|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
403-667 |
1.95e-34 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 136.96 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 403 LIATCSLDRSIRLWNYETNT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDD-IRSFK--EYSVRGcgeC 477
Cdd:COG2319 134 TLASGSADGTVRLWDLATGKlLRTLTGHSGAVTSVAFSPDGKLLASGSDDGtVRLWDLATGKlLRTLTghTGAVRS---V 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 478 SFS-NGGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCS 556
Cdd:COG2319 211 AFSpDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 557 YNCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEY 634
Cdd:COG2319 291 VNSVAFSPDGKLLASGSDDGTVRlwDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL--WDLATGELLRTL 368
|
250 260 270
....*....|....*....|....*....|...
gi 767902640 635 QAHAGPITKMLLTFDDQFLLTAAEDGCLFTWKV 667
Cdd:COG2319 369 TGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
386-678 |
1.48e-31 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 128.49 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 386 PLHSAPITGLATCIRKPLIATCSLDRSIRLWNYETN-TLELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNL----L 459
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGlLLRTLTGHTGAVRSVAFSPDGKTLASGSADGtVRLWDLatgkL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 460 IDDIRSFKE--YSVrgcgecSFSNGGHLFAAVNG-NVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAV 536
Cdd:COG2319 155 LRTLTGHSGavTSV------AFSPDGKLLASGSDdGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 537 YEWNLSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTS 614
Cdd:COG2319 229 RLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRlwDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSD 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902640 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 |
2.01e-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: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 388 HSAPITGLATCIRKPLIATCSLDRSIRLWNYETNTLEL-FKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNL----LID 461
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtLKGHTGPVRDVAASADGTYLASGSSDKtIRLWDLetgeCVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 462 DIRSFKEYsVRGcgeCSFSNGGHLFAAVNG-NVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 540
Cdd:cd00200 88 TLTGHTSY-VSS---VAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 541 LSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTI 618
Cdd:cd00200 164 LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKlwDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTI 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767902640 619 RAmkYPLPLQKEFNEYQAHAGPITKMLLTFDDQFLLTAAEDGCLFTWK 666
Cdd:cd00200 244 RV--WDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
341-579 |
4.98e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 111.93 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 341 VLCLCFSPSEETLvASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWNYET 420
Cdd:COG2319 165 VTSVAFSPDGKLL-ASGSDDG----TVRLWDLATGKLLRT----LTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 421 NT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDDIRSFKEYSVRGCGECSFS-NGGHLFAAVNGNVIHVY 497
Cdd:COG2319 236 GKlLRTLTGHSGSVRSVAFSPDGRLLASGSADGtVRLWDLATGELLRTLTGHSGGVNSVAFSpDGKLLASGSDDGTVRLW 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 498 TTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHT 577
Cdd:COG2319 316 DLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395
|
..
gi 767902640 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 |
1.08e-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: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 338 KQDVLCLCFSPSEeTLVASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:cd00200 93 TSYVSSVAFSPDG-RILSSSSRDK----TIKVWDVETGKCLTT----LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 418 YETNTL-ELFKEYQEEAYSISLHPSGHFIVVGFADKlrlmNLLIDDIRSFKE-YSVRGCGE----CSFSNGGHLFAAVNG 491
Cdd:cd00200 164 LRTGKCvATLTGHTGEVNSVAFSPDGEKLLSSSSDG----TIKLWDLSTGKClGTLRGHENgvnsVAFSPDGYLLASGSE 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767902640 492 -NVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 540
Cdd:cd00200 240 dGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
341-543 |
1.96e-20 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 94.98 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 341 VLCLCFSPSEETLvASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCirkP---LIATCSLDRSIRLWN 417
Cdd:COG2319 207 VRSVAFSPDGKLL-ASGSADG----TVRLWDLATGKLLRT----LTGHSGSVRSVAFS---PdgrLLASGSADGTVRLWD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 418 YETNT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDD-IRSFKEYSVRGCGeCSFS-NGGHLFAAVNGNV 493
Cdd:COG2319 275 LATGElLRTLTGHSGGVNSVAFSPDGKLLASGSDDGtVRLWDLATGKlLRTLTGHTGAVRS-VAFSpDGKTLASGSDDGT 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767902640 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 ... |
703-1035 |
1.05e-19 |
|
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: 95.09 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 703 ELKTRVEELKMENEYQLRLKD-MNYSEKIKELTDKFI-----------QEMESLKTKNQVLRTEKEKQDVYHHEHIEDLL 770
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVeLNKLEKQKKENKKNIdkflteikkkeKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 771 DKQSrelqDMECCNNQKLLLEY---------EKYQELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFYEAKLQEKTTL 841
Cdd:TIGR04523 184 NIQK----NIDKIKNKLLKLELllsnlkkkiQKNKSLESQISELKKQ-NNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 842 LEEAQEDVRQ---QLREFEETKKQIEEDEDReIQDIKTKYEKkLRDEKESNL--RLKGETGIMRKKF------------- 903
Cdd:TIGR04523 259 KDEQNKIKKQlseKQKELEQNNKKIKELEKQ-LNQLKSEISD-LNNQKEQDWnkELKSELKNQEKKLeeiqnqisqnnki 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 904 ----------------------SSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYD 961
Cdd:TIGR04523 337 isqlneqisqlkkeltnsesenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902640 962 LKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQE 1035
Cdd:TIGR04523 417 LQQEKELLEK-------EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
696-1019 |
7.78e-17 |
|
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: 86.28 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 696 EKAQVMLELKTRVEELkmenEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQdvyhHEHIEDLLDKQSR 775
Cdd:TIGR02169 208 EKAERYQALLKEKREY----EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR----LEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 776 ELQDM---ECCNNQKLLLEYEKYQElqlKSQRMQEEYEKQLRDNDETKSQALEELTefyeaKLQEKTTLLEEAQEDVRQQ 852
Cdd:TIGR02169 280 KIKDLgeeEQLRVKEKIGELEAEIA---SLERSIAEKERELEDAEERLAKLEAEID-----KLLAEIEELEREIEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 853 LREFEEtkkqieededrEIQDIKTKYEK---KLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQG 929
Cdd:TIGR02169 352 RDKLTE-----------EYAELKEELEDlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 930 VIKSLEKDIQGLKREIQERDETIQDKEKRIydlKKKNQELgkfkfvldykiKELKKQIEPRENEIRVMKEQIQEMEAELE 1009
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEI---KKQEWKL-----------EQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
330
....*....|
gi 767902640 1010 NFHKQNTQLE 1019
Cdd:TIGR02169 487 KLQRELAEAE 496
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
696-1025 |
2.20e-16 |
|
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: 84.30 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 696 EKAQVMLELKTRVEELKmENEYQLRLKDMNYSEKIKELT--------------------------------------DKF 737
Cdd:TIGR04523 65 KDEEKINNSNNKIKILE-QQIKDLNDKLKKNKDKINKLNsdlskinseikndkeqknklevelnklekqkkenkkniDKF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 738 I-------QEMESLKTKNQVLRTEKEKQDVYHHEHIEDLLDKQSrelqDMECCNNQKLLLEY---------EKYQELQLK 801
Cdd:TIGR04523 144 LteikkkeKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK----NIDKIKNKLLKLELllsnlkkkiQKNKSLESQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 802 SQRMQEEyEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQ---QLREFEETKKQIEEDEDReIQDIKTKY 878
Cdd:TIGR04523 220 ISELKKQ-NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlseKQKELEQNNKKIKELEKQ-LNQLKSEI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 879 EkKLRDEKESNL--RLKGETGIMRKKFSSLQKE-------IEERTNDIETLKGEQM-------KLQGVIKSLEKDIQGLK 942
Cdd:TIGR04523 298 S-DLNNQKEQDWnkELKSELKNQEKKLEEIQNQisqnnkiISQLNEQISQLKKELTnsesensEKQRELEEKQNEIEKLK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 943 REIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNI 1022
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
...
gi 767902640 1023 TEL 1025
Cdd:TIGR04523 457 KNL 459
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
504-665 |
2.81e-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: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 504 NISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHTLK--EI 581
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRlwDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 582 ADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQAHAGPITKMLLTFDDQFLLTAAEDGC 661
Cdd:cd00200 81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKV--WDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158
|
....
gi 767902640 662 LFTW 665
Cdd:cd00200 159 IKLW 162
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
478-669 |
4.08e-16 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 81.88 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 478 SFSNGGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSY 557
Cdd:COG2319 44 ASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 558 NCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQ 635
Cdd:COG2319 124 RSVAFSPDGKTLASGSADGTVRlwDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL--WDLATGKLLRTLT 201
|
170 180 190
....*....|....*....|....*....|....
gi 767902640 636 AHAGPITKMLLTFDDQFLLTAAEDGclfTWKVFD 669
Cdd:COG2319 202 GHTGAVRSVAFSPDGKLLASGSADG---TVRLWD 232
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
764-1042 |
4.84e-16 |
|
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: 83.58 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 764 EHIEDLLDKQSRELQDMECCNNQKllleyEKYQELQLKSQRMqEEYE--KQLRDNDETKSQALEELTEFyEAKLQEKTTL 841
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKA-----ERYQALLKEKREY-EGYEllKEKEALERQKEAIERQLASL-EEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 842 LEEAQEDVRQQLREFEETKKQIE---EDEDREIQ----DIKTKYEKKLRDEKESNLRLKGETGIMRKKFS---SLQKEIE 911
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKdlgEEEQLRVKekigELEAEIASLERSIAEKERELEDAEERLAKLEAeidKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 912 ERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQ-------DKEKRIYDLKKKNQELGKFKFVLDYKIKELK 984
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdelkDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767902640 985 KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQK 1042
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
820-1042 |
5.81e-16 |
|
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: 83.18 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 820 KSQALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNlRLKGETGIM 899
Cdd:TIGR02168 675 RRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYK 979
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902640 980 IKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNItELWQKLRATDQEMRRERQK 1042
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRS 894
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
676-1042 |
1.79e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.18 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 676 KREREVgfaEEVLVTKTDMEEKAQVMLELKTRVEELKmENEYQLRLKDMNYSEKIKELTDKfIQEMESLKTKNQVLRTEK 755
Cdd:PRK03918 273 KEIEEL---EEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEER-IKELEEKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 756 E---------KQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLleyEKYQELQLKSQRMQEEYEK------QLRDNDETK 820
Cdd:PRK03918 348 KelekrleelEERHELYEEAKAKKEELERLKKRLTGLTPEKLE---KELEELEKAKEEIEEEISKitarigELKKEIKEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 821 SQALEEL--------------TEFYEAKLQEKTTLleeaqedvrqQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEK 886
Cdd:PRK03918 425 KKAIEELkkakgkcpvcgrelTEEHRKELLEEYTA----------ELKRIEKELKEIEEKE-RKLRKELRELEKVLKKES 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 887 E--SNLRLKGETGIMRKKFSSLQKE-IEERTNDIETLKGEQMKLQGVIKSLEKDI---QGLKREIQERDETIQDKEKRIY 960
Cdd:PRK03918 494 EliKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELeklEELKKKLAELEKKLDELEEELA 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 961 DLKKKNQELGkFKFV--LDYKIKEL-------------KKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL 1025
Cdd:PRK03918 574 ELLKELEELG-FESVeeLEERLKELepfyneylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
410
....*....|....*..
gi 767902640 1026 WQKLraTDQEMRRERQK 1042
Cdd:PRK03918 653 EKKY--SEEEYEELREE 667
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
690-1038 |
3.19e-14 |
|
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: 77.37 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 690 TKTDMEEKAQVMLELKTRVEELKME-NEYQLRLKDMNySEKIKELTDKFIQEMESLKTKNQVLRTE---KEKQDVYHHEH 765
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQlNQLKSEISDLN-NQKEQDWNKELKSELKNQEKKLEEIQNQisqNNKIISQLNEQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 766 IEDLldkqSRELQDMECCNNQKLLLEYEKYQELQlKSQRMQEEYEKQLRdNDETKSQALEELTEFYEAKLQEKTTLLEEA 845
Cdd:TIGR04523 344 ISQL----KKELTNSESENSEKQRELEEKQNEIE-KLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 846 QEDVRQQLREFEETKKQIEEDED------REIQDIKTKYE--KKLRDEKESNLR-LKGETGIMRKKFSSLQKEIEERTND 916
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSeikdltNQDSVKELIIKnlDNTRESLETQLKvLSRSINKIKQNLEQKQKELKSKEKE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 917 IETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKK---------KNQELGKFKFVLDYKIKELKKQI 987
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQ 577
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 767902640 988 EPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRR 1038
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
726-1038 |
3.50e-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: 77.42 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 726 YSEKIKELTDkfiqEMESLKTKNQVLRTEKEkqdvyhheHIEDLLDKQSRELQDMEccnnqKLLLEYEKYQELQLKSQRM 805
Cdd:TIGR02169 672 EPAELQRLRE----RLEGLKRELSSLQSELR--------RIENRLDELSQELSDAS-----RKIGEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 806 QEEYEKQLRDNDETKSQALEEltefYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDE 885
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIEN----VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 886 KESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK 965
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902640 966 NQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQL------ELNITELWQKLRATDQEMRR 1038
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeeELSLEDVQAELQRVEEEIRA 969
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
685-1035 |
5.70e-14 |
|
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: 76.60 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 685 EEVLVTKTDMEEKAQVMLELKTRVEELKMEneyqLRLKDMNYSEKIKELTDKfIQEMESLKTKNQVLRTEKEKqdvyhhe 764
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEK-QNEIEKLKKENQSYKQEIKN------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 765 hiedlLDKQSRELqdmeccnNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEakLQEKTTLLEE 844
Cdd:TIGR04523 389 -----LESQINDL-------ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD--LTNQDSVKEL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 845 AQEDVRQQLrefEETKKQIEEDEdREIQDIKTKYEKKLR--DEKESNL-RLKGETGIMRKKFSSLQKEIEERTNDIETLK 921
Cdd:TIGR04523 455 IIKNLDNTR---ESLETQLKVLS-RSINKIKQNLEQKQKelKSKEKELkKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 922 GEQMKLQGVIKSLEKDI---------QGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPREn 992
Cdd:TIGR04523 531 SEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKE- 609
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 767902640 993 eirvmkEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQE 1035
Cdd:TIGR04523 610 ------KKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
718-1042 |
1.29e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 718 QLRLKDMNysEKIKELTDKfIQEMES-LKTknqvLRTEKEKQDVYHhehiedlldKQSRELQDMEccnNQKLLLEYEKYQ 796
Cdd:COG1196 178 ERKLEATE--ENLERLEDI-LGELERqLEP----LERQAEKAERYR---------ELKEELKELE---AELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 797 ElQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReiqdikt 876
Cdd:COG1196 239 A-ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER------- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 877 kyekkLRDEKESNLRLKGETgimrkkfSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKE 956
Cdd:COG1196 311 -----RRELEERLEELEEEL-------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 957 KRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEM 1036
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
....*.
gi 767902640 1037 RRERQK 1042
Cdd:COG1196 459 EALLEL 464
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
725-1042 |
1.46e-13 |
|
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: 75.48 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 725 NYSEKIKELTDKfIQEMESLKTKNQVLRTEKEKQdvyhHEHIEDLLDKQSRELQDMEccnnQKLLLEYEKYQELQLKSQR 804
Cdd:TIGR02168 674 ERRREIEELEEK-IEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 805 mqeeYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLLEEAqEDVRQQLREfeetkkQIEEDEDR--EIQDIKTKYEKKL 882
Cdd:TIGR02168 745 ----LEERIAQLSKELTELEAEIEE-LEERLEEAEEELAEA-EAEIEELEA------QIEQLKEElkALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 883 RDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIqglkreiqerdETIQDKEKRIYDL 962
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI-----------EELESELEALLNE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 963 KKKNQELgkfkfvldykIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLrATDQEMRRERQK 1042
Cdd:TIGR02168 882 RASLEEA----------LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI-DNLQERLSEEYS 950
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
692-1010 |
3.41e-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: 73.90 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 692 TDMEEKAQVMLELKTRVEELKMENE-YQLRLKDMNysEKIKELTDKFIQEMESLKTKNQVLRT-EKEKQDVyhHEHIEDL 769
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQsYKQEIKNLE--SQINDLESKIQNQEKLNQQKDEQIKKlQQEKELL--EKEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 770 LD---KQSRELQDMECCNNQKLLL-----EYEKYQELQLKSqrMQEEYEKQLRDNDETKSQALEELTEFyeAKLQEKTTL 841
Cdd:TIGR04523 432 KEtiiKNNSEIKDLTNQDSVKELIiknldNTRESLETQLKV--LSRSINKIKQNLEQKQKELKSKEKEL--KKLNEEKKE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 842 LEEAQEDVRQQLREFEETKKQIEEDE---DREIQDIKTKYEKKLRDEKESNLRlkgetgimrKKFSSLQKEIEERTNDIE 918
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEKkekESKISDLEDELNKDDFELKKENLE---------KEIDEKNKEIEELKQTQK 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 919 TLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMK 998
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
330
....*....|..
gi 767902640 999 EQIQEMEAELEN 1010
Cdd:TIGR04523 659 NKWPEIIKKIKE 670
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
695-1030 |
4.99e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 695 EEKAQVMLELKTRVEELkMENEYQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLRTEKEKqdvyhhEHIEDLLDKQS 774
Cdd:PRK03918 387 EKLEKELEELEKAKEEI-EEEISKITARIGELKKEIKEL-KKAIEELKKAKGKCPVCGRELTE------EHRKELLEEYT 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 775 RELQDMEccNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQ---ALEELTEFYEAKLQEKTTLLEEAQEDVRQ 851
Cdd:PRK03918 459 AELKRIE--KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkeLEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 852 QLREFEETKKQIEEDEdrEIQDIKTKYEKKLRDEKESNLRLKGEtgIMRKKFSSLqKEIEERTNDIETLKGEQMKLQGV- 930
Cdd:PRK03918 537 LKGEIKSLKKELEKLE--ELKKKLAELEKKLDELEEELAELLKE--LEELGFESV-EELEERLKELEPFYNEYLELKDAe 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 931 --IKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKE------------LKKQIEPRENEIRV 996
Cdd:PRK03918 612 keLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELReeylelsrelagLRAELEELEKRREE 691
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767902640 997 MKEQIQEMEAELENFHKQNTQLEL------NITELWQKLR 1030
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKlekaleRVEELREKVK 731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
676-1042 |
8.65e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 8.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 676 KREREVGFAEEvLVTKTDMEEKAQvmlELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEK 755
Cdd:PTZ00121 1438 KKAEEAKKADE-AKKKAEEAKKAE---EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 756 EKQDVYHHEHIEDLLD-KQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAK 834
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 835 LQEKTTLLEEAQEDVRQQLREFEETKKQIEE-DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEER 913
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 914 TNDIETLKGEQmklqgviKSLEKDIQGLKREIQERDETIQDKeKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEP---R 990
Cdd:PTZ00121 1674 KKKAEEAKKAE-------EDEKKAAEALKKEAEEAKKAEELK-KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEdkkK 1745
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 767902640 991 ENEIRV---MKEQIQEMEAELENFHKQNTQLELNITElwQKLRATDQEMRRERQK 1042
Cdd:PTZ00121 1746 AEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDK 1798
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
691-1029 |
9.76e-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: 72.36 E-value: 9.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 691 KTDMEEKAQVMLELKTRVEELKMENEY---QLRLKDM---NYSEKIKELTDKFIQemesLKTKNQVLRTEKEkQDVyhHE 764
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKikkQLSEKQKeleQNNKKIKELEKQLNQ----LKSEISDLNNQKE-QDW--NK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 765 HIEDLLDKQSRELQDME--CCNNQKLLLEYeKYQELQLKSQRMQEEYEKQLRDND-ETKSQALEELTEFYEAKLQEKTTL 841
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQnqISQNNKIISQL-NEQISQLKKELTNSESENSEKQRElEEKQNEIEKLKKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 842 lEEAQEDVRQQLREFEETKKQIEEdedrEIQDIKTKYEKKLRDEKEsnlrlkgetgiMRKKFSSLQKEIEERTNDIETLK 921
Cdd:TIGR04523 390 -ESQINDLESKIQNQEKLNQQKDE----QIKKLQQEKELLEKEIER-----------LKETIIKNNSEIKDLTNQDSVKE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 922 GEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKriyDLKKKNQELGKFKFV---LDYKIKELKKQIEPRENEIRVMK 998
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK---ELKSKEKELKKLNEEkkeLEEKVKDLTKKISSLKEKIEKLE 530
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767902640 999 EQIQEMEAELE---------NFHKQNTQLELNITELWQKL 1029
Cdd:TIGR04523 531 SEKKEKESKISdledelnkdDFELKKENLEKEIDEKNKEI 570
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
670-1035 |
3.76e-12 |
|
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: 70.52 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 670 KDGRGIKREReVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEyQLRLKdmnYSEKIKELTDkFIQEMESLKTKNQ 749
Cdd:pfam05483 85 KEAEKIKKWK-VSIEAELKQKENKLQENRKIIEAQRKAIQELQFENE-KVSLK---LEEEIQENKD-LIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 750 VLRT----EKEKQDVYHHEHiedlldKQSRELQdMECCNN-QKLLLEYE---------------KYQELQLKSQRMQEEY 809
Cdd:pfam05483 159 LLKEtcarSAEKTKKYEYER------EETRQVY-MDLNNNiEKMILAFEelrvqaenarlemhfKLKEDHEKIQHLEEEY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 810 EKQLRDNDETKSQALEELTEfYEAKLQEKTTLLEEAQEDVRQ---QLREFEETKKQIEEDED---REIQDIK-------- 875
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITE-KENKMKDLTFLLEESRDKANQleeKTKLQDENLKELIEKKDhltKELEDIKmslqrsms 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 876 ------------TKYEKKLRDEKESNLRlkgETGIMRKKFSSLQKEIEERTNDIETL-KGEQMKLQG---VIKSLEKDIQ 939
Cdd:pfam05483 311 tqkaleedlqiaTKTICQLTEEKEAQME---ELNKAKAAHSFVVTEFEATTCSLEELlRTEQQRLEKnedQLKIITMELQ 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 940 GLKREIQERDETIQDKEKRIYDLKK----------KNQELGKFKFVLDYKIKELKKQIEPRENEIRVMK----------- 998
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKilaedeklldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqltaiktsee 467
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 767902640 999 ---EQIQEMEAELENFHKQNTQLELNITELWQKLRATDQE 1035
Cdd:pfam05483 468 hylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-1021 |
5.68e-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: 70.09 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 696 EKAQVMLELKTRVEELKMEnEYQLRLKDMNYS-EKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHIEDLLDKQS 774
Cdd:TIGR02168 210 EKAERYKELKAELRELELA-LLVLRLEELREElEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 775 R------ELQDMEccnNQKllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELtefyeAKLQEKTTLLEEAQED 848
Cdd:TIGR02168 289 ElyalanEISRLE---QQK-----QILRERLANLERQLEELEAQLEELESKLDELAEEL-----AELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 849 VRQQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQ 928
Cdd:TIGR02168 356 LEAELEELEAELEELESRL-EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 929 gvIKSLEKDIQGLKREI---QERDETIQDKEKRIYDLKKKNQElgkfkfvldyKIKELKKQieprENEIRVMKEQIQEME 1005
Cdd:TIGR02168 435 --LKELQAELEELEEELeelQEELERLEEALEELREELEEAEQ----------ALDAAERE----LAQLQARLDSLERLQ 498
|
330
....*....|....*.
