|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
392-656 |
2.41e-34 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 136.96 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 392 LIATCSLDRSIRLWNYETNT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDD-IRSFK--EYSVRGcgeC 466
Cdd:COG2319 134 TLASGSADGTVRLWDLATGKlLRTLTGHSGAVTSVAFSPDGKLLASGSDDGtVRLWDLATGKlLRTLTghTGAVRS---V 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 467 SFS-NGGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCS 545
Cdd:COG2319 211 AFSpDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 546 YNCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEY 623
Cdd:COG2319 291 VNSVAFSPDGKLLASGSDDGTVRlwDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL--WDLATGELLRTL 368
|
250 260 270
....*....|....*....|....*....|...
gi 578798459 624 QAHAGPITKMLLTFDDQFLLTAAEDGCLFTWKV 656
Cdd:COG2319 369 TGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
375-667 |
1.82e-31 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 128.49 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 375 PLHSAPITGLATCIRKPLIATCSLDRSIRLWNYETN-TLELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNL----L 448
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGlLLRTLTGHTGAVRSVAFSPDGKTLASGSADGtVRLWDLatgkL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 449 IDDIRSFKE--YSVrgcgecSFSNGGHLFAAVNG-NVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAV 525
Cdd:COG2319 155 LRTLTGHSGavTSV------AFSPDGKLLASGSDdGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 526 YEWNLSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTS 603
Cdd:COG2319 229 RLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRlwDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSD 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578798459 604 VGTIRAmkYPLPLQKEFNEYQAHAGPITKMLLTFDDQFLLTAAEDGclfTWKVFDKDGRGIKRE 667
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 ... |
377-655 |
2.43e-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: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 377 HSAPITGLATCIRKPLIATCSLDRSIRLWNYETNTLEL-FKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNL----LID 450
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtLKGHTGPVRDVAASADGTYLASGSSDKtIRLWDLetgeCVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 451 DIRSFKEYsVRGcgeCSFSNGGHLFAAVNG-NVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 529
Cdd:cd00200 88 TLTGHTSY-VSS---VAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 530 LSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTI 607
Cdd:cd00200 164 LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKlwDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTI 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 578798459 608 RAmkYPLPLQKEFNEYQAHAGPITKMLLTFDDQFLLTAAEDGCLFTWK 655
Cdd:cd00200 244 RV--WDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
330-568 |
6.14e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 111.93 E-value: 6.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 330 VLCLCFSPSEETLvASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWNYET 409
Cdd:COG2319 165 VTSVAFSPDGKLL-ASGSDDG----TVRLWDLATGKLLRT----LTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 410 NT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDDIRSFKEYSVRGCGECSFS-NGGHLFAAVNGNVIHVY 486
Cdd:COG2319 236 GKlLRTLTGHSGSVRSVAFSPDGRLLASGSADGtVRLWDLATGELLRTLTGHSGGVNSVAFSpDGKLLASGSDDGTVRLW 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 487 TTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHT 566
Cdd:COG2319 316 DLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395
|
..
gi 578798459 567 LK 568
Cdd:COG2319 396 VR 397
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
327-529 |
1.30e-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: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 327 KQDVLCLCFSPSEeTLVASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWN 406
Cdd:cd00200 93 TSYVSSVAFSPDG-RILSSSSRDK----TIKVWDVETGKCLTT----LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 407 YETNTL-ELFKEYQEEAYSISLHPSGHFIVVGFADKlrlmNLLIDDIRSFKE-YSVRGCGE----CSFSNGGHLFAAVNG 480
Cdd:cd00200 164 LRTGKCvATLTGHTGEVNSVAFSPDGEKLLSSSSDG----TIKLWDLSTGKClGTLRGHENgvnsVAFSPDGYLLASGSE 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578798459 481 -NVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 529
Cdd:cd00200 240 dGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
692-1210 |
2.36e-21 |
|
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: 100.48 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 692 ELKTRVEELKMENEYQLRLKD-MNYSEKIKELTDKFI-----------QEMESLKTKNQVLRTEKEKQDVYHHEHIEDLL 759
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVeLNKLEKQKKENKKNIdkflteikkkeKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 760 DKQSrelqDMECCNNQKLLLEY---------EKYQELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFYEAKLQEKTTL 830
Cdd:TIGR04523 184 NIQK----NIDKIKNKLLKLELllsnlkkkiQKNKSLESQISELKKQ-NNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 831 LEEAQEDVRQ---QLREFEETKKQIEEDEDReIQDIKTKYEkKLRDEKESNL--RLKGETGIMRKKFSSLQKE------- 898
Cdd:TIGR04523 259 KDEQNKIKKQlseKQKELEQNNKKIKELEKQ-LNQLKSEIS-DLNNQKEQDWnkELKSELKNQEKKLEEIQNQisqnnki 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 899 IEERTNDIETLKGEQM-------KLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKE 971
Cdd:TIGR04523 337 ISQLNEQISQLKKELTnsesensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 972 LKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL-------WQKLRATDQEMRRERQkerDLEALVKRFKT 1044
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntreslETQLKVLSRSINKIKQ---NLEQKQKELKS 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1045 DLHNCVAYIQEPRLLKEKVRGLFEKyvqradmveIAGLNTDlQQEYTRQREHLERNLATLKKKVVK-EGELHRTDYVRIM 1123
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKK---------ISSLKEK-IEKLESEKKEKESKISDLEDELNKdDFELKKENLEKEI 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1124 QENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEpsrdMLSTAPTARLNEQEETGRIIEMQRLEIQRL 1203
Cdd:TIGR04523 564 DEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKE----KKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
....*..
gi 578798459 1204 RDQIQEQ 1210
Cdd:TIGR04523 640 KNKLKQE 646
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
330-532 |
2.40e-20 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 94.98 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 330 VLCLCFSPSEETLvASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCirkP---LIATCSLDRSIRLWN 406
Cdd:COG2319 207 VRSVAFSPDGKLL-ASGSADG----TVRLWDLATGKLLRT----LTGHSGSVRSVAFS---PdgrLLASGSADGTVRLWD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 407 YETNT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDD-IRSFKEYSVRGCGeCSFS-NGGHLFAAVNGNV 482
Cdd:COG2319 275 LATGElLRTLTGHSGGVNSVAFSPDGKLLASGSDDGtVRLWDLATGKlLRTLTGHTGAVRS-VAFSpDGKTLASGSDDGT 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578798459 483 IHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLST 532
Cdd:COG2319 354 VRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
809-1155 |
7.30e-17 |
|
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: 86.65 E-value: 7.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 809 KSQALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNlRLKGETGIM 888
Cdd:TIGR02168 675 RRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 889 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYK 968
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 969 IKELKKQIEPRENEIRVMKEQIQ--------------EMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERD 1034
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIEslaaeieeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1035 LEALVKRFKTDLHNCVAYIQEPRL----LKEKVRglfEKYVQRADMVEIAGLNTDLQQEYTRQRehlernLATLKKKVVK 1110
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVridnLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR------LKRLENKIKE 983
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 578798459 1111 EGELhrtdyvrimqeNVSLIKEINELRRELKFTRSQVYDLEAALK 1155
Cdd:TIGR02168 984 LGPV-----------NLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
493-654 |
3.39e-16 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 80.46 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 493 NISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHTLK--EI 570
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRlwDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 571 ADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQAHAGPITKMLLTFDDQFLLTAAEDGC 650
Cdd:cd00200 81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKV--WDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158
|
....
gi 578798459 651 LFTW 654
Cdd:cd00200 159 IKLW 162
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
467-658 |
4.99e-16 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 81.88 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 467 SFSNGGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSY 546
Cdd:COG2319 44 ASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 547 NCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQ 624
Cdd:COG2319 124 RSVAFSPDGKTLASGSADGTVRlwDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL--WDLATGKLLRTLT 201
|
170 180 190
....*....|....*....|....*....|....
