|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
403-667 |
2.53e-34 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 136.96 E-value: 2.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 403 LIATCSLDRSIRLWNYETNT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDD-IRSFK--EYSVRGcgeC 477
Cdd:COG2319 134 TLASGSADGTVRLWDLATGKlLRTLTGHSGAVTSVAFSPDGKLLASGSDDGtVRLWDLATGKlLRTLTghTGAVRS---V 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 478 SFS-NGGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCS 556
Cdd:COG2319 211 AFSpDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 557 YNCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEY 634
Cdd:COG2319 291 VNSVAFSPDGKLLASGSDDGTVRlwDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL--WDLATGELLRTL 368
|
250 260 270
....*....|....*....|....*....|...
gi 345199335 635 QAHAGPITKMLLTFDDQFLLTAAEDGCLFTWKV 667
Cdd:COG2319 369 TGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
386-678 |
1.91e-31 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 128.49 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 386 PLHSAPITGLATCIRKPLIATCSLDRSIRLWNYETN-TLELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNL----L 459
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGlLLRTLTGHTGAVRSVAFSPDGKTLASGSADGtVRLWDLatgkL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 460 IDDIRSFKE--YSVrgcgecSFSNGGHLFAAVNG-NVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAV 536
Cdd:COG2319 155 LRTLTGHSGavTSV------AFSPDGKLLASGSDdGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 537 YEWNLSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTS 614
Cdd:COG2319 229 RLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRlwDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSD 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345199335 615 VGTIRAmkYPLPLQKEFNEYQAHAGPITKMLLTFDDQFLLTAAEDGclfTWKVFDKDGRGIKRE 678
Cdd:COG2319 309 DGTVRL--WDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDG---TVRLWDLATGELLRT 367
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
388-666 |
2.53e-31 |
|
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: 125.14 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 388 HSAPITGLATCIRKPLIATCSLDRSIRLWNYETNTLEL-FKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNL----LID 461
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtLKGHTGPVRDVAASADGTYLASGSSDKtIRLWDLetgeCVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 462 DIRSFKEYsVRGcgeCSFSNGGHLFAAVNG-NVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 540
Cdd:cd00200 88 TLTGHTSY-VSS---VAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 541 LSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTI 618
Cdd:cd00200 164 LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKlwDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTI 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 345199335 619 RAmkYPLPLQKEFNEYQAHAGPITKMLLTFDDQFLLTAAEDGCLFTWK 666
Cdd:cd00200 244 RV--WDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
341-579 |
6.43e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 111.93 E-value: 6.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 341 VLCLCFSPSEETLvASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWNYET 420
Cdd:COG2319 165 VTSVAFSPDGKLL-ASGSDDG----TVRLWDLATGKLLRT----LTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 421 NT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDDIRSFKEYSVRGCGECSFS-NGGHLFAAVNGNVIHVY 497
Cdd:COG2319 236 GKlLRTLTGHSGSVRSVAFSPDGRLLASGSADGtVRLWDLATGELLRTLTGHSGGVNSVAFSpDGKLLASGSDDGTVRLW 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 498 TTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHT 577
Cdd:COG2319 316 DLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395
|
..
gi 345199335 578 LK 579
Cdd:COG2319 396 VR 397
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
338-540 |
1.36e-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: 96.64 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 338 KQDVLCLCFSPSEeTLVASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:cd00200 93 TSYVSSVAFSPDG-RILSSSSRDK----TIKVWDVETGKCLTT----LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 418 YETNTL-ELFKEYQEEAYSISLHPSGHFIVVGFADKlrlmNLLIDDIRSFKE-YSVRGCGE----CSFSNGGHLFAAVNG 491
Cdd:cd00200 164 LRTGKCvATLTGHTGEVNSVAFSPDGEKLLSSSSDG----TIKLWDLSTGKClGTLRGHENgvnsVAFSPDGYLLASGSE 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 345199335 492 -NVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 540
Cdd:cd00200 240 dGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
341-543 |
2.52e-20 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 94.98 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 341 VLCLCFSPSEETLvASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCirkP---LIATCSLDRSIRLWN 417
Cdd:COG2319 207 VRSVAFSPDGKLL-ASGSADG----TVRLWDLATGKLLRT----LTGHSGSVRSVAFS---PdgrLLASGSADGTVRLWD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 418 YETNT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDD-IRSFKEYSVRGCGeCSFS-NGGHLFAAVNGNV 493
Cdd:COG2319 275 LATGElLRTLTGHSGGVNSVAFSPDGKLLASGSDDGtVRLWDLATGKlLRTLTGHTGAVRS-VAFSpDGKTLASGSDDGT 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 345199335 494 IHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLST 543
Cdd:COG2319 354 VRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
703-1254 |
7.61e-20 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 95.86 E-value: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 703 ELKTRVEELKMENEYQLRLKD-MNYSEKIKELTDKFI-----------QEMESLKTKNQVLRTEKEKQDVYHHEHIEDLL 770
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVeLNKLEKQKKENKKNIdkflteikkkeKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 771 DKQSrelqDMECCNNQKLLLEY---------EKYQELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFYEAKLQEKTTL 841
Cdd:TIGR04523 184 NIQK----NIDKIKNKLLKLELllsnlkkkiQKNKSLESQISELKKQ-NNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 842 LEEAQEDVRQ---QLREFEETKKQIEEDEDReIQDIKTKYEkKLRDEKESNL--RLKGETGIMRKKFSSLQKEIEERTND 916
Cdd:TIGR04523 259 KDEQNKIKKQlseKQKELEQNNKKIKELEKQ-LNQLKSEIS-DLNNQKEQDWnkELKSELKNQEKKLEEIQNQISQNNKI 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 917 IETLKGEqmklqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRV 996
Cdd:TIGR04523 337 ISQLNEQ-------ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ-------EIKNLESQINDLESKIQN 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 997 MKEQIQENDPILKwpqRVEIHLYNFRKQVRKvlLWGTLPQMEAELENFHKQNTQLELNITEL-------WQKLRATDQEM 1069
Cdd:TIGR04523 403 QEKLNQQKDEQIK---KLQQEKELLEKEIER--LKETIIKNNSEIKDLTNQDSVKELIIKNLdntreslETQLKVLSRSI 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1070 RRERQkerDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKyvqradmveIAGLNTDlQQEYTRQREHLERNLATLK 1149
Cdd:TIGR04523 478 NKIKQ---NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK---------ISSLKEK-IEKLESEKKEKESKISDLE 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1150 KKVVK-EGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEpsrdMLSTAPTARLN 1228
Cdd:TIGR04523 545 DELNKdDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKE----KKISSLEKELE 620
|
570 580
....*....|....*....|....*.
gi 345199335 1229 EQEETGRIIEMQRLEIQRLRDQIQEQ 1254
Cdd:TIGR04523 621 KAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
504-665 |
3.53e-16 |
|
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: 80.46 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 504 NISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHTLK--EI 581
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRlwDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 582 ADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQAHAGPITKMLLTFDDQFLLTAAEDGC 661
Cdd:cd00200 81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKV--WDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158
|
....
gi 345199335 662 LFTW 665
Cdd:cd00200 159 IKLW 162
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
478-669 |
5.21e-16 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 81.88 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 478 SFSNGGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSY 557
Cdd:COG2319 44 ASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 558 NCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQ 635
Cdd:COG2319 124 RSVAFSPDGKTLASGSADGTVRlwDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL--WDLATGKLLRTLT 201
|
170 180 190
....*....|....*....|....*....|....
gi 345199335 636 AHAGPITKMLLTFDDQFLLTAAEDGclfTWKVFD 669
Cdd:COG2319 202 GHTGAVRSVAFSPDGKLLASGSADG---TVRLWD 232
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
696-1003 |
3.11e-14 |
|
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: 78.19 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 696 EKAQVMLELKTRVEELkmenEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQdvyhHEHIEDLLDKQSR 775
Cdd:TIGR02169 208 EKAERYQALLKEKREY----EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR----LEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 776 ELQDM---ECCNNQKLLLEYEKYQElqlKSQRMQEEYEKQLRDNDETKSQALEELTefyeaKLQEKTTLLEEAQEDVRQQ 852
Cdd:TIGR02169 280 KIKDLgeeEQLRVKEKIGELEAEIA---SLERSIAEKERELEDAEERLAKLEAEID-----KLLAEIEELEREIEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 853 LREFEEtkkqieededrEIQDIKTKYEK---KLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQG 929
Cdd:TIGR02169 352 RDKLTE-----------EYAELKEELEDlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345199335 930 VIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQE 1003
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
695-1092 |
3.81e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 74.29 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 695 EEKAQVMLELKTRVEELKMENEYQLRLKDmNYSEKIKEL--TDKFIQEMESL--KTKNQVLRTEKEKQDVYHHEhIEDLL 770
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKK-QLSEKQKELeqNNKKIKELEKQlnQLKSEISDLNNQKEQDWNKE-LKSEL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 771 DKQSRELQDME--CCNNQKLLLEYeKYQELQLKSQRMQEEYEKQLRDND-ETKSQALEELTEFYEAKLQEKTTLlEEAQE 847
Cdd:TIGR04523 317 KNQEKKLEEIQnqISQNNKIISQL-NEQISQLKKELTNSESENSEKQRElEEKQNEIEKLKKENQSYKQEIKNL-ESQIN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 848 DVRQQLREFEETKKQIEED----------EDREIQDIK---TKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERT 914
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQikklqqekelLEKEIERLKetiIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 915 NDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEI 994
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 995 R--VMKEQIQENDP-ILKWPQRVEIHLynfRKQVRKVLLwgtLPQMEAELENFHKQNTQLELNITELWQKLRATDQEMRR 1071
Cdd:TIGR04523 555 KkeNLEKEIDEKNKeIEELKQTQKSLK---KKQEEKQEL---IDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
410 420
....*....|....*....|.
gi 345199335 1072 ERQKERDLEALVKRFKTDLHN 1092
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQ 649
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
702-1090 |
5.22e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 73.52 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 702 LELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKqdvyhhehIEDLLDKQSRELQDME 781
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ--------LNQLKDEQNKIKKQLS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 782 ccnnqkllleyEKYQELQlKSQRMQEEYEKQLRdndETKSQaLEELtefyeaKLQEKTTLLEEAQEDVRQQLREFEETKK 861
Cdd:TIGR04523 271 -----------EKQKELE-QNNKKIKELEKQLN---QLKSE-ISDL------NNQKEQDWNKELKSELKNQEKKLEEIQN 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 862 QIEEDEDReIQDIKTKYE--KKLRDEKESNlrlkgetgimrkkFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQ 939
Cdd:TIGR04523 329 QISQNNKI-ISQLNEQISqlKKELTNSESE-------------NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 940 GLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQENDPILK----WPQRVE 1015
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEK-------EIERLKETIIKNNSEIKDLTNQDSVKELIIKnldnTRESLE 467
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 345199335 1016 IHLYNFRKQVRKVLLwgTLPQMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDL 1090
Cdd:TIGR04523 468 TQLKVLSRSINKIKQ--NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
676-1005 |
7.59e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.64 E-value: 7.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 676 KREREVGFAEEvLVTKTDMEEKAQvmlELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEK 755
Cdd:PTZ00121 1438 KKAEEAKKADE-AKKKAEEAKKAE---EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 756 EKQDVYHHEHIEDLLD-KQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAK 834
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 835 LQEKTTLLEEAQEDVRQQLREFEETKKQIE-----EDEDREIQDIKTKYE------KKLRDEKESNL----RLKGETGIM 899
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelkkaEEEKKKVEQLKKKEAeekkkaEELKKAEEENKikaaEEAKKAEED 1673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 900 RKKFSSLQKEIEERTNDIETLKG---EQMKLQGVIKSLEKDI---QGLKREIQERDETIQDKEKRIYDLKKKNQEL---- 969
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKeaeEAKKAEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkde 1753
|
330 340 350
....*....|....*....|....*....|....*.
gi 345199335 970 GKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEND 1005
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
820-1199 |
1.73e-12 |
|
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: 72.40 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 820 KSQALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNlRLKGETGIM 899
Cdd:TIGR02168 675 RRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK----KKNQELGKFKFV 975
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaaNLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 976 LDYK---IKELKKQIEPRENEIRVMKEQIQEndpilkwpqrveihlynfrkqvrkvlLWGTLPQMEAELENFHKQNTQLE 1052
Cdd:TIGR02168 833 IAATerrLEDLEEQIEELSEDIESLAAEIEE--------------------------LEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1053 LNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRL----LKEKVRglfEKYVQRADMVEIAGLNT 1128
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVridnLQERLS---EEYSLTLEEAEALENKI 963
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 345199335 1129 DLQQEYTRQRehlernLATLKKKVVKEGELhrtdyvrimqeNVSLIKEINELRRELKFTRSQVYDLEAALK 1199
Cdd:TIGR02168 964 EDDEEEARRR------LKRLENKIKELGPV-----------NLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
692-999 |
2.33e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.59 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 692 TDMEEKAQVMLELKTRVEELKMENE-YQLRLKDMNYSEKIKELTDKFIQEMESLKTKN-QVLRTEKEKQDvyhhEHIEDL 769
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQsYKQEIKNLESQINDLESKIQNQEKLNQQKDEQiKKLQQEKELLE----KEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 770 LDKQSRELQDMECCNNQKLLLE--------YEKYQELQLKSqrMQEEYEKQLRDNDETKSQALEELTEFyeAKLQEKTTL 841
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKEliiknldnTRESLETQLKV--LSRSINKIKQNLEQKQKELKSKEKEL--KKLNEEKKE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 842 LEEAQEDVRQQLREFEETKKQIEED---EDREIQDIKTKYEKKLRDEKESNLRlkgetgimrKKFSSLQKEIEERTNDIE 918
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEkkeKESKISDLEDELNKDDFELKKENLE---------KEIDEKNKEIEELKQTQK 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 919 TLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMK 998
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
.
gi 345199335 999 E 999
Cdd:TIGR04523 659 N 659
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
673-1205 |
2.60e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.63 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 673 RGIKREREvgFAEEVLVTKTDMEEKAQVMLELKTRVEE---LKMENEYQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQ 749
Cdd:PRK03918 172 KEIKRRIE--RLEKFIKRTENIEELIKEKEKELEEVLReinEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 750 VLRTEKEKQDVYHHEhIEDLLDKQSRELQDMEccNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQaLEELTE 829
Cdd:PRK03918 249 SLEGSKRKLEEKIRE-LEERIEELKKEIEELE--EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR-LEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 830 FYEAKLQEkttlLEEAQEDVRQQLREFEETKKQIEEDED--REIQDIKTKYEKKLRDEKesnlRLKGET-GIMRKKFSSL 906
Cdd:PRK03918 325 GIEERIKE----LEEKEERLEELKKKLKELEKRLEELEErhELYEEAKAKKEELERLKK----RLTGLTpEKLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 907 QKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLK----------REIQE--RDETIQDKEKRIYDLKKKNQELGKFKF 974
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELTEehRKELLEEYTAELKRIEKELKEIEEKER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 975 VLDYKIKELKKQIEpRENEIRVMK---EQIQENDPILK--WPQRVEIHLYNFRKQVRKVL-LWGTLPQMEAELEN---FH 1045
Cdd:PRK03918 477 KLRKELRELEKVLK-KESELIKLKelaEQLKELEEKLKkyNLEELEKKAEEYEKLKEKLIkLKGEIKSLKKELEKleeLK 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1046 KQNTQLELNITELWQKLRATDQEMRRE--------RQKERDLEALVKRFKTdLHNCVayiQEPRLLKEKVRGLFEKYVQR 1117
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEPFYNEYLE-LKDAE---KELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1118 ADmvEIAGLNTDLqqeytrqrEHLERNLATLKKKV-VKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEA 1196
Cdd:PRK03918 632 FE--ELAETEKRL--------EELRKELEELEKKYsEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
....*....
gi 345199335 1197 ALKLTKKVR 1205
Cdd:PRK03918 702 ELEEREKAK 710
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
829-1184 |
2.79e-12 |
|
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: 71.63 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 829 EFYEAKLQEKTTLLEEAQEDVRQQLREfEETKKQIE---EDEDReIQDIKTKYEKKLRdekesNLRLKGETGimrKKFSS 905
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAGISKYKERR-KETERKLErtrENLDR-LEDILNELERQLK-----SLERQAEKA---ERYKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 906 LQKEIEER-----TNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKI 980
Cdd:TIGR02168 218 LKAELRELelallVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 981 KELKKQIE-PRENEIRVMKEQIQENDPILKWPQRVEIHLYNF-RKQVRKVLLWGTLPQMEAELENFHKQNTQLELNITEL 1058
Cdd:TIGR02168 298 SRLEQQKQiLRERLANLERQLEELEAQLEELESKLDELAEELaELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1059 WQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEprlLKEKVRGLfEKYVQRADMVEIAGLNTDLQQEYTRQR 1138
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER---LQQEIEEL-LKKLEEAELKELQAELEELEEELEELQ 453
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 345199335 1139 EHLERNLATLK--KKVVKEGELHRTDYVRIMQENVSLIKEINELRREL 1184
Cdd:TIGR02168 454 EELERLEEALEelREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
698-1255 |
5.09e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 698 AQVMLELKTRVEELKmeneyQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedlLDKQSREL 777
Cdd:PRK03918 168 GEVIKEIKRRIERLE-----KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREE------------LEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 778 QDMEccNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELtefyEAKLQEKTTLLEEAQEDVRqqLREFE 857
Cdd:PRK03918 231 KELE--ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL----EEKVKELKELKEKAEEYIK--LSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 858 ETKKqieeDEDREIQDIKTKYEKKLRDEKEsnlRLKgETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQgVIKSLEKD 937
Cdd:PRK03918 303 EEYL----DELREIEKRLSRLEEEINGIEE---RIK-ELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 938 IQGLKREIQerDETIQDKEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQEndpiLKWPQRV--- 1014
Cdd:PRK03918 374 LERLKKRLT--GLTPEKLEKELEELEKAKEEIEE-------EISKITARIGELKKEIKELKKAIEE----LKKAKGKcpv 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1015 ------EIHLYNFRKQVRKvllwgTLPQMEAELENFHKQNTQLELNITELwQKLRATDQEMRRERQKERDLEALVKRFKT 1088
Cdd:PRK03918 441 cgreltEEHRKELLEEYTA-----ELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1089 -DLHNCVAYIQEPRLLKEKVRGLFEkyvqradmvEIAGLNTDLQ--QEYTRQREHLERNLATLKKKVvkeGELHRtdyvR 1165
Cdd:PRK03918 515 yNLEELEKKAEEYEKLKEKLIKLKG---------EIKSLKKELEklEELKKKLAELEKKLDELEEEL---AELLK----E 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1166 IMQENVSLIKEINELRRELKFTRSQVYDLEAAlkltkkvrPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQ 1245
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDA--------EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
570
....*....|
gi 345199335 1246 RLRDQIQEQE 1255
Cdd:PRK03918 651 ELEKKYSEEE 660
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
692-1248 |
5.49e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 70.53 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 692 TDMEEK-AQVMLELK--TRVEELKMEN-EYQLRLKDMNYSEKIKElTDKFIQEMESLKTKNQVLRTekekqDVYHHEHIE 767
Cdd:pfam15921 320 SDLESTvSQLRSELReaKRMYEDKIEElEKQLVLANSELTEARTE-RDQFSQESGNLDDQLQKLLA-----DLHKREKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 768 DLLDKQSRELQDMECCNN-------QKLLLEYEKYQELQLKSQRMQEEYEKQLrdndETKSQALEELTEFYEaKLQEKTT 840
Cdd:pfam15921 394 SLEKEQNKRLWDRDTGNSitidhlrRELDDRNMEVQRLEALLKAMKSECQGQM----ERQMAAIQGKNESLE-KVSSLTA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 841 LLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKESN---LRLKGETGIMRKKFSSLQKEIEERTN-- 915
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSE-RTVSDLTASLQEKERAIEATNaeiTKLRSRVDLKLQELQHLKNEGDHLRNvq 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 916 -DIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETI-------QDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQI 987
Cdd:pfam15921 548 tECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAgamqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 988 EPRENE-----------IRVMKEQIQENDPILKWPQRVEIHLYNFRKQvrkvllwgtlpqMEAELENFHKQNTQLELNIT 1056
Cdd:pfam15921 628 SDLELEkvklvnagserLRAVKDIKQERDQLLNEVKTSRNELNSLSED------------YEVLKRNFRNKSEEMETTTN 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1057 ELWQKLRATDQEMRRERQKERDLEAlvkrfkTDLHNCVAYIQEPRLLKEKvRGLFEKYVQRADMVEIAGLNTDLQQEYTR 1136
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTLKSMEG------SDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNANKEKHFLK 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1137 QrehlERNlatlkkkvvkegelhrtdyvRIMQENVSLIKEINELRRELKFTRSQvydleaALKLTKKVRPQEVSETEPSR 1216
Cdd:pfam15921 769 E----EKN--------------------KLSQELSTVATEKNKMAGELEVLRSQ------ERRLKEKVANMEVALDKASL 818
|
570 580 590
....*....|....*....|....*....|..
