKVL-SGSEWGNMLLW--EGGLIKVELcRGtskscHNGPINQIML--DEGEVITVGSDG 387
Cdd:COG2319 326 LTGHTGAVRSVAF-----SPDGKTLaSGSDDGTVRLWdlATGELLRTL-TG-----HTGAVTSVAFspDGRTLASGSADG 394
|
....*....
gi 1622909265 388 CVRIWDFET 396
Cdd:COG2319 395 TVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
209-396 |
2.55e-11 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 67.63 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 209 IIIYEYPSLRPYRILRDGTEKGYAyVNFNYSGTLLASVGSnpDYTLTIWNWKEEQPILRTKAFSQEVFKVTFNPDNeEQL 288
Cdd:COG2319 186 VRLWDLATGKLLRTLTGHTGAVRS-VAFSPDGKLLASGSA--DGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDG-RLL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 289 -TTSGSGHIKFWEMAftfTGLKLQGSLGRFGKTTTTDIegymeLPDGKVL-SGSEWGNMLLWEGGLIKvelCRGTSKScH 366
Cdd:COG2319 262 aSGSADGTVRLWDLA---TGELLRTLTGHSGGVNSVAF-----SPDGKLLaSGSDDGTVRLWDLATGK---LLRTLTG-H 329
|
170 180 190
....*....|....*....|....*....|..
gi 1622909265 367 NGPINQIML--DEGEVITVGSDGCVRIWDFET 396
Cdd:COG2319 330 TGAVRSVAFspDGKTLASGSDDGTVRLWDLAT 361
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
469-631 |
1.64e-10 |
|
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: 63.89 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 469 HSGAVEAVAVSPLTYLMATTALDCSVRIYDFASKTLLTQMKFKQGG-TALVWVPRmvnftGAEIIVGFEDGVVRVLELYD 547
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPvRDVAASAD-----GTYLASGSSDKTIRLWDLET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 548 PKGLTIFVGrkkisdadirlkqvfkpHTARVTALAYERDGEILATGSKDQTVFFFEVErDYKPIGYINT-PGPVCQLMWS 626
Cdd:cd00200 83 GECVRTLTG-----------------HTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE-TGKCLTTLRGhTDWVNSVAFS 144
|
....*
gi 1622909265 627 PMSHF 631
Cdd:cd00200 145 PDGTF 149
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1276-1557 |
4.56e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1276 LTLQLREKRLDIEEALVEekkvVDNLKKEYDTLSKKVKIVATNLNAAEEALEAYQREKQQRLNELLVVIpLKLHQIeyvv 1355
Cdd:COG1196 216 RELKEELKELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE-LELEEA---- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1356 fgeipsdlsgtlvfsNHALRRLQERIRELQEENSKQQKLNKEWRERRKQLIREKREMTKTIHKMEETVRQLmiskfgrvv 1435
Cdd:COG1196 287 ---------------QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL--------- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1436 NLEALQTLSVNTTLEELKIRKLRKELANAKEMKMWEEKIAQMRWELMMKTKEHTRKLYQMNDLCIEKKKLDSRLNTLQNQ 1515
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622909265 1516 QGNAFQSLREADVVAREEVTELIQLQAERISALKEEIALLRR 1557
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1271-1558 |
1.17e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1271 VALFELTLQLREKRLDIEEA---LVEEKKVVDNLKKEYDTLSKKVKIVATNLNAAEEALEAYQREKQQrLNELLVVIPLK 1347
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELsrqISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1348 LHQIEYVVfgeipSDLSGTLVFSNHALRRLQERIRELQEENSKQQklnkewrERRKQLIREKREMTKTIHKMEETVRQLm 1427
Cdd:TIGR02168 784 IEELEAQI-----EQLKEELKALREALDELRAELTLLNEEAANLR-------ERLESLERRIAATERRLEDLEEQIEEL- 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1428 iskfgrvvnLEALQTLSVNTTLEELKIRKLRKELANA-KEMKMWEEKIAQMRWE---LMMKTKEHTRKLYQMNDLCIEKK 1503
Cdd:TIGR02168 851 ---------SEDIESLAAEIEELEELIEELESELEALlNERASLEEALALLRSEleeLSEELRELESKRSELRRELEELR 921