gi 578798459 625 AHAGPITKMLLTFDDQFLLTAAEDGclfTWKVFD 658
Cdd:COG2319 202 GHTGAVRSVAFSPDGKLLASGSADG---TVRLWD 232
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
832-1191 |
5.85e-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: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 832 EEAQEDVRQQLREFEETKKQIEEDEdrEIQDIKTKYEKKLRDEKESNLRLKGETGIMRK-KFSSLQKEIEERTNDIETLK 910
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLD--LIIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 911 GEqmklqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGkfkfvlDYKIKELKKQIEPRENEIRVMKEQI 990
Cdd:TIGR02169 244 RQ-------LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 991 QEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEprlLKEKVRGLFEKY 1070
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE---VDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1071 VQRADMVEiaglntdlqqEYTRQREHLERNLATL---KKKVVKEGELHRTDYVRIMQ-------ENVSLIKEINELRREL 1140
Cdd:TIGR02169 388 KDYREKLE----------KLKREINELKRELDRLqeeLQRLSEELADLNAAIAGIEAkineleeEKEDKALEIKKQEWKL 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578798459 1141 KFTRSQVYDLEAAL-KLTKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGR 1191
Cdd:TIGR02169 458 EQLAADLSKYEQELyDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGG 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
782-1036 |
9.98e-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: 82.81 E-value: 9.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 782 EKYQELQLKSQRMqEEYE--KQLRDNDETKSQALEELTEFyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIE---EDE 856
Cdd:TIGR02169 211 ERYQALLKEKREY-EGYEllKEKEALERQKEAIERQLASL-EEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 857 DREIQ----DIKTKYEKKLRDEKESNLRLKGETGIMRKKFS---SLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQG 929
Cdd:TIGR02169 289 QLRVKekigELEAEIASLERSIAEKERELEDAEERLAKLEAeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 930 LKREIQERDETIQ-------DKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHK 1002
Cdd:TIGR02169 369 LRAELEEVDKEFAetrdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
250 260 270
....*....|....*....|....*....|....
gi 578798459 1003 QNTQLELNITELWQKLRATDQEMRRERQKERDLE 1036
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
685-1008 |
3.14e-15 |
|
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: 81.27 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 685 EKAQVMLELKTRVEELkmenEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQdvyhHEHIEDLLDKQSR 764
Cdd:TIGR02169 208 EKAERYQALLKEKREY----EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR----LEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 765 ELQDM---ECCNNQKLLLEYEKYQElqlKSQRMQEEYEKQLRDNDETKSQALEELTefyeaKLQEKTTLLEEAQEDVRQQ 841
Cdd:TIGR02169 280 KIKDLgeeEQLRVKEKIGELEAEIA---SLERSIAEKERELEDAEERLAKLEAEID-----KLLAEIEELEREIEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 842 LREFEEtkkqieededrEIQDIKTKYEK---KLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQG 918
Cdd:TIGR02169 352 RDKLTE-----------EYAELKEELEDlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 919 VIKSLEKDIQGLKREIQERDETIQDKEKRIydlKKKNQELgkfkfvldykiKELKKQIEPRENEIRVMKEQIQEMEAELE 998
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEI---KKQEWKL-----------EQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
330
....*....|
gi 578798459 999 NFHKQNTQLE 1008
Cdd:TIGR02169 487 KLQRELAEAE 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
701-1211 |
1.26e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.95 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 701 KMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKtkNQVLRTEKEKQDVYHH-EHIEDLLDKQSRELQDMEccnnqKLLL 779
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIE--ELIKEKEKELEEVLREiNEISSELPELREELEKLE-----KEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 780 EYEKYQELQLKSQRMQEEYEKQLRdndetksqaleeltefyeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE----- 854
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKR-------------------KLEEKIRELEERIEELKKEIEELEEKVKELKElkeka 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 855 DEDREIQDIKTKYEKKLRDEKESNLRLKGE-TGIMR--KKFSSLQKEIEERTNDIETLKGEQMKLQG------VIKSLEK 925
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEiNGIEEriKELEEKEERLEELKKKLKELEKRLEELEErhelyeEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 926 DIQGLK-----REIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQI-------------------EPREN 981
Cdd:PRK03918 373 ELERLKkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteEHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 982 EIRVMKEQIQEMEAELENFHKQNTQLELNITELwQKLRATDQEMRRERQKERDLEALVKRFKT-DLHNCVAYIQEPRLLK 1060
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1061 EKVRGLFEkyvqradmvEIAGLNTDLQ--QEYTRQREHLERNLATLKKKVvkeGELHRtdyvRIMQENVSLIKEINELRR 1138
Cdd:PRK03918 532 EKLIKLKG---------EIKSLKKELEklEELKKKLAELEKKLDELEEEL---AELLK----ELEELGFESVEELEERLK 595
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578798459 1139 ELKFTRSQVYDLEAAlkltkkvrPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQE 1211
Cdd:PRK03918 596 ELEPFYNEYLELKDA--------EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
818-1159 |
3.75e-14 |
|
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: 77.79 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 818 EFYEAKLQEKTTLLEEA------QEDVRQQLREFEETKKQIEEDED--REI---------QDIKTKYEKKLRDEKEsNLR 880
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAagiskyKERRKETERKLERTRENLDRLEDilNELerqlkslerQAEKAERYKELKAELR-ELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 881 LkgetGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGK 960
Cdd:TIGR02168 227 L----ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 961 FKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVK 1040
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1041 RFKTDLHncvayiqeprLLKEKVrglfekYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEgelHRTDYV 1120
Cdd:TIGR02168 383 TLRSKVA----------QLELQI------ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE---LQAELE 443
|
330 340 350
....*....|....*....|....*....|....*....
gi 578798459 1121 RIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKK 1159
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
715-1038 |
1.20e-13 |
|
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: 75.87 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 715 YSEKIKELTDkfiqEMESLKTKNQVLRTEKEkqdvyhheHIEDLLDKQSRELQDMEccnnqKLLLEYEKYQELQLKSQRM 794
Cdd:TIGR02169 672 EPAELQRLRE----RLEGLKRELSSLQSELR--------RIENRLDELSQELSDAS-----RKIGEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 795 QEEYEKQLRDNDETKSQALEEltefYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDE 874
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIEN----VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 875 KESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK 954
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 955 NQElgkfkfvLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL----WQKLRATDQEMRRERq 1030
Cdd:TIGR02169 891 RDE-------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipEEELSLEDVQAELQR- 962
|
....*...