gi 767902640 1006 AELENFHKQNTQLELN 1021
Cdd:TIGR02168 499 ENLEGFSEGVKALLKN 514
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
794-1042 |
7.71e-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: 69.70 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 794 KYQELQLKSQRMQE--EYEKQLRDNDetKSQALEELTEFyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE--DEDR 869
Cdd:TIGR02168 201 QLKSLERQAEKAERykELKAELRELE--LALLVLRLEEL-REELEELQEELKEAEEELEELTAELQELEEKLEElrLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 870 EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQErd 949
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES-- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 950 etiqdkekriydLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKL 1029
Cdd:TIGR02168 356 ------------LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
250
....*....|...
gi 767902640 1030 RATDQEMRRERQK 1042
Cdd:TIGR02168 424 EELLKKLEEAELK 436
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
791-1042 |
8.81e-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: 69.71 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 791 EYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEeltefYEAKLQEKTTLLEEAQEDvRQQLREFEETKKQIEEDEDRE 870
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDE-----LSQELSDASRKIGEIEKE-IEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 871 IQDIktkyEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERtndietlkgEQMKLQGVIKSLEKDIQGLKREIQERDE 950
Cdd:TIGR02169 746 LSSL----EQEIENVKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 951 TIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLR 1030
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
250
....*....|..
gi 767902640 1031 ATDQEMRRERQK 1042
Cdd:TIGR02169 893 ELEAQLRELERK 904
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
687-1039 |
1.40e-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: 68.93 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 687 VLVTKTDMEEKAQVMLELKTRVEELKME-NEYQLRLKDMNySEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVyhhEH 765
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKAlAELRKELEELE-EELEQLRKELEELSRQISALRKDLARLEAEVEQL---EE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 766 IEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQ------ALEELTEFYeAKLQEKT 839
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelraELTLLNEEA-ANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 840 TLLEEAQEDVRQQLREFEETKKQIEEDEDR---EIQDIKTKYEKKLRD-EKESNLRLKGETGIM--RKKFSSLQKEIEER 913
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESlaaEIEELEELIEELESElEALLNERASLEEALAllRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 914 TNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKF-VLDYKIKELKKQIepreN 992
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEeEARRRLKRLENKI----K 982
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 767902640 993 EI-RVMKEQIQEMEAELENFHKQNTQLElNITELWQKLRATDQEMRRE 1039
Cdd:TIGR02168 983 ELgPVNLAAIEEYEELKERYDFLTAQKE-DLTEAKETLEEAIEEIDRE 1029
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
794-1036 |
2.30e-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: 68.28 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 794 KYQELQlKSQRMQEEYEKQLRDNDETKSQALEELTEFYEaKLQEKTTLLEEAQEdvrqqLREFEETKKQieededrEIQD 873
Cdd:pfam01576 10 KEEELQ-KVKERQQKAESELKELEKKHQQLCEEKNALQE-QLQAETELCAEAEE-----MRARLAARKQ-------ELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 874 IKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDI-------QGLKREIQ 946
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDIllledqnSKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 947 ERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELW 1026
Cdd:pfam01576 156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235
|
250
....*....|
gi 767902640 1027 QKLRATDQEM 1036
Cdd:pfam01576 236 AQLAKKEEEL 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
829-1042 |
2.69e-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: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 829 EFYEAKLQEKTTLLEEA------QEDVRQQLREFEETKKQIEEDED--REI---------QDIKTKYEKKLRDEKEsNLR 891
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAagiskyKERRKETERKLERTRENLDRLEDilNELerqlkslerQAEKAERYKELKAELR-ELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 892 LkgetGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGK 971
Cdd:TIGR02168 227 L----ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 972 FKFVLDYKIKELKKQIEPRENEIRV--------------MKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMR 1037
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEEleskldelaeelaeLEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
....*
gi 767902640 1038 RERQK 1042
Cdd:TIGR02168 383 TLRSK 387
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
843-1040 |
2.75e-11 |
|
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: 68.17 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 843 EEAQEDVRQQLREFEETKKQIEEDEdrEIQDIKTKYEKKLRDEKESNLRlkgetgimrkkFSSLQKEIEE-----RTNDI 917
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLD--LIIDEKRQQLERLRREREKAER-----------YQALLKEKREyegyeLLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 918 ETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGkfkfvlDYKIKELKKQIEPRENEIRVM 997
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASL 306
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767902640 998 KEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRER 1040
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
691-1049 |
5.57e-11 |
|
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: 66.92 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 691 KTDMEEKAQVMLELKTRVEELK--MENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDV------YH 762
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKklIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLlyldylKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 763 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKyQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLL 842
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEK-LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 843 EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKgetgimrkkfssLQKEIEERTNDIETLKG 922
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL------------QEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 923 EQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVM--KEQ 1000
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelKLL 461
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 767902640 1001 IQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKPCLISGP 1049
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLK 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
807-1042 |
6.43e-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: 67.00 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 807 EEYEKQLRDNDETKSQ---ALEELTEFYEaKLQEKTTLLEEAQEdVRQQLREFEET----KKQIEEDEDREIQDIKTKYE 879
Cdd:TIGR02168 175 KETERKLERTRENLDRledILNELERQLK-SLERQAEKAERYKE-LKAELRELELAllvlRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 880 KKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI 959
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 960 YDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKL-----RATDQ 1034
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIerleaRLERL 412
|
....*...
gi 767902640 1035 EMRRERQK 1042
Cdd:TIGR02168 413 EDRRERLQ 420
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
807-1042 |
6.92e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 807 EEYEKQLRDNDETKSQALEELTEfyeakLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReiqdiKTKYEKKLRDEK 886
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINE-----ISSELPELREELEKLEKEVKELEELKEEIEELEKE-----LESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 887 EsnlrLKGETGIMRKKFSSLQKEIEERTNDIETLKG---EQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 963
Cdd:PRK03918 259 E----KIRELEERIEELKKEIEELEEKVKELKELKEkaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 964 KKNQELGKfkfvLDYKIKELKKQIEPRE------NEIRVMKEQIQ------------EMEAELENFHKQNTQLELNITEL 1025
Cdd:PRK03918 335 EKEERLEE----LKKKLKELEKRLEELEerhelyEEAKAKKEELErlkkrltgltpeKLEKELEELEKAKEEIEEEISKI 410
|
250
....*....|....*..
gi 767902640 1026 WQKLRATDQEmRRERQK 1042
Cdd:PRK03918 411 TARIGELKKE-IKELKK 426
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
692-1042 |
7.33e-11 |
|
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: 66.68 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 692 TDMEEK-AQVMLELK--TRVEELKMEN-EYQLRLKDMNYSEKIKElTDKFIQEMESLKTKNQVLRTekekqDVYHHEHIE 767
Cdd:pfam15921 320 SDLESTvSQLRSELReaKRMYEDKIEElEKQLVLANSELTEARTE-RDQFSQESGNLDDQLQKLLA-----DLHKREKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 768 DLLDKQSRELQDMECCNN---QKLLLEYE----KYQELQLKSQRMQEEYEKQLrdndETKSQALEELTEFYEaKLQEKTT 840
Cdd:pfam15921 394 SLEKEQNKRLWDRDTGNSitiDHLRRELDdrnmEVQRLEALLKAMKSECQGQM----ERQMAAIQGKNESLE-KVSSLTA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 841 LLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKESNlrlkgetgimrKKFSSLQKEIEERTNDIETL 920
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSE-RTVSDLTASLQEKERAIEATN-----------AEITKLRSRVDLKLQELQHL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 921 KGEQMKLQGVikslEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRE---NEIRVM 997
Cdd:pfam15921 537 KNEGDHLRNV----QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRlelQEFKIL 612
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 767902640 998 KE----QIQEMEAELENFHKQNTQLelnITELWQKLRATdQEMRRERQK 1042
Cdd:pfam15921 613 KDkkdaKIRELEARVSDLELEKVKL---VNAGSERLRAV-KDIKQERDQ 657
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
685-1058 |
9.29e-11 |
|
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: 66.30 E-value: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 685 EEVLVTKTDMEEKAQVMLELKTRVEElkmeneyQLRLKDMNYSE--KIKELTDKFIQEMESLKTKNQVLR---TEKE--K 757
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASLQE-------KERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRnvqTECEalK 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 758 QDVYHHEHIEDLLDKQSRELQDMECCNNQKL-LLEYEKYQ-ELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAkl 835
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTAgAMQVEKAQlEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL-- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 836 qEKTTLLEEAQEDVRQqLREFEETKKQI--EEDEDR-EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 912
Cdd:pfam15921 633 -EKVKLVNAGSERLRA-VKDIKQERDQLlnEVKTSRnELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 913 RTNDIETLKGEQ-------MKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKK 985
Cdd:pfam15921 711 TRNTLKSMEGSDghamkvaMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902640 986 QIEPRENEIRVMKEQIQEMEAELEnfhkqntQLELNITELWQKLRATDQEMRRERQKPCL----ISGPcRFTSlNSS 1058
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEVALD-------KASLQFAECQDIIQRQEQESVRLKLQHTLdvkeLQGP-GYTS-NSS 858
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
698-1014 |
9.98e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 9.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 698 AQVMLELKTRVEELKmeneyQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedlLDKQSREL 777
Cdd:PRK03918 168 GEVIKEIKRRIERLE-----KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREE------------LEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 778 QDMEccNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTE--------------------FYEAKLQE 837
Cdd:PRK03918 231 KELE--ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkelkekaeeyiklseFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 838 KTTL------LEEAQEDVRQQLREFEETKKQIEEDEDR--EIQDIKTKYEKKLRD-----EKESNL-----RLKGET-GI 898
Cdd:PRK03918 309 LREIekrlsrLEEEINGIEERIKELEEKEERLEELKKKlkELEKRLEELEERHELyeeakAKKEELerlkkRLTGLTpEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 899 MRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLK----------REIQE--RDETIQDKEKRIYDLKKKN 966
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELTEehRKELLEEYTAELKRIEKEL 468
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 767902640 967 QELGKFKFVLDYKIKELKKQIEpRENEIRVMK---EQIQEMEAELENFHKQ 1014
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLK-KESELIKLKelaEQLKELEEKLKKYNLE 518
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
690-1042 |
1.84e-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: 65.13 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 690 TKTDMEEKAQVMLELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEhiedl 769
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME----- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 770 LDKQSRELQDMECCNNQKllleyekyqELQLKS-QRMQEEYEKQLRDNDEtksqaLEELTEFYEAKLQEKTTLLEEAQED 848
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNK---------EVELEElKKILAEDEKLLDEKKQ-----FEKIAEELKGKEQELIFLLQAREKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 849 VRQQLREFEETKKQiEEDEDREIQDIKTKYEK-KLRDEKES---------NLRLKGETGIMRKKFSSLQKEI------EE 912
Cdd:pfam05483 452 IHDLEIQLTAIKTS-EEHYLKEVEDLKTELEKeKLKNIELTahcdkllleNKELTQEASDMTLELKKHQEDIinckkqEE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 913 RT-NDIETLKGEQMKLQGVIKSLEKDIqglkreIQERDET---IQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIE 988
Cdd:pfam05483 531 RMlKQIENLEEKEMNLRDELESVREEF------IQKGDEVkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 767902640 989 PRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQ---EMRRERQK 1042
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQkfeEIIDNYQK 661
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
796-1042 |
2.81e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 62.62 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 796 QELQLKSQRmqEEYEKQLRDNDETKSQALEELTEFYEaklqEKTTLLEEAQEdVRQQLREFEETKKQIEEdedrEIQDIK 875
Cdd:COG1340 9 SLEELEEKI--EELREEIEELKEKRDELNEELKELAE----KRDELNAQVKE-LREEAQELREKRDELNE----KVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 876 TKYE------KKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIET---LKGEQMKLQGVIKSLEKDIQGLKREIQ 946
Cdd:COG1340 78 EERDelneklNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTevlSPEEEKELVEKIKELEKELEKAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 947 ERDEtIQDKEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELW 1026
Cdd:COG1340 158 KNEK-LKELRAELKELRKEAEEIHK-------KIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELH 229
|
250
....*....|....*.
gi 767902640 1027 QKLRATDQEMRRERQK 1042
Cdd:COG1340 230 EEIIELQKELRELRKE 245
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
728-1042 |
3.63e-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: 63.82 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 728 EKIKELTDKFIQEMESLKTKN-QVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQ 806
Cdd:COG5185 159 GIIKDIFGKLTQELNQNLKKLeIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGF 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 807 EEYEKQLRDNDETK---SQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLR 883
Cdd:COG5185 239 QDPESELEDLAQTSdklEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 884 DEKESN-----LRLKGETGIMR------KKFSSLQKEIEERTNDIETLKGEQM--KLQGVIKSLEKDIQGLKREIQERDE 950
Cdd:COG5185 319 AAAEAEqeleeSKRETETGIQNltaeieQGQESLTENLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 951 TIQDKEKRIydlkkkNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELE-NFHKQNTQLELNITELWQKL 1029
Cdd:COG5185 399 NQRGYAQEI------LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNkVMREADEESQSRLEEAYDEI 472
|
330
....*....|...
gi 767902640 1030 RATDQEMRRERQK 1042
Cdd:COG5185 473 NRSVRSKKEDLNE 485
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
677-1016 |
4.58e-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: 63.97 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 677 REREVGFAE-EVLVTKTDMEEKAQVMLELKTRVEELKMENeyqlrLKDMNYSEKIKELTDKFIQEmeslkTKNQVLRTEK 755
Cdd:pfam05483 448 REKEIHDLEiQLTAIKTSEEHYLKEVEDLKTELEKEKLKN-----IELTAHCDKLLLENKELTQE-----ASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 756 EKQDVYHHEHIEDLLDKQSRELQDMEccNNQKLLLEY------EKYQELQLKSQRMQE-----EYE-------------- 810
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLEEKE--MNLRDELESvreefiQKGDEVKCKLDKSEEnarsiEYEvlkkekqmkilenk 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 811 -KQLRDNDETKSQALEELTEfyEAKLQEKTTLLEEAQEDVrqqlREFEETKKQIE-EDEDREIQDIKTKYEKKLRDEKES 888
Cdd:pfam05483 596 cNNLKKQIENKNKNIEELHQ--ENKALKKKGSAENKQLNA----YEIKVNKLELElASAKQKFEEIIDNYQKEIEDKKIS 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 889 NLRLKGE---TGIMRKKFSSLQKEIEERTndietlkgeQMKLQGVIKSLEKDIQGLKREIQERDEtiqdkEKRIYdlKKK 965
Cdd:pfam05483 670 EEKLLEEvekAKAIADEAVKLQKEIDKRC---------QHKIAEMVALMEKHKHQYDKIIEERDS-----ELGLY--KNK 733
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 767902640 966 NQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAElenfHKQNT 1016
Cdd:pfam05483 734 EQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKME----AKENT 780
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-1025 |
6.26e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 675 IKREREVGFAEEVLVTKTDMEEKAQVMLELKtRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTE 754
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 755 KEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQAleeltefYEAK 834
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA-------EEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 835 LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlrlkgetgimRKKFSSLQKEIEERT 914
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE------------KKKIAHLKKEEEKKA 1770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 915 NDIETLKGEQMKlQGVIKSLEKDIQGLKREIQE---RDETIQD--KEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEP 989
Cdd:PTZ00121 1771 EEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDifdNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAF 1849
|
330 340 350
....*....|....*....|....*....|....*.
gi 767902640 990 RENEIRVMKEQIQEMEAElENFHKQNTQLELNITEL 1025
Cdd:PTZ00121 1850 EKHKFNKNNENGEDGNKE-ADFNKEKDLKEDDEEEI 1884
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
766-1010 |
1.68e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 766 IEDLLDKQSRELQDMECCNNQKLLLE-YEKYQELQLKSQRMQEE---YEKQLRDNDETKSQALEELTEfYEAKLQEKTTL 841
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDlHERLNGLESELAELDEEierYEEQREQARETRDEADEVLEE-HEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 842 lEEAQEDVRQQLREFEETKkqieEDEDREIQDIKTKYEKkLRDEKESnlrLKGETGimrkkFSSLqkeieertnDIETLK 921
Cdd:PRK02224 257 -EAEIEDLRETIAETERER----EELAEEVRDLRERLEE-LEEERDD---LLAEAG-----LDDA---------DAEAVE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 922 GEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQI 1001
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
....*....
gi 767902640 1002 QEMEAELEN 1010
Cdd:PRK02224 394 EELRERFGD 402
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
794-1022 |
2.37e-09 |
|
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: 61.30 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 794 KYQELQLKSQRMQEEYE-KQLRDNDETKSQALEELTEFYEAKLQEKTTlleeaqedvRQQLREFEETKKQIEEDEDREIQ 872
Cdd:pfam05557 8 KARLSQLQNEKKQMELEhKRARIELEKKASALKRQLDRESDRNQELQK---------RIRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 873 DIKTKYEK---KLRDEKESNLRLKGETgimrkkFSSLQKEIEErtndietLKGEQMKLQGVIKSLEKDIQGLKREIQERD 949
Cdd:pfam05557 79 RLKKKYLEalnKKLNEKESQLADAREV------ISCLKNELSE-------LRRQIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902640 950 ETIQDKEKRIYDLKKKNQELGkfkfVLDYKIKELKKQIEPRENEIRVMK------EQIQEMEAELENFHKQNTQLELNI 1022
Cdd:pfam05557 146 AKASEAEQLRQNLEKQQSSLA----EAEQRIKELEFEIQSQEQDSEIVKnskselARIPELEKELERLREHNKHLNENI 220
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
796-1036 |
2.61e-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: 60.55 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 796 QELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIK 875
Cdd:COG4942 27 AELEQLQQEIAEL-EKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAELAELEKEIAELR-AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 876 TKYEKKLRdekesNLRLKGETGIMRKKFSSlqkeieertNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDK 955
Cdd:COG4942 104 EELAELLR-----ALYRLGRQPPLALLLSP---------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 956 EKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQE 1035
Cdd:COG4942 170 EAERAELEALLAELEE-------ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
.
gi 767902640 1036 M 1036
Cdd:COG4942 243 T 243
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
675-1045 |
7.34e-09 |
|
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: 59.75 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 675 IKREREVGFAE-EVLVTKTDMEEKAQVMLELKTRVEEL-KMENEYQ---------LRLKDMNYSEKIKELTDKFIQEME- 742
Cdd:pfam05557 23 LEHKRARIELEkKASALKRQLDRESDRNQELQKRIRLLeKREAEAEealreqaelNRLKKKYLEALNKKLNEKESQLADa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 743 -----SLKTKNQVLRTEKEKQDVYHHEHIEDLLDKQSR-ELQDMECCNNQKLLLEYEKYQ-ELQLKSQRMQE-EYEKQLR 814
Cdd:pfam05557 103 revisCLKNELSELRRQIQRAELELQSTNSELEELQERlDLLKAKASEAEQLRQNLEKQQsSLAEAEQRIKElEFEIQSQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 815 DND--ETKS---------------QALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEETKkqiEEDEDREIQdiKTK 877
Cdd:pfam05557 183 EQDseIVKNskselaripelekelERLREHNKHLN-ENIENKLLLKEEVEDLKRKLEREEKYR---EEAATLELE--KEK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 878 YEKKLRDEKesnlRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEK 957
Cdd:pfam05557 257 LEQELQSWV----KLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 958 RIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENE-------------IRVMKEQIQEMEAELENFHKQNTQLELNITE 1024
Cdd:pfam05557 333 KLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKEltmsnyspqllerIEEAEDMTQKMQAHNEEMEAQLSVAEEELGG 412
|
410 420
....*....|....*....|.
gi 767902640 1025 LWQKLRATDQEMRRERQKPCL 1045
Cdd:pfam05557 413 YKQQAQTLERELQALRQQESL 433
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
833-990 |
1.10e-08 |
|
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: 56.86 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 833 AKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKL---RDEKESNlRLKGETGIMRKKFSSLQKE 909
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLgnvRNNKEYE-ALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 910 IEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDlkkknqelgkfkfvldyKIKELKKQIEP 989
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA-----------------EREELAAKIPP 174
|
.