gi 345199335 1217 DMLSTAPTARLNEQEETgRIIEMQRLEIQRLR 1248
Cdd:pfam15921 819 QFAECQDIIQRQEQESV-RLKLQHTLDVKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
843-1220 |
7.23e-12 |
|
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: 70.10 E-value: 7.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 843 EEAQEDVRQQLREFEETKKQIEEDEdrEIQDIKTKYEKKLRDEKESNLRlkgetgimrkkFSSLQKEIEE-----RTNDI 917
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLD--LIIDEKRQQLERLRREREKAER-----------YQALLKEKREyegyeLLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 918 ETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFV-LDYKIKELKKQIEPRENEIRV 996
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 997 MKEQIQENDpilkwpqrveihlynfrkqvrkvllwGTLPQMEAELENFHKQNTQLELNITElWQKLRATDQEMRRERQKE 1076
Cdd:TIGR02169 313 KERELEDAE--------------------------ERLAKLEAEIDKLLAEIEELEREIEE-ERKRRDKLTEEYAELKEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1077 RD-----LEALVKRFKTDLHNCVAYIQE---------------PRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQQEYTR 1136
Cdd:TIGR02169 366 LEdlraeLEEVDKEFAETRDELKDYREKleklkreinelkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1137 QREHL---ERNLATLKKKVVKEgelhRTDYVRIMQENVSLIKEINELRRELkftrsqvydleAALKLTKKVRPQEVSETE 1213
Cdd:TIGR02169 446 KALEIkkqEWKLEQLAADLSKY----EQELYDLKEEYDRVEKELSKLQREL-----------AEAEAQARASEERVRGGR 510
|
....*..
gi 345199335 1214 PSRDMLS 1220
Cdd:TIGR02169 511 AVEEVLK 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
726-1008 |
7.48e-12 |
|
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: 70.10 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 726 YSEKIKELTDkfiqEMESLKTKNQVLRTEKEKQDVYHHEhIEDLLDKQSRELQDMEccNNQKLLLEYEKYQELQLKSQRM 805
Cdd:TIGR02169 672 EPAELQRLRE----RLEGLKRELSSLQSELRRIENRLDE-LSQELSDASRKIGEIE--KEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 806 QEEYEKQLRDNDETKSQALEELTEFYEAKLQE--------KTTLLEEAQEDVRQQLREFEETKKQIE---EDEDREIQDi 874
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKleealndlEARLSHSRIPEIQAELSKLEEEVSRIEarlREIEQKLNR- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 875 KTKYEKKLRDEKESNLRLKGETGIMRKkfsSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQD 954
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIK---SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 345199335 955 KEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEqIQENDPIL 1008
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE-IPEEELSL 953
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
725-1004 |
3.60e-11 |
|
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: 68.16 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 725 NYSEKIKELTDKfIQEMESLKTKNQVLRTEKEKQdvyhHEHIEDLLDKQSRELQDMEccnnQKLLLEYEKYQELQLKSQR 804
Cdd:TIGR02168 674 ERRREIEELEEK-IEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 805 mqeeYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLLEEAqEDVRQQLREfeetkkQIEEDEDR--EIQDIKTKYEKKL 882
Cdd:TIGR02168 745 ----LEERIAQLSKELTELEAEIEE-LEERLEEAEEELAEA-EAEIEELEA------QIEQLKEElkALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 883 RDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKS-------LEKDIQGLKREIQERDETIQDK 955
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEleelieeLESELEALLNERASLEEALALL 892
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 345199335 956 EKRIYDLKKKNQELGKFKFVLDYKIKELKK---QIEPRENEIRVMKEQIQEN 1004
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREklaQLELRLEGLEVRIDNLQER 944
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
740-1255 |
6.11e-11 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 66.69 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 740 EMESLKTKNQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDM--ECCNNQKLLLEYEKYQELQ-LKSQRMQEEYE--KQLR 814
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLdrESDRNQELQKRIRLLEKREaEAEEALREQAElnRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 815 DNDETKSQALEE----LTEFYEAK------LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDR--EIQDIKTKYEKKL 882
Cdd:pfam05557 83 KYLEALNKKLNEkesqLADAREVIsclkneLSELRRQIQRAELELQSTNSELEELQERLDLLKAKasEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 883 RDEKESNLRLKgetgimrkkfsSLQKEIEERTNDIETLKGEQMKLqGVIKSLEKDIQGLKREIQERDETIQDK---EKRI 959
Cdd:pfam05557 163 SSLAEAEQRIK-----------ELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKELERLREHNKHLNENIENKlllKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 960 YDLKKK--NQELGKFKFV--------LDYKIKELKKQIEPRENEIRVMK------EQIQENDPILKwpQRVeihlYNFRK 1023
Cdd:pfam05557 231 EDLKRKleREEKYREEAAtlelekekLEQELQSWVKLAQDTGLNLRSPEdlsrriEQLQQREIVLK--EEN----SSLTS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1024 QVRKvlLWGTLPQMEAELENFHKqntqlelNITELWQKLRATDQEMRR-ERQ-----KERD-LEALVKRFKTDLHNCVAY 1096
Cdd:pfam05557 305 SARQ--LEKARRELEQELAQYLK-------KIEDLNKKLKRHKALVRRlQRRvllltKERDgYRAILESYDKELTMSNYS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1097 IQEPRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVvkegELHRTDYVRimQENVSLIKE 1176
Cdd:pfam05557 376 PQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQE----SLADPSYSK--EEVDSLRRK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1177 INELRRELKFTRSQVYDLEAALKltkKVRPQEVSETEPSRDM-LSTAPTARLNEQeeTGRIIEMQRLEIQRLRDQIQEQE 1255
Cdd:pfam05557 450 LETLELERQRLREQKNELEMELE---RRCLQGDYDPKKTKVLhLSMNPAAEAYQQ--RKNQLEKLQAEIERLKRLLKKLE 524
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
794-1198 |
6.61e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 67.12 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 794 KYQELQlKSQRMQEEYEKQLRDNDETKSQALEELTEFYEaKLQEKTTLLEEAQEdvrqqLREFEETKKQieededrEIQD 873
Cdd:pfam01576 10 KEEELQ-KVKERQQKAESELKELEKKHQQLCEEKNALQE-QLQAETELCAEAEE-----MRARLAARKQ-------ELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 874 IKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDI-------QGLKREIQ 946
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDIllledqnSKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 947 ERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELkkqieprenEIRVMKEQiqendpilKWPQRVEihlynfrKQVR 1026
Cdd:pfam01576 156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDL---------EERLKKEE--------KGRQELE-------KAKR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1027 KvllwgtlpqMEAELENFHKQNTQLELNITELWQKLRATDQEMR----RERQKERDLEALVKRFKtDLHNCVAYIQEPRL 1102
Cdd:pfam01576 212 K---------LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQaalaRLEEETAQKNNALKKIR-ELEAQISELQEDLE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1103 LKEKVRGLFEKyvQRADM-VEIAGLNTDL---------QQEYTRQRehlERNLATLKKKVVKEGELHRTDYVRIMQENVS 1172
Cdd:pfam01576 282 SERAARNKAEK--QRRDLgEELEALKTELedtldttaaQQELRSKR---EQEVTELKKALEEETRSHEAQLQEMRQKHTQ 356
|
410 420
....*....|....*....|....*.
gi 345199335 1173 LIKEINELRRELKFTRSQVYDLEAAL 1198
Cdd:pfam01576 357 ALEELTEQLEQAKRNKANLEKAKQAL 382
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
685-1087 |
7.16e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 685 EEVLVTKTDMEEKAQVMLELKTRVEELKmENEYQLRLKDMNYSEKIKELTDKfIQEMESLKTKNQVLRTEKE-------- 756
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEER-IKELEEKEERLEELKKKLKelekrlee 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 757 -KQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLleyEKYQELQLKSQRMQEEYEK------QLRDNDETKSQALEEL-- 827
Cdd:PRK03918 357 lEERHELYEEAKAKKEELERLKKRLTGLTPEKLE---KELEELEKAKEEIEEEISKitarigELKKEIKELKKAIEELkk 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 828 ------------TEFYEAKLQEKTTLleeaqedvrqQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKE--SNLRLK 893
Cdd:PRK03918 434 akgkcpvcgrelTEEHRKELLEEYTA----------ELKRIEKELKEIEEKE-RKLRKELRELEKVLKKESEliKLKELA 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 894 GETGIMRKKFSSLQKE-IEERTNDIETLKGEQMKLQGVIKSLEKDI---QGLKREIQERDETIQDKEKRIYDLKKKNQEL 969
Cdd:PRK03918 503 EQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELeklEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 970 GkFKFV--LDYKIKEL-------------KKQIEPRENEIRVMKEQIQEndpILKWPQRVEIHLYNFRKQV--------- 1025
Cdd:PRK03918 583 G-FESVeeLEERLKELepfyneylelkdaEKELEREEKELKKLEEELDK---AFEELAETEKRLEELRKELeelekkyse 658
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1026 --------RKVLLWGTLPQMEAELENFHKQNTQLELNItelwQKLRATDQEMRRERQKERDLEALVKRFK 1087
Cdd:PRK03918 659 eeyeelreEYLELSRELAGLRAELEELEKRREEIKKTL----EKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-1032 |
1.64e-10 |
|
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: 65.85 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 696 EKAQVMLELKTRVEELKMEnEYQLRLKDMNYS-EKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEhiedlLDKQS 774
Cdd:TIGR02168 210 EKAERYKELKAELRELELA-LLVLRLEELREElEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-----LEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 775 RELQdmeccnnQKLlleYEKYQELQLKSQRMQEEYEKqlRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLR 854
Cdd:TIGR02168 284 EELQ-------KEL---YALANEISRLEQQKQILRER--LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 855 EFEETKKQIEEDEdREIQDIKTKYEkKLRDEKEsnlRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSL 934
Cdd:TIGR02168 352 ELESLEAELEELE-AELEELESRLE-ELEEQLE---TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 935 EKDIQglKREIQERDETIQDKEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQENDPILKWPQRV 1014
Cdd:TIGR02168 427 LKKLE--EAELKELQAELEELEEELEELQEELERLEE-------ALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
330
....*....|....*...
gi 345199335 1015 EIHLYNFRKQVRKVLLWG 1032
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQ 515
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
677-1009 |
3.85e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.36 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 677 REREVGFAE-EVLVTKTDMEEKAQVMLELKTRVEELKMENeyqlrLKDMNYSEKIKELTDKFIQEmeslkTKNQVLRTEK 755
Cdd:pfam05483 448 REKEIHDLEiQLTAIKTSEEHYLKEVEDLKTELEKEKLKN-----IELTAHCDKLLLENKELTQE-----ASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 756 EKQDVYHHEHIEDLLDKQSRELQdmeccnnqkllleyEKYQELQLKSQRMQEEYeKQLRDNDETKSQALEELTEFYEAKL 835
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLE--------------EKEMNLRDELESVREEF-IQKGDEVKCKLDKSEENARSIEYEV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 836 QEKTTLLEEAQEDVRQQLREFEETKKQIEE--DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSL----QKE 909
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEElhQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIidnyQKE 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 910 IEERTNDIETLKGEQMKLQGVIKS---LEKDIQG------------LKREIQERDETIQDKEKRIYDLKKKNQELGKFKF 974
Cdd:pfam05483 663 IEDKKISEEKLLEEVEKAKAIADEavkLQKEIDKrcqhkiaemvalMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKA 742
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 345199335 975 VLDYKIKEL-------KKQIEPRENEIRVMKEQIQENDPILK 1009
Cdd:pfam05483 743 ALEIELSNIkaellslKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
788-1086 |
3.87e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 788 LLLEYEKYQElQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDE 867
Cdd:COG1196 230 LLLKLRELEA-ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 868 DReiqdiktkyekkLRDEKESNLRLKGETgimrkkfSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQE 947
Cdd:COG1196 309 ER------------RRELEERLEELEEEL-------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 948 RDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENDPILKWPQRVEIHLYNFRKQVRK 1027
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 345199335 1028 VLLwgtlpQMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRF 1086
Cdd:COG1196 450 EEA-----ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
728-1159 |
4.09e-10 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 64.21 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 728 EKIKELTDKFIQEMESLKTKN-QVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQ 806
Cdd:COG5185 159 GIIKDIFGKLTQELNQNLKKLeIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGF 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 807 EEYEKQLRDNDETK---SQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLR 883
Cdd:COG5185 239 QDPESELEDLAQTSdklEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 884 DEKESN-----LRLKGETGIMR------KKFSSLQKEIEERTNDIETLKGEQM--KLQGVIKSLEKDIQGLKREIQERDE 950
Cdd:COG5185 319 AAAEAEqeleeSKRETETGIQNltaeieQGQESLTENLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 951 TIQDKEKRIydlkkkNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENDPILKWPQRVEIHLYNFRKQVRKVLL 1030
Cdd:COG5185 399 NQRGYAQEI------LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEI 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1031 WGTLPQMEAELEnfhKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLhNCVAYIQEPRLLKEKVRGL 1110
Cdd:COG5185 473 NRSVRSKKEDLN---EELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDF-MRARGYAHILALENLIPAS 548
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 345199335 1111 FEKYVQRADMVEIAGlntdlqQEYTRQREHLERNLATLKKKVVKEGELH 1159
Cdd:COG5185 549 ELIQASNAKTDGQAA------NLRTAVIDELTQYLSTIESQQAREDPIP 591
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-971 |
1.60e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 675 IKREREVGFAEEVLVTKTDMEEKAQVMLELKtRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTE 754
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 755 KEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQAleeltefYEAK 834
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA-------EEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 835 LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlrlkgetgimRKKFSSLQKEIEERT 914
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE------------KKKIAHLKKEEEKKA 1770
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 345199335 915 NDIETLKgeqmklQGVIKslekdiQGLKREIQERDETIQDKEKRIYDLKKKNQELGK 971
Cdd:PTZ00121 1771 EEIRKEK------EAVIE------EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
754-1198 |
1.76e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 754 EKEKQDVyhHEHIEDLLDKQSRELQDMECCNNQKllleyEKYQELQLKSQRMQEEYEkQLRDNDETKSQALEELTEFYEA 833
Cdd:PRK02224 198 EKEEKDL--HERLNGLESELAELDEEIERYEEQR-----EQARETRDEADEVLEEHE-ERREELETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 834 KLQEKTTLLEEAQeDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKK--LRDEKESnlrLKGETGIMRKKFSSLQKEIE 911
Cdd:PRK02224 270 TEREREELAEEVR-DLRERLEELEEERDDLLAEAGLDDADAEAVEARReeLEDRDEE---LRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 912 ERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK-------NQELGKFKFVLDYKIKELK 984
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 985 KQIEPRENEIRVMKEQIQENDPIL---KWP---QRVE-----IHLYNFRKQVRKvllwgtlpqMEAELENFHKQNTQLEL 1053
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLeagKCPecgQPVEgsphvETIEEDRERVEE---------LEAELEDLEEEVEEVEE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1054 NITELwQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKV-------RGLFEKYVQRADMV--EIA 1124
Cdd:PRK02224 497 RLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELeaeaeekREAAAEAEEEAEEAreEVA 575
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 345199335 1125 GLNTDLqQEYTRQREHLERNLATLKKKVVKEGELHRtdyvriMQENVSLIKEINELRRE-LKFTRSQVYDLEAAL 1198
Cdd:PRK02224 576 ELNSKL-AELKERIESLERIRTLLAAIADAEDEIER------LREKREALAELNDERRErLAEKRERKRELEAEF 643
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
691-1257 |
2.14e-09 |
|
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: 62.30 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 691 KTDMEEKAQVMLELKTRVEELK--MENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDV------YH 762
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKklIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLlyldylKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 763 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKyQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLL 842
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEK-LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 843 EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKgetgimrkkfssLQKEIEERTNDIETLKG 922
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL------------QEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 923 EQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKfvldykiKELKKQIEPRENEIRVMKEQIQ 1002
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL-------EEEEESIELKQGKLTEEKEELE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1003 ENDPILKWPQRVEIHLYNFRKQVRKVLLWGTLPQMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEAL 1082
Cdd:pfam02463 455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1083 -VKRFKTDLHNCVA------------YIQEPRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLK 1149
Cdd:pfam02463 535 gVAVENYKVAISTAvivevsatadevEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLE 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1150 KKVVKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTAPTARLNE 1229
Cdd:pfam02463 615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694
|
570 580
....*....|....*....|....*...
gi 345199335 1230 QEETGRIIEMQRLEIQRLRDQIQEQEQV 1257
Cdd:pfam02463 695 LRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
842-1205 |
3.42e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 842 LEEAQEDVRQQLREFEETKKQIE------EDEDREIQDIKTKYEKKLR--DEKESNLR-LKGEtgimRKKFSSLQKEIEE 912
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEkfikrtENIEELIKEKEKELEEVLReiNEISSELPeLREE----LEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 913 RTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQErdetiqdKEKRIYDLKKKNQE-------------LGKFKFVLDYK 979
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEE-------LKKEIEELEEKVKElkelkekaeeyikLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 980 IKELKKQIEPRENEIRVMKEQIQENDPILKWPQRVEIHLYNFRKQV----RKVLLWGTLPQMEAELENFHKQNTQLEL-N 1054
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLeeleERHELYEEAKAKKEELERLKKRLTGLTPeK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1055 ITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEP--------RLLKEKVRG-LFEKYVQradmvEIAG 1125
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgRELTEEHRKeLLEEYTA-----ELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1126 LNTDLqQEYTRQREHLERNLATLKKKVVKEGELHRtdyvrimqeNVSLIKEINELRRELKftrsqVYDLEAALKLTKKVR 1205
Cdd:PRK03918 464 IEKEL-KEIEEKERKLRKELRELEKVLKKESELIK---------LKELAEQLKELEEKLK-----KYNLEELEKKAEEYE 528
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
900-1085 |
3.66e-09 |
|
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: 60.16 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfvldyK 979
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-------E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 980 IKELKKQIEPReneIRVMkeQIQENDPILKwpqrVEIHLYNFRKQVRKVLLWGTL-PQMEAELENFHKQNTQLELNITEL 1058
Cdd:COG4942 99 LEAQKEELAEL---LRAL--YRLGRQPPLA----LLLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAELAALRAEL 169
|
170 180
....*....|....*....|....*..