gi 578798459 1031 KERDLEAL 1038
Cdd:TIGR02169 963 VEEEIRAL 970
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
681-1211 |
1.42e-13 |
|
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: 75.93 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 681 TDMEEK-AQVMLELK--TRVEELKMEN-EYQLRLKDMNYSEKIKElTDKFIQEMESLKTKNQVLRTekekqDVYHHEHIE 756
Cdd:pfam15921 320 SDLESTvSQLRSELReaKRMYEDKIEElEKQLVLANSELTEARTE-RDQFSQESGNLDDQLQKLLA-----DLHKREKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 757 DLLDKQSRELQDMECCNN-------QKLLLEYEKYQELQLKSQRMQEEYEKQLrdndETKSQALEELTEFYEaKLQEKTT 829
Cdd:pfam15921 394 SLEKEQNKRLWDRDTGNSitidhlrRELDDRNMEVQRLEALLKAMKSECQGQM----ERQMAAIQGKNESLE-KVSSLTA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 830 LLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKESNlrlkgetgimrKKFSSLQKEIEERTNDIETL 909
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSE-RTVSDLTASLQEKERAIEATN-----------AEITKLRSRVDLKLQELQHL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 910 KGEQMKLQGVikslEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQ 989
Cdd:pfam15921 537 KNEGDHLRNV----QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 990 IQEMEAELENFHKQNTQLELNITELwqkLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEk 1069
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLELEKVKL---VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE- 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1070 yvqradmvEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGElhrtdyvrIMQENVSLIKEINELRRELKFTRSQVYD 1149
Cdd:pfam15921 689 --------EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH--------AMKVAMGMQKQITAKRGQIDALQSKIQF 752
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578798459 1150 LEAALKLTKKVRPQEVSETEPSRDMLSTAPTarlnEQEETGRIIEMQRLEIQRLRDQIQEQE 1211
Cdd:pfam15921 753 LEEAMTNANKEKHFLKEEKNKLSQELSTVAT----EKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
674-1044 |
1.42e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 674 EEVLVTKTDMEEKAQVMLELKTRVEELKmENEYQLRLKDMNYSEKIKELTDKfIQEMESLKTKNQVLRTEKE--KQDVYH 751
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEER-IKELEEKEERLEELKKKLKelEKRLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 752 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQ----------ALEEL----- 816
Cdd:PRK03918 357 LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGElkkeikelkkAIEELkkakg 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 817 ---------TEFYEAKLQEKTTLleeaqedvrqQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKE--SNLRLKGET 885
Cdd:PRK03918 437 kcpvcgrelTEEHRKELLEEYTA----------ELKRIEKELKEIEEKE-RKLRKELRELEKVLKKESEliKLKELAEQL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 886 GIMRKKFSSLQKE-IEERTNDIETLKGEQMKLQGVIKSLEKDI---QGLKREIQERDETIQDKEKRIYDLKKKNQELGkF 961
Cdd:PRK03918 506 KELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELeklEELKKKLAELEKKLDELEEELAELLKELEELG-F 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 962 KFV--LDYKIKEL-------------KKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMR 1026
Cdd:PRK03918 585 ESVeeLEERLKELepfyneylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEEL 664
|
410 420
....*....|....*....|
gi 578798459 1027 RER--QKERDLEALVKRFKT 1044
Cdd:PRK03918 665 REEylELSRELAGLRAELEE 684
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
659-1159 |
1.86e-13 |
|
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: 75.14 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 659 KDGRGIKREReVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEyQLRLKdmnYSEKIKELTDkFIQEMESLKTKNQ 738
Cdd:pfam05483 85 KEAEKIKKWK-VSIEAELKQKENKLQENRKIIEAQRKAIQELQFENE-KVSLK---LEEEIQENKD-LIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 739 VLR------TEKEKQDVYHHEHIEDL-------LDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDN 805
Cdd:pfam05483 159 LLKetcarsAEKTKKYEYEREETRQVymdlnnnIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 806 DETKSQALEELTEfYEAKLQEKTTLLEEAQEDVRQ---QLREFEETKKQIEEDED---REIQDIK--------------- 864
Cdd:pfam05483 239 EKQVSLLLIQITE-KENKMKDLTFLLEESRDKANQleeKTKLQDENLKELIEKKDhltKELEDIKmslqrsmstqkalee 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 865 -----TKYEKKLRDEKESNLRlkgETGIMRKKFSSLQKEIEERTNDIETL-KGEQMKLQG---VIKSLEKDIQGLKREIQ 935
Cdd:pfam05483 318 dlqiaTKTICQLTEEKEAQME---ELNKAKAAHSFVVTEFEATTCSLEELlRTEQQRLEKnedQLKIITMELQKKSSELE 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 936 ERDETIQDKEKRIYDLKK----------KNQELGKFKFVLDYKIKELKKQIEPRENEIRVMK--------------EQIQ 991
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKilaedeklldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqltaiktseehylKEVE 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 992 EMEAELENFHKQNTQLELNITELwqklratDQEMRRERQKERDLEALVKRFKTDLHNCVAyiQEPRLLKEkVRGLFEKYV 1071
Cdd:pfam05483 475 DLKTELEKEKLKNIELTAHCDKL-------LLENKELTQEASDMTLELKKHQEDIINCKK--QEERMLKQ-IENLEEKEM 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1072 QRADMVEiaglntDLQQEYTRQREHLERNLatlkKKVVKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLE 1151
Cdd:pfam05483 545 NLRDELE------SVREEFIQKGDEVKCKL----DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH 614
|
....*...
gi 578798459 1152 AALKLTKK 1159
Cdd:pfam05483 615 QENKALKK 622
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
777-1037 |
2.40e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 777 LLLEYEKYQElQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDE 856
Cdd:COG1196 230 LLLKLRELEA-ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 857 DReiqdiktkyekkLRDEKESNLRLKGETgimrkkfSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQE 936
Cdd:COG1196 309 ER------------RRELEERLEELEEEL-------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 937 RDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQ 1016
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260
....*....|....*....|.
gi 578798459 1017 KLRATDQEMRRERQKERDLEA 1037
Cdd:COG1196 450 EEAELEEEEEALLELLAELLE 470
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
679-1048 |
2.72e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 74.67 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 679 TKTDMEEKAQVMLELKTRVEELKME-NEYQLRLKDMNySEKIKELTDKFIQEMESLKTKNQVLRTE---KEKQDVYHHEH 754
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQlNQLKSEISDLN-NQKEQDWNKELKSELKNQEKKLEEIQNQisqNNKIISQLNEQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 755 IEDLldkqSRELQDMECCNNQKLLLEYEKYQELQlKSQRMQEEYEKQLRdNDETKSQALEELTEFYEAKLQEKTTLLEEA 834
Cdd:TIGR04523 344 ISQL----KKELTNSESENSEKQRELEEKQNEIE-KLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 835 QEDVRQQLREFEETKKQIEEDED------REIQDIKTKYE--KKLRDEKESNLR-LKGETGIMRKKFSSLQKEIEERTND 905
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSeikdltNQDSVKELIIKnlDNTRESLETQLKvLSRSINKIKQNLEQKQKELKSKEKE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 906 IETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKK---------KNQELGKFKFVLDYKIKELKKQI 976
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQ 577
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578798459 977 EPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHN 1048
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
714-1042 |
1.55e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 714 NYSEKIKELTDKfIQEMESLKTKNQVLRTEKEKQdvyhHEHIEDLLDKQSRELQDMEccnnQKLLLEYEKYQELQLKSQR 793
Cdd:TIGR02168 674 ERRREIEELEEK-IEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 794 mqeeYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLLEEAqEDVRQQLREfeetkkQIEEDEDR--EIQDIKTKYEKKL 871
Cdd:TIGR02168 745 ----LEERIAQLSKELTELEAEIEE-LEERLEEAEEELAEA-EAEIEELEA------QIEQLKEElkALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 872 RDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDL 951
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 952 KKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQ-NTQLELNITELWQKLRATDQEMRRERQ 1030
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARR 972
|
330
....*....|..
gi 578798459 1031 KERDLEALVKRF 1042
Cdd:TIGR02168 973 RLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
780-1043 |
2.00e-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: 72.02 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 780 EYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEeltefYEAKLQEKTTLLEEAQEDvRQQLREFEETKKQIEEDEDRE 859
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDE-----LSQELSDASRKIGEIEKE-IEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 860 IQDIktkyEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERtndietlkgEQMKLQGVIKSLEKDIQGLKREIQERDE 939
Cdd:TIGR02169 746 LSSL----EQEIENVKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 940 TIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLR 1019
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
250 260
....*....|....*....|....
gi 578798459 1020 ATDQEMRRERQKERDLEALVKRFK 1043
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKR 916
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
665-1055 |
2.40e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 665 KREREVGFAEEvLVTKTDMEEKAQvmlELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEK 744
Cdd:PTZ00121 1438 KKAEEAKKADE-AKKKAEEAKKAE---EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 745 EKQDVYHHEHIEDLLD-KQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAK 823
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 824 LQEKTTLLEEAQEDVRQQLREFEETKKQIEE-DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEER 902
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 903 TNDIETLKGEQmklqgviKSLEKDIQGLKREIQERDETIQDKeKRIYDLKKKNQELGKFKFVLDYKIKELKKQieprENE 982
Cdd:PTZ00121 1674 KKKAEEAKKAE-------EDEKKAAEALKKEAEEAKKAEELK-KKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEE 1741
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578798459 983 IRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEalVKRFKTDLHNCVAYIQE 1055
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIE 1812
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
681-999 |
4.71e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.43 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 681 TDMEEKAQVMLELKTRVEELKMENE-YQLRLKDMNYSEKIKELTDKFIQEMESLKTKN-QVLRTEKEKQDvyhhEHIEDL 758
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQsYKQEIKNLESQINDLESKIQNQEKLNQQKDEQiKKLQQEKELLE----KEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 759 LDKQSRELQDMECCNNQKLLLE--------YEKYQELQLKSqrMQEEYEKQLRDNDETKSQALEELTEFyeAKLQEKTTL 830
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKEliiknldnTRESLETQLKV--LSRSINKIKQNLEQKQKELKSKEKEL--KKLNEEKKE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 831 LEEAQEDVRQQLREFEETKKQIEED---EDREIQDIKTKYEKKLRDEKESNLRlkgetgimrKKFSSLQKEIEERTNDIE 907
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEkkeKESKISDLEDELNKDDFELKKENLE---------KEIDEKNKEIEELKQTQK 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 908 TLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMK 987
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
330
....*....|..