gi 767902640 990 R 990
Cdd:COG1579 175 E 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
900-1042 |
1.25e-08 |
|
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: 56.86 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIyDLKKKNQELGkfkfVLDYK 979
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-GNVRNNKEYE----ALQKE 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902640 980 IKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQK 1042
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
789-1028 |
3.78e-08 |
|
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: 56.36 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 789 LLEYEKYQELQLKSQRMQEEYEKQLRD------NDETKSQALEELTEFYEAKLQ----EKTTLLEEAQEdVRQQLREF-- 856
Cdd:pfam15905 58 SLELKKKSQKNLKESKDQKELEKEIRAlvqergEQDKRLQALEEELEKVEAKLNaavrEKTSLSASVAS-LEKQLLELtr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 857 -----------EETKKQIE-------------EDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 912
Cdd:pfam15905 137 vnellkakfseDGTQKKMSslsmelmklrnklEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 913 RTNDIETLKGEQMKLQGVIKSLEKdiqgLKREIQERDETiqdkekriydLKKKNQELGKFKFVLDYKIKELKKQIEPR-- 990
Cdd:pfam15905 217 EKSETEKLLEYITELSCVSEQVEK----YKLDIAQLEEL----------LKEKNDEIESLKQSLEEKEQELSKQIKDLne 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767902640 991 ---------ENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQK 1028
Cdd:pfam15905 283 kckllesekEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
699-1044 |
4.83e-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: 57.44 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 699 QVMLELKTRVEELKMENE--YQLRLKDMNYSEKIKELTDKFIQEMESLK-----------TKNQVLRT------------ 753
Cdd:pfam15921 110 QSVIDLQTKLQEMQMERDamADIRRRESQSQEDLRNQLQNTVHELEAAKclkedmledsnTQIEQLRKmmlshegvlqei 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 754 --------EKEKQDVYHHEHIEDL--------LDKQSRELQ--------------------DMECCNNQKLLLEYEKYQE 797
Cdd:pfam15921 190 rsilvdfeEASGKKIYEHDSMSTMhfrslgsaISKILRELDteisylkgrifpvedqlealKSESQNKIELLLQQHQDRI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 798 LQLKSQR---------------------------MQEE-------YEKQLRDNDETKSQALEELTE---FYEAKLQ--EK 838
Cdd:pfam15921 270 EQLISEHeveitgltekassarsqansiqsqleiIQEQarnqnsmYMRQLSDLESTVSQLRSELREakrMYEDKIEelEK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 839 TTLLEEAQ-EDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDI 917
Cdd:pfam15921 350 QLVLANSElTEARTERDQFSQESGNLDDQLQKLLADLH-KREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 918 EtlkgeqmKLQGVIKSLEKDIQGlkrEIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKEL---KKQIEPRENEI 994
Cdd:pfam15921 429 Q-------RLEALLKAMKSECQG---QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTV 498
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 767902640 995 RVMKEQIQEMEAELENFHKQNTQL----ELNITELwQKLRaTDQEMRRERQKPC 1044
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLrsrvDLKLQEL-QHLK-NEGDHLRNVQTEC 550
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
816-1013 |
6.04e-08 |
|
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: 55.84 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 816 NDETKSQALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEetkKQIEEDEDrEIQDIKTKYEKKLRDEKESnlrlkge 895
Cdd:cd22656 108 DDEELEEAKKTIKALLD-DLLKEAKKYQDKAAKVVDKLTDFE---NQTEKDQT-ALETLEKALKDLLTDEGGA------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 896 tgIMRKKFSSLQKEIEERTNDIetlkgeqmklqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKknqelgkfkfv 975
Cdd:cd22656 176 --IARKEIKDLQKELEKLNEEY-------------AAKLKAKIDELKALIADDEAKLAAALRLIADLTA----------- 229
|
170 180 190
....*....|....*....|....*....|....*...
gi 767902640 976 LDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHK 1013
Cdd:cd22656 230 ADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKD 267
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
900-1041 |
9.40e-08 |
|
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: 55.54 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfVLDYK 979
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA---ELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 980 IKELKKQI-----------------------------------EPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITE 1024
Cdd:COG4942 103 KEELAELLralyrlgrqpplalllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170
....*....|....*..
gi 767902640 1025 LWQKLRATDQEMRRERQ 1041
Cdd:COG4942 183 LEEERAALEALKAERQK 199
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
482-669 |
1.02e-07 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 55.69 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 482 GGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSYNCVT 561
Cdd:COG2319 6 GAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 562 VSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQAHAG 639
Cdd:COG2319 86 FSPDGRLLASASADGTVRlwDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRL--WDLATGKLLRTLTGHSG 163
|
170 180 190
....*....|....*....|....*....|..
gi 767902640 640 PITkmLLTF--DDQFLLTAAEDGclfTWKVFD 669
Cdd:COG2319 164 AVT--SVAFspDGKLLASGSDDG---TVRLWD 190
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
847-1036 |
1.39e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 847 EDVRQQLRE-FEETKKQIEEDEDREIQDIKTKYEKKLRD------EKESNLRLKGETgimRKKFSSLQKEIEERTNDIET 919
Cdd:PRK02224 179 ERVLSDQRGsLDQLKAQIEEKEEKDLHERLNGLESELAEldeeieRYEEQREQARET---RDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 920 LKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKnQELGKFKF-VLDYKIKELKKQIEPRENEIRVMK 998
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADAeAVEARREELEDRDEELRDRLEECR 334
|
170 180 190
....*....|....*....|....*....|....*...
gi 767902640 999 EQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEM 1036
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
836-1042 |
1.48e-07 |
|
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: 54.77 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 836 QEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTN 915
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 916 DIETLKGE---------QMKLQGVIKSL--EKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELK 984
Cdd:COG4942 98 ELEAQKEElaellralyRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767902640 985 KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQK 1042
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
797-1041 |
1.69e-07 |
|
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: 55.29 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 797 ELQLKSQRMQEEYeKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEaQEDVRQQLREFEEtkkqieededreiqDIKT 876
Cdd:pfam07888 77 ELESRVAELKEEL-RQSREKHEELEEKYKELSASSEELSEEKDALLAQ-RAAHEARIRELEE--------------DIKT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 877 KYEKKLrdEKESNL-RLKGETgimrKKFSSLQKEIEErtnDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDK 955
Cdd:pfam07888 141 LTQRVL--ERETELeRMKERA----KKAGAQRKEEEA---ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 956 EKRIYDLKKKNQELGKFKFVLDYKIKELK----------KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL 1025
Cdd:pfam07888 212 QDTITTLTQKLTTAHRKEAENEALLEELRslqerlnaseRKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADA 291
|
250
....*....|....*.
gi 767902640 1026 WQKLRATDQEMRRERQ 1041
Cdd:pfam07888 292 SLALREGRARWAQERE 307
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
778-1041 |
1.99e-07 |
|
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: 55.13 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 778 QDMECCNNQKLLLEYEKYQELQ-LKSQRMQEEYEKQLRDNDetKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREF 856
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEkMEQERLRQEKEEKAREVE--RRRKLEEAEKARQAEMDRQAAIYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 857 EETKkqiEEDEDREIQDIKTK-----------YEKKLRDEKESNLRLKGETGIMRKKF---SSLQKEIEERTNDIETLKG 922
Cdd:pfam17380 351 ERIR---QEERKRELERIRQEeiameisrmreLERLQMERQQKNERVRQELEAARKVKileEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 923 EQ-----MKLQGVIKSLEKDIQGLKREIQERDETI----QDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENE 993
Cdd:pfam17380 428 EQeearqREVRRLEEERAREMERVRLEEQERQQQVerlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767902640 994 IRVMKEQIQEMEAELENfhKQNTQLELNITELWQKLRATDQEMRRERQ 1041
Cdd:pfam17380 508 MIEEERKRKLLEKEMEE--RQKAIYEEERRREAEEERRKQQEMEERRR 553
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
816-1022 |
2.30e-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: 53.00 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 816 NDETKSQALEELTEfYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDrEIQDIKTKYEKKLRDEKESNLRLKge 895
Cdd:COG1579 1 AMPEDLRALLDLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 896 tgimrkkfsslqkEIEERTNDIETLKgeqmklqgVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfv 975
Cdd:COG1579 77 -------------KYEEQLGNVRNNK--------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEA---- 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767902640 976 ldyKIKELKKQIEPRENEIRvmkEQIQEMEAELENFHKQNTQLELNI 1022
Cdd:COG1579 132 ---ELAELEAELEEKKAELD---EELAELEAELEELEAEREELAAKI 172
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
754-1042 |
2.44e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 754 EKEKQDVyhHEHIEDLLDKQSRELQDMECCNNQKllleyEKYQELQLKSQRMQEEYEkQLRDNDETKSQALEELTEFYEA 833
Cdd:PRK02224 198 EKEEKDL--HERLNGLESELAELDEEIERYEEQR-----EQARETRDEADEVLEEHE-ERREELETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 834 KLQEKTTLLEEAQeDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKK--LRDEKESnlrLKGETGIMRKKFSSLQKEIE 911
Cdd:PRK02224 270 TEREREELAEEVR-DLRERLEELEEERDDLLAEAGLDDADAEAVEARReeLEDRDEE---LRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 912 ERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK--------------NQELGKFKFVLD 977
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdlgnaedfLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 978 YKIKELKKQIEPRENEIRVM----------------------------KEQIQEMEAELENFHKQNTQLELNITELwQKL 1029
Cdd:PRK02224 426 EREAELEATLRTARERVEEAealleagkcpecgqpvegsphvetieedRERVEELEAELEDLEEEVEEVEERLERA-EDL 504
|
330
....*....|...
gi 767902640 1030 RATDQEMRRERQK 1042
Cdd:PRK02224 505 VEAEDRIERLEER 517
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
803-1041 |
3.10e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 803 QRMQEEYekqLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQedvrQQLREFEETKKQIEEDEDREIqdiktkYEKKL 882
Cdd:COG3206 155 NALAEAY---LEQNLELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQKNGLVDLSEEAKL------LLQQL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 883 RDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQmklqgVIKSLEKDIQGLKREIQERDETIQDKEKRIYDL 962
Cdd:COG3206 222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902640 963 KKKNQELGKFKFvldykiKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLelnitelwQKLRATDQEMRRERQ 1041
Cdd:COG3206 297 RAQIAALRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL--------PELEAELRRLEREVE 361
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
706-1041 |
3.54e-07 |
|
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: 54.41 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 706 TRVEELKMENEYQLrlkdmnysEKIKELTDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedlldkqsreLQDmeccnn 785
Cdd:pfam01576 1 TRQEEEMQAKEEEL--------QKVKERQQKAESELKELEKKHQQLCEEKNA-------------------LQE------ 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 786 qKLLLEYEKYQElqlksqrmQEEYEKQLrdndETKSQALEELTEFYEAKLQE---KTTLLEEAQEDVRQQLREFEEtkkQ 862
Cdd:pfam01576 48 -QLQAETELCAE--------AEEMRARL----AARKQELEEILHELESRLEEeeeRSQQLQNEKKKMQQHIQDLEE---Q 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 863 IEEDED--REIQDIKTKYEKKLRDEKESNLRLKGEtgimRKKFSSLQKEIEERTNDIETLKGEQmklqgvikslEKDIQG 940
Cdd:pfam01576 112 LDEEEAarQKLQLEKVTTEAKIKKLEEDILLLEDQ----NSKLSKERKLLEERISEFTSNLAEE----------EEKAKS 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 941 LKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAEL-------ENFHK 1013
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELqaalarlEEETA 257
|
330 340
....*....|....*....|....*...
gi 767902640 1014 QNTQLELNITELWQKLRATDQEMRRERQ 1041
Cdd:pfam01576 258 QKNNALKKIRELEAQISELQEDLESERA 285
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
891-1038 |
3.75e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.75 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 891 RLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELG 970
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902640 971 KFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFhkQNTQLELNITELWQKLRATDQEMRR 1038
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDELLKEANR 194
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
821-1043 |
3.76e-07 |
|
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: 53.61 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 821 SQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDR--EIQDIKTKYEKKLRDEKESNLRLKGETGI 898
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 899 MRKKFSSLQKEIEERTNDIETLkGEQMKLQGVIKS-----LEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFK 973
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRL-GRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 974 FVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKP 1043
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
693-1035 |
4.30e-07 |
|
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: 54.35 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 693 DMEEKAQVML-ELKTRVEELKMENEYQLRLKDMNYSEKI------KELTDKFI---------------------QEMESL 744
Cdd:pfam15921 374 NLDDQLQKLLaDLHKREKELSLEKEQNKRLWDRDTGNSItidhlrRELDDRNMevqrleallkamksecqgqmeRQMAAI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 745 KTKNQVLrtEKEKQDVYHHEHIEDLLDKQSREL--QDMECCNNQKLLLEYE-KYQELQLKSQRMQEEYEKqLRDNDETKS 821
Cdd:pfam15921 454 QGKNESL--EKVSSLTAQLESTKEMLRKVVEELtaKKMTLESSERTVSDLTaSLQEKERAIEATNAEITK-LRSRVDLKL 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 822 QALEEL-----------TEFYEAKLQ--EKTTLLE---EAQEDVRQQLREFEETKK--QIEEDE-DREIQDIKTKYE--K 880
Cdd:pfam15921 531 QELQHLknegdhlrnvqTECEALKLQmaEKDKVIEilrQQIENMTQLVGQHGRTAGamQVEKAQlEKEINDRRLELQefK 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 881 KLRDEKESNLR-LKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIK-------SLEKDIQGLKREIQERDETI 952
Cdd:pfam15921 611 ILKDKKDAKIReLEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKtsrnelnSLSEDYEVLKRNFRNKSEEM 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 953 QDKEKRI-YDLKKKNQELGKFKFVLD-------YKIK---ELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELN 1021
Cdd:pfam15921 691 ETTTNKLkMQLKSAQSELEQTRNTLKsmegsdgHAMKvamGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEE 770
|
410
....*....|....
gi 767902640 1022 ITELWQKLRATDQE 1035
Cdd:pfam15921 771 KNKLSQELSTVATE 784
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
686-1041 |
4.34e-07 |
|
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: 54.41 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 686 EVLVTKTDMEEKAQVMLELKTRVEelKMENEYQLRLKdmnysekiKEltDKFIQEMESLKTKNQVLRTEKEKQDVYHHEH 765
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHE--AMISDLEERLK--------KE--EKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 766 IEDL---LDKQSRELQ------DMECCNNQKLLleyEKYQELQLKSQRMQE--EYEKQLRDNDETKSQALEELTEFYEAK 834
Cdd:pfam01576 231 IAELraqLAKKEEELQaalarlEEETAQKNNAL---KKIRELEAQISELQEdlESERAARNKAEKQRRDLGEELEALKTE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 835 LqEKTTLLEEAQEDVR-QQLREFEETKKQIEED---EDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEI 910
Cdd:pfam01576 308 L-EDTLDTTAAQQELRsKREQEVTELKKALEEEtrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 911 EERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPR 990
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 767902640 991 ENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRR-ERQ 1041
Cdd:pfam01576 467 ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNvERQ 518
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
842-1006 |
5.24e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 53.71 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 842 LEEAQEDVRQQLREFEETKKQIEEDEDREIQdikTKYEKKLRdekesnlrlkgetgimrkkfsslqkeieertndietlk 921
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEEREL---TEEEEEIR-------------------------------------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 922 geqmKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK-NQELGKFKFV--LDYKIKELKKQIEPRENEIRVMK 998
Cdd:COG2433 417 ----RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEeRREIRKDREIsrLDREIERLERELEEERERIEELK 492
|
....*...
gi 767902640 999 EQIQEMEA 1006
Cdd:COG2433 493 RKLERLKE 500
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
673-1050 |
8.11e-07 |
|
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: 53.20 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 673 RGIKREREVGFAEEVlvTKTDMEEKAQVMLELktrvEELKMENEYQLrlkdmnysEKIKEltdkfiqemESLKTKNQVLR 752
Cdd:pfam17380 310 REVERRRKLEEAEKA--RQAEMDRQAAIYAEQ----ERMAMEREREL--------ERIRQ---------EERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 753 TEKEKQDVYHHEHIEDLL----DKQSRELQDMECCNNQKLLLEyekyqELQLKSQRMQEEYEKQLRDNDETKSQALEELT 828
Cdd:pfam17380 367 QEEIAMEISRMRELERLQmerqQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQIRAEQEEARQREVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 829 EFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQ--IEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKkfsSL 906
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKklELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK---LL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 907 QKEIEERTNDIetLKGEQMKLQGVIKSLEKDIQGlKREIQERDETIQDKEKRIYDLKKKNQELGKFK--------FVLDY 978
Cdd:pfam17380 519 EKEMEERQKAI--YEEERRREAEEERRKQQEMEE-RRRIQEQMRKATEERSRLEAMEREREMMRQIVesekaraeYEATT 595
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902640 979 KIKELKKQIEPRENEIrvmkeQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKP-----CLISGPC 1050
Cdd:pfam17380 596 PITTIKPIYRPRISEY-----QPPDVESHMIRFTTQSPEWATPSPATWNPEWNTVTAEEETPGIPiihsqCQVNGEC 667
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
863-1042 |
9.10e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 863 IEEDEDRE--------IQDIKTKYEKKLRDEKESNLRLKG-ETGIMRKkfSSLQKEIEERTNDIETLKGEQMKLQGVIKS 933
Cdd:PRK03918 141 LESDESREkvvrqilgLDDYENAYKNLGEVIKEIKRRIERlEKFIKRT--ENIEELIKEKEKELEEVLREINEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 934 LEKDIQGLKREIQERDETiqdKEKrIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEA------- 1006
Cdd:PRK03918 219 LREELEKLEKEVKELEEL---KEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaee 294
|
170 180 190
....*....|....*....|....*....|....*...
gi 767902640 1007 --ELENFHKQNTQLELNITELWQKLRATDQEMRRERQK 1042
Cdd:PRK03918 295 yiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
726-1007 |
1.05e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.84 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 726 YSEKIKELTDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiEDLLDKQSRELQDmeccNNQKLLLEYEKYQEL--QLKSQ 803
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEK---------RDELNAQVKELRE----EAQELREKRDELNEKvkELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 804 RmqEEYEKQLRDNDETKSQALEELtefyeAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED--REIQDIKTKYE-- 879
Cdd:COG1340 80 R--DELNEKLNELREELDELRKEL-----AELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKElvEKIKELEKELEka 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 880 KKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI 959
Cdd:COG1340 153 KKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEI 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767902640 960 YDLKKKNQELgkfkfvldykIKELKKQIEPRENEIRVMKEQIQEMEAE 1007
Cdd:COG1340 233 IELQKELREL----------RKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
501-540 |
1.35e-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: 1.35e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 767902640 501 SLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 540
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
685-971 |
1.38e-06 |
|
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: 52.66 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 685 EEVLVTKTDMEEKAQVMLELKTRVEELKME---NEYQLRLKDMNYSekikeltdkfiQEMESLKTKNQVLRTEKEKQDVY 761
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqDLQDVRLHLQQCS-----------QELALKLTALHALQLTLTQERVR 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 762 HH-----EHIEDLLDKQSRELQDMEccnNQKLLLEYEKyQELQLKSQRMQEEYE--KQLRDNDETKSQALEELTEFYEAK 834
Cdd:TIGR00618 662 EHalsirVLPKELLASRQLALQKMQ---SEKEQLTYWK-EMLAQCQTLLRELEThiEEYDREFNEIENASSSLGSDLAAR 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 835 LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQdIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE-- 912
Cdd:TIGR00618 738 EDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQ-TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSde 816
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767902640 913 --RTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGK 971
Cdd:TIGR00618 817 diLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
676-1037 |
1.65e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 676 KREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEEL------------KMENEYQLRLKDMN-YSEKIKELTDKfIQEME 742
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEELrerfgdapvdlgNAEDFLEELREERDeLREREAELEAT-LRTAR 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 743 SLKTKNQVLRTEKE----KQDVYHHEHIEDLLDKQSR------ELQDMEccnnqkllleyEKYQELQLKSQRMQE--EYE 810
Cdd:PRK02224 440 ERVEEAEALLEAGKcpecGQPVEGSPHVETIEEDRERveeleaELEDLE-----------EEVEEVEERLERAEDlvEAE 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 811 KQLRDNDEtKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDR--EIQDIKTKYEKKLRDEKES 888
Cdd:PRK02224 509 DRIERLEE-RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEaeEAREEVAELNSKLAELKER 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 889 NLRLkgetgimrKKFSSLQKEIEERTNDIETLKgEQMKLQGVIKSLEKDIQGLKRE-IQERDETIQdkEKRIYDLKKKNQ 967
Cdd:PRK02224 588 IESL--------ERIRTLLAAIADAEDEIERLR-EKREALAELNDERRERLAEKRErKRELEAEFD--EARIEEAREDKE 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 968 ELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEA-------------ELENFHKQNTQLElnitELWQKLRAtdq 1034
Cdd:PRK02224 657 RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEElrerrealenrveALEALYDEAEELE----SMYGDLRA--- 729
|
...
gi 767902640 1035 EMR 1037
Cdd:PRK02224 730 ELR 732
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
818-1010 |
1.84e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 818 ETKSQALEELTEfyE-AKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED-----REIQDIktkyEKKLRDEKESNLR 891
Cdd:COG4913 613 AALEAELAELEE--ElAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAEL----EAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 892 LKGetgimrkkfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI-----YDLKKKN 966
Cdd:COG4913 687 LAA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERF 755
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767902640 967 QELGKFKFVldykiKELKKQIeprENEIRVMKEQIQEMEAELEN 1010
Cdd:COG4913 756 AAALGDAVE-----RELRENL---EERIDALRARLNRAEEELER 791
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
736-1040 |
2.46e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 736 KFIQEMESLKTKNQVLRTEKEKQDVYHHehIEDLLDKQSRELQDMEccnnqkllleyEKYQELQLKSQRMqeEYEKQLRD 815
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAE--LQEELEELEEELEELE-----------AELEELREELEKL--EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 816 NDETKSQALEELTEFYE--AKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEdedrEIQDIKTKYEKKLRDEKESNLRLK 893
Cdd:COG4717 130 LYQELEALEAELAELPErlEELEERLEELRELEEELEELEAELAELQEELEE----LLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 894 GETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQ-------------------------GVIKSLEKDIQGL------- 941
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAAleerlkearlllliaaallallglgGSLLSLILTIAGVlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 942 ------------KREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEpRENEIRVMKEQIQEMEAELe 1009
Cdd:COG4717 286 lallflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD-RIEELQELLREAEELEEEL- 363
|
330 340 350
....*....|....*....|....*....|.
gi 767902640 1010 nfhkQNTQLELNITELWQKLRATDQEMRRER 1040
Cdd:COG4717 364 ----QLEELEQEIAALLAEAGVEDEEELRAA 390
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
879-1042 |
2.84e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 879 EKKLRDEKESNLRLKGETGIMR-KKFSSLQKEIEERTNDIETLKGEQMKLQgvikSLEKDIQGLKREIQERDETIQDKEK 957
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 958 --RIYDLKKKNQELGKFKFVLDYKIKELKKQIEPR---ENEIRVMKEQIQEMEAELENFHKQNT--------QLELNITE 1024
Cdd:COG4717 124 llQLLPLYQELEALEAELAELPERLEELEERLEELrelEEELEELEAELAELQEELEELLEQLSlateeelqDLAEELEE 203
|
170
....*....|....*...