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622909265 1504 ----KLDSRLNTLQNQQGNAFQSLREADVVAREEVTELIQLQAERISALKEEIALLRRK 1558
Cdd:TIGR02168 922 eklaQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
169-302 |
4.04e-05 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 47.98 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 169 NLKTKEQIYLRSSSGEGIGVIGVHPHKTYFIVAekGSFPDIIIYEYPSLRPYRILRDGTEKGYAyVNFNYSGTLLASVGS 248
Cdd:COG2319 274 DLATGELLRTLTGHSGGVNSVAFSPDGKLLASG--SDDGTVRLWDLATGKLLRTLTGHTGAVRS-VAFSPDGKTLASGSD 350
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622909265 249 npDYTLTIWNWKEEQPILRTKAFSQEVFKVTFNPDNEEQLTTSGSGHIKFWEMA 302
Cdd:COG2319 351 --DGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1279-1466 |
4.10e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1279 QLREKRLDIEEALVEEKKVVDNLKKEYDTLSKKVKivatNLNAAEEALEAYQREKQQRLNELLVVIpLKLHQIEYVVFGE 1358
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRALEQELAALEAELA----ELEKEIAELRAELEAQKEELAELLRAL-YRLGRQPPLALLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1359 IPSDLSGTLVFS-----------------NHALRRLQERIRELQEENSKQQKLNKEWRERRKQLIREKREMTKTIHKMEE 1421
Cdd:COG4942 127 SPEDFLDAVRRLqylkylaparreqaeelRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622909265 1422 TVRQLMiskfgrvvnlEALQTLSVNTTLEELKIRKLRKELANAKE 1466
Cdd:COG4942 207 ELAELA----------AELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
566-603 |
4.28e-05 |
|
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: 41.91 E-value: 4.28e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1622909265 566 RLKQVFKPHTARVTALAYERDGEILATGSKDQTVFFFE 603
Cdd:smart00320 3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1279-1564 |
4.55e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1279 QLREKRLDIEEALVEEKKVVDNLKKEYDTLSKKVKIVATNLNAAEEALEAYQREkqqrlnellvviplklhqieyvvfge 1358
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE-------------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1359 ipsdlsgtlvfsnhaLRRLQERIRELQEEnskQQKLNKEWRERRKQLirekREMTKTIHKMEETVRQLMI----SKFGRV 1434
Cdd:COG4942 78 ---------------LAALEAELAELEKE---IAELRAELEAQKEEL----AELLRALYRLGRQPPLALLlspeDFLDAV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1435 VNLEALQTLSVNTTLEELKIRKLRKELANAKEmkmweeKIAQMRWELMMKTKEHTRKLYQMNDLCIEKKKLDSRLNTLQN 1514
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRA------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1515 QQGNAFQSLREADVVAREEVTELIQLQAERiSALKEEIALLRRKGGLILP 1564
Cdd:COG4942 210 ELAAELAELQQEAEELEALIARLEAEAAAA-AERTPAAGFAALKGKLPWP 258
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1279-1518 |
5.07e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1279 QLREKRLDIEEALVEEKKVVDNLKKEYDTLSKKVKIVA---TNLNAAEEALEAYQREKQQRLNELLvvipLKLHQIEYvv 1355
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRerlANLERQLEELEAQLEELESKLDELA----EELAELEE-- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1356 fgeipsDLSGTLVFSNHALRRLQERIRELQEENSKQQKLNKEWRERRKQLIREKREMT---KTIHKMEETVRQLMiskfG 1432
Cdd:TIGR02168 345 ------KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnNEIERLEARLERLE----D 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1433 RVVNLEAlQTLSVNTTLEELKIRKLRKELANAKEM-KMWEEKIAQMRWELMMKTKEHTRKLYQMNDLCIEKKKLDSRLNT 1511
Cdd:TIGR02168 415 RRERLQQ-EIEELLKKLEEAELKELQAELEELEEElEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
....*..