gi 578798459 988 EQIQEMEAELEN 999
Cdd:TIGR04523 659 NKWPEIIKKIKE 670
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
680-1211 |
7.18e-12 |
|
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: 69.77 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 680 KTDMEEKAQVMLELKTRVEELkmenEYQLRLKDMNYSEKIKELTDKfiqeMESLKTKNQVLRtEKEKQDVYHHEhIEDLL 759
Cdd:pfam05557 40 KRQLDRESDRNQELQKRIRLL----EKREAEAEEALREQAELNRLK----KKYLEALNKKLN-EKESQLADARE-VISCL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 760 DKQSRELQDMEccnnqkllleyeKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQE--- 836
Cdd:pfam05557 110 KNELSELRRQI------------QRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElef 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 837 DVRQQLREFEETKKQIEE-----DEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEErtndIETLKG 911
Cdd:pfam05557 178 EIQSQEQDSEIVKNSKSElaripELEKELERLR-EHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREE----AATLEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 912 EQMKLQGVIKSLEKDIQGLKREIQerdeTIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQ 991
Cdd:pfam05557 253 EKEKLEQELQSWVKLAQDTGLNLR----SPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 992 EMEAELENFHKQNTQLELnitelwQKLRATdqemrrerqKERD-LEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKY 1070
Cdd:pfam05557 329 DLNKKLKRHKALVRRLQR------RVLLLT---------KERDgYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1071 VQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVvkegELHRTDYVRimQENVSLIKEINELRRELKFTRSQVYDL 1150
Cdd:pfam05557 394 AHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQE----SLADPSYSK--EEVDSLRRKLETLELERQRLREQKNEL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578798459 1151 EAALKltkKVRPQEVSETEPSRDM-LSTAPTARLNEQeeTGRIIEMQRLEIQRLRDQIQEQE 1211
Cdd:pfam05557 468 EMELE---RRCLQGDYDPKKTKVLhLSMNPAAEAYQQ--RKNQLEKLQAEIERLKRLLKKLE 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
796-1128 |
3.50e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 796 EEYEKQLRDNDETKSQ---ALEELTEFYEaKLQEKTTLLEEAQEdVRQQLREFEET----KKQIEEDEDREIQDIKTKYE 868
Cdd:TIGR02168 175 KETERKLERTRENLDRledILNELERQLK-SLERQAEKAERYKE-LKAELRELELAllvlRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 869 KKlRDEKESNLRLKGEtgimrkKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI 948
Cdd:TIGR02168 253 EE-LEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 949 YDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRE 1028
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1029 RQKERDLEALVKRFKTDLHNCVAYIQEPRlLKEKVRGLFEKyvqRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKV 1108
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEEL---EEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
330 340
....*....|....*....|.
gi 578798459 1109 VKEGELH-RTDYVRIMQENVS 1128
Cdd:TIGR02168 482 RELAQLQaRLDSLERLQENLE 502
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
680-1214 |
3.77e-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: 67.69 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 680 KTDMEEKAQVMLELKTRVEELK--MENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDV------YH 751
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKklIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLlyldylKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 752 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKyQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLL 831
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEK-LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 832 EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKgetgimrkkfssLQKEIEERTNDIETLKG 911
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL------------QEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 912 EQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVM--KEQ 989
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 990 IQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRR--ERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLF 1067
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSqkESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1068 EKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDYVRImQENVSLIKEINELRRELKFTRSQV 1147
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV-LEIDPILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578798459 1148 YDLEAA--LKLTKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQVT 1214
Cdd:pfam02463 621 RAKVVEgiLKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
782-1111 |
4.18e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 782 EKYQELQLKsqrmQEEYEKQLRdndetkSQALEELtefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEdedreiq 861
Cdd:COG1196 213 ERYRELKEE----LKELEAELL------LLKLREL----EAELEELEAELEELEAELEELEAELAELEAELEE------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 862 diktkyekklrdekesnlrlkgetgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETI 941
Cdd:COG1196 272 --------------------------LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 942 QDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL-WQKLRA 1020
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELaAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1021 TDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRAdmvEIAGLNTDLQQEYTRQREHLERN 1100
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE---ALLELLAELLEEAALLEAALAEL 482
|
330
....*....|.
gi 578798459 1101 LATLKKKVVKE 1111
Cdd:COG1196 483 LEELAEAAARL 493
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
783-1222 |
8.23e-11 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 66.30 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 783 KYQELQLKSQRMQEEYE-KQLRDNDETKSQALEELTEFYEAKLQEKTTlleeaqedvRQQLREFEETKKQIEEDEDREIQ 861
Cdd:pfam05557 8 KARLSQLQNEKKQMELEhKRARIELEKKASALKRQLDRESDRNQELQK---------RIRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 862 DIKTKYEK---KLRDEKESNLRLKGETgimrkkFSSLQKEIEErtndietLKGEQMKLQGVIKSLEKDIQGLKREIQERD 938
Cdd:pfam05557 79 RLKKKYLEalnKKLNEKESQLADAREV------ISCLKNELSE-------LRRQIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 939 ETIQDKEKRIYDLKKKNQELGkfkfVLDYKIKELKKQIEPRENEIRVMK------EQIQEMEAELENFHKQNTQL-ELNI 1011
Cdd:pfam05557 146 AKASEAEQLRQNLEKQQSSLA----EAEQRIKELEFEIQSQEQDSEIVKnskselARIPELEKELERLREHNKHLnENIE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1012 TELWQKLRATDQEMRRERQKER-----DLEALVKRFKTDLHNCVAYIQEPRL---LKEKVRGLFEKYVQR--ADMVEIAG 1081
Cdd:pfam05557 222 NKLLLKEEVEDLKRKLEREEKYreeaaTLELEKEKLEQELQSWVKLAQDTGLnlrSPEDLSRRIEQLQQReiVLKEENSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1082 LNTDLQQEYTRQREhLERNLATLKKKVVKEG-ELHRTD-YVRIMQENVSLI-KEINELRRELKFTRSQVYDLEAALKLTK 1158
Cdd:pfam05557 302 LTSSARQLEKARRE-LEQELAQYLKKIEDLNkKLKRHKaLVRRLQRRVLLLtKERDGYRAILESYDKELTMSNYSPQLLE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1159 KVRP-----QEV---------------SETEPSRDMLSTA---------------PTARLNEQEETGRIIEMQRLEIQRL 1203
Cdd:pfam05557 381 RIEEaedmtQKMqahneemeaqlsvaeEELGGYKQQAQTLerelqalrqqesladPSYSKEEVDSLRRKLETLELERQRL 460
|
490
....*....|....*....
gi 578798459 1204 RDQIQEQEQVTGFHTLAGV 1222
Cdd:pfam05557 461 REQKNELEMELERRCLQGD 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
685-1010 |
1.55e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 685 EKAQVMLELKTRVEELKMEnEYQLRLKDMNYS-EKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHIEDLLDKQS 763
Cdd:TIGR02168 210 EKAERYKELKAELRELELA-LLVLRLEELREElEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 764 R------ELQDMEccnNQKllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELtefyeAKLQEKTTLLEEAQED 837
Cdd:TIGR02168 289 ElyalanEISRLE---QQK-----QILRERLANLERQLEELEAQLEELESKLDELAEEL-----AELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 838 VRQQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQ 917
Cdd:TIGR02168 356 LEAELEELEAELEELESRL-EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 918 gvIKSLEKDIQGLKREI---QERDETIQDKEKRIYDLKKKNQElgkfkfvldyKIKELKKQieprENEIRVMKEQIQEME 994
Cdd:TIGR02168 435 --LKELQAELEELEEELeelQEELERLEEALEELREELEEAEQ----------ALDAAERE----LAQLQARLDSLERLQ 498
|
330
....*....|....*.