gi 767902640 1025 LWQKLRATDQEMRRERQK 1042
Cdd:COG4717 204 LQQRLAELEEELEEAQEE 221
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
880-1042 |
2.86e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 880 KKLRDEKESNLRLKGETGIMrkkFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI 959
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 960 YDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRE 1039
Cdd:COG4372 83 EELNEQLQAAQA-------ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
...
gi 767902640 1040 RQK 1042
Cdd:COG4372 156 EEQ 158
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
827-1042 |
2.99e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 827 LTEFYEAKLQEKttLLEEAQEDVRQQLREFEETKKQIEEDED--REIQDIKTKYEKKLRDEKESnlrlkgetgimRKKFS 904
Cdd:COG4717 39 LLAFIRAMLLER--LEKEADELFKPQGRKPELNLKELKELEEelKEAEEKEEEYAELQEELEEL-----------EEELE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 905 SLQKEIEERTNDIETLK---------GEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELgkfKFV 975
Cdd:COG4717 106 ELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL---EEL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902640 976 LDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQK 1042
Cdd:COG4717 183 LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
726-1042 |
3.33e-06 |
|
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: 51.51 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 726 YSEKIKELTDKFI---QEMESLKTKNQVLRTEKEKqdvyhhehIEDLLDKQSRElQDMECCNNQKLLLeyekyqelqlKS 802
Cdd:TIGR00618 561 LKEQMQEIQQSFSiltQCDNRSKEDIPNLQNITVR--------LQDLTEKLSEA-EDMLACEQHALLR----------KL 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 803 QRMQEEYEKQLRDNDETKSQALEELtefyeAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKY---- 878
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELALKLT-----ALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywk 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 879 ------EKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQG-VIKSLEKDIQGLKREIQERDET 951
Cdd:TIGR00618 697 emlaqcQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARtVLKARTEAHFNNNEEVTAALQT 776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 952 IQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRA 1031
Cdd:TIGR00618 777 GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEE 856
|
330
....*....|.
gi 767902640 1032 TDQEMRRERQK 1042
Cdd:TIGR00618 857 CSKQLAQLTQE 867
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
806-1032 |
3.43e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 806 QEEYEKQLRDNDETKSQALEELtefyeAKLQEKttlLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYEKKlRDE 885
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAEL-----DALQAE---LEELNEEYNELQAELEALQAEIDKLQ-AEIAEAEAEIEER-REE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 886 KESNLRLKGETGIMRKKFSSL--QKEIEE---RTNDIETLKGEQMKLqgvIKSLEKDiqglKREIQERDETIQDKEKRIY 960
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLlgSESFSDfldRLSALSKIADADADL---LEELKAD----KAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902640 961 DLKKKNQElgkfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRAT 1032
Cdd:COG3883 161 ALKAELEA----------AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
691-1040 |
3.46e-06 |
|
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: 51.36 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 691 KTDMEEKAQVMLELKTRVEELKMENEyqlrlkdmNYSEKIKELTdkfiqemESLKTKNQ---VLRTEKEKQDVYHHEHiE 767
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQNS--------DCKQHIEVLK-------ESLTAKEQraaILQTEVDALRLRLEEK-E 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 768 DLLDKQSRELQDMeccNNQKLLLEYE-------------KYQELQLKSQRMQEeyekQLRDNDetksQALEELTEFYEAk 834
Cdd:pfam10174 359 SFLNKKTKQLQDL---TEEKSTLAGEirdlkdmldvkerKINVLQKKIENLQE----QLRDKD----KQLAGLKERVKS- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 835 LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREiqdiktkyEKKLRDEKESnlrLKGETGIMRKKFSSLQKEIEERT 914
Cdd:pfam10174 427 LQTDSSNTDTALTTLEEALSEKERIIERLKEQRERE--------DRERLEELES---LKKENKDLKEKVSALQPELTEKE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 915 NDIETLKGEQ-------MKLQGVIKSLEKDIQGLKRE----------IQERDETIQDKEK---RIYDLKK----KNQELG 970
Cdd:pfam10174 496 SSLIDLKEHAsslassgLKKDSKLKSLEIAVEQKKEEcsklenqlkkAHNAEEAVRTNPEindRIRLLEQevarYKEESG 575
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 971 KFKFVLDYKIKELKKQieprENEIRVMKEQIQEMEAELENFHKQNTQLELNItelwqklRATDQEMRRER 1040
Cdd:pfam10174 576 KAQAEVERLLGILREV----ENEKNDKDKKIAELESLTLRQMKEQNKKVANI-------KHGQQEMKKKG 634
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
827-1042 |
3.52e-06 |
|
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: 51.17 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 827 LTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReIQDIKTKYEKKLRDEKESNLRLKGEtgimRKKFSSL 906
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEK-INNSNNKIKILEQQIKDLNDKLKKN----KDKINKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 907 QKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQ 986
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902640 987 IEPRENEIRVMKEQI-----------------QEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQK 1042
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLlklelllsnlkkkiqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ 254
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
728-1000 |
4.02e-06 |
|
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: 49.95 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 728 EKIKELTDKF---IQEMESLKTKNQVLRTE-----KEKqDVYHHEH-----IEDLLDKQSRELQ----DMECCNNQKLLL 790
Cdd:pfam09728 18 EKLAALCKKYaelLEEMKRLQKDLKKLKKKqdqlqKEK-DQLQSELskailAKSKLEKLCRELQkqnkKLKEESKKLAKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 791 EYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYE--AKLQEKTTLLEE------AQEDVRQQLRE------F 856
Cdd:pfam09728 97 EEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREklKSLIEQYELRELhfekllKTKELEVQLAEaklqqaT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 857 EETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEK 936
Cdd:pfam09728 177 EEEEKKAQEKEVAKARELKAQVQTLSETEKE----LREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEK 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902640 937 DIQGLKREIQERDetiqdkeKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQ 1000
Cdd:pfam09728 253 ENLTWKRKWEKSN-------KALLEMAEERQKLKE-------ELEKLQKKLEKLENLCRALQAE 302
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
882-1022 |
4.71e-06 |
|
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: 49.97 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 882 LRDEKESNLRLKGEtgIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGV------IKSLEKDIQGLKREIQERDETIQDK 955
Cdd:pfam17060 96 IPASFISALELKED--VKSSPRSEADSLGTPIKVDLLRNLKPQESPETPrrinrkYKSLELRVESMKDELEFKDETIMEK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 956 E-------KRIYDLKKKNQELGK-FKFVLDYK-----------------IKELKKQIEPRENEIRVMKEQIQEMEAELEN 1010
Cdd:pfam17060 174 DrelteltSTISKLKDKYDFLSReFEFYKQHHehggnnsiktatkhefiISELKRKLQEQNRLIRILQEQIQFDPGALHD 253
|
170
....*....|..
gi 767902640 1011 FHKQNTQLELNI 1022
Cdd:pfam17060 254 NGPKNLVLNGAI 265
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
764-973 |
4.97e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 764 EHIEDLLDKQS------------REL-QDMECCNNQKLLLE-----YEKYQELQLKS-----QRMQEEYEKQL---RDND 817
Cdd:PHA02562 154 KLVEDLLDISVlsemdklnkdkiRELnQQIQTLDMKIDHIQqqiktYNKNIEEQRKKngeniARKQNKYDELVeeaKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 818 ETKSQALEELTEF------YEAKLQEKTTLLEEAQEDVRQQLRE---FEE-----TKKQIEEDEDREIQDIKTK---YEK 880
Cdd:PHA02562 234 AEIEELTDELLNLvmdiedPSAALNKLNTAAAKIKSKIEQFQKVikmYEKggvcpTCTQQISEGPDRITKIKDKlkeLQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 881 KLRDEKEsnlRLKGETGIMrKKFSSLQKEIEERTNDIETLKGEqmklqgvIKSLEKDIQGLKREIQERDETIQDKEKRIY 960
Cdd:PHA02562 314 SLEKLDT---AIDELEEIM-DEFNEQSKKLLELKNKISTNKQS-------LITLVDKAKKVKAAIEELQAEFVDNAEELA 382
|
250
....*....|...
gi 767902640 961 DLKKKNQELGKFK 973
Cdd:PHA02562 383 KLQDELDKIVKTK 395
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
678-1007 |
6.67e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 678 EREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQlRLKDMNYSEKIKELTDKFIQEM----------ESLKTK 747
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-KAEDARKAEEARKAEDAKRVEIarkaedarkaEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 748 NQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQL-----KSQRMQEEYEKQLRDNDETKSQ 822
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkKAEEAKKDAEEAKKAEEERNNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 823 ALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIE---EDEDREIQDIKTKYEKKlrdEKESNLRLKGETGim 899
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakkAEEKKKADEAKKKAEEA---KKADEAKKKAEEA-- 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQErdetiqdKEKRIYDLKKKNQELgkfkfvldYK 979
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-------AKKKADAAKKKAEEK--------KK 1392
|
330 340
....*....|....*....|....*...
gi 767902640 980 IKELKKQIEprenEIRVMKEQIQEMEAE 1007
Cdd:PTZ00121 1393 ADEAKKKAE----EDKKKADELKKAAAA 1416
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
676-1042 |
7.57e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 676 KREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQlrlkdmnySEKIKELTDKfiQEMESLKTKNQVLRTEK 755
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK--------ADELKKAEEK--KKADEAKKAEEKKKADE 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 756 EKQDVYHHEHIEDLLDKQSRELQDMEccnnqklllEYEKYQELQLKSQRMQEEYEKQLRDndetKSQALEELTEFYEAKL 835
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKAD---------AAKKKAEEAKKAAEAAKAEAEAAAD----EAEAAEEKAEAAEKKK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 836 QEKTTLLEEAQEDVrQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEkesnLRLKGETgimRKKFSSLQKEIEERTN 915
Cdd:PTZ00121 1374 EEAKKKADAAKKKA-EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE----AKKKAEE---KKKADEAKKKAEEAKK 1445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 916 DIETLKG--EQMKLQGVIKSLE--KDIQGLKREIQERDETiQDKEKRIYDLKKKNQELGKfKFVLDYKIKELKKQIEPRE 991
Cdd:PTZ00121 1446 ADEAKKKaeEAKKAEEAKKKAEeaKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKK-AAEAKKKADEAKKAEEAKK 1523
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 767902640 992 NEIRVMKEQIQEMEaELENFHKQNTQLELNITELWQK---LRATDQEMRRERQK 1042
Cdd:PTZ00121 1524 ADEAKKAEEAKKAD-EAKKAEEKKKADELKKAEELKKaeeKKKAEEAKKAEEDK 1576
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
717-1042 |
7.75e-06 |
|
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: 50.11 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 717 YQLRLKDMNY--SEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHiEDLLDKQSRELQDMECcNNQKLLLEYEk 794
Cdd:pfam05483 61 YQEGLKDSDFenSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQEN-RKIIEAQRKAIQELQF-ENEKVSLKLE- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 795 yQELQLKSQRMQEEYEKQLRDN--DETKSQALEElTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE------- 865
Cdd:pfam05483 138 -EEIQENKDLIKENNATRHLCNllKETCARSAEK-TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENarlemhf 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 866 --DEDRE-IQDIKTKYEKKLRD-EKESNLRL--KGETGIMRKKFSSLQKEIEERTNDIEtlkgEQMKLQGvikslekdiQ 939
Cdd:pfam05483 216 klKEDHEkIQHLEEEYKKEINDkEKQVSLLLiqITEKENKMKDLTFLLEESRDKANQLE----EKTKLQD---------E 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 940 GLKREIQERDETiqdkekriydlkkkNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLE 1019
Cdd:pfam05483 283 NLKELIEKKDHL--------------TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHS 348
|
330 340
....*....|....*....|...
gi 767902640 1020 LNITELWQKLRATDQEMRRERQK 1042
Cdd:pfam05483 349 FVVTEFEATTCSLEELLRTEQQR 371
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
900-1042 |
8.72e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIqdkEKRIYDLKKKNQELGKFKFVL--- 976
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGSVSYLDVLLgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 977 ---DY-------------------KIKELKKQIEPRENEIRVMKEQIQEMEAELEnfhKQNTQLELNITELWQKLRATDQ 1034
Cdd:COG3883 113 sfsDFldrlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELE---AAKAELEAQQAEQEALLAQLSA 189
|
....*...
gi 767902640 1035 EMRRERQK 1042
Cdd:COG3883 190 EEAAAEAQ 197
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
62-420 |
8.79e-06 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 49.52 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 62 ALSISPNRRYLAiseTVQEKPAITIYELSSIPCRKrkVLNNFDFQVQkfiSMAFSPDSKYLLAqTSppESNLVYwLWEKQ 141
Cdd:COG2319 125 SVAFSPDGKTLA---SGSADGTVRLWDLATGKLLR--TLTGHSGAVT---SVAFSPDGKLLAS-GS--DDGTVR-LWDLA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 142 KVMAIVRIDTQNNPVYQVSFSPqDNTQVcVTG--NGMFKLLRFAEGTLKQTSfqRGEPQNYLAHTWVADDK-IVVGTDTG 218
Cdd:COG2319 193 TGKLLRTLTGHTGAVRSVAFSP-DGKLL-ASGsaDGTVRLWDLATGKLLRTL--TGHSGSVRSVAFSPDGRlLASGSADG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 219 KLFLfesgdqrWETsimvkeptNGSKSLDVIQESESliefpPVSSplpsyeqmVAASSHSQMsmpqvfaiaayskgFACS 298
Cdd:COG2319 269 TVRL-------WDL--------ATGELLRTLTGHSG-----GVNS--------VAFSPDGKL--------------LASG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 299 AGPGRVLLFEkmeekdfYRESREIRIPVDPQSndpsqsdkqDVLCLCFSPSEETLVASTSKNqlysiTMSLTEISKGEPA 378
Cdd:COG2319 307 SDDGTVRLWD-------LATGKLLRTLTGHTG---------AVRSVAFSPDGKTLASGSDDG-----TVRLWDLATGELL 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 767902640 379 HFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWNYET 420
Cdd:COG2319 366 RT----LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
730-1042 |
9.43e-06 |
|
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: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 730 IKELTDK--FIQEMESLKTKNQVL-RTEKEKQDVyhHEHIEDLLD---KQSRELQDMEccnnqkllleyEKYQELQ--LK 801
Cdd:pfam06160 72 AEELNDKyrFKKAKKALDEIEELLdDIEEDIKQI--LEELDELLEseeKNREEVEELK-----------DKYRELRktLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 802 SQRMQ-----EEYEKQLrDNDETKSQALEELTE---FYEAK------------LQEKT----TLLEEAQEDVRQQLREFE 857
Cdd:pfam06160 139 ANRFSygpaiDELEKQL-AEIEEEFSQFEELTEsgdYLEARevlekleeetdaLEELMedipPLYEELKTELPDQLEELK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 858 ETKKQIEEDE--------DREIQDIKTKYEKKLRDEKESNLrlkgetgimrKKFSSLQKEIEERtndIETLkgeqmklqg 929
Cdd:pfam06160 218 EGYREMEEEGyalehlnvDKEIQQLEEQLEENLALLENLEL----------DEAEEALEEIEER---IDQL--------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 930 vIKSLEKDIQGlKREIQERDETIqdkEKRIYDLKKKNQELG------KFKFVLDY----KIKELKKQIEPRENEIRVMKE 999
Cdd:pfam06160 276 -YDLLEKEVDA-KKYVEKNLPEI---EDYLEHAEEQNKELKeelervQQSYTLNEneleRVRGLEKQLEELEKRYDEIVE 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 767902640 1000 QIQ-------EMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQK 1042
Cdd:pfam06160 351 RLEekevaysELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREK 400
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
683-958 |
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 767902640 683 FAEEVLvTKTDMEEKAQVMLELktrVEELkmeNEYQLRLKDMnySEKIKELTD--KFIQEMESLKTKNQVLRTEKEKQDV 760
Cdd:COG4913 213 VREYML-EEPDTFEAADALVEH---FDDL---ERAHEALEDA--REQIELLEPirELAERYAAARERLAELEYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 761 YHHEHIEDLLDKQSRELQdmeccnnqkllleyEKYQELqlksqrmqeeyEKQLRDNDETKSQALEELTEFYEAKLQEKTT 840
Cdd:COG4913 284 WFAQRRLELLEAELEELR--------------AELARL-----------EAELERLEARLDALREELDELEAQIRGNGGD 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 841 LLEEAQEDVRQQlrefEETKKQIEEDEDReiqdiktkYEKKLRDekesnLRLKGETGimRKKFSSLQKEIEERtndIETL 920
Cdd:COG4913 339 RLEQLEREIERL----ERELEERERRRAR--------LEALLAA-----LGLPLPAS--AEEFAALRAEAAAL---LEAL 396
|
250 260 270
....*....|....*....|....*....|....*...
gi 767902640 921 KGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKR 958
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
709-949 |
1.08e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 709 EELKMENEYQLRLKDMNySEKIKELTDKF---IQEMESLKT-----KNQVLRTEKEKQDVyhHEHIEDLLDKQSRELQDM 780
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKN-GENIARKQNKYdelVEEAKTIKAeieelTDELLNLVMDIEDP--SAALNKLNTAAAKIKSKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 781 ECCnnQKLLLEYEKYQELQLKSQrmqeeyekQLRDNDETKSQALEELTEfyeakLQEKTTLLEEAQEDVRQQLREFEETK 860
Cdd:PHA02562 272 EQF--QKVIKMYEKGGVCPTCTQ--------QISEGPDRITKIKDKLKE-----LQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 861 KqieededrEIQDIKTKYEKKLRDekesnlrLKGEtgimRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQG 940
Cdd:PHA02562 337 K--------KLLELKNKISTNKQS-------LITL----VDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
....*....
gi 767902640 941 LKREIQERD 949
Cdd:PHA02562 398 LVKEKYHRG 406
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
701-1042 |
1.40e-05 |
|
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: 49.17 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 701 MLELKTR----VEELKMENEyqlrlKDMNYSEKIkeltDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedlLDKQSRE 776
Cdd:pfam15818 2 LLDFKTSlleaLEELRMRRE-----AETQYEEQI----GKIIVETQELKWQKETLQNQKET------------LAKQHKE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 777 LqdMECCNNQkllleyekyqeLQLKSQRMQEEYEK-QLRDndETKSQALEELTEFYEAKLQEKTTL---LEEAQEDVRQQ 852
Cdd:pfam15818 61 A--MAVFKKQ-----------LQMKMCALEEEKGKyQLAT--EIKEKEIEGLKETLKALQVSKYSLqkkVSEMEQKLQLH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 853 LREFEETKKQIEEDEdreiqdiktKYEKKLRDE----KESNLRLK---GETGIMRKKFSSLQKEIEertNDIETLKGEqm 925
Cdd:pfam15818 126 LLAKEDHHKQLNEIE---------KYYATITGQfglvKENHGKLEqnvQEAIQLNKRLSALNKKQE---SEICSLKKE-- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 926 kLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLkkknQELGKFKFVLDYKIKELKKQIEPRENEI--------RVM 997
Cdd:pfam15818 192 -LKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQEL----QERLNMELELNKKINEEITHIQEEKQDIiisfqhmqQLL 266
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 767902640 998 KEQIQ---EMEAELENFHKQNTQLElnitelwqklraTDQEMRRERQK 1042
Cdd:pfam15818 267 QQQTQantEMEAELKALKENNQTLE------------RDNELQREKVK 302
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
670-923 |
1.48e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 670 KDGRGIKREREVgFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYqLRLKDMNYSEKIKELTDK----FIQ----EM 741
Cdd:TIGR02169 723 KEIEQLEQEEEK-LKERLEELEEDLSSLEQEIENVKSELKELEARIEE-LEEDLHKLEEALNDLEARlshsRIPeiqaEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 742 ESLKT--KNQVLRTEKEKQDVYHHEHIEDLLDKQSRELQD-MECCNNQK---------LLLEYEKYQELQLKSQRMQEEY 809
Cdd:TIGR02169 801 SKLEEevSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEqRIDLKEQIksiekeienLNGKKEELEEELEELEAALRDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 810 EKQL------RDNDETKSQALEELTEFYEAKLQEKTTL---LEEAQEDVRQQLREFEETKKQIEED--EDREIQDIKTKY 878
Cdd:TIGR02169 881 ESRLgdlkkeRDELEAQLRELERKIEELEAQIEKKRKRlseLKAKLEALEEELSEIEDPKGEDEEIpeEELSLEDVQAEL 960
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767902640 879 EKK---LRDEKESNLRLKGETGIMRKKFSSLQ----------KEIEERTNDIETLKGE 923
Cdd:TIGR02169 961 QRVeeeIRALEPVNMLAIQEYEEVLKRLDELKekrakleeerKAILERIEEYEKKKRE 1018
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
712-1018 |
1.59e-05 |
|
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: 49.27 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 712 KMENEYQLRLK-----DMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKE------KQDVYHhEHIEDLLDKQSrelqdm 780
Cdd:TIGR00606 605 QNKNHINNELEskeeqLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQramlagATAVYS-QFITQLTDENQ------ 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 781 ECCNNQKLLLEYEK-YQELQLKSQRM-------QEEYEKQLRDNDETKSQALEeLTEFYEAKLQEKTTLLEEAQEDVRQQ 852
Cdd:TIGR00606 678 SCCPVCQRVFQTEAeLQEFISDLQSKlrlapdkLKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKV 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 853 LREFEETKKQIEEDEdreiqdiktKYEKKLRDEKESNLRLKGETGIMRKkfssLQKEIEERTNDIETLKGeqmKLQGVik 932
Cdd:TIGR00606 757 NRDIQRLKNDIEEQE---------TLLGTIMPEEESAKVCLTDVTIMER----FQMELKDVERKIAQQAA---KLQGS-- 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 933 SLEKDIQGLKREIQERDET--------------IQDKEKRIYDLKKKNQELGKFKF----------VLDYKIKELKKQIE 988
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHEldtvvskielnrklIQDQQEQIQHLKSKTNELKSEKLqigtnlqrrqQFEEQLVELSTEVQ 898
|
330 340 350
....*....|....*....|....*....|
gi 767902640 989 PRENEIRVMKEQIQEMEAELENFHKQNTQL 1018
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLETFLEKDQQEKEEL 928
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
686-1039 |
1.69e-05 |
|
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: 48.97 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 686 EVLVTKTDMEEKAQVMLELKTRVEELKMENE----YQLRLKDMNysEKIKELTDKF-IQEMESLKTKN------QVLRTE 754
Cdd:pfam05557 126 ELQSTNSELEELQERLDLLKAKASEAEQLRQnlekQQSSLAEAE--QRIKELEFEIqSQEQDSEIVKNskselaRIPELE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 755 KEKQDvyHHEHIEDLLD-KQSRELQDMECCNNQKLLLEYEKYQE----LQLKSQRMQEEYE--KQLRDNDETKSQALEEL 827
Cdd:pfam05557 204 KELER--LREHNKHLNEnIENKLLLKEEVEDLKRKLEREEKYREeaatLELEKEKLEQELQswVKLAQDTGLNLRSPEDL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 828 TEFYEAKLQEKTTLLEEaQEDVRQQLREFEETKkqieededREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQ 907
Cdd:pfam05557 282 SRRIEQLQQREIVLKEE-NSSLTSSARQLEKAR--------RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 908 KEIE------ERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK------------KKNQEL 969
Cdd:pfam05557 353 KERDgyrailESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKqqaqtlerelqaLRQQES 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902640 970 GKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNT---------QLELNITELWQKLRATDQEMRRE 1039
Cdd:pfam05557 433 LADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDydpkktkvlHLSMNPAAEAYQQRKNQLEKLQA 511
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
766-1015 |
1.85e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 766 IEDLLDKQSRELQDMEccNNQKLLLEYEKYQELQLKS-QRMQEEYEKQLRDNDETKSQ-----ALEELTEFYEAKLQEKT 839
Cdd:PRK01156 185 IDYLEEKLKSSNLELE--NIKKQIADDEKSHSITLKEiERLSIEYNNAMDDYNNLKSAlnelsSLEDMKNRYESEIKTAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 840 TLLEEAQEDVrQQLREFEETKKQIEEDE---DREIQDIKTKYEKKLRDEKESNLRLKGETG----IMRK---------KF 903
Cdd:PRK01156 263 SDLSMELEKN-NYYKELEERHMKIINDPvykNRNYINDYFKYKNDIENKKQILSNIDAEINkyhaIIKKlsvlqkdynDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 904 SSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKdiqgLKREIQERDETIQDKEKRIYDLKKKN----QELGKFKFVLDYK 979
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIES----LKKKIEEYSKNIERMSAFISEILKIQeidpDAIKKELNEINVK 417
|
250 260 270
....*....|....*....|....*....|....*.