gi 1622909265 1512 LQNQQGN 1518
Cdd:TIGR02168 494 LERLQEN 500
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
566-603 |
1.17e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 40.79 E-value: 1.17e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1622909265 566 RLKQVFKPHTARVTALAYERDGEILATGSKDQTVFFFE 603
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
567-631 |
1.57e-04 |
|
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: 45.40 E-value: 1.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622909265 567 LKQVFKPHTARVTALAYERDGEILATGSKDQTVFFFEVERDYKPIGYINTPGPVCQLMWSPMSHF 631
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTY 65
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
642-1558 |
1.99e-04 |
|
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: 46.12 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 642 IEDPKAYSIENARRKREHDKLMKEVEEIKAQKREQIKALRTEFcKLLEMNEELPTHMQFKRTDFDVDSKIRAEmhrrtaf 721
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQEL-KLKEQAKKALEYYQLKEKLELEEEYLLYL------- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 722 KIQQVEKElaWEKEKHELGLKKLKnrfrdplesdtivvhailsdhKISSYRLVQPSKYSKFKRTSQSERKPSKLDRFEKE 801
Cdd:pfam02463 230 DYLKLNEE--RIDLLQELLRDEQE---------------------EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 802 GTGRKDSQRDAGGSIAIQEESIIEKGKkfRPKTLSEIMVENQIEKTRKLILKAERAQ--LKIQQRKKEWEELYKSKPGDD 879
Cdd:pfam02463 287 ELKLLAKEEEELKSELLKLERRKVDDE--EKLKESEKEKKKAEKELKKEKEEIEELEkeLKELEIKREAEEEEEEELEKL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 880 YE-DPKDLQAIKEAQVYMGDFNLKTAPDYKIPEHMRINAAKKEEELGHLDSlvhgNKRYMNKCILSLRDLKVAVVEEIQC 958
Cdd:pfam02463 365 QEkLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELAR----QLEDLLKEEKKEELEILEEEEESIE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 959 LVQELKNIQST-LHVSKHIpipQIPQIHPEEVPEKRFQYDEETLLNFKQQHMKSD-DEKSPGVEQTGSGGPGGGFLKLSS 1036
Cdd:pfam02463 441 LKQGKLTEEKEeLEKQELK---LLKDELELKKSEDLLKETQLVKLQEQLELLLSRqKLEERSQKESKARSGLKVLLALIK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1037 GKDGDLTTRDSMSRSSKASTLSLDIPKYMEFEKAEPTDVELEIMKRDEIKHVYMQQYLVNRVKELIVTFDAELRLLRHQK 1116
Cdd:pfam02463 518 DGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1117 LKLDTQMKLSDLHHVTLFQEI----LLLKNFEKQENILQERVNSLDKEEQYMQWKINETLKEMEEKKNEITKLQEQEKAL 1192
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDdkraKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1193 YAGFQTAIGENNKFANFLMKVLKKKIKRVKKKEVEGDADEDEESEESSEEESSLESDEDESESEDEVFDDSICPTNCDVA 1272
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1273 LFELTLQLREKRLDIEEALvEEKKVVDNLKKEYDTLSKKVKIVATNLNAAEEALEAYQREKQQRLNELLVVIPLKLHQIE 1352
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKEL-AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1353 YvvfgeipsdLSGTLVFSNHALRRLQERIRELQEENSKQQKLNKEWRERRKQLIREKREMTKTIHKMEETVRQlmiskfg 1432
Cdd:pfam02463 837 E---------LALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKK------- 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1433 rvvnlEALQTLSVNTTLEELKIRKLRKELANAKEMKMWEEkiaqmrWELMMKTKEHTRKLYQMNDLCIEKKKLDSRLNTL 1512
Cdd:pfam02463 901 -----ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEE------EPEELLLEEADEKEKEENNKEEEEERNKRLLLAK 969
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 1622909265 1513 Q---NQQGNAFQSLREADVVAREEVTELIQLQAERISALKEEIALLRRK 1558
Cdd:pfam02463 970 EelgKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
459-498 |
1.48e-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: 37.68 E-value: 1.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1622909265 459 TQDPECLFSFHSGAVEAVAVSPLTYLMATTALDCSVRIYD 498
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| NBCH_WD40 |
pfam20426 |
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ... |
560-606 |
1.48e-03 |
|
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at the C-terminus of neurobeachin-like proteins.