gi 578798459 995 AELENFHKQNTQLELN 1010
Cdd:TIGR02168 499 ENLEGFSEGVKALLKN 514
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
783-1106 |
4.33e-10 |
|
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: 64.43 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 783 KYQELQlKSQRMQEEYEKQLRDNDETKSQALEELTEFYEaKLQEKTTLLEEAQEdvrqqLREFEETKKQieededrEIQD 862
Cdd:pfam01576 10 KEEELQ-KVKERQQKAESELKELEKKHQQLCEEKNALQE-QLQAETELCAEAEE-----MRARLAARKQ-------ELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 863 IKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGL----------KR 932
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLedqnsklskeRK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 933 EIQER-------------------------DETIQDKEKRIYDLKKKNQELGKFKFVLD--------------YKIKELK 973
Cdd:pfam01576 156 LLEERiseftsnlaeeeekakslsklknkhEAMISDLEERLKKEEKGRQELEKAKRKLEgestdlqeqiaelqAQIAELR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 974 KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCV--- 1050
Cdd:pfam01576 236 AQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLdtt 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578798459 1051 AYIQEPRLLKEKVRGLF------EKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKK 1106
Cdd:pfam01576 316 AAQQELRSKREQEVTELkkaleeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
717-1055 |
1.24e-09 |
|
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: 62.28 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 717 EKIKELTDKFIQEMESLKTKN-QVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQ 795
Cdd:COG5185 159 GIIKDIFGKLTQELNQNLKKLeIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGF 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 796 EEYEKQLRDNDETK---SQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLR 872
Cdd:COG5185 239 QDPESELEDLAQTSdklEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 873 DEKESN-----LRLKGETGIMR------KKFSSLQKEIEERTNDIETLKGEQM--KLQGVIKSLEKDIQGLKREIQERDE 939
Cdd:COG5185 319 AAAEAEqeleeSKRETETGIQNltaeieQGQESLTENLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 940 TIQDKEKRIydlkkkNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELE-NFHKQNTQLELNITELWQKL 1018
Cdd:COG5185 399 NQRGYAQEI------LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNkVMREADEESQSRLEEAYDEI 472
|
330 340 350
....*....|....*....|....*....|....*...
gi 578798459 1019 RATDQEMRRERQKER-DLEALVKRFKTDLHNCVAYIQE 1055
Cdd:COG5185 473 NRSVRSKKEDLNEELtQIESRVSTLKATLEKLRAKLER 510
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
688-1215 |
1.24e-09 |
|
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: 62.83 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 688 QVMLELKTRVEELKMENE--YQLRLKDMNYSEKIKELTDKFIQEMESLK-----------TKNQVLRT------------ 742
Cdd:pfam15921 110 QSVIDLQTKLQEMQMERDamADIRRRESQSQEDLRNQLQNTVHELEAAKclkedmledsnTQIEQLRKmmlshegvlqei 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 743 --------EKEKQDVYHHEHIEDL--------LDKQSRELQ--------------------DMECCNNQKLLLEYEKYQE 786
Cdd:pfam15921 190 rsilvdfeEASGKKIYEHDSMSTMhfrslgsaISKILRELDteisylkgrifpvedqlealKSESQNKIELLLQQHQDRI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 787 LQLKSQR---------------------------MQEE-------YEKQLRDNDETKSQALEELTE---FYEAKLQ--EK 827
Cdd:pfam15921 270 EQLISEHeveitgltekassarsqansiqsqleiIQEQarnqnsmYMRQLSDLESTVSQLRSELREakrMYEDKIEelEK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 828 TTLLEEAQ-EDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDI 906
Cdd:pfam15921 350 QLVLANSElTEARTERDQFSQESGNLDDQLQKLLADLH-KREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 907 EtlkgeqmKLQGVIKSLEKDIQGlkrEIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKEL---KKQIEPRENEI 983
Cdd:pfam15921 429 Q-------RLEALLKAMKSECQG---QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTV 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 984 RVMKEQIQEMEAELENFHKQNTQLELNITELWQKLratdQEMRRERQKERDLEALVKRFKTDLHNCVAYIQeprLLKEKV 1063
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL----QHLKNEGDHLRNVQTECEALKLQMAEKDKVIE---ILRQQI 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1064 RGLFEKYVQR-----ADMVEIAGLNTDLQ------QEYTRQREHLERNLATLKKKvVKEGELHRTDYVRIMQENVSLIKE 1132
Cdd:pfam15921 572 ENMTQLVGQHgrtagAMQVEKAQLEKEINdrrlelQEFKILKDKKDAKIRELEAR-VSDLELEKVKLVNAGSERLRAVKD 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1133 I----NELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIE-MQRLEIQRLRDQI 1207
Cdd:pfam15921 651 IkqerDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKsMEGSDGHAMKVAM 730
|
....*...
gi 578798459 1208 QEQEQVTG 1215
Cdd:pfam15921 731 GMQKQITA 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
664-1140 |
1.27e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 664 IKREREVGFAEEVLVTKTDMEEKAQVMLELKtRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTE 743
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 744 KEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQAleeltefYEAK 823
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA-------EEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 824 LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlrlkgetgimRKKFSSLQKEIEERT 903
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE------------KKKIAHLKKEEEKKA 1770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 904 NDIETLKgeqmklQGVIKslekdiQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfvldykikelkkqieprENEI 983
Cdd:PTZ00121 1771 EEIRKEK------EAVIE------EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK-------------------EGNL 1819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 984 RVMKEQIQEMEAELENFHKQNTQLElNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNcvayIQEPRLLKEKV 1063
Cdd:PTZ00121 1820 VINDSKEMEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE----IEEADEIEKID 1894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1064 RGLFEKYVQRADMveiAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELH------RTDYVRIMQENVSLIKEINELR 1137
Cdd:PTZ00121 1895 KDDIEREIPNNNM---AGKNNDIIDDKLDKDEYIKRDAEETREEIIKISKKDmcindfSSKFCDYMKDNISSGNCSDEER 1971
|
...
gi 578798459 1138 REL 1140
Cdd:PTZ00121 1972 KEL 1974
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
725-1212 |
1.54e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 725 KFIQEM--ESLKTKNQVLRTEKEKQDVYHHEHIEDLlDKQSRELQDmeccnnqklllEYEKYQELQLKSQRMQEEYE--K 800
Cdd:COG4717 41 AFIRAMllERLEKEADELFKPQGRKPELNLKELKEL-EEELKEAEE-----------KEEEYAELQEELEELEEELEelE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 801 QLRDNDETKSQALEELTEFYEA-----KLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDrEIQDIKTKYEKKLRDek 875
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLyqeleALEAELAELPERLEELEERLEELRELEEELEELEA-ELAELQEELEELLEQ-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 876 eSNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKD--IQGLKREIQERDET---------IQDK 944
Cdd:COG4717 186 -LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEleAAALEERLKEARLLlliaaallaLLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 945 EKRIYDLKKKNQELGK--------FKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQ 1016
Cdd:COG4717 265 GGSLLSLILTIAGVLFlvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1017 KLRATDQEMR--RERQKERDLEALVKRFKTDLHNCVAyiqeprllkekvrGLFEKYVQRADMVEIaglntdlQQEYTRQR 1094
Cdd:COG4717 345 RIEELQELLReaEELEEELQLEELEQEIAALLAEAGV-------------EDEEELRAALEQAEE-------YQELKEEL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1095 EHLERNLATLKKKVvkEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALkltkkvrpqevsetepsrdm 1174
Cdd:COG4717 405 EELEEQLEELLGEL--EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-------------------- 462
|
490 500 510
....*....|....*....|....*....|....*...
gi 578798459 1175 lstaptarlnEQEETGRIIEMQRLEIQRLRDQIQEQEQ 1212
Cdd:COG4717 463 ----------EQLEEDGELAELLQELEELKAELRELAE 490
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
674-998 |
1.79e-09 |
|
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: 62.44 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 674 EEVLVTKTDMEEKAQVMLELKTRVEElkmeneyQLRLKDMNYSE--KIKELTDKFIQEMESLKTKNQVLR---TEKE--K 746
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASLQE-------KERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRnvqTECEalK 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 747 QDVYHHEHIEDLLDKQSRELQDMECCNNQKL-LLEYEKYQ-ELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAkl 824
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTAgAMQVEKAQlEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL-- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 825 qEKTTLLEEAQEDVRQqLREFEETKKQI--EEDEDR-EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 901
Cdd:pfam15921 633 -EKVKLVNAGSERLRA-VKDIKQERDQLlnEVKTSRnELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 902 RTNDIETLKGEQ-------MKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKK 974
Cdd:pfam15921 711 TRNTLKSMEGSDghamkvaMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
330 340
....*....|....*....|....