gi 767902640 980 IKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN 1015
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQS 453
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
703-1005 |
1.89e-05 |
|
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: 48.89 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 703 ELKTRVEELKmeneyQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLR------TEKEKQDVYHH------EHIEDLL 770
Cdd:TIGR00606 249 PLKNRLKEIE-----HNLSKIMKLDNEIKAL-KSRKKQMEKDNSELELKMekvfqgTDEQLNDLYHNhqrtvrEKERELV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 771 DKQsrelQDMECCNNQKLLLEYEKYQ------ELQLKSQRMQEEYEKqlRDNDETKSQALEELTEFyeaklqekttlleE 844
Cdd:TIGR00606 323 DCQ----RELEKLNKERRLLNQEKTEllveqgRLQLQADRHQEHIRA--RDSLIQSLATRLELDGF-------------E 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 845 AQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKES----NLRLKGETGIMRKKFSSLQKEIEERTNDIETL 920
Cdd:TIGR00606 384 RGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQadeiRDEKKGLGRTIELKKEILEKKQEELKFVIKEL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 921 KGEQMKLQGVIKsLEKDIQGLKREIQERDE--TIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMK 998
Cdd:TIGR00606 464 QQLEGSSDRILE-LDQELRKAERELSKAEKnsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK 542
|
....*..
gi 767902640 999 EQIQEME 1005
Cdd:TIGR00606 543 DKMDKDE 549
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
791-971 |
1.99e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 791 EYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYE--AKLQEKTTLLEEAQEDVR-----QQLREFEETKKQI 863
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDriEELQELLREAEELEEELQleeleQEIAALLAEAGVE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 864 EEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKE-IEERtndIETLKGEQMKLQGVIKSLEKDIQGLK 942
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeLEEE---LEELEEELEELEEELEELREELAELE 459
|
170 180 190
....*....|....*....|....*....|.
gi 767902640 943 REIQ--ERDETIQDKEKRIYDLKKKNQELGK 971
Cdd:COG4717 460 AELEqlEEDGELAELLQELEELKAELRELAE 490
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
503-540 |
1.99e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 42.33 E-value: 1.99e-05
10 20 30
....*....|....*....|....*....|....*...
gi 767902640 503 ENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 540
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
685-1018 |
2.41e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.29 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 685 EEVLVTKTDMEE------KAQVML-----ELKTRVEELKMENEYqlrLKDMNYSEKIKELTDKfIQEMESLKTKNQVLRT 753
Cdd:PRK04778 205 EELAALEQIMEEipellkELQTELpdqlqELKAGYRELVEEGYH---LDHLDIEKEIQDLKEQ-IDENLALLEELDLDEA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 754 EKEKQDVyhHEHIEDLLDKqsrelqdMEccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKsqalEELTEfyea 833
Cdd:PRK04778 281 EEKNEEI--QERIDQLYDI-------LE--------REVKARKYVEKNSDTLPDFLEHAKEQNKELK----EEIDR---- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 834 kLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTkyekklrdekesnlrlkgetgimrkkFSSLQKEIEER 913
Cdd:PRK04778 336 -VKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIA--------------------------YSELQEELEEI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 914 TNDIETLKGEQMKLQGVIKSLEKDiqglkrEIQERdETIQDKEKRIYDLK----KKN-----QELGKFKFVLDYKIKELK 984
Cdd:PRK04778 389 LKQLEEIEKEQEKLSEMLQGLRKD------ELEAR-EKLERYRNKLHEIKryleKSNlpglpEDYLEMFFEVSDEIEALA 461
|
330 340 350
....*....|....*....|....*....|....
gi 767902640 985 KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQL 1018
Cdd:PRK04778 462 EELEEKPINMEAVNRLLEEATEDVETLEEETEEL 495
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
748-1041 |
2.60e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.61 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 748 NQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQ----ELQLKSQRMQEEYEKQLRDNDETKSQA 823
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEeqieEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 824 LEELTEFYEAKLQEKTTLLEEAQEDVRQQlREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGEtgiMRKKF 903
Cdd:pfam13868 111 QEEDQAEAEEKLEKQRQLREEIDEFNEEQ-AEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEE---KEREI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 904 SSLQKEIEERTNDIETLkgEQMKLQGVIKslEKDIQGLKREIQERDETIQDKEkriyDLKKKNQElgkfkfvlDYKIKEL 983
Cdd:pfam13868 187 ARLRAQQEKAQDEKAER--DELRAKLYQE--EQERKERQKEREEAEKKARQRQ----ELQQAREE--------QIELKER 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767902640 984 KKQIEPRENE---IRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQ 1041
Cdd:pfam13868 251 RLAEEAEREEeefERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAERE 311
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
832-1018 |
2.98e-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: 48.09 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 832 EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDiKTKYEKKLRDEKESNLRLKGETGIMRKK---FSSLQK 908
Cdd:TIGR04523 53 EKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKN-KDKINKLNSDLSKINSEIKNDKEQKNKLeveLNKLEK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 909 EIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERD-------ETIQDKEKRIYDLKKKNQELGKFKFVLDYKIK 981
Cdd:TIGR04523 132 QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELEnelnlleKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767902640 982 ----------ELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQL 1018
Cdd:TIGR04523 212 knkslesqisELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
725-952 |
3.03e-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: 47.36 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 725 NYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDvyHHEHIEDLLDKQSRELQdmeccnnqkllleyekyqELQLKSQR 804
Cdd:cd22656 80 NYAQNAGGTIDSYYAEILELIDDLADATDDEELEE--AKKTIKALLDDLLKEAK------------------KYQDKAAK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 805 MQEEYeKQLRDNDETKSQALEELTEFYEAKLQEKttLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKkLRD 884
Cdd:cd22656 140 VVDKL-TDFENQTEKDQTALETLEKALKDLLTDE--GGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIAD-DEA 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902640 885 EKESNLRLKGETGIMRKKFSSLQKEIEERTNDIEtlkgeqmKLQGVIKSLEKDIQGLKREIQERDETI 952
Cdd:cd22656 216 KLAAALRLIADLTAADTDLDNLLALIGPAIPALE-------KLQGAWQAIATDLDSLKDLLEDDISKI 276
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
726-1024 |
3.76e-05 |
|
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: 48.12 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 726 YSEKIKELTDKfiqEMESLKTKNQVLRTEKEKQDVY------------HHEHIEDLLDKQSRELQDM----ECCNNQKLL 789
Cdd:TIGR00606 665 YSQFITQLTDE---NQSCCPVCQRVFQTEAELQEFIsdlqsklrlapdKLKSTESELKKKEKRRDEMlglaPGRQSIIDL 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 790 LEYEkYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAK-LQEKTTLLEEAQEDVRQQLREFEETKKQIEE-DE 867
Cdd:TIGR00606 742 KEKE-IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvCLTDVTIMERFQMELKDVERKIAQQAAKLQGsDL 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 868 DREIQDIKTKYEKKlrDEKESNLRLKGETgimrkkfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQE 947
Cdd:TIGR00606 821 DRTVQQVNQEKQEK--QHELDTVVSKIEL---------NRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQ 889
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902640 948 RDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITE 1024
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQD 966
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
825-1010 |
4.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 825 EELTEFYEA--KLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKY---EKKLRDEKESNLRLKGETGIM 899
Cdd:COG4913 235 DDLERAHEAleDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLellEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 900 RKKFSSLQKEIEERTNDIETLKGEQmklqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK----------KKNQEL 969
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDR------LEQLEREIERLERELEERERRRARLEALLAALGlplpasaeefAALRAE 388
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767902640 970 GK-FKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELEN 1010
Cdd:COG4913 389 AAaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
900-1030 |
4.53e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 900 RKKFSSLQKEIEERTnDIETLKGEQMK---LQGVIKSLEKDIQGLK-----REIQERDETIQDKEKRIYDLKKKNQELGK 971
Cdd:COG2433 349 KNKFERVEKKVPPDV-DRDEVKARVIRglsIEEALEELIEKELPEEepeaeREKEHEERELTEEEEEIRRLEEQVERLEA 427
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902640 972 FKFVLDYKIKELKKQIEPRENEIRVMKEQ----------IQEMEAELENFHKQNTQLELNITELWQKLR 1030
Cdd:COG2433 428 EVEELEAELEEKDERIERLERELSEARSEerreirkdreISRLDREIERLERELEEERERIEELKRKLE 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
832-1019 |
6.99e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 832 EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReiqdiKTKYEkKLRDEKESNLRLKGetgiMRKKFSSLQKEIE 911
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-----REALQ-RLAEYSWDEIDVAS----AEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 912 --ERTN-DIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFV-LDYKIKELKKQI 987
Cdd:COG4913 679 rlDASSdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFAAA 758
|
170 180 190
....*....|....*....|....*....|..
gi 767902640 988 EPRENEIRVMKEQIQEMEAELENFHKQNTQLE 1019
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARLNRAEEELE 790
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
695-988 |
7.09e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 695 EEKAQVMLELK-----TRVEELKMENEYQLRLKDMNYSEKIKELTDKfiqEMESLKTKNQVLRTEKEKQDVyhHEHIEDL 769
Cdd:COG5022 902 LELESEIIELKkslssDLIENLEFKTELIARLKKLLNNIDLEEGPSI---EYVKLPELNKLHEVESKLKET--SEEYEDL 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 770 LDKQS---RELQDMeccnNQKLLLEYEKYQELQLKSQRMQEEyEKQLRDNDeTKSQALEELTEFY---------EAKLQE 837
Cdd:COG5022 977 LKKSTilvREGNKA----NSELKNFKKELAELSKQYGALQES-TKQLKELP-VEVAELQSASKIIssestelsiLKPLQK 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 838 KTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKK---LRDEKESNLRLKGETGIMR------KKFSSLQK 908
Cdd:COG5022 1051 LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKtinVKDLEVTNRNLVKPANVLQfivaqmIKLNLLQE 1130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 909 EIEERTNDIETLKGEQMKLqgviKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVL-DYKIKELKKQI 987
Cdd:COG5022 1131 ISKFLSQLVNTLEPVFQKL----SVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLsSSEVNDLKNEL 1206
|
.
gi 767902640 988 E 988
Cdd:COG5022 1207 I 1207
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
784-884 |
9.90e-05 |
|
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: 43.33 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 784 NNQKLLLEYEKYQELQLKSQRMQEEYEKQLrdndETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQI 863
Cdd:pfam03938 6 DMQKILEESPEGKAAQAQLEKKFKKRQAEL----EAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKA 81
|
90 100
....*....|....*....|.
gi 767902640 864 EEDEDREIQDIKTKYEKKLRD 884
Cdd:pfam03938 82 QQELQKKQQELLQPIQDKINK 102
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
843-1014 |
1.00e-04 |
|
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: 46.17 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 843 EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFsslqKEIEERTNDIEtlkg 922
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESSIK-QVEEELEELKEQNEELEKQYKVKKKTL----DLLPDAEENIA---- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 923 eqmKLQGVIKSLEKDIQGLKREIQERDETIQdKEKRIYDLKKKNQELgKFKFVLDyKIKELKKQIEPRENEIRVMKEQIQ 1002
Cdd:pfam05667 405 ---KLQALVDASAQRLVELAGQWEKHRVPLI-EEYRALKEAKSNKED-ESQRKLE-EIKELREKIKEVAEEAKQKEELYK 478
|
170
....*....|..
gi 767902640 1003 EMEAELENFHKQ 1014
Cdd:pfam05667 479 QLVAEYERLPKD 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
676-954 |
1.10e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 676 KREREVGFAEEVLVTKTDMEEKAQVMLE----LKTRVEELKME-----NEYQLRLKDMNYSEKIKELTDKFIQEMESLKT 746
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEelkaLREALDELRAEltllnEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 747 KNQVLRTEKEKQdvyhHEHIEDLLDKQSRELQdmeccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEE 826
Cdd:TIGR02168 849 ELSEDIESLAAE----IEELEELIEELESELE-----------ALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 827 ltefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGetgiMRKKFSSL 906
Cdd:TIGR02168 914 -----RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR----LENKIKEL 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902640 907 Q----------KEIEERtndIETLKGEQMKLQGVIKSLEKDIQGLKREIQER-DETIQD 954
Cdd:TIGR02168 985 GpvnlaaieeyEELKER---YDFLTAQKEDLTEAKETLEEAIEEIDREARERfKDTFDQ 1040
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
728-1031 |
1.14e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 728 EKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHH--EHIEDLLDKQS--RELQDMEccnnqkllleyEKYQELQLKSQ 803
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASaeREIAELE-----------AELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 804 RMQEeyekqLRDNDETKSQALEELTEFYEAkLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDRE-IQDIKTKYEKKL 882
Cdd:COG4913 686 DLAA-----LEEQLEELEAELEELEEELDE-LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 883 RDEKESNLR--LKGETGIMRKKFSSLQKEIEERTND-IETLKGEQMKLQGVIKSLEkDIQGLKREIQERDetIQDKEKRI 959
Cdd:COG4913 760 GDAVERELRenLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLP-EYLALLDRLEEDG--LPEYEERF 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 960 YDLKKKNQElgkfkfvldYKIKELKKQIeprENEIRVMKEQIQEMEAELEN----------FHKQNTQLElNITELWQKL 1029
Cdd:COG4913 837 KELLNENSI---------EFVADLLSKL---RRAIREIKERIDPLNDSLKRipfgpgrylrLEARPRPDP-EVREFRQEL 903
|
..
gi 767902640 1030 RA 1031
Cdd:COG4913 904 RA 905
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
763-1042 |
1.20e-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: 46.12 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 763 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQ------LKSQRMQEEYEKQLRDNDETKSQA--LEELTEFYEAK 834
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEkelkhlREALQQTQQSHAYLTQKREAQEEQlkKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 835 LQEKTTL---LEEAQEDV---RQQLREFEETKK--QIEEDEDREIQDIKTKYEK--KLRDEKESNLRLKGETGIMRKKFS 904
Cdd:TIGR00618 269 IEELRAQeavLEETQERInraRKAAPLAAHIKAvtQIEQQAQRIHTELQSKMRSraKLLMKRAAHVKQQSSIEEQRRLLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 905 SLQKEIE--ERTNDIETLKGEQMKLQgviKSLEKDIqglkREIQERDETIQDKEKRIYDLKKKNQelgkfkfvldykikE 982
Cdd:TIGR00618 349 TLHSQEIhiRDAHEVATSIREISCQQ---HTLTQHI----HTLQQQKTTLTQKLQSLCKELDILQ--------------R 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 983 LKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQK 1042
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS 467
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
825-963 |
1.33e-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: 43.77 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 825 EELTEFYeAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYE---KKLRDEKESNLRLKGEtgimrk 901
Cdd:pfam08614 3 LELIDAY-NRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllAQLREELAELYRSRGE------ 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902640 902 kfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 963
Cdd:pfam08614 76 ----LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQ 133
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
875-1039 |
1.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 875 KTKYEKKLRDEKESNLRLKGETgimRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKR---------EI 945
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVLGFDN---RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDV 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 946 QERDETIQDKEKRIYDLKKKNQELgkfkfvldykiKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL 1025
Cdd:COG4913 664 ASAEREIAELEAELERLDASSDDL-----------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
170
....*....|....
gi 767902640 1026 WQKLRATDQEMRRE 1039
Cdd:COG4913 733 QDRLEAAEDLARLE 746
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
681-889 |
1.48e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 681 VGFAEEVLVTKTDMEEKAQVMLEL-KTRVEELKMENEYQLRLKDMNYSEKIKELTDKFiqEMESLKTKNQVLRTEKEKQD 759
Cdd:PRK12704 16 VGAVIGYFVRKKIAEAKIKEAEEEaKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF--EKELRERRNELQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 760 VyhhehiEDLLDKQSRELQDMEccnnqkllleyekyQELQLKsqrmQEEYEKQLRDndetksqaLEELTEFYEAKLQEKT 839
Cdd:PRK12704 94 K------EENLDRKLELLEKRE--------------EELEKK----EKELEQKQQE--------LEKKEEELEELIEEQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767902640 840 TLLEEA----QEDVRQQLreFEETKKQIEEDEDREIQDIKTKYekKLRDEKESN 889
Cdd:PRK12704 142 QELERIsgltAEEAKEIL--LEKVEEEARHEAAVLIKEIEEEA--KEEADKKAK 191
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
694-1045 |
1.50e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.84 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 694 MEEKAQVMLELKTRVEELkmeNEYQlRLKDMN--YSEKIKELTdkfiQEMESLKTKNqvLRTEKEKQDvyHHEHIEDLlD 771
Cdd:pfam05622 27 QEEKNSLQQENKKLQERL---DQLE-SGDDSGtpGGKKYLLLQ----KQLEQLQEEN--FRLETARDD--YRIKCEEL-E 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 772 KQSRELQdmeccnnqkllLEYEKYQELQLKSQRMQEEYEkQLRDNDEtKSQALEELTEFYEAKLQE------KTTLLEEA 845
Cdd:pfam05622 94 KEVLELQ-----------HRNEELTSLAEEAQALKDEMD-ILRESSD-KVKKLEATVETYKKKLEDlgdlrrQVKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 846 QEDVRQQLREFEE-------TKKQIEEDEdREIQDIktkyEKKLRDEKESNLRLKGETGIMRKKFSSLQKE----IEER- 913
Cdd:pfam05622 161 NAEYMQRTLQLEEelkkanaLRGQLETYK-RQVQEL----HGKLSEESKKADKLEFEYKKLEEKLEALQKEkerlIIERd 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 914 ----TND-------------------------IETLKGEQM---------KLQGVIKSL---------EK--DIQGLKRE 944
Cdd:pfam05622 236 tlreTNEelrcaqlqqaelsqadallspssdpGDNLAAEIMpaeirekliRLQHENKMLrlgqegsyrERltELQQLLED 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 945 IQERDETIQDKEK----RIYDLKKKNQELGKFKFVLDYKIKE---LKKQIEPRENEIRVMKEQIQEMEAELENFH-KQNT 1016
Cdd:pfam05622 316 ANRRKNELETQNRlanqRILELQQQVEELQKALQEQGSKAEDsslLKQKLEEHLEKLHEAQSELQKKKEQIEELEpKQDS 395
|
410 420 430
....*....|....*....|....*....|.
gi 767902640 1017 QLELNITELWQKLRATDQEMR--RERQKPCL 1045
Cdd:pfam05622 396 NLAQKIDELQEALRKKDEDMKamEERYKKYV 426
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
676-1031 |
1.56e-04 |
|
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: 45.94 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 676 KREREVGFAEEVLVTKTDMEEkAQvMLELKTR----VEELKMENEyQLRLKDMNYsEKIKELTDKFIQEM-ESLKTKNQV 750
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHE-AQ-LQEMRQKhtqaLEELTEQLE-QAKRNKANL-EKAKQALESENAELqAELRTLQQA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 751 lrtekeKQDVyhhEHIEDLLDKQSRELQdmeccnnQKLLLEYEKYQELQLKSQRMQEEYE--------------KQLRDN 816
Cdd:pfam01576 400 ------KQDS---EHKRKKLEGQLQELQ-------ARLSESERQRAELAEKLSKLQSELEsvssllneaegkniKLSKDV 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 817 DETKSQ---ALEELTEFYEAKLQEKTTL--LEEAQEDVRQQLREFEETKKQIE---EDEDREIQDIKTKYE--------- 879
Cdd:pfam01576 464 SSLESQlqdTQELLQEETRQKLNLSTRLrqLEDERNSLQEQLEEEEEAKRNVErqlSTLQAQLSDMKKKLEedagtleal 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 880 ----KKLRDEKES-NLRLKGETGI---MRKKFSSLQKEIEERTND-------IETLKGEQMKLQGVI------------- 931
Cdd:pfam01576 544 eegkKRLQRELEAlTQQLEEKAAAydkLEKTKNRLQQELDDLLVDldhqrqlVSNLEKKQKKFDQMLaeekaisaryaee 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 932 ------KSLEKDIQGLK--REIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQE 1003
Cdd:pfam01576 624 rdraeaEAREKETRALSlaRALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEE 703
|
410 420
....*....|....*....|....*...