gi 345199335 1059 WQKLRATDQEMRRERQKERDLEALVKR 1085
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAE 196
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
796-1011 |
7.34e-09 |
|
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: 59.39 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 796 QELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIK 875
Cdd:COG4942 27 AELEQLQQEIAEL-EKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAELAELEKEIAELR-AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 876 TKYEKKLR--------------------DEKESNLR-LKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSL 934
Cdd:COG4942 104 EELAELLRalyrlgrqpplalllspedfLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 345199335 935 EKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENeiRVMKEQIQENDPILKWP 1011
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE--RTPAAGFAALKGKLPWP 258
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
791-1087 |
7.49e-09 |
|
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: 60.47 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 791 EYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEeltefYEAKLQEKTTLLEEAQEDvRQQLREFEETKKQIEEDEDRE 870
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDE-----LSQELSDASRKIGEIEKE-IEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 871 IQDIktkyEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIeertNDIETLKGEQMklqgvikslekdIQGLKREIQERDE 950
Cdd:TIGR02169 746 LSSL----EQEIENVKSELKELEARIEELEEDLHKLEEAL----NDLEARLSHSR------------IPEIQAELSKLEE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 951 TIQDKEKRIYDLkkkNQELGKfkfvLDYKIKELKKQIEPRENEIRVMKEQIQENdpilkwpqRVEIHLYNFRKQvrkvll 1030
Cdd:TIGR02169 806 EVSRIEARLREI---EQKLNR----LTLEKEYLEKEIQELQEQRIDLKEQIKSI--------EKEIENLNGKKE------ 864
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 345199335 1031 wgtlpQMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFK 1087
Cdd:TIGR02169 865 -----ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
684-1253 |
1.28e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 59.35 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 684 AEEVLVTKTDMEEKAQVMLELKTRVEELKMENEyQLRLKDMN----YSEKIKELTDKfIQEMEslktknqvlrtEKEKQD 759
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEKMILAFE-ELRVQAENarleMHFKLKEDHEK-IQHLE-----------EEYKKE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 760 VYHHEHIEDLLDKQSRELQDMecCNNQKLLLEYEKYQELQLKSQ-RMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEK 838
Cdd:pfam05483 235 INDKEKQVSLLLIQITEKENK--MKDLTFLLEESRDKANQLEEKtKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 839 TTLLEEAQEDVRQQLREFEETKKQIEEDED---------REIQDIKTKYEKKLRDEKE----SNLRLKGETGIMRKKFSS 905
Cdd:pfam05483 313 KALEEDLQIATKTICQLTEEKEAQMEELNKakaahsfvvTEFEATTCSLEELLRTEQQrlekNEDQLKIITMELQKKSSE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 906 LQKEIEERTN------DIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK-----KKNQELGKFKF 974
Cdd:pfam05483 393 LEEMTKFKNNkeveleELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqltaIKTSEEHYLKE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 975 VLDYKI---KELKKQIEPRENEIRVM---KEQIQENDPILKWPQRVEIHLYNFRKQVRKVL-----LWGTLPQMEAELE- 1042
Cdd:pfam05483 473 VEDLKTeleKEKLKNIELTAHCDKLLlenKELTQEASDMTLELKKHQEDIINCKKQEERMLkqienLEEKEMNLRDELEs 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1043 ---NFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRAD 1119
Cdd:pfam05483 553 vreEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLN 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1120 MVEIAGLNTDLQQEYTRQRehLERNLATLK-----KKVVKEGELHRTDYVR-IMQENVSLIKEIN--------ELRRELK 1185
Cdd:pfam05483 633 AYEIKVNKLELELASAKQK--FEEIIDNYQkeiedKKISEEKLLEEVEKAKaIADEAVKLQKEIDkrcqhkiaEMVALME 710
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 345199335 1186 FTRSQ----VYDLEAALKLTKKvRPQEVSETEPSrdmLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQE 1253
Cdd:pfam05483 711 KHKHQydkiIEERDSELGLYKN-KEQEQSSAKAA---LEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
794-1266 |
1.86e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 58.98 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 794 KYQELQLKSQRMQEEYE-KQLRDNDETKSQALEELTEFYEAKLQEKTTlleeaqedvRQQLREFEETKKQIEEDEDREIQ 872
Cdd:pfam05557 8 KARLSQLQNEKKQMELEhKRARIELEKKASALKRQLDRESDRNQELQK---------RIRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 873 DIKTKYEK---KLRDEKESNLRLKGETgimrkkFSSLQKEIEErtndietLKGEQMKLQGVIKSLEKDIQGLKREIQERD 949
Cdd:pfam05557 79 RLKKKYLEalnKKLNEKESQLADAREV------ISCLKNELSE-------LRRQIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 950 ETIQDKEKRIYDLKKKNQELGkfkfVLDYKIKELKKQIEPRENEIRVMKEQIQEndpilkwpqrveihlynfrkqvrkvl 1029
Cdd:pfam05557 146 AKASEAEQLRQNLEKQQSSLA----EAEQRIKELEFEIQSQEQDSEIVKNSKSE-------------------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1030 lWGTLPQMEAELENFHKQNTQL-ELNITELWQKLRATDQEMRRERQKER-----DLEALVKRFKTDLHNCVAYIQEPRL- 1102
Cdd:pfam05557 196 -LARIPELEKELERLREHNKHLnENIENKLLLKEEVEDLKRKLEREEKYreeaaTLELEKEKLEQELQSWVKLAQDTGLn 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1103 --LKEKVRGLFEKYVQR--ADMVEIAGLNTDLQQEYTRQREhLERNLATLKKKVVKEG-ELHRTD-YVRIMQENVSLI-K 1175
Cdd:pfam05557 275 lrSPEDLSRRIEQLQQReiVLKEENSSLTSSARQLEKARRE-LEQELAQYLKKIEDLNkKLKRHKaLVRRLQRRVLLLtK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1176 EINELRRELKFTRSQVYDLEAALKLTKKVRP-----QEV---------------SETEPSRDMLSTA------------- 1222
Cdd:pfam05557 354 ERDGYRAILESYDKELTMSNYSPQLLERIEEaedmtQKMqahneemeaqlsvaeEELGGYKQQAQTLerelqalrqqesl 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 345199335 1223 --PTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQVTGFHTLAGV 1266
Cdd:pfam05557 434 adPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGD 479
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
699-1255 |
1.92e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 699 QVMLELKTRVEELKMENE--YQLRLKDMNYSEKIKELTDKFIQEMESLK-----------TKNQVLRT------------ 753
Cdd:pfam15921 110 QSVIDLQTKLQEMQMERDamADIRRRESQSQEDLRNQLQNTVHELEAAKclkedmledsnTQIEQLRKmmlshegvlqei 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 754 --------EKEKQDVYHHEHIEDL--------LDKQSRELQ--------------------DMECCNNQKLLLEYEKYQE 797
Cdd:pfam15921 190 rsilvdfeEASGKKIYEHDSMSTMhfrslgsaISKILRELDteisylkgrifpvedqlealKSESQNKIELLLQQHQDRI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 798 LQLKSQR---------------------------MQEE-------YEKQLRDNDETKSQALEELTE---FYEAKLQ--EK 838
Cdd:pfam15921 270 EQLISEHeveitgltekassarsqansiqsqleiIQEQarnqnsmYMRQLSDLESTVSQLRSELREakrMYEDKIEelEK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 839 TTLLEEAQ-EDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDI 917
Cdd:pfam15921 350 QLVLANSElTEARTERDQFSQESGNLDDQLQKLLADLH-KREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 918 E-------TLKGE---QMK-----LQGVIKSLEK-------------DIQGLKREIQERDETIQDKEKRIYDL------- 962
Cdd:pfam15921 429 QrleallkAMKSEcqgQMErqmaaIQGKNESLEKvssltaqlestkeMLRKVVEELTAKKMTLESSERTVSDLtaslqek 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 963 ----KKKNQELGKFKFVLDYKIKELK------KQIEPRENEIRVMKEQIQENDPILK-WPQRVEihlyNFRK-------- 1023
Cdd:pfam15921 509 eraiEATNAEITKLRSRVDLKLQELQhlknegDHLRNVQTECEALKLQMAEKDKVIEiLRQQIE----NMTQlvgqhgrt 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1024 ----QVRKVLLWGTLPQMEAELENFHKQNTQLELNITELwqKLRATDQEMRR--------ER-------QKERD-LEALV 1083
Cdd:pfam15921 585 agamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL--EARVSDLELEKvklvnagsERlravkdiKQERDqLLNEV 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1084 KRFKTDLHNCVayiQEPRLLKEKVRGLFEkyvqradmvEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGElhrtdy 1163
Cdd:pfam15921 663 KTSRNELNSLS---EDYEVLKRNFRNKSE---------EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH------ 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1164 vrIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTAPTarlnEQEETGRIIEMQRLE 1243
Cdd:pfam15921 725 --AMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVAT----EKNKMAGELEVLRSQ 798
|
730
....*....|..
gi 345199335 1244 IQRLRDQIQEQE 1255
Cdd:pfam15921 799 ERRLKEKVANME 810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
807-1152 |
1.94e-08 |
|
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: 58.91 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 807 EEYEKQLRDNDETKSQ---ALEELTEFYEaKLQEKTTLLEEAQEdVRQQLREFEET----KKQIEEDEDREIQDIKTKYE 879
Cdd:TIGR02168 175 KETERKLERTRENLDRledILNELERQLK-SLERQAEKAERYKE-LKAELRELELAllvlRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 880 KKlRDEKESNLRLKGEtgimrkKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI 959
Cdd:TIGR02168 253 EE-LEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 960 YDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENDPILKWPQRveiHLYNFRKQVRKVLLwgTLPQMEA 1039
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE---QLETLRSKVAQLEL--QIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1040 ELENFHKQNTQLELNITELWQklRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQrad 1119
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQ--EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ--- 475
|
330 340 350
....*....|....*....|....*....|....*
gi 345199335 1120 mvEIAGLNTDLQQEYTRQR--EHLERNLATLKKKV 1152
Cdd:TIGR02168 476 --ALDAAERELAQLQARLDslERLQENLEGFSEGV 508
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
803-1202 |
2.27e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 803 QRMQEEYEKQLRDNDE--TKSQALEELTEFYeaklqekttlLEEAQEDVRQQLREFeetkkQIEEDEDREIQDIKTKYEK 880
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRrlNESNELHEKQKFY----------LRQSVIDLQTKLQEM-----QMERDAMADIRRRESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 881 KLRDEKESNLRlkgETGIMRkkfsSLQKEIEERTN-DIETLKGEQMKLQGV---IKSLEKDI-QGLKREIQERDETiqdk 955
Cdd:pfam15921 142 DLRNQLQNTVH---ELEAAK----CLKEDMLEDSNtQIEQLRKMMLSHEGVlqeIRSILVDFeEASGKKIYEHDSM---- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 956 ekRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQendpilkwpQRVEIHLYNFRKQVRKVLlwgtlP 1035
Cdd:pfam15921 211 --STMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQ---------NKIELLLQQHQDRIEQLI-----S 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1036 QMEAELENFHKQNTQLELNITELWQKLRATDQEMRRER----QKERDLEALVKRFKTDLHncvayiQEPRLLKEKVRGLF 1111
Cdd:pfam15921 275 EHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmymRQLSDLESTVSQLRSELR------EAKRMYEDKIEELE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1112 EKYV-QRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVvKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQ 1190
Cdd:pfam15921 349 KQLVlANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE-KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNME 427
|
410
....*....|..
gi 345199335 1191 VYDLEAALKLTK 1202
Cdd:pfam15921 428 VQRLEALLKAMK 439
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
675-1218 |
3.17e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.52 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 675 IKREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQ------EMESLKTKN 748
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKElqqlegSSDRILELD 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 749 QVLRTE---------------KEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEyekyQELQLKSQRMQEEyeKQL 813
Cdd:TIGR00606 478 QELRKAerelskaeknsltetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT----QMEMLTKDKMDKD--EQI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 814 RDNDETKSQALEELTEFYEAKLQEKTTL---------LEEAQEDVRQQLREFEETKKQIEEDEDREIQDIkTKYEKKLRD 884
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYFPNKKQLEDWLhskskeinqTRDRLAKLNKELASLEQNKNHINNELESKEEQL-SSYEDKLFD 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 885 -----EKESNL-RLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQmklQGVIKSLEKDIQgLKREIQERDETIQDKEKR 958
Cdd:TIGR00606 631 vcgsqDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEN---QSCCPVCQRVFQ-TEAELQEFISDLQSKLRL 706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 959 IYDlkkknqelgkfkfvldyKIKELKKQIEPRENEIRVMKEQIQENDPILkwpQRVEIHLYNFRKQVRKVLlwgtlPQME 1038
Cdd:TIGR00606 707 APD-----------------KLKSTESELKKKEKRRDEMLGLAPGRQSII---DLKEKEIPELRNKLQKVN-----RDIQ 761
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1039 AELENFHKQNTQLE-LNITELWQKLRATD----QEMRRE-RQKERDLEALVKrfKTDLHNCVAYIQEPRLLKEKVRGLFE 1112
Cdd:TIGR00606 762 RLKNDIEEQETLLGtIMPEEESAKVCLTDvtimERFQMElKDVERKIAQQAA--KLQGSDLDRTVQQVNQEKQEKQHELD 839
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1113 KYVQRADmveiagLNTDLQQEYTRQREHLERNLATLKKKVVKEGE-LHRTDyvRIMQENVSLIKEINELRRELKFTRSQV 1191
Cdd:TIGR00606 840 TVVSKIE------LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTnLQRRQ--QFEEQLVELSTEVQSLIREIKDAKEQD 911
|
570 580
....*....|....*....|....*..
gi 345199335 1192 YDLEAALKLTKKVRPQEVSETEPSRDM 1218
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSNKK 938
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
685-1001 |
3.21e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.21 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 685 EEVLVTKTDMEEKAQVMLELKTRVEElkmeneyQLRLKDMNYSE--KIKELTDKFIQEMESLKTKNQVLR---TEKE--K 757
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASLQE-------KERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRnvqTECEalK 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 758 QDVYHHEHIEDLLDKQSRELQDMECCNNQKL-LLEYEKYQ-ELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAkl 835
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTAgAMQVEKAQlEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL-- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 836 qEKTTLLEEAQEDVRQqLREFEETKKQI--EEDEDR-EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 912
Cdd:pfam15921 633 -EKVKLVNAGSERLRA-VKDIKQERDQLlnEVKTSRnELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 913 RTNDIETLKGEQ-------MKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKK 985
Cdd:pfam15921 711 TRNTLKSMEGSDghamkvaMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
330
....*....|....*.
gi 345199335 986 QIEPRENEIRVMKEQI 1001
Cdd:pfam15921 791 ELEVLRSQERRLKEKV 806
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
736-1256 |
3.23e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 736 KFIQEM--ESLKTKNQVLRTEKEKQDVYHHEHIEDLlDKQSRELQDmeccnnqklllEYEKYQELQLKSQRMQEEYE--K 811
Cdd:COG4717 41 AFIRAMllERLEKEADELFKPQGRKPELNLKELKEL-EEELKEAEE-----------KEEEYAELQEELEELEEELEelE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 812 QLRDNDETKSQALEELTEFYEA-----KLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDrEIQDIKTKYEKKLRDEK 886
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLyqeleALEAELAELPERLEELEERLEELRELEEELEELEA-ELAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 887 ESnlrlkgetgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQerdetIQDKEKRIYDLKKKN 966
Cdd:COG4717 188 LA----------TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE-----AAALEERLKEARLLL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 967 QELGKFkFVLDYKIKELKKQIEPREN------EIRVMKEQIQENDPILKWPQRVEIHLYNFRKQVRKVLLwgtlpqmEAE 1040
Cdd:COG4717 253 LIAAAL-LALLGLGGSLLSLILTIAGvlflvlGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEL-------EEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1041 LENFHKQNTQLELNITELWQKLRATDQEMR--RERQKERDLEALVKRFKTDLHNCVAyiqeprllkekvrGLFEKYVQRA 1118
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLReaEELEEELQLEELEQEIAALLAEAGV-------------EDEEELRAAL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1119 DMVEIaglntdlQQEYTRQREHLERNLATLKKKVvkEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAAL 1198
Cdd:COG4717 392 EQAEE-------YQELKEELEELEEQLEELLGEL--EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 345199335 1199 kltkkvrpqevsetepsrdmlstaptarlnEQEETGRIIEMQRLEIQRLRDQIQEQEQ 1256
Cdd:COG4717 463 ------------------------------EQLEEDGELAELLQELEELKAELRELAE 490
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
863-1255 |
7.39e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 863 IEEDEDRE--------IQDIKTKYEKKLRDEKESNLRLKG-ETGIMRKkfSSLQKEIEERTNDIETLKGEQMKLQGVIKS 933
Cdd:PRK03918 141 LESDESREkvvrqilgLDDYENAYKNLGEVIKEIKRRIERlEKFIKRT--ENIEELIKEKEKELEEVLREINEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 934 LEKDIQGLKREIQERDETiqdKEKrIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENdPILKWPQR 1013
Cdd:PRK03918 219 LREELEKLEKEVKELEEL---KEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1014 VEIHLYNFRKQVRKVLlwgtlPQMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTdlhnc 1093
Cdd:PRK03918 294 EYIKLSEFYEEYLDEL-----REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL----- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1094 vayIQEPRLLKEKVRGLFEKyvqradmveIAGLNTdlqqeytrqrEHLERNLATLKKKvvKEgelhrtdyvrimqenvSL 1173
Cdd:PRK03918 364 ---YEEAKAKKEELERLKKR---------LTGLTP----------EKLEKELEELEKA--KE----------------EI 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1174 IKEINELRRELKFTRSQVYDLEAALKLTKKVRpqevsetepsrdmlSTAPT-ARLNEQEETGRIIEMQRLEIQRLRDQIQ 1252
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAK--------------GKCPVcGRELTEEHRKELLEEYTAELKRIEKELK 469
|
...
gi 345199335 1253 EQE 1255
Cdd:PRK03918 470 EIE 472
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
793-1146 |
7.56e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 793 EKYQELQLKsqrmQEEYEKQLRdndetkSQALEELtefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEdedreiq 872
Cdd:COG1196 213 ERYRELKEE----LKELEAELL------LLKLREL----EAELEELEAELEELEAELEELEAELAELEAELEE------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 873 diktkyekklrdekesnlrlkgetgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETI 952
Cdd:COG1196 272 --------------------------LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 953 QDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENdpilkwpqrvEIHLYNFRKQVRkvllwg 1032
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA----------EEELEELAEELL------ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1033 tlpQMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFE 1112
Cdd:COG1196 390 ---EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
330 340 350
....*....|....*....|....*....|....
gi 345199335 1113 KYVQRADMVEIAGLNTDLQQEYTRQREHLERNLA 1146
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
816-990 |
1.11e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 816 NDETKSQALEELTEfYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDrEIQDIKTKYEKKLRDEKESNLRLKGE 895
Cdd:COG1579 1 AMPEDLRALLDLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 896 TGIMR-----KKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYD-LKKKNQEL 969
Cdd:COG1579 79 EEQLGnvrnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEeLAELEAEL 158
|
170 180
....*....|....*....|.
gi 345199335 970 GKfkfvLDYKIKELKKQIEPR 990
Cdd:COG1579 159 EE----LEAEREELAAKIPPE 175
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
482-669 |
1.28e-07 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 55.69 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 482 GGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSYNCVT 561
Cdd:COG2319 6 GAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 562 VSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQAHAG 639
Cdd:COG2319 86 FSPDGRLLASASADGTVRlwDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRL--WDLATGKLLRTLTGHSG 163
|
170 180 190
....*....|....*....|....*....|..
gi 345199335 640 PITkmLLTF--DDQFLLTAAEDGclfTWKVFD 669
Cdd:COG2319 164 AVT--SVAFspDGKLLASGSDDG---TVRLWD 190
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
803-1256 |
1.57e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 803 QRMQEEYEKQLRDNDETKSQALEELTEFYEAklqekttlLEEAQEdvrqQLREFEETKKQIEEDEdREIQDIKTKYEkKL 882
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEE--------LKEAEE----KEEEYAELQEELEELE-EELEELEAELE-EL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 883 RDEKESnLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGV---IKSLEKDIQGLKREIQE-RDETIQDKEKR 958
Cdd:COG4717 115 REELEK-LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELeeeLEELEAELAELQEELEElLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 959 IYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENDPI--LKWPQRV-------------EIHLYNFRK 1023
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerLKEARLLlliaaallallglGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1024 QVRKVL-------------LWGTLPQMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDL 1090
Cdd:COG4717 274 TIAGVLflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1091 HNCVAYIQEPRL--LKEKVRGLFEKY-VQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVvkEGELHRTDYVRIM 1167
Cdd:COG4717 354 REAEELEEELQLeeLEQEIAALLAEAgVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL--EELLEALDEEELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1168 QENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRpqEVSETEPSRDMLStaptARLNEQEETGRIIEMQRLEIQRL 1247
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEEDG--ELAELLQELEELK----AELRELAEEWAALKLALELLEEA 505
|
....*....
gi 345199335 1248 RDQIQEQEQ 1256
Cdd:COG4717 506 REEYREERL 514
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
666-1185 |
1.89e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.82 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 666 KVFDKDGRGIKREREVGFAEEVLVTKTDM-------EEKAQVMLELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFI 738
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEKNSLTETLKkevkslqNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 739 QEMESLKTKNQVlrteKEKQDVYHHEHIEDLLDKQSRELQDMEccnnqkllleyEKYQELQL---KSQRMQEEYEKQLRD 815
Cdd:TIGR00606 552 RKIKSRHSDELT----SLLGYFPNKKQLEDWLHSKSKEINQTR-----------DRLAKLNKelaSLEQNKNHINNELES 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 816 NDETKSQALEEL-----TEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDR----------------EIQDI 874
Cdd:TIGR00606 617 KEEQLSSYEDKLfdvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcqrvfqteaELQEF 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 875 KTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERD---ET 951
Cdd:TIGR00606 697 ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQEtllGT 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 952 IQDKEKRIYDL------------------KKKNQELGKFKFV-LDYKIKELKKQIEPRENEIRVMKEQIQENDPILKWPQ 1012
Cdd:TIGR00606 777 IMPEEESAKVCltdvtimerfqmelkdveRKIAQQAAKLQGSdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQ 856
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1013 RVEIHLYNFRKQVR--KVLLWGTLPQMEAELENFHKQNTQLELNITELWQKlraTDQEMRRERQKERDL---EALVKRFK 1087
Cdd:TIGR00606 857 EQIQHLKSKTNELKseKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA---KEQDSPLETFLEKDQqekEELISSKE 933
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1088 TDLHNCVAYIQEprlLKEKVRGL------FEKYVQ-------RADMVEIAGLNTDLqQEYTRQREHLERNLATLKKKVVK 1154
Cdd:TIGR00606 934 TSNKKAQDKVND---IKEKVKNIhgymkdIENKIQdgkddylKQKETELNTVNAQL-EECEKHQEKINEDMRLMRQDIDT 1009
|
570 580 590
....*....|....*....|....*....|....