gi 578798459 975 QIEPRENEIRVMKEQIQEMEAELE 998
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEVALD 814
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
725-1212 |
1.86e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 725 KFIQEMESLKTKNQVLRTEKEKQDVYHHehIEDLLDKQSRELQDMEccnnqkllleyEKYQELQLKSQRMqeEYEKQLRD 804
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAE--LQEELEELEEELEELE-----------AELEELREELEKL--EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 805 NDETKSQALEELTEFYE--AKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEdedrEIQDIKTKYEKKLRDEKESNLRLK 882
Cdd:COG4717 130 LYQELEALEAELAELPErlEELEERLEELRELEEELEELEAELAELQEELEE----LLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 883 GETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQgVIKSLEK------------DIQGLKREIQERDETIQDKEKRIYD 950
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEarlllliaaallALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 951 LkkknqeLGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMR--RE 1028
Cdd:COG4717 285 L------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLReaEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1029 RQKERDLEALVKRFKTDLHNCVAyiqeprllkekvrGLFEKYVQRADMVEIaglntdlQQEYTRQREHLERNLATLKKKV 1108
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGV-------------EDEEELRAALEQAEE-------YQELKEELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1109 vkEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRpqEVSETEPSRDMLStaptARLNEQEE 1188
Cdd:COG4717 419 --EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG--ELAELLQELEELK----AELRELAE 490
|
490 500
....*....|....*....|....
gi 578798459 1189 TGRIIEMQRLEIQRLRDQIQEQEQ 1212
Cdd:COG4717 491 EWAALKLALELLEEAREEYREERL 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
852-1220 |
2.07e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 852 IEEDEDRE--------IQDIKTKYEKKLRDEKESNLRLKG-ETGIMRKkfSSLQKEIEERTNDIETLKGEQMKLQGVIKS 922
Cdd:PRK03918 141 LESDESREkvvrqilgLDDYENAYKNLGEVIKEIKRRIERlEKFIKRT--ENIEELIKEKEKELEEVLREINEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 923 LEKDIQGLKREIQERDETiqdKEKrIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEaELENFHK 1002
Cdd:PRK03918 219 LREELEKLEKEVKELEEL---KEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1003 QNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKrfktDLHNCVAYIQEprlLKEKVRGLFEKYvqrADMVEIAGL 1082
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEE---LKKKLKELEKRL---EELEERHEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1083 NTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAAlKLTKKVRP 1162
Cdd:PRK03918 364 YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA-KGKCPVCG 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1163 QEVSETEPSRDMLS-TAPTARL-NEQEETGRIIEMQRLEIQRLRDQIQEQEQVTGFHTLA 1220
Cdd:PRK03918 443 RELTEEHRKELLEEyTAELKRIeKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA 502
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
802-1044 |
3.87e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.19 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 802 LRDNDETKSQA-LEELTEFY-EAKLQEKTTLLEEAQEDVRQQLrefEETKKQIEEDEdREIQDIKTKYekklrdekeSNL 879
Cdd:COG3206 142 YTSPDPELAAAvANALAEAYlEQNLELRREEARKALEFLEEQL---PELRKELEEAE-AALEEFRQKN---------GLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 880 RLKGETGIMRKKFSSLQKEIEErtndietLKGEQMKLQGVIKSLEKDIQGLKREIQE--RDETIQDKEKRIYDLKKKNQE 957
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAE-------ARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 958 LGKfKFVLDY-KIKELKKQIEPRENEIRVMKEQI-QEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDL 1035
Cdd:COG3206 282 LSA-RYTPNHpDVIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
....*....
gi 578798459 1036 EALVKRFKT 1044
Cdd:COG3206 361 EVARELYES 369
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
786-1037 |
5.43e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.15 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 786 ELQLKSQRMQEEYEkQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEdVRQQLREFEETKKQIEEDEDREIQDIKT 865
Cdd:COG1340 12 ELEEKIEELREEIE-ELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 866 KYEK--KLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIEtlkgEQMKLQGVIKSLEKDIQGLKREIQERDEtIQD 943
Cdd:COG1340 90 LREEldELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPE----EEKELVEKIKELEKELEKAKKALEKNEK-LKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 944 KEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQ 1023
Cdd:COG1340 165 LRAELKELRKEAEEIHK-------KIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250
....*....|....
gi 578798459 1024 EMRRERQKERDLEA 1037
Cdd:COG1340 238 ELRELRKELKKLRK 251
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
796-1209 |
5.63e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 796 EEYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLlEEAQEDVRQQLREFEETKkqieEDEDREIQDIKTKYEKkLRDEK 875
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEE-HEERREELETL-EAEIEDLRETIAETERER----EELAEEVRDLRERLEE-LEEER 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 876 ESnlrLKGETGimrkkFSSLqkeieertnDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKN 955
Cdd:PRK02224 296 DD---LLAEAG-----LDDA---------DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 956 QELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENfhkQNTQLElNITELWQKLRATDQEMrreRQKERDL 1035
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD---APVDLG-NAEDFLEELREERDEL---REREAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1036 EAlvkrfktDLHNCVAYIQEPR-LLKEKVRGLFEKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGEL 1114
Cdd:PRK02224 432 EA-------TLRTARERVEEAEaLLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1115 HRT-DYVRIMQENVSLIKE--------INELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTAPTAR--L 1183
Cdd:PRK02224 505 VEAeDRIERLEERREDLEEliaerretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaeL 584
|
410 420
....*....|....*....|....*.
gi 578798459 1184 NEQEETGRIIEMQRLEIQRLRDQIQE 1209
Cdd:PRK02224 585 KERIESLERIRTLLAAIADAEDEIER 610
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
673-1152 |
9.14e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 9.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 673 AEEVLvtkTDMEEKAQVMLELKTRVEELKMENEYQLRLKDmNYSEKIKELTDkfiqEMESLKTKNQVLRTEKEKQDVyHH 752
Cdd:PRK02224 239 ADEVL---EEHEERREELETLEAEIEDLRETIAETERERE-ELAEEVRDLRE----RLEELEEERDDLLAEAGLDDA-DA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 753 EHIEDLLDKQSRELQDMEccnnqkllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQAlEELTEfyEAKLQEKTtlLE 832
Cdd:PRK02224 310 EAVEARREELEDRDEELR-----------DRLEECRVAAQAHNEEAESLREDADDLEERA-EELRE--EAAELESE--LE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 833 EAQEDVRQQLREFEETKKQIEEDEDReIQDIKTKYEK--KLRDEKESNL-RLKGETGIMRKKFSSLQK------------ 897
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRER-FGDAPVDLGNaeDFLEELREERdELREREAELEATLRTARErveeaealleag 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 898 ----------------EIEERTNDIETLKGEQMKLQGVIKSLEKDIqglkreiqERDETIQDKEKRIYDLKKKNQELGKf 961
Cdd:PRK02224 453 kcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERL--------ERAEDLVEAEDRIERLEERREDLEE- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 962 kfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQemRRERQKERdLEALvKR 1041
Cdd:PRK02224 524 ------LIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKER-IESL-ER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1042 FKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADMVE-----IAGLN--------TDLQQEYTRQREHLERNLATLKKKV 1108
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrerKRELEaefdeariEEAREDKERAEEYLEQVEEKLDELR 673
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 578798459 1109 VKEGELHRtdyvRI-MQENVslIKEINELRRELKFTRSQVYDLEA 1152
Cdd:PRK02224 674 EERDDLQA----EIgAVENE--LEELEELRERREALENRVEALEA 712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
889-1046 |
1.07e-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: 58.62 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 889 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfVLDYK 968
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA---ELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 969 IKELKKQI-------------------EPRENEIRVM---------KEQIQEMEAELENFHKQNTQLELNITELWQKLRA 1020
Cdd:COG4942 103 KEELAELLralyrlgrqpplalllspeDFLDAVRRLQylkylaparREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180
....*....|....*....|....*.