gi 767902640 1004 MEAELENFHKQNTQLELNItelwQKLRA 1031
Cdd:pfam01576 704 LEDELQATEDAKLRLEVNM----QALKA 727
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
789-1043 |
1.92e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 789 LLEYEKYQELQlKSQRMQEEYEKQlRDNDETKSQALEELTEfyeaklQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED 868
Cdd:pfam02029 64 FLDRTAKREER-RQKRLQEALERQ-KEFDPTIADEKESVAE------RKENNEEEENSSWEKEEKRDSRLGRYKEEETEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 869 REIQDIKTKYEKKLRDEKEsnlrlKGEtgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQER 948
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEE-----EGE---EEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 949 deTIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPrENEIRVMKEQIQEME-AELENFHKQNTQLELNITELWQ 1027
Cdd:pfam02029 208 --KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEA-EQKLEELRRRRQEKEsEEFEKLRQKQQEAELELEELKK 284
|
250 260
....*....|....*....|...
gi 767902640 1028 K-------LRATDQEMRRERQKP 1043
Cdd:pfam02029 285 KreerrklLEEEEQRRKQEEAER 307
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
691-969 |
1.93e-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: 45.61 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 691 KTDMEEKAQVMLELKTRVEELkmeneyqlrlkdMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedll 770
Cdd:pfam09726 408 KAELQASRQTEQELRSQISSL------------TSLERSLKSELGQLRQENDLLQTKLHNAVSAKQK------------- 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 771 DKQSreLQDMEccnnQKLLLEyekyqelqlksQRMQEEYEKQLrdNDETKSQALEELTEFYEAKLQEKTTllEEAQEDVR 850
Cdd:pfam09726 463 DKQT--VQQLE----KRLKAE-----------QEARASAEKQL--AEEKKRKKEEEATAARAVALAAASR--GECTESLK 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 851 QQLREFEETKKQIEED---EDREIQDIKTKyEKKLRDEKESnlrlKGETGIMRKKFSSLQKEIEERTNDI--ETlkgeQM 925
Cdd:pfam09726 522 QRKRELESEIKKLTHDiklKEEQIRELEIK-VQELRKYKES----EKDTEVLMSALSAMQDKNQHLENSLsaET----RI 592
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767902640 926 KLqgvikSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQEL 969
Cdd:pfam09726 593 KL-----DLFSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEV 631
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
728-1041 |
2.34e-04 |
|
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: 45.42 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 728 EKIKELTDKFIQEMESLKTKNQVLRTEKEKQdvyhhEHIEDLLdkQSRELQdMECcnnqkllleyekyqelqlkSQRMQE 807
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKA-----CEIRDQI--TSKEAQ-LES-------------------SREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 808 EYEKQLRDNDETKSQALEELTEFYeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE 887
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIM--KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKER 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 888 SNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQ----ERDETIQDKEKRIYDLK 963
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfERGPFSERQIKNFHTLV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 964 KKNQElGKFKFV----LDYKIKELKKQIEPRENEIRvMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRE 1039
Cdd:TIGR00606 400 IERQE-DEAKTAaqlcADLQSKERLKQEQADEIRDE-KKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELD 477
|
..
gi 767902640 1040 RQ 1041
Cdd:TIGR00606 478 QE 479
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
702-887 |
2.47e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 702 LELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRT-EKEKQDVYHHEHIEDLLDK-QSRELQD 779
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAALLAEaGVEDEEE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 780 MEccnnqKLLLEYEKYQELQLKsqrmQEEYEKQLRDNDETKSQALEELT-EFYEAKLQEKTTLLEEAQEDVRQQLREFEE 858
Cdd:COG4717 387 LR-----AALEQAEEYQELKEE----LEELEEQLEELLGELEELLEALDeEELEEELEELEEELEELEEELEELREELAE 457
|
170 180 190
....*....|....*....|....*....|
gi 767902640 859 TKKQIEE-DEDREIQDIKTKYEKKLRDEKE 887
Cdd:COG4717 458 LEAELEQlEEDGELAELLQELEELKAELRE 487
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
791-999 |
2.72e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 791 EYEKYQELQLKSQRMQEEYEK-QLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE--DE 867
Cdd:COG5022 811 EYRSYLACIIKLQKTIKREKKlRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQElkID 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 868 DREIQDIKTKYEK------KLRDEKESNLRLKGEtgIMRKKFSSLQKEIEERtnDIETLKGEQMKLQGVIKSLEKDIQGL 941
Cdd:COG5022 891 VKSISSLKLVNLEleseiiELKKSLSSDLIENLE--FKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLHEVESKL 966
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767902640 942 KREIQERDETIQDKEKRIYDLKKKNQELGKFKfvldYKIKELKKQIEPRENEIRVMKE 999
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFK----KELAELSKQYGALQESTKQLKE 1020
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
796-876 |
2.91e-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: 42.04 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 796 QELQLKSQRMQEEYEKQLRdndETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLrefEETKKQIEEDEDREIQDIK 875
Cdd:cd06503 43 EKAKEEAEELLAEYEEKLA---EARAEAQEIIEEARKEAEKIKEEILAEAKEEAERIL---EQAKAEIEQEKEKALAELR 116
|
.
gi 767902640 876 T 876
Cdd:cd06503 117 K 117
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
817-1019 |
2.96e-04 |
|
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: 44.63 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 817 DETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQ---QLREFEETKKQIEEdedreiqdiKTKYEKKLRDEKESNLRLK 893
Cdd:pfam05667 319 PPTKVETEEELQQQREEELEELQEQLEDLESSIQElekEIKKLESSIKQVEE---------ELEELKEQNEELEKQYKVK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 894 getgimrKKFSSLQKEIEErtnDIEtlkgeqmKLQGVIKSLEKDIQGLKREIQERDETIQDKekrIYDLKKKNQElgkfk 973
Cdd:pfam05667 390 -------KKTLDLLPDAEE---NIA-------KLQALVDASAQRLVELAGQWEKHRVPLIEE---YRALKEAKSN----- 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767902640 974 fvldyKIKELKKQIEprenEIRVMKEQIQEMEAEL---ENFHKQ-NTQLE 1019
Cdd:pfam05667 445 -----KEDESQRKLE----EIKELREKIKEVAEEAkqkEELYKQlVAEYE 485
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
837-1035 |
3.13e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.21 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 837 EKTTLLEEAQEDVRQQLREFEETKKQIEE---DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIM-------------- 899
Cdd:PTZ00440 404 KYTNIISLSEHTLKAAEDVLKENSQKIADyalYSNLEIIEIKKKYDEKINELKKSINQLKTLISIMksfydliisekdsm 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 900 ------RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLE---KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELG 970
Cdd:PTZ00440 484 dskekkESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEdyyITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKR 563
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902640 971 KFKFVLDYKIKELK------KQIEPRENEIRVMKEQIQEMEAE----LENFHKQNTQLELNITELWQKLRATDQE 1035
Cdd:PTZ00440 564 SMKNDIKNKIKYIEenvdhiKDIISLNDEIDNIIQQIEELINEalfnKEKFINEKNDLQEKVKYILNKFYKGDLQ 638
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
739-1041 |
3.54e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 44.26 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 739 QEMESLKTKNQVLRTEKEKQDVYHHEHIED---LLDKQSRE--LQDMEccnNQKLLLEYEKYQELQLKSQ---------- 803
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERerrLLLQQSQEqwQAEKE---QRKARLGREERRRADRREKqviekesrwr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 804 RMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEET---KKQIEEDED-REIQDI----K 875
Cdd:pfam15558 98 EQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEachKRQLKEREEqKKVQENnlseL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 876 TKYEKKLRD----EKESNLRLKGET------------GIMRKKFSSL----QKEIE--ERTNDIETLKGEQMKLQGVIKS 933
Cdd:pfam15558 178 LNHQARKVLvdcqAKAEELLRRLSLeqslqrsqenyeQLVEERHRELrekaQKEEEqfQRAKWRAEEKEEERQEHKEALA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 934 LEKDiQGLKREIQERDETIQDKEKRIYDL---KKKNQelgkfkfvldykiKELKKQIEPREN-EIRVMKEQIQEMEAELE 1009
Cdd:pfam15558 258 ELAD-RKIQQARQVAHKTVQDKAQRARELnleREKNH-------------HILKLKVEKEEKcHREGIKEAIKKKEQRSE 323
|
330 340 350
....*....|....*....|....*....|..
gi 767902640 1010 NFHKQNtqlELNITELWQKLRATDQEMRRERQ 1041
Cdd:pfam15558 324 QISREK---EATLEEARKTARASFHMREKVRE 352
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
388-417 |
3.58e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.87 E-value: 3.58e-04
10 20 30
....*....|....*....|....*....|
gi 767902640 388 HSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:pfam00400 10 HTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
685-895 |
4.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 685 EEVLVTKTDMEEKAQvmlELKTRVEELKMENEYQLrlkdmnySEKIKELtDKFIQEMESLKTKNQVLRTEKEKQDVYHHE 764
Cdd:PRK03918 559 AELEKKLDELEEELA---ELLKELEELGFESVEEL-------EERLKEL-EPFYNEYLELKDAEKELEREEKELKKLEEE 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 765 hIEDLLDKQSRELQDMECCNNQ--KLLLEY--EKYQELQLKSQRMQEEYE------KQLRDNDETKSQALEELTEFYEA- 833
Cdd:PRK03918 628 -LDKAFEELAETEKRLEELRKEleELEKKYseEEYEELREEYLELSRELAglraelEELEKRREEIKKTLEKLKEELEEr 706
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902640 834 -KLQEKTTLLEEAQEDVrQQLRE-FEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGE 895
Cdd:PRK03918 707 eKAKKELEKLEKALERV-EELREkVKKYKALLKERALSKVGEIASEIFEELTEGKYSGVRVKAE 769
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-179 |
4.50e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.75 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 26 DEQIIIFPSGNHCVK-YNVD-QKWQKFIPGSekSQGMLALSISPNRRYLAiseTVQEKPAITIYELSSipcrkRKVLNNF 103
Cdd:COG2319 257 DGRLLASGSADGTVRlWDLAtGELLRTLTGH--SGGVNSVAFSPDGKLLA---SGSDDGTVRLWDLAT-----GKLLRTL 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902640 104 DFQVQKFISMAFSPDSKYLLAQTSppeSNLVYwLWEKQKVMAIVRIDTQNNPVYQVSFSPQDNTQVCVTGNGMFKL 179
Cdd:COG2319 327 TGHTGAVRSVAFSPDGKTLASGSD---DGTVR-LWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
385-417 |
4.52e-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: 4.52e-04
10 20 30
....*....|....*....|....*....|...
gi 767902640 385 YPLHSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:smart00320 8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
703-1035 |
4.77e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 703 ELKTRVEElKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDvYHHEHIEDLLDKQSRELQDMEc 782
Cdd:COG4372 3 RLGEKVGK-ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR-EELEQLEEELEQARSELEQLE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 783 cnnQKLLLEYEKYQELQLKSQRMQEEYEkQLRDNDETKSQALEELT------EFYEAKLQEKTTLLEEAQEDVRQQLREF 856
Cdd:COG4372 80 ---EELEELNEQLQAAQAELAQAQEELE-SLQEEAEELQEELEELQkerqdlEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 857 EETKKQIEEDEDREIQDIKTKYE-------KKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQG 929
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEaeaeqalDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 930 VIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELE 1009
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
330 340
....*....|....*....|....*.
gi 767902640 1010 NFHKQNTQLELNITELWQKLRATDQE 1035
Cdd:COG4372 316 ALLAALLELAKKLELALAILLAELAD 341
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
728-945 |
4.88e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 728 EKIKELTD--KFIQE----MESLKTKNQVLRTEKE-----KQDVYHHEHIEDLLDKQSRELQDMeccNNQKLLLEYEKYQ 796
Cdd:PRK04863 901 EQLDEAEEakRFVQQhgnaLAQLEPIVSVLQSDPEqfeqlKQDYQQAQQTQRDAKQQAFALTEV---VQRRAHFSYEDAA 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 797 ELQLKSQRMQEEYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLLEEAQE--DV-RQQLREFEetkkqieededREIQD 873
Cdd:PRK04863 978 EMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQ-AQAQLAQYNQVLASLKSsyDAkRQMLQELK-----------QELQD 1045
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 874 IKTKY----EKKL---RDEKESNLRlkgetgIMRKKFSSLQKEIeertndieTLKGEQMK-LQGVIKSLEKDIQGLKREI 945
Cdd:PRK04863 1046 LGVPAdsgaEERArarRDELHARLS------ANRSRRNQLEKQL--------TFCEAEMDnLTKKLRKLERDYHEMREQV 1111
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
699-1036 |
5.33e-04 |
|
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: 43.73 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 699 QVMLE--LKTRVEELK-MENEYQLRLKDMNYSEKIKELTDKFIQEMES----LKTKNQVLRTEKEKQDVYHHE--HIEDL 769
Cdd:pfam07888 33 QNRLEecLQERAELLQaQEAANRQREKEKERYKRDREQWERQRRELESrvaeLKEELRQSREKHEELEEKYKElsASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 770 LDKQSRELQDMECCNNQKLLleyEKYQELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFYEAK--LQEKttlLEEAQE 847
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIR---ELEEDIKTLTQRVLER-ETELERMKERAKKAGAQRKEEEAERkqLQAK---LQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 848 DVRQQLREFEETKKQIEEDEDR--EIQDIKTKYEKKLrdekESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGE-- 923
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAQRDTQvlQLQDTITTLTQKL----TTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEls 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 924 --------------QMKLQGVIKSLEKDIQGLK-RE-----IQERDETIQDKEKRIYDLKKKNQELGKfkfvLDYKIKEL 983
Cdd:pfam07888 262 smaaqrdrtqaelhQARLQAAQLTLQLADASLAlREgrarwAQERETLQQSAEADKDRIEKLSAELQR----LEERLQEE 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902640 984 KKQIEPRENEI-------RVM----KEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEM 1036
Cdd:pfam07888 338 RMEREKLEVELgrekdcnRVQlsesRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
666-1004 |
5.57e-04 |
|
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: 43.79 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 666 KVFDKDGRGIKREREVGFAEEVLVTKTDmEEKAQVMLELKTRVEELKMENEyQLRLKDMNYSEKIKELTDKFIQEMESLK 745
Cdd:COG5185 236 KGFQDPESELEDLAQTSDKLEKLVEQNT-DLRLEKLGENAESSKRLNENAN-NLIKQFENTKEKIAEYTKSIDIKKATES 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 746 TKNQVLRTEKEKqdvyhheHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELqlKSQRMQEEYEKQLRDNDETKSQA-- 823
Cdd:COG5185 314 LEEQLAAAEAEQ-------ELEESKRETETGIQNLTAEIEQGQESLTENLEAI--KEEIENIVGEVELSKSSEELDSFkd 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 824 -LEELTEFYEAKLQ-------------EKTTL-----LEEAQEDVRQQLREFEETKKQIeededREIQDIKTKYEKKLRD 884
Cdd:COG5185 385 tIESTKESLDEIPQnqrgyaqeilatlEDTLKaadrqIEELQRQIEQATSSNEEVSKLL-----NELISELNKVMREADE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 885 ekESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQM-KLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDL- 962
Cdd:COG5185 460 --ESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKaTLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAh 537
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 767902640 963 KKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEM 1004
Cdd:COG5185 538 ILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLST 579
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
702-1014 |
6.33e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 702 LELKTRVEELKMENEyQLRLKDMNYSEKIKELtdkfiqemESLKTKnqvlRTEKEKQdvyhhehIEDLLDKQSRELQDME 781
Cdd:PRK01156 342 IKKKSRYDDLNNQIL-ELEGYEMDYNSYLKSI--------ESLKKK----IEEYSKN-------IERMSAFISEILKIQE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 782 CcNNQKLLLEYE----KYQELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFYEAKLQeKTTLLEEAQEDVRQqlrEFE 857
Cdd:PRK01156 402 I-DPDAIKKELNeinvKLQDISSKVSSLNQR-IRALRENLDELSRNMEMLNGQSVCPVC-GTTLGEEKSNHIIN---HYN 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 858 ETKKQIEEDED---REIQDI--KTKYEKKLRDEKESNLRLKGETgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGV-- 930
Cdd:PRK01156 476 EKKSRLEEKIReieIEVKDIdeKIVDLKKRKEYLESEEINKSIN--EYNKIESARADLEDIKIKINELKDKHDKYEEIkn 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 931 -IKSLEKDIQGLKRE-------------IQERDETIQDKEKRIYDLKKKNQEL-GKFKFVLDYKIKELKK------QIEP 989
Cdd:PRK01156 554 rYKSLKLEDLDSKRTswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIeIGFPDDKSYIDKSIREieneanNLNN 633
|
330 340
....*....|....*....|....*
gi 767902640 990 RENEIRVMKEQIQEMEAELENFHKQ 1014
Cdd:PRK01156 634 KYNEIQENKILIEKLRGKIDNYKKQ 658
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
702-1019 |
6.36e-04 |
|
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: 44.27 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 702 LELKTRVEELKMENEYQLRLKDMnysEKIKELTDKFIQEM---------ESLKTKNQVLRTEKEKQDVYHHEHIEDLLDK 772
Cdd:TIGR01612 603 LELKEKIKNISDKNEYIKKAIDL---KKIIENNNAYIDELakispyqvpEHLKNKDKIYSTIKSELSKIYEDDIDALYNE 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 773 QSRELQDMECCNNQ---KLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTefyeakLQEKTTLLEEAQEDV 849
Cdd:TIGR01612 680 LSSIVKENAIDNTEdkaKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDII------VEIKKHIHGEINKDL 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 850 RQQLREFEETKKQI---------EEDE----DREIQDIKTKYEK-------KLRDEKESNLRLKGETgimrKKFSSLQKE 909
Cdd:TIGR01612 754 NKILEDFKNKEKELsnkindyakEKDElnkyKSKISEIKNHYNDqinidniKDEDAKQNYDKSKEYI----KTISIKEDE 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 910 IEERTNDIETLKGEQMKLQGVIKSLEKD---------------IQGLKREIQerDETIQDKEKRIYDLKKknqelgkfkf 974
Cdd:TIGR01612 830 IFKIINEMKFMKDDFLNKVDKFINFENNckekidseheqfaelTNKIKAEIS--DDKLNDYEKKFNDSKS---------- 897
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 767902640 975 vldyKIKELKKQIEPRENEIRVMKE-----QIQEMEAE-LENFHKQNTQLE 1019
Cdd:TIGR01612 898 ----LINEINKSIEEEYQNINTLKKvdeyiKICENTKEsIEKFHNKQNILK 944
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
749-1035 |
6.47e-04 |
|
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: 43.89 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 749 QVLRTEKEKQDV-----YHHEHIEDLLDKQSRELQdmECCNNQKLLLEYekyqelqLKSQRMQEEYEKQLRdndETKSQA 823
Cdd:TIGR01612 328 KILESEGEQGHIinkliFLEKEFEDTIHKSDIYKD--ECLSNHLFMEDY-------LKDDKISPYYYEFLE---EIKKIA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 824 LEELTEFYEAKLQEKTTLLEEAQEDVrqqLREFEETKKQ--IEEDEDREIQDIKTKYEKKLRDEKESNLRL--KGETGIM 899
Cdd:TIGR01612 396 KQRAIFFYNAKKLKHLEILYKHQEDI---LNNFHKTIERliFEKPDPNNNNIFKDDFDEFNKPIPKSKLKAleKRFFEIF 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 900 RKKFSS--LQKEIEERTNDIETLKG--EQMK-LQGVIKSLEkdiQGLKREIQERDETIQDKEKRIYDLKKKNQELGkfkf 974
Cdd:TIGR01612 473 EEEWGSydIKKDIDENSKQDNTVKLilMRMKdFKDIIDFME---LYKPDEVPSKNIIGFDIDQNIKAKLYKEIEAG---- 545
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767902640 975 vldykikeLKKQIEPRENeirvMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQE 1035
Cdd:TIGR01612 546 --------LKESYELAKN----WKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDE 594
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
800-974 |
6.69e-04 |
|
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: 43.08 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 800 LKSQRMQEEYEKQLRDNDEtksqalEELTEFYEAKLQEKTTLLEEAQE--DVRQQLRE-FEETKKQIEEdedreiqdikt 876
Cdd:smart00787 128 LEAKKMWYEWRMKLLEGLK------EGLDENLEGLKEDYKLLMKELELlnSIKPKLRDrKDALEEELRQ----------- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 877 kyEKKLRDEKESNLrlKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIqdKE 956
Cdd:smart00787 191 --LKQLEDELEDCD--PTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL--EQ 264
|
170
....*....|....*...
gi 767902640 957 KRIYDLKKKNQELGKFKF 974
Cdd:smart00787 265 CRGFTFKEIEKLKEQLKL 282
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
695-874 |
6.91e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 695 EEKAQVMLELKTRVEELKMENEYQLRLKDmnysEKIKELTDKFIQEMESLKTKnqvlrtekekqdvyhhehiEDLLDKQS 774
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERR----NELQKLEKRLLQKEENLDRK-------------------LELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 775 RELQDMECCNNQKLlleyekyQELQLKSQRMQEEYEKQLrdndetksQALEE---LTEFyEAKLQEKTTLLEEAQEDVRQ 851
Cdd:PRK12704 110 EELEKKEKELEQKQ-------QELEKKEEELEELIEEQL--------QELERisgLTAE-EAKEILLEKVEEEARHEAAV 173
|
170 180
....*....|....*....|...
gi 767902640 852 QLREFEEtkkQIEEDEDREIQDI 874
Cdd:PRK12704 174 LIKEIEE---EAKEEADKKAKEI 193
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-190 |
7.31e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.36 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 26 DEQIIIFPSGNHCVK-YNVD-QKWQKFIPGSekSQGMLALSISPNRRYLAiseTVQEKPAITIYELSSipcrkRKVLNNF 103
Cdd:COG2319 215 DGKLLASGSADGTVRlWDLAtGKLLRTLTGH--SGSVRSVAFSPDGRLLA---SGSADGTVRLWDLAT-----GELLRTL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 104 DFQVQKFISMAFSPDSKYLLAQTsppESNLVyWLWEKQKVMAIVRIDTQNNPVYQVSFSPQDNTQVCVTGNGMFKLLRFA 183
Cdd:COG2319 285 TGHSGGVNSVAFSPDGKLLASGS---DDGTV-RLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA 360
|
....*..