gi 345199335 1155 EGELHrtdyvRIMQENVSLIK---EINELRRELK 1185
Cdd:TIGR00606 1010 QKIQE-----RWLQDNLTLRKrenELKEVEEELK 1038
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
676-1257 |
2.76e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 676 KREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQlrlkdmnySEKIKELTDKfiQEMESLKTKNQVLRTEK 755
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK--------ADELKKAEEK--KKADEAKKAEEKKKADE 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 756 EKQDVYHHEHIEDLLDKQSRELQDMEccnnqklllEYEKYQELQLKSQRMQEEYEKQLRDndetKSQALEELTEFYEAKL 835
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKAD---------AAKKKAEEAKKAAEAAKAEAEAAAD----EAEAAEEKAEAAEKKK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 836 QEKTTLLEEAQEDVrQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTN 915
Cdd:PTZ00121 1374 EEAKKKADAAKKKA-EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 916 DIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKE---KRIYDLKKKNQELGKF----KFVLDYKIKELKKQIE 988
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEeakKKADEAKKAAEAKKKAdeakKAEEAKKADEAKKAEE 1532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 989 PRENEIRVMKEQIQENDPILKWPQRVEIHLYNFRKQVRKVLLWGTLPQMEAE-LENFHKQNTQLELNITELWQKLRAtdQ 1067
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEeAKKAEEARIEEVMKLYEEEKKMKA--E 1610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1068 EMRRERQKERDLEALVKRfktdlhncvayiQEPRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLAT 1147
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKA------------EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1148 LKKKvVKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLtkKVRPQEVSETEPSRdmlsTAPTARL 1227
Cdd:PTZ00121 1679 EAKK-AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI--KAEEAKKEAEEDKK----KAEEAKK 1751
|
570 580 590
....*....|....*....|....*....|
gi 345199335 1228 NEqEETGRIIEMQRLEIQRLRDQIQEQEQV 1257
Cdd:PTZ00121 1752 DE-EEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
692-1281 |
5.05e-07 |
|
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: 54.67 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 692 TDMEEKAQVMLELKTRVE-------ELKMENEYQ----LRLKDMNYSEKIKELT-------DKFIQEMESLKTKNQVLRT 753
Cdd:TIGR01612 613 SDKNEYIKKAIDLKKIIEnnnayidELAKISPYQvpehLKNKDKIYSTIKSELSkiyeddiDALYNELSSIVKENAIDNT 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 754 EkekqDVYHHEHIEDLLDKQSRELQDMECC-----------NNQKLL---LEYEKY--QELQLKSQRMQEEY---EKQLR 814
Cdd:TIGR01612 693 E----DKAKLDDLKSKIDKEYDKIQNMETAtvelhlsnienKKNELLdiiVEIKKHihGEINKDLNKILEDFknkEKELS 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 815 DNDETKSQALEELTEfYEAKLQE-------KTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKyeKKLRDE-- 885
Cdd:TIGR01612 769 NKINDYAKEKDELNK-YKSKISEiknhyndQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEM--KFMKDDfl 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 886 KESNLRLKGETGiMRKKFSSLQKEIEERTNDIET-LKGEQMKLqgviksLEKDIQGLKREIQERDETIQDKEKRIYDLKK 964
Cdd:TIGR01612 846 NKVDKFINFENN-CKEKIDSEHEQFAELTNKIKAeISDDKLND------YEKKFNDSKSLINEINKSIEEEYQNINTLKK 918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 965 KNQELgkfkfvldyKI-KELKKQIEPRENEIRVMKEQIQENDPILK--------WPQRVEIHLYNFRKQVRKVLLWGTLP 1035
Cdd:TIGR01612 919 VDEYI---------KIcENTKESIEKFHNKQNILKEILNKNIDTIKesnlieksYKDKFDNTLIDKINELDKAFKDASLN 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1036 QMEAELENFHKQNTQLELNI-----TELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPrllkekvrgl 1110
Cdd:TIGR01612 990 DYEAKNNELIKYFNDLKANLgknkeNMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDE---------- 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1111 FEKYVQRadmvEIAGLNTDLQQEYTRQREHLERNLATLK----KKVVKEGELHRTDYVRIMQENVSL--------IKEIN 1178
Cdd:TIGR01612 1060 IEKEIGK----NIELLNKEILEEAEINITNFNEIKEKLKhynfDDFGKEENIKYADEINKIKDDIKNldqkidhhIKALE 1135
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1179 ELRRE----LKFTRSQVYDLEAALKltKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEmqrlEIQRLRDQIQEQ 1254
Cdd:TIGR01612 1136 EIKKKsenyIDEIKAQINDLEDVAD--KAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLN----EIAEIEKDKTSL 1209
|
650 660
....*....|....*....|....*..
gi 345199335 1255 EQVTGFHTLAGVRLPSLSNSEVDLEVK 1281
Cdd:TIGR01612 1210 EEVKGINLSYGKNLGKLFLEKIDEEKK 1236
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
826-1132 |
6.11e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.37 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 826 ELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKY---EKKLRDEKESNLRLKGETGIMRKK 902
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLE-EELEQARSELeqlEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 903 FSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLD--YKI 980
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSeaEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 981 KELKKQIEPRENEIRVMKEQIQENDPILKWPQRVEIHLYNFRKQVRKVLLWgtlpqmeAELENFHKQNTQLELNITELWQ 1060
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL-------ALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 345199335 1061 KLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQQ 1132
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
676-1253 |
7.61e-07 |
|
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: 53.92 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 676 KREREVGFAEEVL--VTKTDMEEKAQVMLELKTRVEELKME--------NEYQLRLKDM-NYSEKIKELTDKFIQEMESL 744
Cdd:TIGR02169 262 ELEKRLEEIEQLLeeLNKKIKDLGEEEQLRVKEKIGELEAEiaslersiAEKERELEDAeERLAKLEAEIDKLLAEIEEL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 745 KTKNQVLRTEKEK-QDVYhhEHIEDLLDKQSRELQDMECcNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQA 823
Cdd:TIGR02169 342 EREIEEERKRRDKlTEEY--AELKEELEDLRAELEEVDK-EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 824 LEELTEFYE--AKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDedreiqdiKTKYEKKLRDEKEsnlrlkgETGIMRK 901
Cdd:TIGR02169 419 SEELADLNAaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD--------LSKYEQELYDLKE-------EYDRVEK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 902 KFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQG---LKREIQERDETIQ--------------------DKEKR 958
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgTVAQLGSVGERYAtaievaagnrlnnvvveddaVAKEA 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 959 IYDLKKKNqeLGKFKF--------------------VLDYKIK--ELKKQIEP--------------------------- 989
Cdd:TIGR02169 564 IELLKRRK--AGRATFlplnkmrderrdlsilsedgVIGFAVDlvEFDPKYEPafkyvfgdtlvvedieaarrlmgkyrm 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 990 ------------------------------RENEIRVMKEQIQENDPILKWPQRVEIHLYNFRKQVRKVL--LWGTLPQM 1037
Cdd:TIGR02169 642 vtlegelfeksgamtggsraprggilfsrsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELsdASRKIGEI 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1038 EAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEP--RLLKEKVRGLFEKY- 1114
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELs 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1115 VQRADMVEIAGLNTDLQQEYtrQREHLERNLATLKKKVVKEGELHRTD-YVRIMQENVSLIKEINELRRELKFTRSQVYD 1193
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKL--NRLTLEKEYLEKEIQELQEQRIDLKEqIKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 345199335 1194 LEAALKLTKKVRPQ---EVSETEPSRDMLSTA---PTARLNEQEETGRIIEMQRLEIQRLRDQIQE 1253
Cdd:TIGR02169 880 LESRLGDLKKERDEleaQLRELERKIEELEAQiekKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
832-1114 |
8.16e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 832 EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEK--KLRDEKESNLRLKGEtgiMRKKFSSLQKE 909
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEaqELREKRDELNEKVKE---LKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 910 IEERTNDIETLKGEQMKLQGV---IKSLEKDIQGLKREIQ--------ERD--ETIQDKEKRIYDLKKKNQELGKFKFVL 976
Cdd:COG1340 87 LNELREELDELRKELAELNKAggsIDKLRKEIERLEWRQQtevlspeeEKElvEKIKELEKELEKAKKALEKNEKLKELR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 977 DyKIKELKKQIEPRENEIRVMKEQIQENDPILkwpqrveIHLYNFRKQVRKvllwgtlpqmeaELENFHKQNTQLELNIT 1056
Cdd:COG1340 167 A-ELKELRKEAEEIHKKIKELAEEAQELHEEM-------IELYKEADELRK------------EADELHKEIVEAQEKAD 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 345199335 1057 ELWQKLRATDQEMRRERQKERDLEALVKRFKTDlhncvayiQEPRLLKEKVRGLFEKY 1114
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLRKKQRALKRE--------KEKEELEEKAEEIFEKL 276
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
800-1009 |
8.46e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 800 LKSQRmqEEYEKQLRDNDETKSQALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED--REIQDIKTK 877
Cdd:COG1340 41 LAEKR--DELNAQVKELREEAQELREKRDELNE-KVKELKEERDELNEKLNELREELDELRKELAELNKagGSIDKLRKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 878 YEKKLRDEKESNLRLKGETGIMrKKFSSLQKEIEER------TNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDET 951
Cdd:COG1340 118 IERLEWRQQTEVLSPEEEKELV-EKIKELEKELEKAkkalekNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 345199335 952 IQDKEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQENDPILK 1009
Cdd:COG1340 197 MIELYKEADELRKEADELHK-------EIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
909-1257 |
1.43e-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: 52.76 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 909 EIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREiqerdetiQDKEKRIYDLKKKNQE-----LGKFKFVLDYKIKEL 983
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE--------REKAERYQALLKEKREyegyeLLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 984 KKQIEPRENEIRVMKEQIQENDpilKWPQRVEIHLYNFRKQVRKvLLWGTLPQMEAELENFHKQNTQLELNITELwqklr 1063
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELE---KRLEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGELEAEIASLERSIAEK----- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1064 atDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRglfEKYVQRADmvEIAGLNTDLQQEYTRQREhLER 1143
Cdd:TIGR02169 314 --ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT---EEYAELKE--ELEDLRAELEEVDKEFAE-TRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1144 NLATLKKKVVK---EGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALK-LTKKVRPQEvSETEPSRDML 1219
Cdd:TIGR02169 386 ELKDYREKLEKlkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEdKALEIKKQE-WKLEQLAADL 464
|
330 340 350
....*....|....*....|....*....|....*...
gi 345199335 1220 STApTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQV 1257
Cdd:TIGR02169 465 SKY-EQELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
939-1256 |
1.47e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 939 QGLKREIQERDETIQDKEKRIY---DLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENDPILKWPQRVE 1015
Cdd:PRK03918 134 QGEIDAILESDESREKVVRQILgldDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1016 IHLYNFRKQVRKV-LLWGTLPQMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTdlhncv 1094
Cdd:PRK03918 214 SELPELREELEKLeKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE------ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1095 ayIQEPRLLKEKVRGLFEKYVQRADMVEiaglntDLQQEYTRQREHLERNLATLKKKVvkegelhrtdyvrimqenvsli 1174
Cdd:PRK03918 288 --LKEKAEEYIKLSEFYEEYLDELREIE------KRLSRLEEEINGIEERIKELEEKE---------------------- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1175 KEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQ 1254
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
..
gi 345199335 1255 EQ 1256
Cdd:PRK03918 418 KK 419
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
501-540 |
1.63e-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: 45.77 E-value: 1.63e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 345199335 501 SLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 540
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
703-1259 |
2.14e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.36 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 703 ELKTRVEELKmeneyQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLR------TEKEKQDVYHHEHIE--DLLDKQS 774
Cdd:TIGR00606 249 PLKNRLKEIE-----HNLSKIMKLDNEIKAL-KSRKKQMEKDNSELELKMekvfqgTDEQLNDLYHNHQRTvrEKERELV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 775 RELQDMECCNNQKLLLEYEKYQ------ELQLKSQRMQEEYEKqlRDNDETKSQALEELTEFyeaklqekttlleEAQED 848
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTEllveqgRLQLQADRHQEHIRA--RDSLIQSLATRLELDGF-------------ERGPF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 849 VRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKES----NLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQ 924
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQadeiRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 925 MKLQGVIKsLEKDIQGLKREIQ--ERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQ 1002
Cdd:TIGR00606 468 GSSDRILE-LDQELRKAERELSkaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1003 ENDPILKwpqrveihlYNFRKQVRKVLLWGTLP---QMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDL 1079
Cdd:TIGR00606 547 KDEQIRK---------IKSRHSDELTSLLGYFPnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESK 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1080 EALVKRFKTDLHN-CVAYIQEPRLlkEKVRGLFEKyvQRADMVEIAGlNTDLQQEYTRQREHLERNLATLKKKVVKEGel 1158
Cdd:TIGR00606 618 EEQLSSYEDKLFDvCGSQDEESDL--ERLKEEIEK--SSKQRAMLAG-ATAVYSQFITQLTDENQSCCPVCQRVFQTE-- 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1159 hrtdyvrimqenvsliKEINELRRELK-FTRSQVYDLEAALKLTKKV--RPQEVSETEPSRDMLSTAPTARLNEQEETGR 1235
Cdd:TIGR00606 691 ----------------AELQEFISDLQsKLRLAPDKLKSTESELKKKekRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
570 580
....*....|....*....|....
gi 345199335 1236 IIEMqrlEIQRLRDQIQEQEQVTG 1259
Cdd:TIGR00606 755 KVNR---DIQRLKNDIEEQETLLG 775
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
703-1147 |
2.32e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.36 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 703 ELKTRVEELKMENEYQLRLKDMNYSEkikelTDKFIQEMESLKTKNQVLRTE--KEKQDVyhhEHIEDLLDKQSRELQDM 780
Cdd:TIGR00606 713 STESELKKKEKRRDEMLGLAPGRQSI-----IDLKEKEIPELRNKLQKVNRDiqRLKNDI---EEQETLLGTIMPEEESA 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 781 ECCnnqklLLEYEKYQELQLKSQRMQEEYEKQLRDNDETksqaleELTEFYEAKLQEKttllEEAQEDVRQQLREFEETK 860
Cdd:TIGR00606 785 KVC-----LTDVTIMERFQMELKDVERKIAQQAAKLQGS------DLDRTVQQVNQEK----QEKQHELDTVVSKIELNR 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 861 KQIEeDEDREIQDIKTKYeKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQgviKSLEKDIQG 940
Cdd:TIGR00606 850 KLIQ-DQQEQIQHLKSKT-NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLE---TFLEKDQQE 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 941 LKREIQERDETIQDKEKRIYDLKKK-NQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENdpilkwpqrvEIHLY 1019
Cdd:TIGR00606 925 KEELISSKETSNKKAQDKVNDIKEKvKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEEC----------EKHQE 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1020 NFRKQVRkvllwgtlpQMEAELENFHKQNTQLELNITelwqklratdqemRRERQKErdlealVKRFKTDLHNCVAYIQE 1099
Cdd:TIGR00606 995 KINEDMR---------LMRQDIDTQKIQERWLQDNLT-------------LRKRENE------LKEVEEELKQHLKEMGQ 1046
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 345199335 1100 PRLLKEKvrglfEKYVQRADMVEIAGLNTDL----QQEYTRQREHLERNLAT 1147
Cdd:TIGR00606 1047 MQVLQMK-----QEHQKLEENIDLIKRNHVLalgrQKGYEKEIKHFKKELRE 1093
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
691-1199 |
2.59e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 691 KTDMEEKAQVMLELKTRVEELKMENEyQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQdvyhhEHIEDLL 770
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELE-ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-----RELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 771 DKQSRELQDMEccnnQKLLLEYEKYQELQLKsqrmQEEYEKQLRDNDETKSQALEELTEFyEAKLQEKTTLLEEAQEDVR 850
Cdd:COG1196 319 EELEEELAELE----EELEELEEELEELEEE----LEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 851 QQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKESNLRLKGEtgimRKKFSSLQKEIEERTNDIETLKGEQMKLQGV 930
Cdd:COG1196 390 EALRAAAELAAQLEELE-EAEEALLERLERLEEELEELEEALAEL----EEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 931 IKSLEKDIQGLKREIQERDETIQDKEKRIYDLKK-KNQELGKFKFVLDYK------------------------------ 979
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEaEADYEGFLEGVKAALllaglrglagavavligveaayeaaleaal 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 980 ------------------IKELKKQIEPRENEIRVMKEQIQENDPILKWPQRVE----------IHLYNFRKQVRKVLLW 1031
Cdd:COG1196 545 aaalqnivveddevaaaaIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGaavdlvasdlREADARYYVLGDTLLG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1032 GTLPQMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEpRLLKEKVRGLF 1111
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE-LELEEALLAEE 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1112 EKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDYVRIMQENVSLIKEINELRRELK------ 1185
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEalgpvn 783
|
570 580
....*....|....*....|....*....
gi 345199335 1186 ---------------FTRSQVYDLEAALK 1199
Cdd:COG1196 784 llaieeyeeleerydFLSEQREDLEEARE 812
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
786-1090 |
3.41e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.71 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 786 QKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEaKLQEKTTLLEEAQEDV-------RQQLREFEE 858
Cdd:pfam01576 523 QAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD-KLEKTKNRLQQELDDLlvdldhqRQLVSNLEK 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 859 TKKQIEEDEDREiQDIKTKYEKKlRDEKESNLRLKgETgimrkKFSSLQKEIEErtndietlkgeqmkLQGVIKSLEKDI 938
Cdd:pfam01576 602 KQKKFDQMLAEE-KAISARYAEE-RDRAEAEAREK-ET-----RALSLARALEE--------------ALEAKEELERTN 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 939 QGLKREIqerDETIQDKEkriyDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVM---KEQIQENDPILKWPQRVE 1015
Cdd:pfam01576 660 KQLRAEM---EDLVSSKD----DVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATedaKLRLEVNMQALKAQFERD 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1016 IHLYNFRKQVRKVLLWGTLPQMEAELENFHKQNTQ-------LELNITELWQKLRATDQEMRRERQKERDLEALVKRFKT 1088
Cdd:pfam01576 733 LQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQavaakkkLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQR 812
|
..
gi 345199335 1089 DL 1090
Cdd:pfam01576 813 EL 814
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
684-1196 |
4.02e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 684 AEEVLvtkTDMEEKAQVMLELKTRVEELKMENEYQLRLKDmNYSEKIKELTDkfiqEMESLKTKNQVLRTEKEKQDVyHH 763
Cdd:PRK02224 239 ADEVL---EEHEERREELETLEAEIEDLRETIAETERERE-ELAEEVRDLRE----RLEELEEERDDLLAEAGLDDA-DA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 764 EHIEDLLDKQSRELQDMEccnnqkllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQAlEELTEfyEAKLQEKTtlLE 843
Cdd:PRK02224 310 EAVEARREELEDRDEELR-----------DRLEECRVAAQAHNEEAESLREDADDLEERA-EELRE--EAAELESE--LE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 844 EAQEDVRQQLREFEETKKQIEEDEDReIQDIKTKYEKkLRDEKESNLRLKGETgimRKKFSSLQKEIEERTNDIEtlKGE 923
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRER-FGDAPVDLGN-AEDFLEELREERDEL---REREAELEATLRTARERVE--EAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 924 QMKLQGVIKSLEKDIQGLKR--EIQERDETIQDKEKRIYDLKKKNQELGKfKFVLDYKIKELKKQIEPRENEIRVMKEQI 1001
Cdd:PRK02224 447 ALLEAGKCPECGQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELI 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1002 QENDPILkwpQRVEIHLYNFRKQVRKvllwgtlpqMEAELENFHKQNTQLELNITELWQKLRATDQemRRERQKERdLEA 1081
Cdd:PRK02224 526 AERRETI---EEKRERAEELRERAAE---------LEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKER-IES 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1082 LvKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADMVE-----IAGLN--------TDLQQEYTRQREHLERNLATL 1148
Cdd:PRK02224 591 L-ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrerKRELEaefdeariEEAREDKERAEEYLEQVEEKL 669
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 345199335 1149 KKKVVKEGELHRtdyvRI-MQENVslIKEINELRRELKFTRSQVYDLEA 1196
Cdd:PRK02224 670 DELREERDDLQA----EIgAVENE--LEELEELRERREALENRVEALEA 712
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
686-1087 |
4.32e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.33 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 686 EVLVTKTDMEEKAQVMLELKTRVEelKMENEYQLRLKdmnysekiKEltDKFIQEMESLKTKNQVLRTEKEKQDVYHHEH 765
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHE--AMISDLEERLK--------KE--EKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 766 IEDL---LDKQSRELQ------DMECCNNQKLLleyEKYQELQLKSQRMQE--EYEKQLRDNDETKSQALEELTEFYEAK 834
Cdd:pfam01576 231 IAELraqLAKKEEELQaalarlEEETAQKNNAL---KKIRELEAQISELQEdlESERAARNKAEKQRRDLGEELEALKTE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 835 LqEKTTLLEEAQEDVR-QQLREFEETKKQIEED---EDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEI 910
Cdd:pfam01576 308 L-EDTLDTTAAQQELRsKREQEVTELKKALEEEtrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 911 EERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPR 990
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 991 ENEIRVMKEQIQENdpilkwpQRVEIHLYNFRKQVRKVLLwGTLPQMEAELE---NFHKQNTQLELNITELWQKLR---- 1063
Cdd:pfam01576 467 ESQLQDTQELLQEE-------TRQKLNLSTRLRQLEDERN-SLQEQLEEEEEakrNVERQLSTLQAQLSDMKKKLEedag 538
|
410 420
....*....|....*....|....