Pssm-ID: 466575 [Multi-domain] Cd Length: 350 Bit Score: 42.75 E-value: 1.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1622909265 560 ISDADIRLKQVFKPHTARVTALAYERDGEILATGSKDQTVFFFEVER 606
Cdd:pfam20426 109 ISLNDGRMVQSIRQHKDVVSCVAVTSDGSILATGSYDTTVMVWEVLR 155
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1306-1526 |
1.92e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1306 DTLSKKVKIVATNLNAAEEALEAYQREKQQRLNELLVviplkLHQIEYVVFGEIpsDLSGTLvfsnHALRRLQERIRELQ 1385
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREA-----LQRLAEYSWDEI--DVASAE----REIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1386 EENSKQQKLNKEW---RERRKQLIREKREMTKTIHKMEETVRQLmiskfgrvvnlealqtlsvnttleELKIRKLRKELA 1462
Cdd:COG4913 682 ASSDDLAALEEQLeelEAELEELEEELDELKGEIGRLEKELEQA------------------------EEELDELQDRLE 737
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622909265 1463 NAKEMKMWE--EKIAQMRWELMmkTKEHTRKLyqmndlcieKKKLDSRLNTLQNQQGNAFQSLREA 1526
Cdd:COG4913 738 AAEDLARLElrALLEERFAAAL--GDAVEREL---------RENLEERIDALRARLNRAEEELERA 792
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1275-1553 |
2.24e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1275 ELTLQLREKRLDIEEALVEEKKVVDNLKKEYDTLSKKVKI-----VATNLNAAEEALEAYQREKQQRLNELLVVIPLKLH 1349
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELiklkeLAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1350 QIEyvvfGEIpsdlsgtlvfsnhalRRLQERIRELQEENSKQQKLNKEWR---ERRKQLIREKREMT-KTIHKMEETVRQ 1425
Cdd:PRK03918 536 KLK----GEI---------------KSLKKELEKLEELKKKLAELEKKLDeleEELAELLKELEELGfESVEELEERLKE 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1426 L--MISKFGRVVN----LEALQTL--SVNTTLEEL---------KIRKLRKELaNAKEMKMWEEKIAQMRWELMMKTKEH 1488
Cdd:PRK03918 597 LepFYNEYLELKDaekeLEREEKElkKLEEELDKAfeelaetekRLEELRKEL-EELEKKYSEEEYEELREEYLELSREL 675
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622909265 1489 TRKLYQMNDLCIEKKKLDSRLNTLQNQQGNAFQSLREADVV--AREEVTELIqlqaERISALKEEIA 1553
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLekALERVEELR----EKVKKYKALLK 738
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1374-1558 |
5.50e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1374 LRRLQERIRELQEENSKQQKLNKEWRERRKQLIREKREMTKTIHKMEETVRQLmiskfgrvvnLEALQTLSVNTTLEELK 1453
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEL----------EEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1454 IRKLRKELANAKEMKMWEEKIAQMRwELMMKTKEHTRKLYQMNDLCIEKKKLDSRLNTLQNQQGNAFQSLREADVVAREE 1533
Cdd:COG4717 118 LEKLEKLLQLLPLYQELEALEAELA-ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180
....*....|....*....|....*
gi 1622909265 1534 VTELIQLQAERISALKEEIALLRRK 1558
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEE 221
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1292-1514 |
7.36e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1292 VEEKKVVDNLKKEYDTLSKKVKivatnlNAAEEALEAYQREKQQRLNELL-VVIPLKLHqieyvVFGEIPSDLSGTLV-- 1368
Cdd:TIGR01612 692 TEDKAKLDDLKSKIDKEYDKIQ------NMETATVELHLSNIENKKNELLdIIVEIKKH-----IHGEINKDLNKILEdf 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1369 -------------FSNH--ALRRLQERIRELQEENSKQQKLNKEWRERRKQLIREKREMTKTIH-KMEETVRQL------ 1426
Cdd:TIGR01612 761 knkekelsnkindYAKEkdELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISiKEDEIFKIInemkfm 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1427 ---MISKFGRVVNLEALQTLSVNTTLEELK--IRKLRKELANAKeMKMWEEKIAQMRwELMMKTKEHTRKLYQ-MNDLci 1500
Cdd:TIGR01612 841 kddFLNKVDKFINFENNCKEKIDSEHEQFAelTNKIKAEISDDK-LNDYEKKFNDSK-SLINEINKSIEEEYQnINTL-- 916
|
250
....*....|....