gi 767902640 184 EGTLKQT 190
Cdd:COG2319 361 TGELLRT 367
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
706-897 |
7.98e-04 |
|
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: 42.70 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 706 TRVEELKMENEYQLRLkdmnySEKIKELTDKfiqEMESLKTKNQVLRTEKEKQDVYHHEhIEDLLDKQSRELQDMeccnn 785
Cdd:smart00787 126 ARLEAKKMWYEWRMKL-----LEGLKEGLDE---NLEGLKEDYKLLMKELELLNSIKPK-LRDRKDALEEELRQL----- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 786 QKLLLEYEKYQELQLKSQRmqEEYEKQLRDNDEtKSQALEELTEfyeaKLQEKTTLLEEAQE---DVRQQLREFEETKKQ 862
Cdd:smart00787 192 KQLEDELEDCDPTELDRAK--EKLKKLLQEIMI-KVKKLEELEE----ELQELESKIEDLTNkksELNTEIAEAEKKLEQ 264
|
170 180 190
....*....|....*....|....*....|....*
gi 767902640 863 IEEDEDREIQDIKTKYEKKlrdEKESNLRLKGETG 897
Cdd:smart00787 265 CRGFTFKEIEKLKEQLKLL---QSLTGWKITKLSG 296
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
792-909 |
9.50e-04 |
|
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: 40.67 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 792 YEKYQELQLKS---QRMQEEYEKqLRDNDETKSQALE---ELTEFYEAKLQEKTTLLEEAQEDVRQQLRE-FEETKKQIE 864
Cdd:cd12923 11 KEINKEYLDKSreyDELYEKYNK-LSQEIQLKRQALEafeEAVKMFEEQLRTQEKFQKEAQPHEKQRLMEnNELLKSRLK 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767902640 865 ededrEIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKE 909
Cdd:cd12923 90 -----ELEESKEQLEEDLRKQVAYNRELEREMNSLKPELMQLRKQ 129
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
676-1044 |
9.68e-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: 43.42 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 676 KREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQLRLKDmnYSEKIKELTD---KFIQEMESLKTKNQVLR 752
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE--ISCQQHTLTQhihTLQQQKTTLTQKLQSLC 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 753 TEKEKQDVYHHEhIEDLLDKQSRELQDMECCNNQ-KLLLEY---------EKYQELQLKS---QRMQEEY--EKQLRDND 817
Cdd:TIGR00618 400 KELDILQREQAT-IDTRTSAFRDLQGQLAHAKKQqELQQRYaelcaaaitCTAQCEKLEKihlQESAQSLkeREQQLQTK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 818 ETKSQALEELTEFYEAKLQEKTTL-------------------------------------LEEAQEDVRQQLREFEETK 860
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLELQEEpcplcgscihpnparqdidnpgpltrrmqrgeqtyaqLETSEEDVYHQLTSERKQR 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 861 KQIEEDEDREIQDiktkyEKKLRDEKEsnlRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQ--MKLQGVIKSLEKDI 938
Cdd:TIGR00618 559 ASLKEQMQEIQQS-----FSILTQCDN---RSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQhaLLRKLQPEQDLQDV 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 939 QGLKREIQER-----------DETIQDKEKRIYDLKKKNQELGKFKFVLDY--KIKELKKQIEPRENEIRVMKEQIQEME 1005
Cdd:TIGR00618 631 RLHLQQCSQElalkltalhalQLTLTQERVREHALSIRVLPKELLASRQLAlqKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 767902640 1006 AELENFHKQNTQLELNITELWQKLRATD-------QEMRRERQKPC 1044
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAAREdalnqslKELMHQARTVL 756
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
793-1021 |
1.06e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 43.13 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 793 EKYQELQLKSQRMQEEYEKQlrdndetKSQALEELTEfyeakLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReiq 872
Cdd:pfam13166 279 DEFTEFQNRLQKLIEKVESA-------ISSLLAQLPA-----VSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRA--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 873 diktKYEKKLRDEKESNL-RLKGETGIMRKKFSSLQKEIE---ERTNDIETLKGEQMKL--QGVIKSLEKDIQGLKREIQ 946
Cdd:pfam13166 344 ----LEAKRKDPFKSIELdSVDAKIESINDLVASINELIAkhnEITDNFEEEKNKAKKKlrLHLVEEFKSEIDEYKDKYA 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902640 947 ERDETIQDKEKRIYDLKKKNQELGKfkfvldyKIKELkkqieprENEIRVMKEQIQEMEAELENFHKQNTQLELN 1021
Cdd:pfam13166 420 GLEKAINSLEKEIKNLEAEIKKLRE-------EIKEL-------EAQLRDHKPGADEINKLLKAFGFGELELSFN 480
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
841-991 |
1.11e-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: 41.47 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 841 LLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE-------SNLRLKgetgiMRKKFSSLQKEIEER 913
Cdd:COG1390 11 ILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAErekrriiSSAELE-----ARKELLEAKEELIEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 914 TNDietlkgeqmKLQGVIKSLEKDI---QGLKREIQERDETIQDKEKRIYdLKKKNQELGKfKFVLDYKIKELKKQIEPR 990
Cdd:COG1390 86 VFE---------EALEKLKNLPKDPeykELLKKLLKEAAEELGSGDLVVY-VNEKDKELLE-ELLKELKKKGLEVSEEDI 154
|
.
gi 767902640 991 E 991
Cdd:COG1390 155 D 155
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
801-1042 |
1.21e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 801 KSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQL---REFEETKKQIEEDEDR--EIQDIK 875
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSIneyNKIESARADLEDIKIKinELKDKH 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 876 TKYEKKlrDEKESNLRLkgetGIMRKKFSSLQKEIEERTN-DIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQD 954
Cdd:PRK01156 546 DKYEEI--KNRYKSLKL----EDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 955 KEKRIYDlkKKNQELGKFKfvldyKIKELKKQIEPRENEIRVMKEQIQEM---EAELENFHKQNTQLELNITELWQKLRA 1031
Cdd:PRK01156 620 SIREIEN--EANNLNNKYN-----EIQENKILIEKLRGKIDNYKKQIAEIdsiIPDLKEITSRINDIEDNLKKSRKALDD 692
|
250
....*....|.
gi 767902640 1032 TDQEMRRERQK 1042
Cdd:PRK01156 693 AKANRARLEST 703
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
707-934 |
1.29e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 707 RVEELKMENEYQLRLKDMNysEKIKELTdkfiQEMESLKTKNQVLRTEKEKQdvyhhEHIEDLLDKQSRELqdmeccnNQ 786
Cdd:TIGR02168 325 LEELESKLDELAEELAELE--EKLEELK----EELESLEAELEELEAELEEL-----ESRLEELEEQLETL-------RS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 787 KLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQE---KTTLLEEAQEDVRQQLREFEETKKQI 863
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaELEELEEELEELQEELERLEEALEEL 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767902640 864 EEdedrEIQDIKTKYEKKLRDEKESNLRLKGetgimrkkFSSLQKEIEERTNDIETLKGEQMKLQGVIKSL 934
Cdd:TIGR02168 467 RE----ELEEAEQALDAAERELAQLQARLDS--------LERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
703-998 |
1.38e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 703 ELKTRVEELKME-NEYQLRLKDMNYS-EKIKELTDKFIQEMESLKTKNQV------LRTEKEKQDVYHHEH----IEDLL 770
Cdd:PRK01156 406 AIKKELNEINVKlQDISSKVSSLNQRiRALRENLDELSRNMEMLNGQSVCpvcgttLGEEKSNHIINHYNEkksrLEEKI 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 771 DKQSRELQDM-ECCNNQKLLLEYEKYQELQ--LKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQE 847
Cdd:PRK01156 486 REIEIEVKDIdEKIVDLKKRKEYLESEEINksINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDS 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 848 ---------------DVRQQLREFEETKKQIEEDEDR------EIQDIKTKYEKKLR--DEKESNLRLKgetgimRKKFS 904
Cdd:PRK01156 566 krtswlnalavisliDIETNRSRSNEIKKQLNDLESRlqeieiGFPDDKSYIDKSIReiENEANNLNNK------YNEIQ 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 905 SLQKEIEERTNDIETLKGEQMKlqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELK 984
Cdd:PRK01156 640 ENKILIEKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELS 715
|
330
....*....|....
gi 767902640 985 KQIEPRENEIRVMK 998
Cdd:PRK01156 716 DRINDINETLESMK 729
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
708-1035 |
1.53e-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: 42.73 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 708 VEELKMENEYQLRLKDMNYS-EKIKELTDKFIQEMESLKT--KNQvlrTEKEKQDVYHHEHIEDLLDKQSRELQDMECCN 784
Cdd:TIGR01612 1401 LEECKSKIESTLDDKDIDECiKKIKELKNHILSEESNIDTyfKNA---DENNENVLLLFKNIEMADNKSQHILKIKKDNA 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 785 NQKLLLEYEKYQELQLKSQRMQEEYEK---QLRDNDETKSQALEELTE----FYEAKLQEKttlLEEAQEDVRQQLREFE 857
Cdd:TIGR01612 1478 TNDHDFNINELKEHIDKSKGCKDEADKnakAIEKNKELFEQYKKDVTEllnkYSALAIKNK---FAKTKKDSEIIIKEIK 1554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 858 ETKKQIEEDEDREIQDIKTKYEKKLRDEKE---SNLRLKGETGI------MRKKFSSLQkEIEERTNDIETlkgEQMKLQ 928
Cdd:TIGR01612 1555 DAHKKFILEAEKSEQKIKEIKKEKFRIEDDaakNDKSNKAAIDIqlslenFENKFLKIS-DIKKKINDCLK---ETESIE 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 929 GVIKSLEKDIQGLK--------REIQERDETIQDKEKRIYDLKKKNQElgkfkfvLDYKIKELKKQIEPREN--EIRVMk 998
Cdd:TIGR01612 1631 KKISSFSIDSQDTElkengdnlNSLQEFLESLKDQKKNIEDKKKELDE-------LDSEIEKIEIDVDQHKKnyEIGII- 1702
|
330 340 350
....*....|....*....|....*....|....*...
gi 767902640 999 EQIQEM-EAELENFHKQNTQLELNITELWQKLRATDQE 1035
Cdd:TIGR01612 1703 EKIKEIaIANKEEIESIKELIEPTIENLISSFNTNDLE 1740
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
695-1042 |
1.53e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 695 EEKAQVMLELKTRVEELKME-NEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHH--EHIEDLLD 771
Cdd:COG4717 91 AELQEELEELEEELEELEAElEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELREleEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 772 KQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQE---EYEKQLRDNDETKSQALEELTEFY--------EAKLQEKTT 840
Cdd:COG4717 171 ELAELQEELEELLEQLSLATEEELQDLAEELEELQQrlaELEEELEEAQEELEELEEELEQLEneleaaalEERLKEARL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 841 LLEEA----------------------------------------QEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEK 880
Cdd:COG4717 251 LLLIAaallallglggsllsliltiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 881 KLRDEKESNLRLKGETGIMRKKFSSLQKEIEE-RTNDIETLKGEQMKLQGViksleKDIQGLkREIQERDETIQDKEKRI 959
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEAGV-----EDEEEL-RAALEQAEEYQELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 960 YDLKKK-NQELGKFKFVLDY--------KIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNT---------QLELN 1021
Cdd:COG4717 405 EELEEQlEELLGELEELLEAldeeeleeELEELEEELEELEEELEELREELAELEAELEQLEEDGElaellqeleELKAE 484
|
410 420
....*....|....*....|....
gi 767902640 1022 ITEL---WQKLRATDQEMRRERQK 1042
Cdd:COG4717 485 LRELaeeWAALKLALELLEEAREE 508
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
836-1025 |
1.56e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 836 QEKTTLLEEAQEdvrQQLREFEETKKQIEEDEDREIQDIKTKYEK---KLRDEKESNLRLKGETGIMRKK---------- 902
Cdd:PRK05771 16 SYKDEVLEALHE---LGVVHIEDLKEELSNERLRKLRSLLTKLSEaldKLRSYLPKLNPLREEKKKVSVKsleelikdve 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 903 --FSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEK------DIQ-------------GLKREIQERDETI--------- 952
Cdd:PRK05771 93 eeLEKIEKEIKELEEEISELENEIKELEQEIERLEPwgnfdlDLSlllgfkyvsvfvgTVPEDKLEELKLEsdvenveyi 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 953 -QDKEKRIY-------DLKKKNQELGKF---KFVLDYK--IKELKKQIEPRENEIrvmKEQIQEMEAELENFHKQNTQLE 1019
Cdd:PRK05771 173 sTDKGYVYVvvvvlkeLSDEVEEELKKLgfeRLELEEEgtPSELIREIKEELEEI---EKERESLLEELKELAKKYLEEL 249
|
....*.
gi 767902640 1020 LNITEL 1025
Cdd:PRK05771 250 LALYEY 255
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
699-1039 |
1.74e-03 |
|
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: 42.47 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 699 QVMLELKTRVEELkmENEYQ------LRLkDMNysekIKELTDKFIQEMESLKTKNQvlrtEKEKQdvyhhehiedlLDK 772
Cdd:pfam01576 692 QQVEEMKTQLEEL--EDELQatedakLRL-EVN----MQALKAQFERDLQARDEQGE----EKRRQ-----------LVK 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 773 QSRELQ-DMECCNNQK-LLLEYEKYQELQLK--------SQRMQEEYEKQL-----------RDNDETKSQALEELTEFY 831
Cdd:pfam01576 750 QVRELEaELEDERKQRaQAVAAKKKLELDLKeleaqidaANKGREEAVKQLkklqaqmkdlqRELEEARASRDEILAQSK 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 832 EA--KLQEKTTLLEEAQEDvrqqLREFEETKKQIEEDEDR---EI----------QDIKTKYEKKLRDEKESNLRLKGET 896
Cdd:pfam01576 830 ESekKLKNLEAELLQLQED----LAASERARRQAQQERDEladEIasgasgksalQDEKRRLEARIAQLEEELEEEQSNT 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 897 GIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDK--------EKRIYDLK----- 963
Cdd:pfam01576 906 ELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKfkssiaalEAKIAQLEeqleq 985
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902640 964 --KKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLElnitELWQKLRATDQEMRRE 1039
Cdd:pfam01576 986 esRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAE----EEASRANAARRKLQRE 1059
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
675-1040 |
1.75e-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: 42.73 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 675 IKREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQ------EMESLKTKN 748
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKElqqlegSSDRILELD 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 749 QVLRTE---------------KEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEyekyQELQLKSQRMQEEyeKQL 813
Cdd:TIGR00606 478 QELRKAerelskaeknsltetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT----QMEMLTKDKMDKD--EQI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 814 RDNDETKSQALEELTEFYEAKLQEKTTL---------LEEAQEDVRQQLREFEETKKQIEEDEDREIQDIkTKYEKKLRD 884
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYFPNKKQLEDWLhskskeinqTRDRLAKLNKELASLEQNKNHINNELESKEEQL-SSYEDKLFD 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 885 -----EKESNL-RLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQmklQGVIKSLEKDIQgLKREIQERDETIQDKEKR 958
Cdd:TIGR00606 631 vcgsqDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEN---QSCCPVCQRVFQ-TEAELQEFISDLQSKLRL 706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 959 IYDlkkknqelgkfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQntqlelnITELWQKLRATDQEMRR 1038
Cdd:TIGR00606 707 APD-----------------KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE-------IPELRNKLQKVNRDIQR 762
|
..
gi 767902640 1039 ER 1040
Cdd:TIGR00606 763 LK 764
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
849-1014 |
1.83e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 849 VRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQ 928
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKT----IKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 929 GVIKSLEKDIQGLkreiQERDE------TIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKqiepRENEIRVMKEQIQ 1002
Cdd:PHA02562 269 SKIEQFQKVIKMY----EKGGVcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEE----IMDEFNEQSKKLL 340
|
170
....*....|..
gi 767902640 1003 EMEAELENFHKQ 1014
Cdd:PHA02562 341 ELKNKISTNKQS 352
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
764-1042 |
1.83e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 764 EHIEDLLDKQSRELQDMECcNNQKLLLEYE----KYQELQ--LKSQRMQ-----EEYEKQLrDNDETKSQALEELTE--- 829
Cdd:PRK04778 115 DLIEEDIEQILEELQELLE-SEEKNREEVEqlkdLYRELRksLLANRFSfgpalDELEKQL-ENLEEEFSQFVELTEsgd 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 830 FYEA-----KLQEKTT-----------LLEEAQEDVRQQLREFEETKKQIEEDE--------DREIQDIKTKYEKKLrdE 885
Cdd:PRK04778 193 YVEAreildQLEEELAaleqimeeipeLLKELQTELPDQLQELKAGYRELVEEGyhldhldiEKEIQDLKEQIDENL--A 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 886 KESNLRLkgetgimrKKFSSLQKEIEERtndIETLkgeqmklqgvIKSLEKDIQGlKREIQERDETIQDKEKRiydLKKK 965
Cdd:PRK04778 271 LLEELDL--------DEAEEKNEEIQER---IDQL----------YDILEREVKA-RKYVEKNSDTLPDFLEH---AKEQ 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 966 NQELG------KFKFVLDYKIKELKKQIEPRENEIRVMKEQIQ-----------EMEAELENFHKQNTQLELNITELWQK 1028
Cdd:PRK04778 326 NKELKeeidrvKQSYTLNESELESVRQLEKQLESLEKQYDEITeriaeqeiaysELQEELEEILKQLEEIEKEQEKLSEM 405
|
330
....*....|....
gi 767902640 1029 LRATDQEMRRERQK 1042
Cdd:PRK04778 406 LQGLRKDELEAREK 419
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
697-950 |
1.89e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 41.91 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 697 KAQVMLELKTRVEELKmeNEYQLRLKDMNysekikELTDKFIQEMESLKT------KNQVLRTEKEKQDVyhHEHIEDLL 770
Cdd:pfam03999 141 SLEELESFRKHLENLR--NEKERRLEEVN------ELKKQIKLLMEELDLvpgtdfEEDLLCESEDNFCL--SRENIDKL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 771 DKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEaKLQE-KTTLLEEAQEDV 849
Cdd:pfam03999 211 RKLIKQLEEQKAEREEKIDDLREKILELWNRLQVPQEEQESFVRENNSLSQDTIDALREELQ-RLEElKKKNIKKLIEDL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 850 RQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNL-RLKGETGIMRK------KFSSLQK---EIEERTNDIE- 918
Cdd:pfam03999 290 RVEIEELWDKLFYSTEQRKRFIPFFEELYTEDLLELHELELkRLKEEYESNKEilelveKWEELWEdmeELEAKANDPSr 369
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767902640 919 --------TLKGEQM--KLQgviKSLEKDIQGLKREIQERDE 950
Cdd:pfam03999 370 fnnrggklLLKEEKErkRLT---RKLPKIEQELTEKVEAWES 408
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
909-1042 |
1.96e-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: 42.52 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 909 EIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIY----DLKKKNQELGKFKFVLDYKIKELK 984
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRtlddQWKEKRDELNGELSAADAAVAKDR 321
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902640 985 KQIEPRENEIRV-MKEQIQEMEAELENFHKQNTQLEL---NITELWQKLRATDQEMRRERQK 1042
Cdd:pfam12128 322 SELEALEDQHGAfLDADIETAAADQEQLPSWQSELENleeRLKALTGKHQDVTAKYNRRRSK 383
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
703-956 |
2.15e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 41.34 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 703 ELKTRVEELKMEN-EYQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLRTEKEKQdvyhhehiedlLDKQSRELQdme 781
Cdd:pfam17045 27 EGQTRALETRLDIrEEELLSARNTLERKHKEI-GLLRQQLEELEKGKQELVAKYEQQ-----------LQKLQEELS--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 782 ccnnqKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELT------EFYEAKLQEKTTLLEEAQEDVRQQLRE 855
Cdd:pfam17045 92 -----KLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRqkslewEQQRLQYQQQVASLEAQRKALAEQSSL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 856 FE--------ETKKQIEEDEDREIQDIKTKYEKKlrdeKESNLRLKGETgimrKKFSSLQKEIeerTNDIETLKGEQMKL 927
Cdd:pfam17045 167 IQsaayqvqlEGRKQCLEASQSEIQRLRSKLERA----QDSLCAQELEL----ERLRMRVSEL---GDSNRKLLEEQQRL 235
|
250 260
....*....|....*....|....*....