gi 345199335 1064 ATDQEMRRERQKERDLEALVKRFK 1087
Cdd:pfam01576 539 TLEALEEGKKRLQRELEALTQQLE 562
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
673-1024 |
4.89e-06 |
|
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: 50.89 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 673 RGIKREREVGFAEEVlvTKTDMEEKAQVMLELktrvEELKMENEYQLrlkdmnysEKIKEltdkfiqemESLKTKNQVLR 752
Cdd:pfam17380 310 REVERRRKLEEAEKA--RQAEMDRQAAIYAEQ----ERMAMEREREL--------ERIRQ---------EERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 753 TEKEKQDVYHHEHIEDLL----DKQSRELQDMECCNNQKLLLEyekyqELQLKSQRMQEEYEKQLRDNDETKSQALEELT 828
Cdd:pfam17380 367 QEEIAMEISRMRELERLQmerqQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQIRAEQEEARQREVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 829 EFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQ--IEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKkfsSL 906
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKklELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK---LL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 907 QKEIEERTNDIetLKGEQMKLQGVIKSLEKDIQGlKREIQERDETIQDKEKRIYDLKKKnqelgkfkfvldykiKELKKQ 986
Cdd:pfam17380 519 EKEMEERQKAI--YEEERRREAEEERRKQQEMEE-RRRIQEQMRKATEERSRLEAMERE---------------REMMRQ 580
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 345199335 987 IEPRENEIRVMK--EQIQENDPILK------WPQRVEIHLYNFRKQ 1024
Cdd:pfam17380 581 IVESEKARAEYEatTPITTIKPIYRpriseyQPPDVESHMIRFTTQ 626
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
791-1090 |
5.89e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.60 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 791 EYEKYQELQLKSQRmQEEYEKQLRDNDETKSQALEELTE-------------FYEAKLQEKTT--LLEEAQEDVRQQLRE 855
Cdd:PRK04778 49 ELEKVKKLNLTGQS-EEKFEEWRQKWDEIVTNSLPDIEEqlfeaeelndkfrFRKAKHEINEIesLLDLIEEDIEQILEE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 856 FEETKKQiEEDEDREIQDIKTKYEKkLRDEKESNlrlkgetgimRKKFSSLQKEIEERTNDIETL---------KGEQMK 926
Cdd:PRK04778 128 LQELLES-EEKNREEVEQLKDLYRE-LRKSLLAN----------RFSFGPALDELEKQLENLEEEfsqfvelteSGDYVE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 927 LQGVIKSLEKDIQGLKREIQERDETIQDKEK----RIYDLKKKNQELGKFKFVLDYK-----IKELKKQIEPRENEIRV- 996
Cdd:PRK04778 196 AREILDQLEEELAALEQIMEEIPELLKELQTelpdQLQELKAGYRELVEEGYHLDHLdiekeIQDLKEQIDENLALLEEl 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 997 -MKEQIQENDPIlkwpqRVEI-HLYN-FRKQV--RKVLLwGTLPQMEAELENFHKQNTQLELNITELWQKLRATDQEMRR 1071
Cdd:PRK04778 276 dLDEAEEKNEEI-----QERIdQLYDiLEREVkaRKYVE-KNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELES 349
|
330
....*....|....*....
gi 345199335 1072 ERQKERDLEALVKRFKTDL 1090
Cdd:PRK04778 350 VRQLEKQLESLEKQYDEIT 368
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
822-970 |
6.31e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 822 QALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED--------REIQDIK---TKYEKKLRDEKESNL 890
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnKEYEALQkeiESLKRRISDLEDEIL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 891 RLKGETGIMRKKFSSLQKEIEERTNDIETLKGEqmkLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYD-LKKKNQEL 969
Cdd:COG1579 114 ELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKIPPELLALYErIRKRKNGL 190
|
.
gi 345199335 970 G 970
Cdd:COG1579 191 A 191
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
813-1088 |
8.10e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 813 LRDNDETKSQA-LEELTEFY-EAKLQEKTTLLEEAQEDVRQQLrefEETKKQIEEDEdREIQDIKTKYekklrdekeSNL 890
Cdd:COG3206 142 YTSPDPELAAAvANALAEAYlEQNLELRREEARKALEFLEEQL---PELRKELEEAE-AALEEFRQKN---------GLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 891 RLKGETGIMRKKFSSLQKEIEErtndietLKGEQMKLQGVIKSLEKDIQGLKREIQE--RDETIQDKEKRIYDLKKKNQE 968
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAE-------ARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 969 LGKfKFVLDY-KIKELKKQIEpreneirVMKEQIQEndpilkwpqrveihlynfrkQVRKVLLwgtlpQMEAELENFHKQ 1047
Cdd:COG3206 282 LSA-RYTPNHpDVIALRAQIA-------ALRAQLQQ--------------------EAQRILA-----SLEAELEALQAR 328
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 345199335 1048 NTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKT 1088
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
797-965 |
8.53e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.89 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 797 ELQLKSQRMQEEYeKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEaQEDVRQQLREFEEtkkqieededreiqDIKT 876
Cdd:pfam07888 77 ELESRVAELKEEL-RQSREKHEELEEKYKELSASSEELSEEKDALLAQ-RAAHEARIRELEE--------------DIKT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 877 KYEKKLrdEKESNL-RLKGETgimrKKFSSLQKEIEErtnDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDK 955
Cdd:pfam07888 141 LTQRVL--ERETELeRMKERA----KKAGAQRKEEEA---ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQL 211
|
170
....*....|
gi 345199335 956 EKRIYDLKKK 965
Cdd:pfam07888 212 QDTITTLTQK 221
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
816-989 |
1.01e-05 |
|
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: 48.91 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 816 NDETKSQALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEetkKQIEEDEDrEIQDIKTKYEKKLRDEKESnlrlkge 895
Cdd:cd22656 108 DDEELEEAKKTIKALLD-DLLKEAKKYQDKAAKVVDKLTDFE---NQTEKDQT-ALETLEKALKDLLTDEGGA------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 896 tgIMRKKFSSLQKEIEERTNDIetlkgeqmklqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKknqelgkfkfv 975
Cdd:cd22656 176 --IARKEIKDLQKELEKLNEEY-------------AAKLKAKIDELKALIADDEAKLAAALRLIADLTA----------- 229
|
170
....*....|....
gi 345199335 976 LDYKIKELKKQIEP 989
Cdd:cd22656 230 ADTDLDNLLALIGP 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
875-1255 |
1.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 875 KTKYEKKLRDEKESNLRLKGETgimRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKR---------EI 945
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVLGFDN---RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDV 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 946 QERDETIQDKEKRIYDLKKKNQELGKfkfvLDYKIKELKKQIEPRENEIRVMKEQIQENDpilkwpQRVEihlyNFRKQV 1025
Cdd:COG4913 664 ASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLE------KELE----QAEEEL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1026 RkvllwgtlpQMEAELENF-HKQNTQLELNITELWQKLRATdqemRRERQKERDLEALVKRFKTDLHNcvayiqeprlLK 1104
Cdd:COG4913 730 D---------ELQDRLEAAeDLARLELRALLEERFAAALGD----AVERELRENLEERIDALRARLNR----------AE 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1105 EKVRGLFEKYVQRADMvEIAGLNTDL------QQEYTR-QREHLERNLATLKKKVVKEGELHRTDYVRIMQENVSLIKE- 1176
Cdd:COG4913 787 EELERAMRAFNREWPA-ETADLDADLeslpeyLALLDRlEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKEr 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1177 ---INELRRELKFTRSQVYDLEAalkltKKVRPQEVSETepsRDMLStapTARLNEQEETGRIIEMQRLEIQRLRDQIQE 1253
Cdd:COG4913 866 idpLNDSLKRIPFGPGRYLRLEA-----RPRPDPEVREF---RQELR---AVTSGASLFDEELSEARFAALKRLIERLRS 934
|
..
gi 345199335 1254 QE 1255
Cdd:COG4913 935 EE 936
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
62-420 |
1.10e-05 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 49.52 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 62 ALSISPNRRYLAiseTVQEKPAITIYELSSIPCRKrkVLNNFDFQVQkfiSMAFSPDSKYLLAqTSppESNLVYwLWEKQ 141
Cdd:COG2319 125 SVAFSPDGKTLA---SGSADGTVRLWDLATGKLLR--TLTGHSGAVT---SVAFSPDGKLLAS-GS--DDGTVR-LWDLA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 142 KVMAIVRIDTQNNPVYQVSFSPqDNTQVcVTG--NGMFKLLRFAEGTLKQTSfqRGEPQNYLAHTWVADDK-IVVGTDTG 218
Cdd:COG2319 193 TGKLLRTLTGHTGAVRSVAFSP-DGKLL-ASGsaDGTVRLWDLATGKLLRTL--TGHSGSVRSVAFSPDGRlLASGSADG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 219 KLFLfesgdqrWETsimvkeptNGSKSLDVIQESESliefpPVSSplpsyeqmVAASSHSQMsmpqvfaiaayskgFACS 298
Cdd:COG2319 269 TVRL-------WDL--------ATGELLRTLTGHSG-----GVNS--------VAFSPDGKL--------------LASG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 299 AGPGRVLLFEkmeekdfYRESREIRIPVDPQSndpsqsdkqDVLCLCFSPSEETLVASTSKNqlysiTMSLTEISKGEPA 378
Cdd:COG2319 307 SDDGTVRLWD-------LATGKLLRTLTGHTG---------AVRSVAFSPDGKTLASGSDDG-----TVRLWDLATGELL 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 345199335 379 HFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWNYET 420
Cdd:COG2319 366 RT----LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
842-964 |
1.12e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.86 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 842 LEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlRLKGETGIMRKKFSSLQKEIEERTNDIETLK 921
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE---RLEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 345199335 922 GEQ---MKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKK 964
Cdd:COG2433 455 SEErreIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
833-1092 |
1.15e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.47 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 833 AKLQEKTTLLEEAQEDVRQQLREFEETKKQiEEDEDREIQDIKTKYEKkLRDEKESNlrlkgetgimRKKFSSLQKEIEE 912
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLES-EEKNREEVEELKDKYRE-LRKTLLAN----------RFSYGPAIDELEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 913 RTNDIE---------TLKGEQMKLQGVIKSLEKDIQGLKR---EIQERDETIQDK-EKRIYDLKKKNQELGKFKFVLDY- 978
Cdd:pfam06160 154 QLAEIEeefsqfeelTESGDYLEAREVLEKLEEETDALEElmeDIPPLYEELKTElPDQLEELKEGYREMEEEGYALEHl 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 979 ----KIKELKKQIEPR------------ENEIRVMKEQIQENDPILkwpqRVEIHLYNFRKQvrkvllwgTLPQMEAELE 1042
Cdd:pfam06160 234 nvdkEIQQLEEQLEENlallenleldeaEEALEEIEERIDQLYDLL----EKEVDAKKYVEK--------NLPEIEDYLE 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 345199335 1043 NFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHN 1092
Cdd:pfam06160 302 HAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVER 351
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
707-1254 |
1.63e-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: 49.67 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 707 RVEELKMENEYQLRLKDMNysEKIKELTdkfiQEMESLKTKNQVLRTEKEKQdvyhhEHIEDLLDKQSRELqdmeccnNQ 786
Cdd:TIGR02168 325 LEELESKLDELAEELAELE--EKLEELK----EELESLEAELEELEAELEEL-----ESRLEELEEQLETL-------RS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 787 KLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQE---KTTLLEEAQEDVRQQLREFEETKKQI 863
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaELEELEEELEELQEELERLEEALEEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 864 EEdedrEIQDIKTKYEKKLRDEKESNLRLKGETGIMRkKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKR 943
Cdd:TIGR02168 467 RE----ELEEAEQALDAAERELAQLQARLDSLERLQE-NLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEA 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 944 EIQER-----DETIQDKEKRIYDLKKKNqeLGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENDPIlKWPQRVEI-- 1016
Cdd:TIGR02168 542 ALGGRlqavvVENLNAAKKAIAFLKQNE--LGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV-KFDPKLRKal 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1017 -----HLY---------NFRKQVRKVLLWGTLP----------------------QMEAELENFHKQNTQLELNITELWQ 1060
Cdd:TIGR02168 619 syllgGVLvvddldnalELAKKLRPGYRIVTLDgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEK 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1061 KLRATDQEMRRERQKERDLEALVKRFKTDLHNcvayiqeprlLKEKVRGLFEKYVQRADMVE-IAGLNTDLQQEYTRQRE 1139
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISA----------LRKDLARLEAEVEQLEERIAqLSKELTELEAEIEELEE 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1140 HLERNLATLKKKVVKEGELhRTDYVRIMQENVSLIKEINELRRELKFTRSQVydleAALKLTKKVRPQEVSETEPSRDML 1219
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEEL-EAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDL 843
|
570 580 590
....*....|....*....|....*....|....*
gi 345199335 1220 StaptARLNEQEETGRIIEMQRLEIQRLRDQIQEQ 1254
Cdd:TIGR02168 844 E----EQIEELSEDIESLAAEIEELEELIEELESE 874
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
709-949 |
1.64e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 709 EELKMENEYQLRLKDMNySEKIKELTDKF---IQEMESLKT-----KNQVLRTEKEKQDVyhHEHIEDLLDKQSRELQDM 780
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKN-GENIARKQNKYdelVEEAKTIKAeieelTDELLNLVMDIEDP--SAALNKLNTAAAKIKSKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 781 ECCnnQKLLLEYEKYQELQLKSQrmqeeyekQLRDNDETKSQALEELTEfyeakLQEKTTLLEEAQEDVRQQLREFEETK 860
Cdd:PHA02562 272 EQF--QKVIKMYEKGGVCPTCTQ--------QISEGPDRITKIKDKLKE-----LQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 861 KqieededrEIQDIKTKYEKKLRDekesnlrLKGEtgimRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQG 940
Cdd:PHA02562 337 K--------KLLELKNKISTNKQS-------LITL----VDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
....*....
gi 345199335 941 LKREIQERD 949
Cdd:PHA02562 398 LVKEKYHRG 406
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
791-1077 |
1.71e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.31 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 791 EYEKYQELQLKSQRMQEEYEK-QLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE--DE 867
Cdd:COG5022 811 EYRSYLACIIKLQKTIKREKKlRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQElkID 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 868 DREIQDIKTKYEK------KLRDEKESNLRLKGEtgIMRKKFSSLQKEIEERtnDIETLKGEQMKLQGVIKSLEKDIQGL 941
Cdd:COG5022 891 VKSISSLKLVNLEleseiiELKKSLSSDLIENLE--FKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLHEVESKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 942 KREIQERDETIQDKEKRIYDLKKKNQELGKFKfvldYKIKELKKQIEPRENEIRVMKEQIQENDPILKwpqrvEIHLYNF 1021
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFK----KELAELSKQYGALQESTKQLKELPVEVAELQS-----ASKIISS 1037
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 345199335 1022 RKQVRKVllwgtlPQMEAELENFH-KQNTQLELNITELWQKLRATDQEMRRERQKER 1077
Cdd:COG5022 1038 ESTELSI------LKPLQKLKGLLlLENNQLQARYKALKLRRENSLLDDKQLYQLES 1088
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
503-540 |
2.41e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 42.33 E-value: 2.41e-05
10 20 30
....*....|....*....|....*....|....*...
gi 345199335 503 ENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 540
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
678-1003 |
2.57e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 678 EREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQlRLKDMNYSEKIKELTDKFIQEM----------ESLKTK 747
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-KAEDARKAEEARKAEDAKRVEIarkaedarkaEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 748 NQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQL-----KSQRMQEEYEKQLRDNDETKSQ 822
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkKAEEAKKDAEEAKKAEEERNNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 823 ALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIE---EDEDREIQDIKTKYEKKlrdEKESNLRLKGETGim 899
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakkAEEKKKADEAKKKAEEA---KKADEAKKKAEEA-- 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQErdetiqdKEKRIYDLKKKNQELgkfkfvldYK 979
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-------AKKKADAAKKKAEEK--------KK 1392
|
330 340
....*....|....*....|....
gi 345199335 980 IKELKKQIEPRENEIRVMKEQIQE 1003
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAA 1416
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
818-1006 |
2.70e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 818 ETKSQALEELTEFYeAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED-----REIQDIktkyEKKLRDEKESNLRL 892
Cdd:COG4913 613 AALEAELAELEEEL-AEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAEL----EAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 893 KGetgimrkkfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI-----YDLKKKNQ 967
Cdd:COG4913 688 AA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERFA 756
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 345199335 968 ELG------KFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENDP 1006
Cdd:COG4913 757 AALgdaverELRENLEERIDALRARLNRAEEELERAMRAFNREWP 801
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
827-1092 |
2.89e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 827 LTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReIQDIKTKYEKKLRDEKESNLRLKGEtgimRKKFSSL 906
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEK-INNSNNKIKILEQQIKDLNDKLKKN----KDKINKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 907 QKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQ 986
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 987 IEPRENEIRVMKEQIqendpilkwpQRVEIHLYNFRKQVRKVllwgtlPQMEAELENFHKQNTQLELNITELWQKLRATD 1066
Cdd:TIGR04523 182 KLNIQKNIDKIKNKL----------LKLELLLSNLKKKIQKN------KSLESQISELKKQNNQLKDNIEKKQQEINEKT 245
|
250 260
....*....|....*....|....*.