gi 578798459 1021 TDQEMRRERQKERDLEALVKRFKTDL 1046
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKEL 208
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
785-982 |
1.09e-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: 58.62 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 785 QELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIK 864
Cdd:COG4942 27 AELEQLQQEIAEL-EKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAELAELEKEIAELR-AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 865 TKYEKKLR--------------------DEKESNLR-LKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSL 923
Cdd:COG4942 104 EELAELLRalyrlgrqpplalllspedfLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578798459 924 EKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENE 982
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
664-1174 |
1.32e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.68 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 664 IKREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQ------EMESLKTKN 737
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKElqqlegSSDRILELD 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 738 QVLRTE---------------KEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEyekyQELQLKSQRMQEEyeKQL 802
Cdd:TIGR00606 478 QELRKAerelskaeknsltetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT----QMEMLTKDKMDKD--EQI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 803 RDNDETKSQALEELTEFYEAKLQEKTTL---------LEEAQEDVRQQLREFEETKKQIEEDEDREIQDIkTKYEKKLRD 873
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYFPNKKQLEDWLhskskeinqTRDRLAKLNKELASLEQNKNHINNELESKEEQL-SSYEDKLFD 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 874 -----EKESNL-RLKGETGIMRKKFSSLQKEIEERTNDIETLKGE--------------QMKLQGVIKSLEKDIQGLKRE 933
Cdd:TIGR00606 631 vcgsqDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcqrvfqtEAELQEFISDLQSKLRLAPDK 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 934 IQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITE 1013
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTD 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1014 LwqklRATDQEMRRERQKERDLEALVKrfKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADmveiagLNTDLQQEYTRQ 1093
Cdd:TIGR00606 791 V----TIMERFQMELKDVERKIAQQAA--KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIE------LNRKLIQDQQEQ 858
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1094 REHLERNLATLKKKVVKEGE-LHRTDyvRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSR 1172
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTnLQRRQ--QFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN 936
|
..
gi 578798459 1173 DM 1174
Cdd:TIGR00606 937 KK 938
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
889-1046 |
1.54e-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: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 889 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIyDLKKKNQELGkfkfVLDYK 968
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-GNVRNNKEYE----ALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578798459 969 IKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQK-ERDLEALVKRFKTDL 1046
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEElEAEREELAAKIPPEL 176
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
666-998 |
2.27e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.58 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 666 REREVGFAE-EVLVTKTDMEEKAQVMLELKTRVEELKMENeyqlrLKDMNYSEKIKELTDKFIQEmeslkTKNQVLRTEK 744
Cdd:pfam05483 448 REKEIHDLEiQLTAIKTSEEHYLKEVEDLKTELEKEKLKN-----IELTAHCDKLLLENKELTQE-----ASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 745 EKQDVYHHEHIEDLLDKQSRELQdmeccnnqkllleyEKYQELQLKSQRMQEEYeKQLRDNDETKSQALEELTEFYEAKL 824
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLE--------------EKEMNLRDELESVREEF-IQKGDEVKCKLDKSEENARSIEYEV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 825 QEKTTLLEEAQEDVRQQLREFEETKKQIEE--DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSL----QKE 898
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEElhQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIidnyQKE 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 899 IEERTNDIETLKGEQMKLQGVIKS---LEKDIQG------------LKREIQERDETIQDKEKRIYDLKKKNQELGKFKF 963
Cdd:pfam05483 663 IEDKKISEEKLLEEVEKAKAIADEavkLQKEIDKrcqhkiaemvalMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKA 742
|
330 340 350
....*....|....*....|....*....|....*
gi 578798459 964 VLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELE 998
Cdd:pfam05483 743 ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
692-1103 |
2.65e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.52 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 692 ELKTRVEELKMENEYQLRLKDMNYSEkikelTDKFIQEMESLKTKNQVLRTE--KEKQDVyhhEHIEDLLDKQSRELQDM 769
Cdd:TIGR00606 713 STESELKKKEKRRDEMLGLAPGRQSI-----IDLKEKEIPELRNKLQKVNRDiqRLKNDI---EEQETLLGTIMPEEESA 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 770 ECCnnqklLLEYEKYQELQLKSQRMQEEYEKQLRDNDETksqaleELTEFYEAKLQEKttllEEAQEDVRQQLREFEETK 849
Cdd:TIGR00606 785 KVC-----LTDVTIMERFQMELKDVERKIAQQAAKLQGS------DLDRTVQQVNQEK----QEKQHELDTVVSKIELNR 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 850 KQIEeDEDREIQDIKTKYeKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQgviKSLEKDIQG 929
Cdd:TIGR00606 850 KLIQ-DQQEQIQHLKSKT-NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLE---TFLEKDQQE 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 930 LKREIQERDETIQDKEKRIYDLKKK-NQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLE 1008
Cdd:TIGR00606 925 KEELISSKETSNKKAQDKVNDIKEKvKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMR 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1009 LNITELWQKLR-ATDQEMRRERQKErdlealVKRFKTDLHNCVAYIQEPRLLKEKvrglfEKYVQRADMVEIAGLNTDL- 1086
Cdd:TIGR00606 1005 QDIDTQKIQERwLQDNLTLRKRENE------LKEVEEELKQHLKEMGQMQVLQMK-----QEHQKLEENIDLIKRNHVLa 1073
|
410 420
....*....|....*....|
gi 578798459 1087 ---QQEYTRQREHLERNLAT 1103
Cdd:TIGR00606 1074 lgrQKGYEKEIKHFKKELRE 1093
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
925-1155 |
3.37e-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: 57.08 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 925 KDIQGLKREIQERDETIQDKEKRIYDLKKKnqelgkfkfvldykIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN 1004
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE--------------EKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1005 TQLELNITELWQKLratdqemrrERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGL-FEKYVQRADMVEIAGLN 1083
Cdd:COG4942 86 AELEKEIAELRAEL---------EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578798459 1084 TDlQQEYTRQREHLERNLATLkKKVVKEGELHRTDYVRIMQENVSLI----KEINELRRELKFTRSQVYDLEAALK 1155
Cdd:COG4942 157 AD-LAELAALRAELEAERAEL-EALLAELEEERAALEALKAERQKLLarleKELAELAAELAELQQEAEELEALIA 230
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
684-1010 |
6.18e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 684 EEKAQVMLELKTRVEELkMENEYQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLRTEKEKqdvyhhEHIEDLLDKQS 763
Cdd:PRK03918 387 EKLEKELEELEKAKEEI-EEEISKITARIGELKKEIKEL-KKAIEELKKAKGKCPVCGRELTE------EHRKELLEEYT 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 764 RELQDMEccNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQ---ALEELTEFYEAKLQEKTTLLEEAQEDVRQ 840
Cdd:PRK03918 459 AELKRIE--KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkeLEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 841 QLREFEETKKQIEEDEdrEIQDIKTKYEKKLRDEKESNLRLKGEtgIMRKKFSSLqKEIEERTNDIETLKGEQMKLQGV- 919
Cdd:PRK03918 537 LKGEIKSLKKELEKLE--ELKKKLAELEKKLDELEEELAELLKE--LEELGFESV-EELEERLKELEPFYNEYLELKDAe 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 920 --IKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDY------------------------------ 967
Cdd:PRK03918 612 keLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYeelreeylelsrelaglraeleelekrree 691
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 578798459 968 ------KIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELN 1010
Cdd:PRK03918 692 ikktleKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
821-1211 |
9.52e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 821 EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReiqdiKTKYEkKLRDEKESNLRLKgetgimrkkfsSLQKEIE 900
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-----REALQ-RLAEYSWDEIDVA-----------SAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 901 ERTNDIETLKGEQmklqgviksleKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELgkfkfvldykikelkkqieprE 980
Cdd:COG4913 672 ELEAELERLDASS-----------DDLAALEEQLEELEAELEELEEELDELKGEIGRL---------------------E 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 981 NEIRVMKEQIQEMEAELENF-HKQNTQLELNITELWQKLRATdqemRRERQKERDLEALVKRFKTDLHNcvayiqeprlL 1059
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALGD----AVERELRENLEERIDALRARLNR----------A 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1060 KEKVRGLFEKYVQRADMvEIAGLNTDL------QQEYTR-QREHLERNLATLKKKVVKEGELHRTDYVRIMQENVSLIKE 1132
Cdd:COG4913 786 EEELERAMRAFNREWPA-ETADLDADLeslpeyLALLDRlEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKE 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1133 ----INELRRELKFTRSQVYDLEAalkltKKVRPQEVSETepsRDMLStapTARLNEQEETGRIIEMQRLEIQRLRDQIQ 1208
Cdd:COG4913 865 ridpLNDSLKRIPFGPGRYLRLEA-----RPRPDPEVREF---RQELR---AVTSGASLFDEELSEARFAALKRLIERLR 933
|
...