gi 767902640 928 QGVIKSLEKDIQGLKREIQERDETIQDKE 956
Cdd:pfam17045 236 LEELRMSQRQLQVLQNELMELKATLQSQD 264
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
725-1025 |
2.17e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 725 NYSEKIKELTDKF---IQEMESLKTKNQVLRTEkekqdvyhhehIEDLLDKQSRELQDMECCnnqkllleYEKY------ 795
Cdd:pfam00038 1 NEKEQLQELNDRLasyIDKVRFLEQQNKLLETK-----------ISELRQKKGAEPSRLYSL--------YEKEiedlrr 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 796 QELQLKSQRMQEEYEkqlRDNdetksqaLEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEET-------KKQIEEDED 868
Cdd:pfam00038 62 QLDTLTVERARLQLE---LDN-------LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEAtlarvdlEAKIESLKE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 869 rEIQDIKTKYEKKLRDekesnlrlkgetgimrkkfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGL-KREIQE 947
Cdd:pfam00038 132 -ELAFLKKNHEEEVRE---------------------LQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIaAKNREE 189
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902640 948 RDETIQDKEKRIYDLKKKNQElgkfkfvldykikelkkQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL 1025
Cdd:pfam00038 190 AEEWYQSKLEELQQAAARNGD-----------------ALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAET 250
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
815-963 |
2.35e-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: 40.43 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 815 DNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREiqdiKTKYEKKLRDEKESNLRLKG 894
Cdd:pfam05010 7 DAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQ----KELEHAEIQKVLEEKDQALA 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902640 895 ETGIMRKKFSSLQKEIEertndietlkgeqmKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 963
Cdd:pfam05010 83 DLNSVEKSFSDLFKRYE--------------KQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALK 137
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
799-926 |
2.53e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 39.64 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 799 QLKSQRMQEEYEKQLRDndETKSQALEELTEFYEaklQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKY 878
Cdd:pfam05672 22 QAREQREREEQERLEKE--EEERLRKEELRRRAE---EERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQ 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767902640 879 EKKLRDEKESNLRLKGETGIMR----KKFSSLQKEIEERTNDIEtlkgEQMK 926
Cdd:pfam05672 97 ERLQKQKEEAEAKAREEAERQRqereKIMQQEEQERLERKKRIE----EIMK 144
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
731-879 |
2.72e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 40.87 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 731 KELTDKFIQEMeslktKNQVLRTEKEKQDVYHH-EHIE-DLLDKQSRE---------LQDMECCNNQKllleyEKYQELQ 799
Cdd:COG4026 72 RELAEKFFEEL-----KGMVGHVERMKLPLGHDvEYVDvELVRKEIKNaiiraglksLQNIPEYNELR-----EELLELK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 800 LKSQRMQEEYEKQLRDNDETKSQaLEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYE 879
Cdd:COG4026 142 EKIDEIAKEKEKLTKENEELESE-LEELREEYK-KLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEVFSLEELWK 219
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
848-1025 |
2.86e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 848 DVRQQLREFEETKKQIEEdedrEIQDIKTKyEKKLRDEKESnLRLKGETgiMRK-------KFSSLQKEIEERTNDIETL 920
Cdd:PRK04778 109 EIESLLDLIEEDIEQILE----ELQELLES-EEKNREEVEQ-LKDLYRE--LRKsllanrfSFGPALDELEKQLENLEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 921 ---------KGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEK----RIYDLKKKNQELGKFKFVLDykikelKKQI 987
Cdd:PRK04778 181 fsqfvelteSGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTelpdQLQELKAGYRELVEEGYHLD------HLDI 254
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767902640 988 EPrenEIRVMKEQIQEMEAELENFH-----KQNTQLELNITEL 1025
Cdd:PRK04778 255 EK---EIQDLKEQIDENLALLEELDldeaeEKNEEIQERIDQL 294
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
898-1048 |
2.94e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 898 IMRKKFSSLQKEIEERTNDIetlkgeqmklqgvIKSLEKDIQGLKREI--QERDETIQDKEKRIYDLKKKNQELgkfkfv 975
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRI-------------LEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNEL------ 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902640 976 ldykiKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKpclISG 1048
Cdd:PRK12704 85 -----QKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER---ISG 149
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
827-1024 |
3.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 827 LTEFYEAKLQEKTTLLEEAqEDVRQQLREFEETKKQIEEDEDR-----EIQDIKTKYEKKLRDEKESN-LRLKGETGIMR 900
Cdd:COG4913 209 LDDFVREYMLEEPDTFEAA-DALVEHFDDLERAHEALEDAREQiellePIRELAERYAAARERLAELEyLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 901 KKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDetiqdkekriydlkkknqelGKfkfvldyki 980
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG--------------------GD--------- 338
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767902640 981 kelkkQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITE 1024
Cdd:COG4913 339 -----RLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
673-883 |
3.06e-03 |
|
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: 41.88 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 673 RGIKREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLR 752
Cdd:pfam02463 798 AQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEE 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 753 TEKEKQDVyhhEHIEDLLDKQSRELQDMEccnnQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSqalEELTEFYE 832
Cdd:pfam02463 878 ELEEQKLK---DELESKEEKEKEEKKELE----EESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEE---LLLEEADE 947
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902640 833 AKLQEKTTLLEEaqEDVRQQLREFEET-------------KKQIEEDEDREIQDIKTKYEKKLR 883
Cdd:pfam02463 948 KEKEENNKEEEE--ERNKRLLLAKEELgkvnlmaieefeeKEERYNKDELEKERLEEEKKKLIR 1009
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
841-936 |
3.90e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 38.32 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 841 LLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETL 920
Cdd:pfam13863 14 ALDAKREEIERLEELLKQREEELEKKE-QELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQIEEL 92
|
90
....*....|....*.
gi 767902640 921 KGEQMKLQGVIKSLEK 936
Cdd:pfam13863 93 KSEISKLEEKLEEYKP 108
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
822-932 |
3.96e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 822 QALEELtefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE---------SNLRL 892
Cdd:PRK00409 523 ASLEEL----ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikelRQLQK 598
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767902640 893 KGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIK 932
Cdd:PRK00409 599 GGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
703-861 |
4.04e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 703 ELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKnqvLRTEKEKQDVYHHEHI---------EDLLDKQ 773
Cdd:PRK04863 963 EVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQ---LRQAQAQLAQYNQVLAslkssydakRQMLQEL 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 774 SRELQDMEccnnqkllLEYEKYQELQLKSQRmqEEYEKQLRDNDETKSQALEELTeFYEAKLQEKTTLLEEAQEDVRQQL 853
Cdd:PRK04863 1040 KQELQDLG--------VPADSGAEERARARR--DELHARLSANRSRRNQLEKQLT-FCEAEMDNLTKKLRKLERDYHEMR 1108
|
....*...
gi 767902640 854 REFEETKK 861
Cdd:PRK04863 1109 EQVVNAKA 1116
|
|
| WDR74 |
cd22857 |
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ... |
343-420 |
4.12e-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: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 343 CLCFSPSEETLVASTSKNQLYSI---TMSLTEISKGepahfeylmypLHSAPITGLATCIRKPLIATCSLDRSIRLWNYE 419
Cdd:cd22857 228 AVAEDPDGHTVYVGDTSGDLASIdlrTGKLLGCFKG-----------KCGGSIRSIARHPELPLIASCGLDRYLRIWDTE 296
|
.
gi 767902640 420 T 420
Cdd:cd22857 297 T 297
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
936-1025 |
4.18e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.50 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 936 KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEI---RVMKEQIQEMEAELENFH 1012
Cdd:pfam13851 26 ELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKqslKNLKARLKVLEKELKDLK 105
|
90
....*....|...
gi 767902640 1013 KQNTQLELNITEL 1025
Cdd:pfam13851 106 WEHEVLEQRFEKV 118
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
931-1042 |
4.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 931 IKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVL--DYKIKELKKQIEPRENEI----------RVMK 998
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELEAELerldassddlAALE 691
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767902640 999 EQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQK 1042
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
706-994 |
4.44e-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: 41.19 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 706 TRVEELKMENEYQLRlKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEK--QDVYHHEHIEDLLDKQSRELQD---- 779
Cdd:TIGR00606 825 QQVNQEKQEKQHELD-TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQigTNLQRRQQFEEQLVELSTEVQSlire 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 780 MECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQAlEELTE--FYEAKLQEKttlLEEAQED--------- 848
Cdd:TIGR00606 904 IKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK-EKVKNihGYMKDIENK---IQDGKDDylkqketel 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 849 --VRQQLREFEETKKQIEEDEDREIQDIKT---------------KYEKKLRDEKESNLRLKGETGIMRkkFSSLQKEIE 911
Cdd:TIGR00606 980 ntVNAQLEECEKHQEKINEDMRLMRQDIDTqkiqerwlqdnltlrKRENELKEVEEELKQHLKEMGQMQ--VLQMKQEHQ 1057
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 912 ERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDetIQDKEKRIYDL-------KKKNQELGKFKFVLDYKIKELK 984
Cdd:TIGR00606 1058 KLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ--FRDAEEKYREMmivmrttELVNKDLDIYYKTLDQAIMKFH 1135
|
330
....*....|
gi 767902640 985 KQIEPRENEI 994
Cdd:TIGR00606 1136 SMKMEEINKI 1145
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
737-895 |
4.55e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.71 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 737 FIQEMESLKTKNQVLRTEKEKQDVYHHEHIEDLLDKQSRELQD-MECCNNQKLLLEYE---KYQELQLKSQRMQEEyekQ 812
Cdd:pfam15709 324 LLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEqLERAEKMREELELEqqrRFEEIRLRKQRLEEE---R 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 813 LRDNDETKSQALEELT---------EFYEAKLQE--KTTLLEEAQ--EDVRQQLREFE-----ETKKQIE--EDEDREIQ 872
Cdd:pfam15709 401 QRQEEEERKQRLQLQAaqerarqqqEEFRRKLQElqRKKQQEEAEraEAEKQRQKELEmqlaeEQKRLMEmaEEERLEYQ 480
|
170 180
....*....|....*....|...
gi 767902640 873 DIKTKYEKKLRDEKESNlRLKGE 895
Cdd:pfam15709 481 RQKQEAEEKARLEAEER-RQKEE 502
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
694-880 |
4.77e-03 |
|
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: 39.91 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 694 MEEKAQVMLELKTRVEELkmeNEYQLRLKDMNysEKIKELTDKFI---QEMESLKTKNQVLRTEKEKQDvyhhEHIEDLL 770
Cdd:COG1579 2 MPEDLRALLDLQELDSEL---DRLEHRLKELP--AELAELEDELAaleARLEAAKTELEDLEKEIKRLE----LEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 771 DKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELtefyEAKLQEKTTLLEEAQEDVR 850
Cdd:COG1579 73 ARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAEL----EAELAELEAELEEKKAELD 148
|
170 180 190
....*....|....*....|....*....|....
gi 767902640 851 QQLREFEETKKQIEEDEDREI----QDIKTKYEK 880
Cdd:COG1579 149 EELAELEAELEELEAEREELAakipPELLALYER 182
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
789-870 |
4.96e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 789 LLEYEKYQELQLKSQRMQEEYEKQLrDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED 868
Cdd:COG3096 521 LAELEQRLRQQQNAERLLEEFCQRI-GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
..
gi 767902640 869 RE 870
Cdd:COG3096 600 RA 601
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
793-1004 |
5.07e-03 |
|
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.
Pssm-ID: 185746 [Multi-domain] Cd Length: 342 Bit Score: 40.40 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 793 EKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLL-EEAQEDvrQQLREFEETKKQIEEDEDREI 871
Cdd:cd08915 51 QKPENLPDSIQHSQEIIEEGGLDNIEQSFKELSKLRQNVEELLQECEELLeEEAAED--DQLRAKFGTLRWRRPSSDEAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 872 QDIKTKYEK---KLRDEKESNLRL-------KGETGIMRKKFSSLQKEIEERTNDIETlkgeqmKLQGVIKSLEKDIQGL 941
Cdd:cd08915 129 KELYEKVTKlrgYLEQASNSDNEVlqcyesiDPNLVLLCGGYKELKAFIPSPYPALDP------EVSEVVSSLRPLLNEV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 942 KREIQERDETIQDKEKRIYD---------LKKKNQ----------ELGKFKFVLDYKIKELKKQIEpRENEIRVMKEQIQ 1002
Cdd:cd08915 203 SELEKERERFISELEIKSRNndilpklitEYKKNGttefedlfeeHLKKFDKDLTYVEKTKKKQIE-LIKEIDAANQEFS 281
|
..
gi 767902640 1003 EM 1004
Cdd:cd08915 282 QV 283
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
669-990 |
5.34e-03 |
|
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: 40.96 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 669 DKDGR-GIKREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQLRlkdmnysEKIKELTDkFIQEMESLKTK 747
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDR-------ERLEELES-LKKENKDLKEK 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 748 NQVLR---TEKEKQDVYHHEHIEDL----LDKQSReLQDMECCNNQK------LLLEYEKYQELQLkSQRMQEEYEKQLR 814
Cdd:pfam10174 484 VSALQpelTEKESSLIDLKEHASSLassgLKKDSK-LKSLEIAVEQKkeecskLENQLKKAHNAEE-AVRTNPEINDRIR 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 815 D---------NDETKSQA-----LEELTEFYEAKLQ--------EKTTLL---EEAQEDVRQQLREFEETKKQIEEDED- 868
Cdd:pfam10174 562 LleqevarykEESGKAQAeverlLGILREVENEKNDkdkkiaelESLTLRqmkEQNKKVANIKHGQQEMKKKGAQLLEEa 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 869 --REIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMK-LQGViksLEKDIQGLKREI 945
Cdd:pfam10174 642 rrREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKqLEEI---LEMKQEALLAAI 718
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 767902640 946 QERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPR 990
Cdd:pfam10174 719 SEKDANIALLELSSSKKKKTQEEVMALKREKDRLVHQLKQQTQNR 763
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
691-1014 |
5.46e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 691 KTDMEEKAQVMLELKTRVEELKMENEYQLRLKdmnysEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVyHHEHIEDLL 770
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLE-----EELEQARSELEQLEEELEELNEQLQAAQAELAQ-AQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 771 DKQSRELQDMECCNNQKLLLEYE--KYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQED 848
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQrkQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 849 VRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQ 928
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 929 GVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAEL 1008
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
....*.
gi 767902640 1009 ENFHKQ 1014
Cdd:COG4372 348 VGLLDN 353
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
676-887 |
5.57e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.29 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 676 KREREVGFAEEVLVTKTDMEEKAQVMLElKTRVEELKMEnEYQLRL--KDMNYSEKIKELTDKFIQEMESLKTKNQVLRT 753
Cdd:pfam13868 121 KLEKQRQLREEIDEFNEEQAEWKELEKE-EEREEDERIL-EYLKEKaeREEEREAEREEIEEEKEREIARLRAQQEKAQD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 754 EKEKQD----VYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELte 829
Cdd:pfam13868 199 EKAERDelraKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEI-- 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767902640 830 fYEAKLQEKTTLLEEAQEDVRQQLREFEETK---KQIEEDEDREIQDIKTKYEKKLRDEKE 887
Cdd:pfam13868 277 -EQEEAEKRRMKRLEHRRELEKQIEEREEQRaaeREEELEEGERLREEEAERRERIEEERQ 336
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
703-969 |
6.00e-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: 40.59 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 703 ELKTRVEELKMENEYQLRLKDMNYSEKIKELT-DKFIQEMESLKTKNQVLRTEKEKQdVYHHEHIEDLLDKQSRELQDME 781
Cdd:pfam12128 276 SRQEERQETSAELNQLLRTLDDQWKEKRDELNgELSAADAAVAKDRSELEALEDQHG-AFLDADIETAAADQEQLPSWQS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 782 CCNNQkllleyEKYQELQLKSQR-MQEEYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLLEEAQEDVRQQLrefEETK 860
Cdd:pfam12128 355 ELENL------EERLKALTGKHQdVTAKYNRRRSKIKEQNNRDIAGIKD-KLAKIREARDRQLAVAEDDLQAL---ESEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 861 KQIEEDEDREIQDIKTKYEKKLrdeKESNLRLKGETGImrkkfSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQG 940
Cdd:pfam12128 425 REQLEAGKLEFNEEEYRLKSRL---GELKLRLNQATAT-----PELLLQLENFDERIERAREEQEAANAEVERLQSELRQ 496
|
250 260
....*....|....*....|....*....
gi 767902640 941 LKREIQERDETIQDKEKRIYDLKKKNQEL 969
Cdd:pfam12128 497 ARKRRDQASEALRQASRRLEERQSALDEL 525
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
669-869 |
6.31e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.24 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 669 DKDGRGIKREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQLRL--KDMNYSEKIKELTDkfiQEMESLKT 746
Cdd:pfam02029 131 EETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKikKEKKVKYESKVFLD---QKRGHPEV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 747 KNQVLRTEKEKQDVYHHEHIEDLLDKQSRELQdmeccnnQKLLLEYE-KYQELQLKSQRMQEEYEKQLRDNDETKSQALE 825
Cdd:pfam02029 208 KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEE-------AEVFLEAEqKLEELRRRRQEKESEEFEKLRQKQQEAELELE 280
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767902640 826 ELTEfyeaKLQEKTTLLEEA-----QEDVRQQLREFEETKKQIEEDEDR 869
Cdd:pfam02029 281 ELKK----KREERRKLLEEEeqrrkQEEAERKLREEEEKRRMKEEIERR 325
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
739-921 |
6.65e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 739 QEMESLKTKNQVLRTEKEKQDVYhhEHIEDLlDKQSRELQdmeccnnqkLLLEYEKYQELQLKSQRMQEEYEKQLRDNDE 818
Cdd:COG3206 196 AALEEFRQKNGLVDLSEEAKLLL--QQLSEL-ESQLAEAR---------AELAEAEARLAALRAQLGSGPDALPELLQSP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 819 TKSQALEELTEFyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGI 898
Cdd:COG3206 264 VIQQLRAQLAEL-EAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
170 180
....*....|....*....|...
gi 767902640 899 MrKKFSSLQKEIEERTNDIETLK 921
Cdd:COG3206 343 L-AELPELEAELRRLEREVEVAR 364
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
810-1009 |
6.96e-03 |
|
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: 40.58 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 810 EKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQlREFEETKKQIEEDEDREIQDIKTKYEKklrdEKESN 889
Cdd:pfam10174 44 ERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQ-RDLNQLLQQDFTTSPVDGEDKFSTPEL----TEENF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 890 LRLKGETGIMRKKFSSLQKEIEERTNDIETLKG-------------EQMKLQGVIKSLEKDIQGLKREIQERDETIQDKE 956
Cdd:pfam10174 119 RRLQSEHERQAKELFLLRKTLEEMELRIETQKQtlgardesikkllEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902640 957 KRiydLKKKNQELGKFKFVLDY---------KIKELKKQIEPRENEIRVMKEQIQEMEAELE 1009
Cdd:pfam10174 199 VL---LDQKEKENIHLREELHRrnqlqpdpaKTKALQTVIEMKDTKISSLERNIRDLEDEVQ 257
|
|
| PHA01351 |
PHA01351 |
putative minor structural protein |
721-1027 |
7.31e-03 |
|
putative minor structural protein
Pssm-ID: 107029 Cd Length: 1070 Bit Score: 40.31 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 721 LKDMNYSEKIKELTDKFIqemeslkTKNQVLRTEKekqdvyhhehiedLLDKQSRELQDMECCNNQKLLLEyekyqelqL 800
Cdd:PHA01351 455 FKDLGYPEEVRTVFDTMI-------TQSQLIQTNQ-------------LLLRQLQQIVSLGIFDQKKIKEE--------L 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 801 KSQRMQEEYEKQLRDNDETKSQALEELTEfYEAKLqeKTTLLeeAQEDVRQQLREFEETKKQIEededreiQDIKTKYEK 880
Cdd:PHA01351 507 KANKFNEQVALQILESELQFAQLQNQLKE-YQFKL--NNFLI--SPQDLEKDLKHLGFDSAIIS-------ALIYENQVE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 881 KLRDEKESNLRlkgetGIMRKKFSSLqKEIEERTNDIETLKGEQMKLQGVIkSLEKDIQGLKREIQERDETIQ-DKEKRI 959
Cdd:PHA01351 575 QLIKFQLNNIE-----SLAKKGYLSL-DEIKKQFKAIGIIKEYEDAFINFY-NQELQISAFLTILKSQLRQFQiDPKEAE 647
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 960 YDLKKK--NQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQ 1027
Cdd:PHA01351 648 TELKKLniNEYLANQIIQEEYNINIAKLQLSVLETIAKTLYYDQQQLSGELKKIHKDKTALELYITKFYY 717
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
705-1062 |
7.46e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.59 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 705 KTRVEELkMENEYQLRLKDMNYSEKIKelTDKFIQEMESLKTKNqVLRTEKEKqdvyhhehIEDLLDKQSRELQDMECcn 784
Cdd:PTZ00440 896 KQLVEHL-LNNKIDLKNKLEQHMKIIN--TDNIIQKNEKLNLLN-NLNKEKEK--------IEKQLSDTKINNLKMQI-- 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 785 nQKLLLEYEKYQE-LQLKSQRMQEEYEKQLRDNDETKSQaLEELTEFYEAKLQEKTTLLEEAQEDVRQQL-REFEETKKQ 862
Cdd:PTZ00440 962 -EKTLEYYDKSKEnINGNDGTHLEKLDKEKDEWEHFKSE-IDKLNVNYNILNKKIDDLIKKQHDDIIELIdKLIKEKGKE 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 863 IEEDEDREIQ---DIKTKYEKKLRD---EKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLK-----------GEQM 925
Cdd:PTZ00440 1040 IEEKVDQYISlleKMKTKLSSFHFNidiKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKnkshehvvnadKEKN 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 926 KLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVL----DYKIKELKKQIEPRENEIRVMKEQI 1001
Cdd:PTZ00440 1120 KQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEVNEIEIEYERILidhiVEQINNEAKKSKTIMEEIESYKKDI 1199
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902640 1002 QEMEAELENFHKQNTQlELNITELWQKLRATDQEMRRERQKP-CLISGPCRFTSLNSSETIK 1062
Cdd:PTZ00440 1200 DQVKKNMSKERNDHLT-TFEYNAYYDKATASYENIEELTTEAkGLKGEANRSTNVDELKEIK 1260
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
786-912 |
7.87e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.58 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 786 QKLLLEYEKYQELQLKSQRMQEEYEKQlrdndetkSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE 865
Cdd:pfam02841 179 QEFLQSKEAVEEAILQTDQALTAKEKA--------IEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE 250
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767902640 866 --DEDRE--IQDIKTKYEKKLRDEKEsnLRLKGetgiMRKKFSSLQKEIEE 912
Cdd:pfam02841 251 kmEAEREqlLAEQERMLEHKLQEQEE--LLKEG----FKTEAESLQKEIQD 295
|
|
| BAR_ACAP3 |
cd07637 |
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain ... |
817-875 |
9.88e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ACAP3 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 3), also called centaurin beta-5, is presumed to be an Arf GTPase activating protein (GAP) based on its similarity to the Arf6-specific GAPs ACAP1 and ACAP2. The specific function of ACAP3 is still unknown. ACAP3 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, and C-terminal ankyrin (ANK) repeats. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153321 Cd Length: 200 Bit Score: 38.44 E-value: 9.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902640 817 DETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQL--------REFEETKKQIEE-DEDREIQDIK 875
Cdd:cd07637 56 DEMISECLDKFGDSLQEMVNYHMILFDQAQRSVRQQLhsfvkedvRKFKETKKQFDKvREDLEIALVK 123
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
787-969 |
9.90e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 38.60 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 787 KLLLEYekyqeLQLKSQRMQEEYEKQLRDNDETKSQALE---ELTEFYEAKLQEKTTLLEEA---QEDVRQQLREFEETK 860
Cdd:pfam14988 3 KFFLEY-----LAKKTEEKQKKIEKLWNQYVQECEEIERrrqELASRYTQQTAELQTQLLQKekeQASLKKELQALRPFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902640 861 KqIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGEtgiMRKKFSSLQKEIEE-------RTNDIETLKGEQMKLQGVIKS 933
Cdd:pfam14988 78 K-LKESQEREIQDLEEEKEKVRAETAEKDREAHLQ---FLKEKALLEKQLQElrilelgERATRELKRKAQALKLAAKQA 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 767902640 934 LEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQEL 969
Cdd:pfam14988 154 LSEFCRSIKRENRQLQKELLQLIQETQALEAIKSKL 189
|
|
| |