gi 345199335 1067 QEMRRERQKERDLEALVKRFKTDLHN 1092
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSE 271
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
706-1150 |
2.98e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 706 TRVEELKMENEYQLrlkdmnysEKIKELTDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedlldkqsreLQDmeccnn 785
Cdd:pfam01576 1 TRQEEEMQAKEEEL--------QKVKERQQKAESELKELEKKHQQLCEEKNA-------------------LQE------ 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 786 qKLLLEYEKYQElqlksqrmQEEYEKQLrdndETKSQALEELTEFYEAKLQE---KTTLLEEAQEDVRQQLREFEEtkkQ 862
Cdd:pfam01576 48 -QLQAETELCAE--------AEEMRARL----AARKQELEEILHELESRLEEeeeRSQQLQNEKKKMQQHIQDLEE---Q 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 863 IEEDED--REIQDIKTKYEKKLRDEKESNLRLKGEtgimRKKFSSLQKEIEERTNDIETLKGEQmklqgvikslEKDIQG 940
Cdd:pfam01576 112 LDEEEAarQKLQLEKVTTEAKIKKLEEDILLLEDQ----NSKLSKERKLLEERISEFTSNLAEE----------EEKAKS 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 941 LKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENDPILKWPQrveihlyn 1020
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL-------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1021 frkqvrkvllwGTLPQMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCV---AYI 1097
Cdd:pfam01576 250 -----------ARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLdttAAQ 318
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 345199335 1098 QEPRLLKEKVRGLF------EKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKK 1150
Cdd:pfam01576 319 QELRSKREQEVTELkkaleeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
728-1000 |
2.99e-05 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 47.64 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 728 EKIKELTDKFIQ----------EMESLKTKNQVLRTEKEKQDVYHHEHIE--DLLDKQSRELQ----DMECCNNQKLLLE 791
Cdd:pfam09728 18 EKLAALCKKYAElleemkrlqkDLKKLKKKQDQLQKEKDQLQSELSKAILakSKLEKLCRELQkqnkKLKEESKKLAKEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 792 YEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYE--AKLQEKTTLLEE------AQEDVRQQLRE------FE 857
Cdd:pfam09728 98 EEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREklKSLIEQYELRELhfekllKTKELEVQLAEaklqqaTE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 858 ETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKD 937
Cdd:pfam09728 178 EEEKKAQEKEVAKARELKAQVQTLSETEKE----LREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKE 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 345199335 938 IQGLKREIQERDetiqdkeKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQ 1000
Cdd:pfam09728 254 NLTWKRKWEKSN-------KALLEMAEERQKLKE-------ELEKLQKKLEKLENLCRALQAE 302
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
850-988 |
3.58e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 850 RQQLREFEETKKQIEEDEDREIQDIKtkyEKKLRDEKESNLRLKGEtgimrkkfssLQKEIEERTNDIETLkgeQMKLQG 929
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIK---KEALLEAKEEIHKLRNE----------FEKELRERRNELQKL---EKRLLQ 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 345199335 930 VIKSLEKDIQGLKReiqeRDETIQDKEKRiydLKKKNQELGKFKFVLDYKIKELKKQIE 988
Cdd:PRK12704 94 KEENLDRKLELLEK----REEELEKKEKE---LEQKQQELEKKEEELEELIEEQLQELE 145
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
882-1002 |
3.78e-05 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 47.28 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 882 LRDEKESNLRLKGEtgIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGV------IKSLEKDIQGLKREIQERDETIQDK 955
Cdd:pfam17060 96 IPASFISALELKED--VKSSPRSEADSLGTPIKVDLLRNLKPQESPETPrrinrkYKSLELRVESMKDELEFKDETIMEK 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 345199335 956 E-------KRIYDLKKKNQELGK-FKFVLDYK-----------------IKELKKQIEPRENEIRVMKEQIQ 1002
Cdd:pfam17060 174 DrelteltSTISKLKDKYDFLSReFEFYKQHHehggnnsiktatkhefiISELKRKLQEQNRLIRILQEQIQ 245
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
778-1079 |
4.42e-05 |
|
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: 47.81 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 778 QDMECCNNQKLLLEYEKYQELQ-LKSQRMQEEYEKQLRDNDetKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREF 856
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEkMEQERLRQEKEEKAREVE--RRRKLEEAEKARQAEMDRQAAIYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 857 EETKkqiEEDEDREIQDIKTK-----------YEKKLRDEKESNLRLKGETGIMRKKF---SSLQKEIEERTNDIETLKG 922
Cdd:pfam17380 351 ERIR---QEERKRELERIRQEeiameisrmreLERLQMERQQKNERVRQELEAARKVKileEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 923 EQMKL-QGVIKSLEKDiqgLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDykiKELKKQIEPRENEIRVMKEQI 1001
Cdd:pfam17380 428 EQEEArQREVRRLEEE---RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE---KEKRDRKRAEEQRRKILEKEL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1002 QENdpilkwpQRVEIHLYNFRKQVRKVL------LWGTLPQMEAELENFHKQNTQLELNITElwQKLRATDQEMRRE-RQ 1074
Cdd:pfam17380 502 EER-------KQAMIEEERKRKLLEKEMeerqkaIYEEERRREAEEERRKQQEMEERRRIQE--QMRKATEERSRLEaME 572
|
....*
gi 345199335 1075 KERDL 1079
Cdd:pfam17380 573 REREM 577
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
764-960 |
5.07e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 764 EHIEDLLDKQS------------REL-QDMECCNNQKLLLE-----YEKYQELQLKS-----QRMQEEYEKQL---RDND 817
Cdd:PHA02562 154 KLVEDLLDISVlsemdklnkdkiRELnQQIQTLDMKIDHIQqqiktYNKNIEEQRKKngeniARKQNKYDELVeeaKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 818 ETKSQALEELTEF------YEAKLQEKTTLLEEAQEDVRQQLRE---FEE-----TKKQIEEDEDREIQDIKTK---YEK 880
Cdd:PHA02562 234 AEIEELTDELLNLvmdiedPSAALNKLNTAAAKIKSKIEQFQKVikmYEKggvcpTCTQQISEGPDRITKIKDKlkeLQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 881 KLRDEKESNLRLKG---ETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKD-------IQGLKREIQERDE 950
Cdd:PHA02562 314 SLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdnaeeLAKLQDELDKIVK 393
|
250
....*....|
gi 345199335 951 TIQDKEKRIY 960
Cdd:PHA02562 394 TKSELVKEKY 403
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
695-1006 |
5.67e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 695 EEKAQVMLELK-----TRVEELKMENEYQLRLKDMNYSEKIKELTDKfiqEMESLKTKNQVLRTEKEKQDVyhHEHIEDL 769
Cdd:COG5022 902 LELESEIIELKkslssDLIENLEFKTELIARLKKLLNNIDLEEGPSI---EYVKLPELNKLHEVESKLKET--SEEYEDL 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 770 LDKQS---RELQDMeccnNQKLLLEYEKYQELQLKSQRMQEEyEKQLRDNDeTKSQALEELTEFY---------EAKLQE 837
Cdd:COG5022 977 LKKSTilvREGNKA----NSELKNFKKELAELSKQYGALQES-TKQLKELP-VEVAELQSASKIIssestelsiLKPLQK 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 838 KTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKK---LRDEKESNLRLKGETGIMR------KKFSSLQK 908
Cdd:COG5022 1051 LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKtinVKDLEVTNRNLVKPANVLQfivaqmIKLNLLQE 1130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 909 EIEERTNDIETLKGEQMKLqgviKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFvldykiKELKKQIE 988
Cdd:COG5022 1131 ISKFLSQLVNTLEPVFQKL----SVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKS------KLSSSEVN 1200
|
330
....*....|....*...
gi 345199335 989 PRENEIRVMKEQIQENDP 1006
Cdd:COG5022 1201 DLKNELIALFSKIFSGWP 1218
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
725-952 |
5.71e-05 |
|
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: 46.59 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 725 NYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDvyHHEHIEDLLDKQSRELQdmeccnnqkllleyekyqELQLKSQR 804
Cdd:cd22656 80 NYAQNAGGTIDSYYAEILELIDDLADATDDEELEE--AKKTIKALLDDLLKEAK------------------KYQDKAAK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 805 MQEEYeKQLRDNDETKSQALEELTEFYEAKLQEKttLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKkLRD 884
Cdd:cd22656 140 VVDKL-TDFENQTEKDQTALETLEKALKDLLTDE--GGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIAD-DEA 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 345199335 885 EKESNLRLKGETGIMRKKFSSLQKEIEERTNDIEtlkgeqmKLQGVIKSLEKDIQGLKREIQERDETI 952
Cdd:cd22656 216 KLAAALRLIADLTAADTDLDNLLALIGPAIPALE-------KLQGAWQAIATDLDSLKDLLEDDISKI 276
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
872-1085 |
6.06e-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: 47.07 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 872 QDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDET 951
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 952 IQDKEKRIYDLKKKNQELGK---FKFVLD-------YKIKELKKQIEP-RENEIRVMKEQIQENdpilkwpQRVEIHLYN 1020
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRqppLALLLSpedfldaVRRLQYLKYLAPaRREQAEELRADLAEL-------AALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 345199335 1021 FRKQVRKVLLwgtlpQMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKR 1085
Cdd:COG4942 172 ERAELEALLA-----ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
764-1062 |
6.08e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 764 EHIEDLLDKQSRElQDMECCNNQKLLLeyekyqelqlKSQRMQEEYEKQLRDNDETKSQALEELtefyeAKLQEKTTLLE 843
Cdd:TIGR00618 594 VRLQDLTEKLSEA-EDMLACEQHALLR----------KLQPEQDLQDVRLHLQQCSQELALKLT-----ALHALQLTLTQ 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 844 EAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGE 923
Cdd:TIGR00618 658 ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 924 QMKLQGVIKSLEKDiqgLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELkkqiEPRENEIRVMKEQIQE 1003
Cdd:TIGR00618 738 EDALNQSLKELMHQ---ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLR----EEDTHLLKTLEAEIGQ 810
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 345199335 1004 NDPILKWPQRVEIHLY-----NFRKQVR-KVLLWGTLPQMEAELENFHKQNTQLELNITELWQKL 1062
Cdd:TIGR00618 811 EIPSDEDILNLQCETLvqeeeQFLSRLEeKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
766-1257 |
8.34e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 766 IEDLLDKQSRELQDMEccNNQKLLLEYEKYQELQLKS-QRMQEEYEKQLRDNDETKSQ-----ALEELTEFYEAKLQEKT 839
Cdd:PRK01156 185 IDYLEEKLKSSNLELE--NIKKQIADDEKSHSITLKEiERLSIEYNNAMDDYNNLKSAlnelsSLEDMKNRYESEIKTAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 840 TLLEEAQEDVrQQLREFEETKKQIEEDE---DREIQDIKTKYEKKLRDEKESNLRLKGETG----IMRK---------KF 903
Cdd:PRK01156 263 SDLSMELEKN-NYYKELEERHMKIINDPvykNRNYINDYFKYKNDIENKKQILSNIDAEINkyhaIIKKlsvlqkdynDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 904 SSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKdiqgLKREIQERDETIQDKEKRIYDLKKKN----QELGKFKFVLDYK 979
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIES----LKKKIEEYSKNIERMSAFISEILKIQeidpDAIKKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 980 IKELKKQIEPRENEIRVM---KEQIQENDPILKWPQRVEI---HLynfrkqvrkvllwGTlPQMEAELENFHKQNTQLEL 1053
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALrenLDELSRNMEMLNGQSVCPVcgtTL-------------GE-EKSNHIINHYNEKKSRLEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1054 NITELWQKLRATDQEMRRERQKERdlealvkrfktdlhncvayiqepRLLKEKVRGLFEKYVQRADMVeiAGLNTDLQQE 1133
Cdd:PRK01156 484 KIREIEIEVKDIDEKIVDLKKRKE-----------------------YLESEEINKSINEYNKIESAR--ADLEDIKIKI 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1134 YTRQREHLERNLATLKKKVVKEGELH--RTDYVRIMQEnVSLI------KEINELRRELKFTRSQVYDLEAALKLTKKVR 1205
Cdd:PRK01156 539 NELKDKHDKYEEIKNRYKSLKLEDLDskRTSWLNALAV-ISLIdietnrSRSNEIKKQLNDLESRLQEIEIGFPDDKSYI 617
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 345199335 1206 PQEVSETEPSRDMLSTaptaRLNEQEETGRIIEMQRLEIQRLRDQIQEQEQV 1257
Cdd:PRK01156 618 DKSIREIENEANNLNN----KYNEIQENKILIEKLRGKIDNYKKQIAEIDSI 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
683-958 |
9.85e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 683 FAEEVLvTKTDMEEKAQVMLELktrVEELkmeNEYQLRLKDMnySEKIKELTD--KFIQEMESLKTKNQVLRTEKEKQDV 760
Cdd:COG4913 213 VREYML-EEPDTFEAADALVEH---FDDL---ERAHEALEDA--REQIELLEPirELAERYAAARERLAELEYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 761 YHHEHIEDLLDKQSRELQdmeccnnqkllleyEKYQELqlksqrmqeeyEKQLRDNDETKSQALEELTEFYEAKLQEKTT 840
Cdd:COG4913 284 WFAQRRLELLEAELEELR--------------AELARL-----------EAELERLEARLDALREELDELEAQIRGNGGD 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 841 LLEEAQEDVRQQlrefEETKKQIEEDEDReiqdiktkYEKKLRDekesnLRLKGETGimRKKFSSLQKEIEERtndIETL 920
Cdd:COG4913 339 RLEQLEREIERL----ERELEERERRRAR--------LEALLAA-----LGLPLPAS--AEEFAALRAEAAAL---LEAL 396
|
250 260 270
....*....|....*....|....*....|....*...
gi 345199335 921 KGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKR 958
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1048-1256 |
1.02e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1048 NTQLEL-----NITELWQKLRATDQEMRRERQKERDLEALVKRFK------TDLHNcVAYI-QEPRLLKEKVRGLFEKYV 1115
Cdd:COG3206 84 ETQIEIlksrpVLERVVDKLNLDEDPLGEEASREAAIERLRKNLTvepvkgSNVIE-ISYTsPDPELAAAVANALAEAYL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1116 QRadmveiaglNTDLQQEYTRQ-REHLERNLATLKKKVVK-EGELH----RTDYVRIMQENVSLIKEINELRRELKFTRS 1189
Cdd:COG3206 163 EQ---------NLELRREEARKaLEFLEEQLPELRKELEEaEAALEefrqKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345199335 1190 QVYDLEAALK-LTKKVRPQEVSETEPSRDMLSTAPTARLNEQEetGRIIEMQRL------EIQRLRDQIQEQEQ 1256
Cdd:COG3206 234 ELAEAEARLAaLRAQLGSGPDALPELLQSPVIQQLRAQLAELE--AELAELSARytpnhpDVIALRAQIAALRA 305
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
806-1003 |
1.20e-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: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 806 QEEYEKQLRDNDETKSQALEELtefyeAKLQEKttlLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYEKKlRDE 885
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAEL-----DALQAE---LEELNEEYNELQAELEALQAEIDKLQ-AEIAEAEAEIEER-REE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 886 KESNLRLKGETGIMRKKFSSL--QKEIEE---RTNDIETLKGEQMKLqgvIKSLEKDIQGLKREIQERDETIQDKEKRIY 960
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLlgSESFSDfldRLSALSKIADADADL---LEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 345199335 961 DLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQE 1003
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
802-1254 |
1.21e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 802 SQRMQEEYEKQLRDNDETKSQALEELTEFY--EAKLQEKTTLLeEAQEDVRQQLrEFEETK------KQIEEDEDREIQD 873
Cdd:pfam05483 73 SEGLSRLYSKLYKEAEKIKKWKVSIEAELKqkENKLQENRKII-EAQRKAIQEL-QFENEKvslkleEEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 874 IKTKYEKKLRDEK-----ESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLK--GEQMKLQGVIKsLEKDIQGLKREIQ 946
Cdd:pfam05483 151 NATRHLCNLLKETcarsaEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRvqAENARLEMHFK-LKEDHEKIQHLEE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 947 ERDETIQDKEKRIYDL----KKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENDPILKWPQRVEIHLYNFR 1022
Cdd:pfam05483 230 EYKKEINDKEKQVSLLliqiTEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1023 K---------QVRKVLLWGTLPQMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNC 1093
Cdd:pfam05483 310 StqkaleedlQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1094 VAYIQEPRLLKEKvrglfeKYVQRADMVEIAGLNTDLQQEyTRQREHLERNLATLKKKVV-----KEGELH--RTDYVRI 1166
Cdd:pfam05483 390 SSELEEMTKFKNN------KEVELEELKKILAEDEKLLDE-KKQFEKIAEELKGKEQELIfllqaREKEIHdlEIQLTAI 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1167 MQENVSLIKEINELRRELKFTRSQVYDLEA---ALKLTKKVRPQEVSE-----TEPSRDMLSTAPT-ARLNEQEETGRII 1237
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAhcdKLLLENKELTQEASDmtlelKKHQEDIINCKKQeERMLKQIENLEEK 542
|
490
....*....|....*...
gi 345199335 1238 EMQ-RLEIQRLRDQIQEQ 1254
Cdd:pfam05483 543 EMNlRDELESVREEFIQK 560
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
900-1003 |
1.22e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKR----------------IYDLK 963
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyealqkeIESLK 102
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 345199335 964 KKNQElgkfkfvLDYKIKELKKQIEPRENEIRVMKEQIQE 1003
Cdd:COG1579 103 RRISD-------LEDEILELMERIEELEEELAELEAELAE 135
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
803-1003 |
1.94e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 803 QRMQEEYekqLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQedvrQQLREFEETKKQIEEDEDR-----EIQDIKTK 877
Cdd:COG3206 155 NALAEAY---LEQNLELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQKNGLVDLSEEAklllqQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 878 YEKKLRDEKESNLRLKGetgiMRKKFSSLQKEIEERTND--IETLKGEQMKLQGVIKSLEK-------DIQGLKREIQER 948
Cdd:COG3206 228 LAEARAELAEAEARLAA----LRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAAL 303
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 345199335 949 DETIQDKEKRIYDLKKKNQElgkfkfVLDYKIKELKKQIEPRENEIRVMKEQIQE 1003
Cdd:COG3206 304 RAQLQQEAQRILASLEAELE------ALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
784-884 |
2.56e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 42.56 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 784 NNQKLLLEYEKYQELQLKSQRMQEEYEKQLrdndETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQI 863
Cdd:pfam03938 6 DMQKILEESPEGKAAQAQLEKKFKKRQAEL----EAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKA 81
|
90 100
....*....|....*....|.
gi 345199335 864 EEDEDREIQDIKTKYEKKLRD 884
Cdd:pfam03938 82 QQELQKKQQELLQPIQDKINK 102
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
685-988 |
2.76e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 685 EEVLVTKTDMEE------KAQVML-----ELKTRVEELKMENEYqlrLKDMNYSEKIKELTDKfIQEMESLKTKNQVLRT 753
Cdd:PRK04778 205 EELAALEQIMEEipellkELQTELpdqlqELKAGYRELVEEGYH---LDHLDIEKEIQDLKEQ-IDENLALLEELDLDEA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 754 EKEKQDVyhHEHIEDLLDKqsrelqdMEccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKsqalEELTEfyea 833
Cdd:PRK04778 281 EEKNEEI--QERIDQLYDI-------LE--------REVKARKYVEKNSDTLPDFLEHAKEQNKELK----EEIDR---- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 834 kLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTkyekklrdekesnlrlkgetgimrkkFSSLQKEIEER 913
Cdd:PRK04778 336 -VKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIA--------------------------YSELQEELEEI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 914 TNDIETLKGEQMKLQGVIKSLEKDiqglkrEIQERdETIQDKEKRIYDLK----KKN-----QELGKFKFVLDYKIKELK 984
Cdd:PRK04778 389 LKQLEEIEKEQEKLSEMLQGLRKD------ELEAR-EKLERYRNKLHEIKryleKSNlpglpEDYLEMFFEVSDEIEALA 461
|
....
gi 345199335 985 KQIE 988
Cdd:PRK04778 462 EELE 465
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
691-969 |
3.59e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 44.84 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 691 KTDMEEKAQVMLELKTRVEELkmeneyqlrlkdMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedll 770
Cdd:pfam09726 408 KAELQASRQTEQELRSQISSL------------TSLERSLKSELGQLRQENDLLQTKLHNAVSAKQK------------- 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 771 DKQSreLQDMEccnnQKLLLEyekyqelqlksQRMQEEYEKQLrdNDETKSQALEELTEFYEAKLQEKTTllEEAQEDVR 850
Cdd:pfam09726 463 DKQT--VQQLE----KRLKAE-----------QEARASAEKQL--AEEKKRKKEEEATAARAVALAAASR--GECTESLK 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 851 QQLREFEETKKQIEED---EDREIQDIKTKyEKKLRDEKESnlrlKGETGIMRKKFSSLQKEIEERTNDI--ETlkgeQM 925
Cdd:pfam09726 522 QRKRELESEIKKLTHDiklKEEQIRELEIK-VQELRKYKES----EKDTEVLMSALSAMQDKNQHLENSLsaET----RI 592
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 345199335 926 KLqgvikSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQEL 969
Cdd:pfam09726 593 KL-----DLFSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEV 631
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
691-969 |
3.61e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.81 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 691 KTDMEEKAQVMLELKTRVEELKMENEyqlrlkdmNYSEKIKELTdkfiqemESLKTKNQ---VLRTEKEKQDVYHHEHiE 767
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQNS--------DCKQHIEVLK-------ESLTAKEQraaILQTEVDALRLRLEEK-E 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 768 DLLDKQSRELQDMeccNNQKLLLEYE-------------KYQELQLKSQRMQEeyekQLRDNDetksQALEELTEFYEAk 834
Cdd:pfam10174 359 SFLNKKTKQLQDL---TEEKSTLAGEirdlkdmldvkerKINVLQKKIENLQE----QLRDKD----KQLAGLKERVKS- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 835 LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREiqdiktkyEKKLRDEKESnlrLKGETGIMRKKFSSLQKEIEERT 914
Cdd:pfam10174 427 LQTDSSNTDTALTTLEEALSEKERIIERLKEQRERE--------DRERLEELES---LKKENKDLKEKVSALQPELTEKE 495
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 345199335 915 NDIETLKGEQ-------MKLQGVIKSLEKDIQgLKREIQERDETIQDKEKRIYDLKKKNQEL 969
Cdd:pfam10174 496 SSLIDLKEHAsslassgLKKDSKLKSLEIAVE-QKKEECSKLENQLKKAHNAEEAVRTNPEI 556
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
703-969 |
3.68e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 703 ELKTRVEELKMENEYQLRLKDMNYsEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHIEdlLDKQSRELQDME- 781
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELN-EKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS--IDKLRKEIERLEw 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 782 CCNNQKLLLEYEKyqELQLKSQRMQEEYEKqLRDNDETKSQALEELTEFYEAKLQekttlleeaQEDVRQQLREFEETKK 861
Cdd:COG1340 124 RQQTEVLSPEEEK--ELVEKIKELEKELEK-AKKALEKNEKLKELRAELKELRKE---------AEEIHKKIKELAEEAQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 862 QIEEdedrEIQDIKTKYEKkLRDEKESnlrlkgetgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGL 941
Cdd:COG1340 192 ELHE----EMIELYKEADE-LRKEADE----------LHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
250 260
....*....|....*....|....*...