gi 1622909265 1501 ekKKLDSRLNTLQN 1514
Cdd:TIGR01612 917 --KKVDEYIKICEN 928
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
463-498 |
7.45e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 35.78 E-value: 7.45e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1622909265 463 ECLFSF--HSGAVEAVAVSPLTYLMATTALDCSVRIYD 498
Cdd:pfam00400 2 KLLKTLegHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1272-1481 |
7.47e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1272 ALFELTLQLRE-----KRLDIEEaLVEEKKVVDNLKKEYDTLSKKVKIVATNLNAAEE------ALEAYQREKQQRLNEL 1340
Cdd:PRK03918 497 KLKELAEQLKEleeklKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAEL 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1341 LVviplKLHQIEYVVFGEIPSDLSG---------TLVFSNHALRRLQERIRELQEENSKQ----QKLNKEWRERRKQLIR 1407
Cdd:PRK03918 576 LK----ELEELGFESVEELEERLKElepfyneylELKDAEKELEREEKELKKLEEELDKAfeelAETEKRLEELRKELEE 651
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622909265 1408 EKREMTKTIHkmeETVRQLMISKFGRVVNLEAlQTLSVNTTLEELK--IRKLRKELANAKEMKMWEEKIAQMRWEL 1481
Cdd:PRK03918 652 LEKKYSEEEY---EELREEYLELSRELAGLRA-ELEELEKRREEIKktLEKLKEELEEREKAKKELEKLEKALERV 723
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
643-955 |
7.64e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 643 EDPKAYSIENARRKREHDKLMKEVEEIKAQkrEQIKALRTEFCKLLEMNEELPTHMQFKRTDFDVDSKIRAEMHRRTAFK 722
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKAD--EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 723 IQQVEKELAWEKEKHELGLKKLKNRFRDPLESDTIVVHAILSDHKISSYRLVQPSKYSKFKRTSQSERKPSKLDRFEKEG 802
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 803 TGRKDSQRDAGGSIAIQEESiiEKGKKfrpktlseimvENQIEKTRKLILKAERAQLKIQQRKKEWEELYKSkpgDDYED 882
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEE--DEKKA-----------AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA---EEENK 1729
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622909265 883 PKDLQAIKEAQvymgdfnlktaPDYKIPEHMRINAAKKEEelghldslVHGNKRYMNKCILSLRDLKVAVVEE 955
Cdd:PTZ00121 1730 IKAEEAKKEAE-----------EDKKKAEEAKKDEEEKKK--------IAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1293-1562 |
8.99e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1293 EEKKV---VDNLKKEYDTLskkvkivatnlNAAEEALEayqREKQQRlnELLVVIPlKLHQ------IEYVVFGEIPSDL 1363
Cdd:COG4913 219 EEPDTfeaADALVEHFDDL-----------ERAHEALE---DAREQI--ELLEPIR-ELAEryaaarERLAELEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1364 sgTLVFSNHALRRLQERIRELQEENSKQQKLNKEWRERRKQLIREKREMTktihkmeetvRQLMISKFGRVVNLEAlqtl 1443
Cdd:COG4913 282 --RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE----------AQIRGNGGDRLEQLER---- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909265 1444 svnttleelKIRKLRKELAN-AKEMKMWEEKIAQMRWELmmktkEHTRKLYQMNdlcieKKKLDSRLNTLQNQQGNAFQS 1522
Cdd:COG4913 346 ---------EIERLERELEErERRRARLEALLAALGLPL-----PASAEEFAAL-----RAEAAALLEALEEELEALEEA 406
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622909265 1523 LREADVvareevtELIQLQAERiSALKEEIALLRRKGGLI 1562
Cdd:COG4913 407 LAEAEA-------ALRDLRREL-RELEAEIASLERRKSNI 438
|
|
| |