gi 345199335 942 KREiqERDETIQDKEKRIYDLKKKNQEL 969
Cdd:COG1340 257 KRE--KEKEELEEKAEEIFEKLKKGEKL 282
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
789-1003 |
3.92e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 789 LLEYEKYQELQLKSQRMQEEYEKQLRD------NDETKSQALEELTEFYEAKLQ----EKTTLLEEAQEdVRQQLREF-- 856
Cdd:pfam15905 58 SLELKKKSQKNLKESKDQKELEKEIRAlvqergEQDKRLQALEEELEKVEAKLNaavrEKTSLSASVAS-LEKQLLELtr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 857 -----------EETKKQIE-------------EDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 912
Cdd:pfam15905 137 vnellkakfseDGTQKKMSslsmelmklrnklEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 913 RTNDIETLKGEQMKLQGVIKSLEKdiqgLKREIQERDETiqdkekriydLKKKNQELGKFKFVLDYKIKELKKQIEPREN 992
Cdd:pfam15905 217 EKSETEKLLEYITELSCVSEQVEK----YKLDIAQLEEL----------LKEKNDEIESLKQSLEEKEQELSKQIKDLNE 282
|
250
....*....|.
gi 345199335 993 EIRVMKEQIQE 1003
Cdd:pfam15905 283 KCKLLESEKEE 293
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
388-417 |
4.33e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.87 E-value: 4.33e-04
10 20 30
....*....|....*....|....*....|
gi 345199335 388 HSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:pfam00400 10 HTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
681-889 |
4.37e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 681 VGFAEEVLVTKTDMEEKAQVMLEL-KTRVEELKMENEYQLRLKDMNYSEKIKELTDKFiqEMESLKTKNQVLRTEKEKQD 759
Cdd:PRK12704 16 VGAVIGYFVRKKIAEAKIKEAEEEaKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF--EKELRERRNELQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 760 VyhhehiEDLLDKQSRELQDMEccnnqkllleyekyQELQLKsqrmQEEYEKQLRDndetksqaLEELTEFYEAKLQEKT 839
Cdd:PRK12704 94 K------EENLDRKLELLEKRE--------------EELEKK----EKELEQKQQE--------LEKKEEELEELIEEQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 345199335 840 TLLEEA----QEDVRQQLreFEETKKQIEEDEDREIQDIKTKYekKLRDEKESN 889
Cdd:PRK12704 142 QELERIsgltAEEAKEIL--LEKVEEEARHEAAVLIKEIEEEA--KEEADKKAK 191
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
837-1054 |
5.16e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.82 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 837 EKTTLLEEAQEDVRQQLREFEETKKQIEE---DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIM-------------- 899
Cdd:PTZ00440 404 KYTNIISLSEHTLKAAEDVLKENSQKIADyalYSNLEIIEIKKKYDEKINELKKSINQLKTLISIMksfydliisekdsm 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 900 ------RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLE---KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELG 970
Cdd:PTZ00440 484 dskekkESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEdyyITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKR 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 971 KFKfvldykiKELKKQIEPRENEIRVMKEQIQENDPILKWPQRVE--IHLYNFRKQVRKVLLWGTLPQMEAELENFHKQN 1048
Cdd:PTZ00440 564 SMK-------NDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEelINEALFNKEKFINEKNDLQEKVKYILNKFYKGD 636
|
....*.
gi 345199335 1049 TQLELN 1054
Cdd:PTZ00440 637 LQELLD 642
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
763-1281 |
5.31e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 763 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQ------LKSQRMQEEYEKQLRDNDETKSQA--LEELTEFYEAK 834
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEkelkhlREALQQTQQSHAYLTQKREAQEEQlkKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 835 LQEKTTL---LEEAQEDV---RQQLREFEETKKQIEEDEDR-----EIQDIKTKYEKKLRD------------------- 884
Cdd:TIGR00618 269 IEELRAQeavLEETQERInraRKAAPLAAHIKAVTQIEQQAqrihtELQSKMRSRAKLLMKraahvkqqssieeqrrllq 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 885 ---EKESNLRLKGETGIMRKKFSSLQKEIEER----TNDIETLKgEQMKLQGVIKSLEKDIQG--LKREIQERDETIQ-- 953
Cdd:TIGR00618 349 tlhSQEIHIRDAHEVATSIREISCQQHTLTQHihtlQQQKTTLT-QKLQSLCKELDILQREQAtiDTRTSAFRDLQGQla 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 954 ------------------DKEKRIYDLKKKNQELGKFKFVLDYKIKEL--KKQIEPRENEIRVMKEQIQENDPILKWP-Q 1012
Cdd:TIGR00618 428 hakkqqelqqryaelcaaAITCTAQCEKLEKIHLQESAQSLKEREQQLqtKEQIHLQETRKKAVVLARLLELQEEPCPlC 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1013 RVEIHLYNFRKQVrkVLLWGTLPQMEAeLENFHKQNTQLELNI----TELWQKLRATDQEMRRERQKERDLEALVKRFKT 1088
Cdd:TIGR00618 508 GSCIHPNPARQDI--DNPGPLTRRMQR-GEQTYAQLETSEEDVyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1089 DLHNCVAYIQE-----PRLLKEKVRGLFEKYVQ------RADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGE 1157
Cdd:TIGR00618 585 DIPNLQNITVRlqdltEKLSEAEDMLACEQHALlrklqpEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1158 LHrtdyVRIMQENVSLIKEiNELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSR-----DMLSTAPTARLNEQEE 1232
Cdd:TIGR00618 665 LS----IRVLPKELLASRQ-LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRefneiENASSSLGSDLAARED 739
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 345199335 1233 TGR--IIEMQRLEIQRLRDQIQEQEQVTGFHTLAGVRLPSLSNSEVDLEVK 1281
Cdd:TIGR00618 740 ALNqsLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF 790
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
385-417 |
5.46e-04 |
|
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: 38.83 E-value: 5.46e-04
10 20 30
....*....|....*....|....*....|...
gi 345199335 385 YPLHSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:smart00320 8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-179 |
5.60e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.75 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 26 DEQIIIFPSGNHCVK-YNVD-QKWQKFIPGSekSQGMLALSISPNRRYLAiseTVQEKPAITIYELSSipcrkRKVLNNF 103
Cdd:COG2319 257 DGRLLASGSADGTVRlWDLAtGELLRTLTGH--SGGVNSVAFSPDGKLLA---SGSDDGTVRLWDLAT-----GKLLRTL 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 345199335 104 DFQVQKFISMAFSPDSKYLLAQTSppeSNLVYwLWEKQKVMAIVRIDTQNNPVYQVSFSPQDNTQVCVTGNGMFKL 179
Cdd:COG2319 327 TGHTGAVRSVAFSPDGKTLASGSD---DGTVR-LWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
825-963 |
6.43e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 42.23 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 825 EELTEFYeAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYE---KKLRDEKESNLRLKGEtgimrk 901
Cdd:pfam08614 3 LELIDAY-NRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllAQLREELAELYRSRGE------ 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 345199335 902 kfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 963
Cdd:pfam08614 76 ----LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQ 133
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
676-954 |
6.61e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 676 KREREVGFAEEVLVTKTDMEEKAQVMLE----LKTRVEELKME-----NEYQLRLKDMNYSEKIKELTDKFIQEMESLKT 746
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEelkaLREALDELRAEltllnEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 747 KNQVLRTEKEKQdvyhHEHIEDLLDKQSRELQdmeccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEE 826
Cdd:TIGR02168 849 ELSEDIESLAAE----IEELEELIEELESELE-----------ALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 827 ltefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGetgiMRKKFSSL 906
Cdd:TIGR02168 914 -----RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR----LENKIKEL 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 345199335 907 Q----------KEIEERtndIETLKGEQMKLQGVIKSLEKDIQGLKREIQER-DETIQD 954
Cdd:TIGR02168 985 GpvnlaaieeyEELKER---YDFLTAQKEDLTEAKETLEEAIEEIDREARERfKDTFDQ 1040
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
812-999 |
7.82e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.26 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 812 QLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQqlreFEETKKQIEededREIQDIKTKYEKKLRDEKE-SNL 890
Cdd:pfam15905 163 KLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQ----LEEKLVSTE----KEKIEEKSETEKLLEYITElSCV 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 891 RLKGETgiMRKKFSSLQKEIEERTNDIETLKgeqmklqgviKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELg 970
Cdd:pfam15905 235 SEQVEK--YKLDIAQLEELLKEKNDEIESLK----------QSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEK- 301
|
170 180
....*....|....*....|....*....
gi 345199335 971 kfKFVLDYKIKELKKQIEPRENEIRVMKE 999
Cdd:pfam15905 302 --EQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
796-876 |
8.12e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.88 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 796 QELQLKSQRMQEEYEKQLRdndETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLrefEETKKQIEEDEDREIQDIK 875
Cdd:cd06503 43 EKAKEEAEELLAEYEEKLA---EARAEAQEIIEEARKEAEKIKEEILAEAKEEAERIL---EQAKAEIEQEKEKALAELR 116
|
.
gi 345199335 876 T 876
Cdd:cd06503 117 K 117
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-190 |
9.08e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.36 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 26 DEQIIIFPSGNHCVK-YNVD-QKWQKFIPGSekSQGMLALSISPNRRYLAiseTVQEKPAITIYELSSipcrkRKVLNNF 103
Cdd:COG2319 215 DGKLLASGSADGTVRlWDLAtGKLLRTLTGH--SGSVRSVAFSPDGRLLA---SGSADGTVRLWDLAT-----GELLRTL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 104 DFQVQKFISMAFSPDSKYLLAQTsppESNLVyWLWEKQKVMAIVRIDTQNNPVYQVSFSPQDNTQVCVTGNGMFKLLRFA 183
Cdd:COG2319 285 TGHSGGVNSVAFSPDGKLLASGS---DDGTV-RLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA 360
|
....*..
gi 345199335 184 EGTLKQT 190
Cdd:COG2319 361 TGELLRT 367
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
690-955 |
9.60e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 690 TKTDMEEKAQvmlELKTRVEELKMENEY--QLRLKDMNYSEKIKELTDKfIQEMESLKT-KNQVLRTEKEK----QDVYH 762
Cdd:TIGR04523 480 IKQNLEQKQK---ELKSKEKELKKLNEEkkELEEKVKDLTKKISSLKEK-IEKLESEKKeKESKISDLEDElnkdDFELK 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 763 HEHIEDLLDKQSRELQDMECcNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYE--AKLQEKTT 840
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEELKQ-TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKenEKLSSIIK 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 841 LLEEAQEDVRQQLREFEETKKQIEEDE---DREIQDIKTK---YEKKLRD-EKESNLRLKgetgimrkkfsslqKEIEE- 912
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQIKETIKEIRNKWpeiIKKIKESKTKiddIIELMKDwLKELSLHYK--------------KYITRm 700
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 345199335 913 -RTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDK 955
Cdd:TIGR04523 701 iRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
891-1165 |
1.03e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 891 RLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELG 970
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 971 KFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENDPILKWPQRVeihlynfRKQVRKVLLWGTLPQMEAELENFHKQNTQ 1050
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE-------LQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1051 LELNITELWQKLRATDQEmrRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADMVEIAGLNTDL 1130
Cdd:COG4372 202 LAEAEKLIESLPRELAEE--LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250 260 270
....*....|....*....|....*....|....*
gi 345199335 1131 QQEYTRQREHLERNLATLKKKVVKEGELHRTDYVR 1165
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
900-1003 |
1.13e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 900 RKKFSSLQKEIEERTnDIETLKGEQMK---LQGVIKSLEKDIQGLK-----REIQERDETIQDKEKRIYDLKKKNQELGK 971
Cdd:COG2433 349 KNKFERVEKKVPPDV-DRDEVKARVIRglsIEEALEELIEKELPEEepeaeREKEHEERELTEEEEEIRRLEEQVERLEA 427
|
90 100 110
....*....|....*....|....*....|..
gi 345199335 972 FKFVLDYKIKELKKQIEPRENEIRVMKEQIQE 1003
Cdd:COG2433 428 EVEELEAELEEKDERIERLERELSEARSEERR 459
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
704-1194 |
1.41e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 704 LKTRVEELKMENEYQLRLKDMN-----YSEKIKELTDKF-----------IQEMESLKTKNQVLRTEKEKQdvyhHEHIE 767
Cdd:pfam12128 339 IETAAADQEQLPSWQSELENLEerlkaLTGKHQDVTAKYnrrrskikeqnNRDIAGIKDKLAKIREARDRQ----LAVAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 768 DLLDKQSRELQDMEccNNQKLLLEYEKYQ--------ELQLKSQRMQEEYEKQLRDNDETKSQALEELT------EFYEA 833
Cdd:pfam12128 415 DDLQALESELREQL--EAGKLEFNEEEYRlksrlgelKLRLNQATATPELLLQLENFDERIERAREEQEaanaevERLQS 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 834 KLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYE---KKLRDEKESNLRLKGETGIMRkkfSSLQKEI 910
Cdd:pfam12128 493 ELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHflrKEAPDWEQSIGKVISPELLHR---TDLDPEV 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 911 -EERTNDIETLKGEQMKLQGV-IKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK----NQELGKFKFVLDYKIKELK 984
Cdd:pfam12128 570 wDGSVGGELNLYGVKLDLKRIdVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQlvqaNGELEKASREETFARTALK 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 985 KQiepRENEIRVMKEQIQENDpilKWPQRVEIHLYNFRKQVRKV--LLWGTLPQMEAELENFHKQNTQLELNITELWQ-- 1060
Cdd:pfam12128 650 NA---RLDLRRLFDEKQSEKD---KKNKALAERKDSANERLNSLeaQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQvv 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1061 ------KLRATDQEMRRER------------QKERDLEAL------VKRFKTDLHNCVAYIQEPRLLKEKVRGLF----E 1112
Cdd:pfam12128 724 egaldaQLALLKAAIAARRsgakaelkaletWYKRDLASLgvdpdvIAKLKREIRTLERKIERIAVRRQEVLRYFdwyqE 803
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1113 KYVQRADMVEIAGLNT-----DLQQEYTRQ-------REHLERNLATLKKKVVKEGELHRTdyVRIMQENVSLIKE---I 1177
Cdd:pfam12128 804 TWLQRRPRLATQLSNIeraisELQQQLARLiadtklrRAKLEMERKASEKQQVRLSENLRG--LRCEMSKLATLKEdanS 881
|
570
....*....|....*..
gi 345199335 1178 NELRRELKFTRSQVYDL 1194
Cdd:pfam12128 882 EQAQGSIGERLAQLEDL 898
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
728-1085 |
1.64e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 728 EKIKELTDKFIQEMESLKTKNQVLRTEKEKQdvyhhEHIEDLLdkQSRELQdMECcnNQKLLLEYE-KYQELQLKSQRMQ 806
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKA-----CEIRDQI--TSKEAQ-LES--SREIVKSYEnELDPLKNRLKEIE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 807 EEYEKQLRDNDETKsqALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEK 886
Cdd:TIGR00606 259 HNLSKIMKLDNEIK--ALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 887 ESNLR---LKGETGIMRKKFSSLQKEIEERTNDIETLKgEQMKLQGVIKSLEKDIQ-----GLKREIQERD-----ETIQ 953
Cdd:TIGR00606 337 LLNQEkteLLVEQGRLQLQADRHQEHIRARDSLIQSLA-TRLELDGFERGPFSERQiknfhTLVIERQEDEaktaaQLCA 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 954 DKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENDPILKwpqrveiHLYNFRKQVRKVLLWGT 1033
Cdd:TIGR00606 416 DLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD-------RILELDQELRKAERELS 488
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 345199335 1034 LPQMEAELENFHKQNTQLELNITELWQKLRATDQEMR---RERQKERDLEALVKR 1085
Cdd:TIGR00606 489 KAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEqlnHHTTTRTQMEMLTKD 543
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
800-974 |
1.71e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 800 LKSQRMQEEYEKQLRDNDEtksqalEELTEFYEAKLQEKTTLLEEAQE--DVRQQLRE-FEETKKQIEEdedreiqdikt 876
Cdd:smart00787 128 LEAKKMWYEWRMKLLEGLK------EGLDENLEGLKEDYKLLMKELELlnSIKPKLRDrKDALEEELRQ----------- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 877 kyEKKLRDEKESNLrlKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIqdKE 956
Cdd:smart00787 191 --LKQLEDELEDCD--PTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL--EQ 264
|
170
....*....|....*...
gi 345199335 957 KRIYDLKKKNQELGKFKF 974
Cdd:smart00787 265 CRGFTFKEIEKLKEQLKL 282
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
825-963 |
1.72e-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: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 825 EELTEFYEA--KLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKY---EKKLRDEKESNLRLKGETGIM 899
Cdd:COG4913 235 DDLERAHEAleDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLellEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345199335 900 RKKFSSLQKEIEERTNDIETLKGEQmklqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 963
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDR------LEQLEREIERLERELEERERRRARLEALLAALG 372
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
695-874 |
1.89e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 695 EEKAQVMLELKTRVEELKMENEYQLRLKDmnysEKIKELTDKFIQEMESLKTKnqvlrtekekqdvyhhehiEDLLDKQS 774
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERR----NELQKLEKRLLQKEENLDRK-------------------LELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 775 RELQDMECCNNQKLlleyekyQELQLKSQRMQEEYEKQLrdndetksQALEE---LTEFyEAKLQEKTTLLEEAQEDVRQ 851
Cdd:PRK12704 110 EELEKKEKELEQKQ-------QELEKKEEELEELIEEQL--------QELERisgLTAE-EAKEILLEKVEEEARHEAAV 173
|
170 180
....*....|....*....|...
gi 345199335 852 QLREFEEtkkQIEEDEDREIQDI 874
Cdd:PRK12704 174 LIKEIEE---EAKEEADKKAKEI 193
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
728-989 |
1.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 728 EKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHH--EHIEDLLDKQS--RELQDMEccnnqkllleyEKYQELQLKSQ 803
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASaeREIAELE-----------AELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 804 RMQEeyekqLRDNDETKSQALEELTEFYEAkLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDRE-IQDIKTKYEKKL 882
Cdd:COG4913 686 DLAA-----LEEQLEELEAELEELEEELDE-LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 883 RDEKESNLR--LKGETGIMRKKFSSLQKEIEERTND-IETLKGEQMKLQGVIKSLEkDIQGLKREIQERDetIQDKEKRI 959
Cdd:COG4913 760 GDAVERELRenLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLP-EYLALLDRLEEDG--LPEYEERF 836
|
250 260 270
....*....|....*....|....*....|..
gi 345199335 960 YDLKKKN--QELGKFKFVLDYKIKELKKQIEP 989
Cdd:COG4913 837 KELLNENsiEFVADLLSKLRRAIREIKERIDP 868
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
702-887 |
1.92e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 702 LELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRT-EKEKQDVYHHEHIEDLLDK-QSRELQD 779
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAALLAEaGVEDEEE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 780 MEccnnqKLLLEYEKYQELQLKsqrmQEEYEKQLRDNDETKSQALEELT-EFYEAKLQEKTTLLEEAQEDVRQQLREFEE 858
Cdd:COG4717 387 LR-----AALEQAEEYQELKEE----LEELEEQLEELLGELEELLEALDeEELEEELEELEEELEELEEELEELREELAE 457
|
170 180 190
....*....|....*....|....*....|
gi 345199335 859 TKKQIEE-DEDREIQDIKTKYEKKLRDEKE 887
Cdd:COG4717 458 LEAELEQlEEDGELAELLQELEELKAELRE 487
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
701-1114 |
1.94e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 42.63 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 701 MLELKTR----VEELKMENEyqlrlKDMNYSEKIkeltDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedlLDKQSRE 776
Cdd:pfam15818 2 LLDFKTSlleaLEELRMRRE-----AETQYEEQI----GKIIVETQELKWQKETLQNQKET------------LAKQHKE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 777 LqdMECCNNQkllleyekyqeLQLKSQRMQEEYEK-QLRDndETKSQALEELTEFYEAKLQEKTTL---LEEAQEDVRQQ 852
Cdd:pfam15818 61 A--MAVFKKQ-----------LQMKMCALEEEKGKyQLAT--EIKEKEIEGLKETLKALQVSKYSLqkkVSEMEQKLQLH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 853 LREFEETKKQIEEDEdreiqdiktKYEKKLrdekesnlrlKGETGIMRKKFSSLQKEIEERtndIETLKgeqmKLQGVIK 932
Cdd:pfam15818 126 LLAKEDHHKQLNEIE---------KYYATI----------TGQFGLVKENHGKLEQNVQEA---IQLNK----RLSALNK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 933 SLEKDIQGLKREiqerdetiqdkekriydLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQENDPILKWPQ 1012
Cdd:pfam15818 180 KQESEICSLKKE-----------------LKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMELELNKKIN 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1013 RVEIHLynfrkQVRKVLLWGTLPQMEAELENFHKQNTQLELNITELWQKLRA--TDQEMRRERQKE---------RDLEA 1081
Cdd:pfam15818 243 EEITHI-----QEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQTleRDNELQREKVKEneekflnlqNEHEK 317
|
410 420 430
....*....|....*....|....*....|....*..
gi 345199335 1082 LVKRFKTDLHNCVAYIQEPR----LLKEKVRGLFEKY 1114
Cdd:pfam15818 318 ALGTWKKHVEELNGEINEIKnelsSLKETHIKLQEHY 354
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
676-1159 |
2.00e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 676 KREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQLRLKDmnYSEKIKELTD---KFIQEMESLKTKNQVLR 752
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE--ISCQQHTLTQhihTLQQQKTTLTQKLQSLC 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 753 TEKEKQDVYHHEhIEDLLDKQSRELQDM-----ECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLR---DNDETKSQAL 824
Cdd:TIGR00618 400 KELDILQREQAT-IDTRTSAFRDLQGQLahakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAqslKEREQQLQTK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 825 EELTEFYEAKLQEKTTLLEEAQE--------------------------------------------DVRQQLREFEETK 860
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLELQEepcplcgscihpnparqdidnpgpltrrmqrgeqtyaqletseeDVYHQLTSERKQR 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 861 KQIEEDEDREIQDIKTKYEKKlrdekesnLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQ--MKLQGVIKSLEKDI 938
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCD--------NRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQhaLLRKLQPEQDLQDV 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 939 QGLKREIQER-----------DETIQDKEKRIYDLKKKNQELGKFKFVLDY--KIKELKKQIEPRENEIRVMKEQIQEND 1005
Cdd:TIGR00618 631 RLHLQQCSQElalkltalhalQLTLTQERVREHALSIRVLPKELLASRQLAlqKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1006 PILK--WPQRVEIHLYNFRKQVRKVLLWGTLPQMEAELEnfHKQNTQLELNITELWQK-LRATDQEMR--RERQKERDLE 1080
Cdd:TIGR00618 711 THIEeyDREFNEIENASSSLGSDLAAREDALNQSLKELM--HQARTVLKARTEAHFNNnEEVTAALQTgaELSHLAAEIQ 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1081 ALVKRFKTDLHNCV---AYIQEPRLLKEKVRGL-FEKYVQR-ADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKE 1155
Cdd:TIGR00618 789 FFNRLREEDTHLLKtleAEIGQEIPSDEDILNLqCETLVQEeEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ 868
|
....
gi 345199335 1156 GELH 1159
Cdd:TIGR00618 869 AKII 872
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
703-1117 |
2.03e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 703 ELKTRVEELKmeneyQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLRTEKEK--QDVYHHEHIEDLLDKQsRELQDM 780
Cdd:COG4717 72 ELKELEEELK-----EAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKleKLLQLLPLYQELEALE-AELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 781 EccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEdVRQQLREFEETK 860
Cdd:COG4717 145 P--------ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE-LQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 861 KQIEEDEDREIQDIKTKYEKKLRDEKESNLR--------------------------------LKGETGIMRKKFSSLQK 908
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKearlllliaaallallglggsllsliltiagvLFLVLGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 909 EIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKfvLDYKIKELKKQIE 988
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE--EELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 989 PR--------ENEIRVMKEQIQENDPILKWPQRVEIHLYNFRKQVRKVLLWGTLPQMEAELENFHKQNTQLELNITELWQ 1060
Cdd:COG4717 374 ALlaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 345199335 1061 KLRATDQEMRRERQKER--DLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQR 1117
Cdd:COG4717 454 ELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
706-897 |
2.07e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 706 TRVEELKMENEYQLRLkdmnySEKIKELTDKfiqEMESLKTKNQVLRTEKEKQDVYHHEhIEDLLDKQSRELQDMeccnn 785
Cdd:smart00787 126 ARLEAKKMWYEWRMKL-----LEGLKEGLDE---NLEGLKEDYKLLMKELELLNSIKPK-LRDRKDALEEELRQL----- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 786 QKLLLEYEKYQELQLKSQRmqEEYEKQLRDNDEtKSQALEELTEfyeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE 865
Cdd:smart00787 192 KQLEDELEDCDPTELDRAK--EKLKKLLQEIMI-KVKKLEELEE----ELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
170 180 190
....*....|....*....|....*....|..
gi 345199335 866 DEDREIQDIKTKYEKKLRDEKESNLRLKGETG 897
Cdd:smart00787 265 CRGFTFKEIEKLKEQLKLLQSLTGWKITKLSG 296
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
685-895 |
2.47e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 685 EEVLVTKTDMEEKaqvMLELKTRVEELKMENEYQLrlkdmnySEKIKELtDKFIQEMESLKTKNQVLRTEKEKQDVYHHE 764
Cdd:PRK03918 559 AELEKKLDELEEE---LAELLKELEELGFESVEEL-------EERLKEL-EPFYNEYLELKDAEKELEREEKELKKLEEE 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 765 hIEDLLDKQSRELQDMECCNNQ--KLLLEY--EKYQELQLKSQRMQEEYE------KQLRDNDETKSQALEELTEFYEA- 833
Cdd:PRK03918 628 -LDKAFEELAETEKRLEELRKEleELEKKYseEEYEELREEYLELSRELAglraelEELEKRREEIKKTLEKLKEELEEr 706
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345199335 834 -KLQEKTTLLEEAQEDVrQQLRE-FEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGE 895
Cdd:PRK03918 707 eKAKKELEKLEKALERV-EELREkVKKYKALLKERALSKVGEIASEIFEELTEGKYSGVRVKAE 769
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
801-1062 |
2.50e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 801 KSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQL---REFEETKKQIEEDEDR--EIQDIK 875
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSIneyNKIESARADLEDIKIKinELKDKH 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 876 TKYEKKlrDEKESNLRLkgetGIMRKKFSSLQKEIEERTN-DIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQD 954
Cdd:PRK01156 546 DKYEEI--KNRYKSLKL----EDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 955 KEKRIYDlkKKNQELGKFKfvldyKIKELKKQIEPRENEIRVMKEQIQENDPILKWPQRVEIHLYNFR---KQVRKVL-- 1029
Cdd:PRK01156 620 SIREIEN--EANNLNNKYN-----EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEdnlKKSRKALdd 692
|
250 260 270
....*....|....*....|....*....|...
gi 345199335 1030 LWGTLPQMEAELENFHKQNTQLELNITELWQKL 1062
Cdd:PRK01156 693 AKANRARLESTIEILRTRINELSDRINDINETL 725
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
899-1185 |
2.53e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 899 MRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLkkkNQELGKFKfvldY 978
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKL---NSDLSKIN----S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 979 KIKELKKQIEPRENEIRVMKEQIQENDPILKwpqRVEIHLYNFRKQVRKvllwgtlpqMEAELENFHKQNTQLELNITEL 1058
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNID---KFLTEIKKKEKELEK---------LNNKYNDLKKQKEELENELNLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1059 WQKLRATDQEMRRERQKERDLEALvkrfktdLHNCVAYIQEPRLLKEKVRGLFEKYVQRADMVEiaglntDLQQEYTRQR 1138
Cdd:TIGR04523 179 EKEKLNIQKNIDKIKNKLLKLELL-------LSNLKKKIQKNKSLESQISELKKQNNQLKDNIE------KKQQEINEKT 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 345199335 1139 EHLER------NLATLKKKVVKEGELHRTDYVRIMQENVSLIKEINELRRELK 1185
Cdd:TIGR04523 246 TEISNtqtqlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
728-1132 |
3.04e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 728 EKIKELTDKFIQEMESLKTKNQVLRTEkekqdvyhhehIEDLLDKQsRELQdmeccnnQKLLLEYEKYQELqlksqrmQE 807
Cdd:PRK04778 115 DLIEEDIEQILEELQELLESEEKNREE-----------VEQLKDLY-RELR-------KSLLANRFSFGPA-------LD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 808 EYEKQLrDNDETKSQALEELTE---FYEA-----KLQEKTTLLEEAQEDVRQQLREFEETKKQieededrEIQDIKTKYe 879
Cdd:PRK04778 169 ELEKQL-ENLEEEFSQFVELTEsgdYVEAreildQLEEELAALEQIMEEIPELLKELQTELPD-------QLQELKAGY- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 880 kklRDEKESNLRLKgETGIMrKKFSSLQKEIEERTNDIETLKGEQMKLQgvIKSLEKDIQGL----------KREIQERD 949
Cdd:PRK04778 240 ---RELVEEGYHLD-HLDIE-KEIQDLKEQIDENLALLEELDLDEAEEK--NEEIQERIDQLydilerevkaRKYVEKNS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 950 ETIQDKEKRiydLKKKNQELGKfkfvldyKIKELKKQIEPRENEI---RVMKEQIQEndpilkwpqrveihLYNFRKQVR 1026
Cdd:PRK04778 313 DTLPDFLEH---AKEQNKELKE-------EIDRVKQSYTLNESELesvRQLEKQLES--------------LEKQYDEIT 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 1027 KVLLWGTLP--QMEAELENFHKQNTQLELNITELWQKLRATdqemrreRQKERDLEALVKRFKTDLHNCVAYIQeprllK 1104
Cdd:PRK04778 369 ERIAEQEIAysELQEELEEILKQLEEIEKEQEKLSEMLQGL-------RKDELEAREKLERYRNKLHEIKRYLE-----K 436
|
410 420 430
....*....|....*....|....*....|
gi 345199335 1105 EKVRGLFEKYVQRADMV--EIAGLNTDLQQ 1132
Cdd:PRK04778 437 SNLPGLPEDYLEMFFEVsdEIEALAEELEE 466
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
769-1003 |
3.51e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.55 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 769 LLDKQSREL---QDMECCNNQKLLLEYEKYQEL-QLKSQRMQEEYEKQLRdndeTKSQALEELTEFYEAKLQEKTTLLEE 844
Cdd:pfam05667 208 LLERNAAELaaaQEWEEEWNSQGLASRLTPEEYrKRKRTKLLKRIAEQLR----SAALAGTEATSGASRSAQDLAELLSS 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 845 AQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGEtgimrKKFSSLQKEIEERTNDIETLKGEq 924
Cdd:pfam05667 284 FSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQRE-----EELEELQEQLEDLESSIQELEKE- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 925 mklqgvIKSLEKDIQGLKREIQERDETIQDKEKrIYDLKKKNQEL--------GKFKFVLDY------------------ 978
Cdd:pfam05667 358 ------IKKLESSIKQVEEELEELKEQNEELEK-QYKVKKKTLDLlpdaeeniAKLQALVDAsaqrlvelagqwekhrvp 430
|
250 260
....*....|....*....|....*...
gi 345199335 979 ---KIKELKKQIEPRENEIRVMKEQIQE 1003
Cdd:pfam05667 431 lieEYRALKEAKSNKEDESQRKLEEIKE 458
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
758-998 |
3.53e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 758 QDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQElQLKSQRMQ----EEYEKQLRDNDETKSQALEELTEFYEA 833
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYN-KIESARADlediKIKINELKDKHDKYEEIKNRYKSLKLE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 834 KLQEKTTLLEEAQE-----DVRQQLREFEETKKQIEEDEDR------EIQDIKTKYEKKLR--DEKESNLRLKgetgimR 900
Cdd:PRK01156 562 DLDSKRTSWLNALAvisliDIETNRSRSNEIKKQLNDLESRlqeieiGFPDDKSYIDKSIReiENEANNLNNK------Y 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 901 KKFSSLQKEIEERTNDIETLKGEQMKlqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKI 980
Cdd:PRK01156 636 NEIQENKILIEKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
250
....*....|....*...
gi 345199335 981 KELKKQIEPRENEIRVMK 998
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
792-909 |
3.88e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.
Pssm-ID: 214016 [Multi-domain] Cd Length: 152 Bit Score: 39.13 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 792 YEKYQELQLKS---QRMQEEYEKqLRDNDETKSQALE---ELTEFYEAKLQEKTTLLEEAQEDVRQQLRE-FEETKKQIE 864
Cdd:cd12923 11 KEINKEYLDKSreyDELYEKYNK-LSQEIQLKRQALEafeEAVKMFEEQLRTQEKFQKEAQPHEKQRLMEnNELLKSRLK 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 345199335 865 ededrEIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKE 909
Cdd:cd12923 90 -----ELEESKEQLEEDLRKQVAYNRELEREMNSLKPELMQLRKQ 129
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
841-991 |
4.69e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 39.93 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 841 LLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE-------SNLRLKgetgiMRKKFSSLQKEIEER 913
Cdd:COG1390 11 ILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAErekrriiSSAELE-----ARKELLEAKEELIEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 914 TNDietlkgeqmKLQGVIKSLEKDI---QGLKREIQERDETIQDKEKRIYdLKKKNQELGKfKFVLDYKIKELKKQIEPR 990
Cdd:COG1390 86 VFE---------EALEKLKNLPKDPeykELLKKLLKEAAEELGSGDLVVY-VNEKDKELLE-ELLKELKKKGLEVSEEDI 154
|
.
gi 345199335 991 E 991
Cdd:COG1390 155 D 155
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
676-994 |
4.86e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 676 KREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMEneyQLRL-KDMNYSEKIKELTDKFIQEMESLKT-----KNQ 749
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE---KLQIgTNLQRRQQFEEQLVELSTEVQSLIReikdaKEQ 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 750 VLRTE-------KEKQDVYHHEHIEDllDKQSRELQDMEccnnQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQ 822
Cdd:TIGR00606 911 DSPLEtflekdqQEKEELISSKETSN--KKAQDKVNDIK----EKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNA 984
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 823 ALEEltefyEAKLQEKTtlleeaQEDVRQQLREFEETKKQieedeDREIQDIKT--KYEKKLRDEKESNLRLKGETGIMR 900
Cdd:TIGR00606 985 QLEE-----CEKHQEKI------NEDMRLMRQDIDTQKIQ-----ERWLQDNLTlrKRENELKEVEEELKQHLKEMGQMQ 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 901 kkFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDetIQDKEKRIYDL-------KKKNQELGKFK 973
Cdd:TIGR00606 1049 --VLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ--FRDAEEKYREMmivmrttELVNKDLDIYY 1124
|
330 340
....*....|....*....|.
gi 345199335 974 FVLDYKIKELKKQIEPRENEI 994
Cdd:TIGR00606 1125 KTLDQAIMKFHSMKMEEINKI 1145
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
708-1002 |
5.01e-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: 41.58 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 708 VEELKMENEYQLRLKDMNYS-EKIKELTDKFIQEMESLKT--KNQvlrTEKEKQDVYHHEHIEDLLDKQSRELQDMECCN 784
Cdd:TIGR01612 1401 LEECKSKIESTLDDKDIDECiKKIKELKNHILSEESNIDTyfKNA---DENNENVLLLFKNIEMADNKSQHILKIKKDNA 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 785 NQKLLLEYEKYQELQLKSQRMQEEYEK---QLRDNDETKSQALEELTE----FYEAKLQEKttlLEEAQEDVRQQLREFE 857
Cdd:TIGR01612 1478 TNDHDFNINELKEHIDKSKGCKDEADKnakAIEKNKELFEQYKKDVTEllnkYSALAIKNK---FAKTKKDSEIIIKEIK 1554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 858 ETKKQIEEDEDREIQDIKTKYEKKLRDEKE---SNLRLKGETGI------MRKKFSSLQkEIEERTNDIETlkgEQMKLQ 928
Cdd:TIGR01612 1555 DAHKKFILEAEKSEQKIKEIKKEKFRIEDDaakNDKSNKAAIDIqlslenFENKFLKIS-DIKKKINDCLK---ETESIE 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 929 GVIKSLEKDIQGLK--------REIQERDETIQDKEKRIYDLKKK----NQELGKFKFVLD-----YKI---KELKKQIE 988
Cdd:TIGR01612 1631 KKISSFSIDSQDTElkengdnlNSLQEFLESLKDQKKNIEDKKKEldelDSEIEKIEIDVDqhkknYEIgiiEKIKEIAI 1710
|
330
....*....|....
gi 345199335 989 PRENEIRVMKEQIQ 1002
Cdd:TIGR01612 1711 ANKEEIESIKELIE 1724
|
|
| WDR74 |
cd22857 |
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ... |
343-420 |
5.10e-03 |
|
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and plants is an essential factor for ribosome assembly. In cooperation with the assembly factor NVL2, WDR74 participates in an early cleavage of the pre-rRNA processing pathway. NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of WDR74 from nucleolar pre-60S particles. WDR74 has been implicated in tumorigenesis. In lung cancer, it regulates cell proliferation, cell cycle progression, chemoresistance and cell aggressiveness, by inducing nuclear beta-catenin accumulation and driving downstream Wnt-responsive genes expression. In melanoma, it promotes apoptosis resistance and aggressive behavior by regulating the RPL5-MDM2-p53 pathway. WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.
Pssm-ID: 439303 [Multi-domain] Cd Length: 325 Bit Score: 40.67 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 343 CLCFSPSEETLVASTSKNQLYSI---TMSLTEISKGepahfeylmypLHSAPITGLATCIRKPLIATCSLDRSIRLWNYE 419
Cdd:cd22857 228 AVAEDPDGHTVYVGDTSGDLASIdlrTGKLLGCFKG-----------KCGGSIRSIARHPELPLIASCGLDRYLRIWDTE 296
|
.
gi 345199335 420 T 420
Cdd:cd22857 297 T 297
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
822-932 |
6.51e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 822 QALEELtefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE---------SNLRL 892
Cdd:PRK00409 523 ASLEEL----ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikelRQLQK 598
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 345199335 893 KGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIK 932
Cdd:PRK00409 599 GGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
703-969 |
6.55e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 703 ELKTRVEELKMENEyQLRLKDMNYSEKIKELTDkfIQEMESlktknQVLRTEKEKQDVyhhehiEDLLDKQSRELQDMEc 782
Cdd:PRK02224 472 EDRERVEELEAELE-DLEEEVEEVEERLERAED--LVEAED-----RIERLEERREDL------EELIAERRETIEEKR- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 783 cnnqkllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQA---LEELTEFyEAKLQEKTTLLE---------EAQEDVR 850
Cdd:PRK02224 537 ----------ERAEELRERAAELEAEAEEKREAAAEAEEEAeeaREEVAEL-NSKLAELKERIEslerirtllAAIADAE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 851 QQLREFEETKKQIEEDEDREIQDIKTKYEKK--LRDEKESNlRLKGetgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQ 928
Cdd:PRK02224 606 DEIERLREKREALAELNDERRERLAEKRERKreLEAEFDEA-RIEE----AREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 345199335 929 GVIKSLEKDIQGLkREIQERDETIQDKEKRIYDLKKKNQEL 969
Cdd:PRK02224 681 AEIGAVENELEEL-EELRERREALENRVEALEALYDEAEEL 720
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
731-879 |
6.75e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 40.10 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 731 KELTDKFIQEMeslktKNQVLRTEKEKQDVYHH-EHIE-DLLDKQSRE---------LQDMECCNNQKllleyEKYQELQ 799
Cdd:COG4026 72 RELAEKFFEEL-----KGMVGHVERMKLPLGHDvEYVDvELVRKEIKNaiiraglksLQNIPEYNELR-----EELLELK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 800 LKSQRMQEEYEKQLRDNDETKSQaLEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYE 879
Cdd:COG4026 142 EKIDEIAKEKEKLTKENEELESE-LEELREEYK-KLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEVFSLEELWK 219
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
815-963 |
7.12e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 39.27 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 815 DNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREiqdiKTKYEKKLRDEKESNLRLKG 894
Cdd:pfam05010 7 DAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQ----KELEHAEIQKVLEEKDQALA 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 345199335 895 ETGIMRKKFSSLQKEIEertndietlkgeqmKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 963
Cdd:pfam05010 83 DLNSVEKSFSDLFKRYE--------------KQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALK 137
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
697-950 |
9.82e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 39.99 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 697 KAQVMLELKTRVEELKmeNEYQLRLKDMNysekikELTDKFIQEMESLKT------KNQVLRTEKEKQDVyhHEHIEDLL 770
Cdd:pfam03999 141 SLEELESFRKHLENLR--NEKERRLEEVN------ELKKQIKLLMEELDLvpgtdfEEDLLCESEDNFCL--SRENIDKL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 771 DKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEaKLQE-KTTLLEEAQEDV 849
Cdd:pfam03999 211 RKLIKQLEEQKAEREEKIDDLREKILELWNRLQVPQEEQESFVRENNSLSQDTIDALREELQ-RLEElKKKNIKKLIEDL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345199335 850 RQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNL-RLKGETGIMRK------KFSSLQK---EIEERTNDIE- 918
Cdd:pfam03999 290 RVEIEELWDKLFYSTEQRKRFIPFFEELYTEDLLELHELELkRLKEEYESNKEilelveKWEELWEdmeELEAKANDPSr 369
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 345199335 919 --------TLKGEQM--KLQgviKSLEKDIQGLKREIQERDE 950
Cdd:pfam03999 370 fnnrggklLLKEEKErkRLT---RKLPKIEQELTEKVEAWES 408
|
|
| |