gi 578798459 1209 EQE 1211
Cdd:COG4913 934 SEE 936
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-1212 |
1.21e-07 |
|
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: 56.22 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 696 RVEELKMENEYQLRLKDMNysEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHhEHIEDLLDKQSRELQDMECCNNQ 775
Cdd:TIGR02168 325 LEELESKLDELAEELAELE--EKLEELKEELESLEAELEELEAELEELESRLEELE-EQLETLRSKVAQLELQIASLNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 776 KLLLEYEKyQELQLKSQRMQEEYEKQLRDNDETKSQALE---ELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQI 852
Cdd:TIGR02168 402 IERLEARL-ERLEDRRERLQQEIEELLKKLEEAELKELQaelEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 853 EEDEDR------EIQDIKTKYEKKLRDEKE---SNLRLKGETGIMRKKFS---SLQKEIE----ERTNDIETlKGEQMKL 916
Cdd:TIGR02168 481 ERELAQlqarldSLERLQENLEGFSEGVKAllkNQSGLSGILGVLSELISvdeGYEAAIEaalgGRLQAVVV-ENLNAAK 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 917 QGvIKSLEK-----------------DIQGLKREIQERDETIQDKEKRIY---------------------------DLK 952
Cdd:TIGR02168 560 KA-IAFLKQnelgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVkfdpklrkalsyllggvlvvddldnalELA 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 953 KKNQELGKFkFVLD------------------YKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNIT-- 1012
Cdd:TIGR02168 639 KKLRPGYRI-VTLDgdlvrpggvitggsaktnSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEql 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1013 -----ELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEkyvqrADMVEIAGLNTDLQ 1087
Cdd:TIGR02168 718 rkeleELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----EAEAEIEELEAQIE 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1088 QeYTRQREHLERNLATLKKKVvkegELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKvrpqEVSE 1167
Cdd:TIGR02168 793 Q-LKEELKALREALDELRAEL----TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA----EIEE 863
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 578798459 1168 TEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQ 1212
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
471-658 |
1.23e-07 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 55.69 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 471 GGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSYNCVT 550
Cdd:COG2319 6 GAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 551 VSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQAHAG 628
Cdd:COG2319 86 FSPDGRLLASASADGTVRlwDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRL--WDLATGKLLRTLTGHSG 163
|
170 180 190
....*....|....*....|....*....|..
gi 578798459 629 PITkmLLTF--DDQFLLTAAEDGclfTWKVFD 658
Cdd:COG2319 164 AVT--SVAFspDGKLLASGSDDG---TVRLWD 190
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
792-1043 |
1.25e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 792 QRMQEEYekqLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQedvrQQLREFEETKKQIEEDEDREIqdiktkYEKKL 871
Cdd:COG3206 155 NALAEAY---LEQNLELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQKNGLVDLSEEAKL------LLQQL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 872 RDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQmklqgVIKSLEKDIQGLKREIQERDETIQDKEKRIYDL 951
Cdd:COG3206 222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 952 KKKNQELGKFKFvldykiKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLelnitelwQKLRATDQEMRRERQK 1031
Cdd:COG3206 297 RAQIAALRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL--------PELEAELRRLEREVEV 362
|
250
....*....|...
gi 578798459 1032 ERDL-EALVKRFK 1043
Cdd:COG3206 363 ARELyESLLQRLE 375
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
805-1002 |
1.44e-07 |
|
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: 54.68 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 805 NDETKSQALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEetkKQIEEDEDrEIQDIKTKYEKKLRDEKESnlrlkge 884
Cdd:cd22656 108 DDEELEEAKKTIKALLD-DLLKEAKKYQDKAAKVVDKLTDFE---NQTEKDQT-ALETLEKALKDLLTDEGGA------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 885 tgIMRKKFSSLQKEIEERTNDIetlkgeqmklqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKknqelgkfkfv 964
Cdd:cd22656 176 --IARKEIKDLQKELEKLNEEY-------------AAKLKAKIDELKALIADDEAKLAAALRLIADLTA----------- 229
|
170 180 190
....*....|....*....|....*....|....*...
gi 578798459 965 LDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHK 1002
Cdd:cd22656 230 ADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKD 267
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
692-1167 |
1.68e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 692 ELKTRVEELKmeneyQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLRTEKEK--QDVYHHEHIEDLLDKQsRELQDM 769
Cdd:COG4717 72 ELKELEEELK-----EAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKleKLLQLLPLYQELEALE-AELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 770 EccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEdVRQQLREFEETK 849
Cdd:COG4717 145 P--------ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE-LQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 850 KQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVI-KSLEKDIQ 928
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLaLLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 929 GLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEpRENEIRVMKEQIQEMEAELenfhkQNTQLE 1008
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD-RIEELQELLREAEELEEEL-----QLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1009 LNITELWQKLRATDQEMRRERQKE-RDLEALVKRFktdlhncvayiqepRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQ 1087
Cdd:COG4717 370 QEIAALLAEAGVEDEEELRAALEQaEEYQELKEEL--------------EELEEQLEELLGELEELLEALDEEELEEELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1088 Q------EYTRQREHLERNLATLKKKVvkEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVR 1161
Cdd:COG4717 436 EleeeleELEEELEELREELAELEAEL--EQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
....*.
gi 578798459 1162 PQEVSE 1167
Cdd:COG4717 514 LPPVLE 519
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
822-948 |
2.54e-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: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 822 AKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKL---RDEKESNlRLKGETGIMRKKFSSLQKE 898
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLgnvRNNKEYE-ALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 578798459 899 IEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI 948
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
665-1209 |
2.58e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 665 KREREVGFAEEVL--VTKTDMEEKAQVMLELKTRVEELKME--------NEYQLRLKDM-NYSEKIKELTDKFIQEMESL 733
Cdd:TIGR02169 262 ELEKRLEEIEQLLeeLNKKIKDLGEEEQLRVKEKIGELEAEiaslersiAEKERELEDAeERLAKLEAEIDKLLAEIEEL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 734 KTKNQVLRTEKEK-QDVYhhEHIEDLLDKQSRELQDMECcNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQA 812
Cdd:TIGR02169 342 EREIEEERKRRDKlTEEY--AELKEELEDLRAELEEVDK-EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 813 LEELTEFY------EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEeDEDREIQDIKTKY---EKKLRDEKESNLRLKG 883
Cdd:TIGR02169 419 SEELADLNaaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLS-KYEQELYDLKEEYdrvEKELSKLQRELAEAEA 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 884 ETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGV----IKSLE-------------------KDIQGLKRE------- 933
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVgeryATAIEvaagnrlnnvvveddavakEAIELLKRRkagratf 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 934 -------IQERDETIQDKEKRI--------YDLKKKN-------------------QELGKFKFV--------------- 964
Cdd:TIGR02169 578 lplnkmrDERRDLSILSEDGVIgfavdlveFDPKYEPafkyvfgdtlvvedieaarRLMGKYRMVtlegelfeksgamtg 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 965 ---------------------LDYKIKELKKQ----------IEPRENE----IRVMKEQIQEMEAELENFHKQNTQLEL 1009
Cdd:TIGR02169 658 gsraprggilfsrsepaelqrLRERLEGLKRElsslqselrrIENRLDElsqeLSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1010 NITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEP--RLLKEKVRGLFEKY-VQRADMVEIAGLNTDL 1086
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELsKLEEEVSRIEARLREI 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1087 QQEYtrQREHLERNLATLKKKVVKEGELHRTDY-VRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQ-- 1163
Cdd:TIGR02169 818 EQKL--NRLTLEKEYLEKEIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEle 895
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 578798459 1164 -EVSETEPSRDMLSTA---PTARLNEQEETGRIIEMQRLEIQRLRDQIQE 1209
Cdd:TIGR02169 896 aQLRELERKIEELEAQiekKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
810-1041 |
2.79e-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: 54.38 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 810 SQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIktkyEKKLRDekesnlrLKGETGIMR 889
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-RRIAAL----ARRIRA-------LEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 890 KKFSSLQKEIEERTNDIETLKGEqmkLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKI 969
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578798459 970 KELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKR 1041
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
675-1107 |
8.80e-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: 53.64 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 675 EVLVTKTDMEEKAQVMLELKTRVEelKMENEYQLRLKdmnysekiKEltDKFIQEMESLKTKNQVLRTEKEKQDVYHHEH 754
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHE--AMISDLEERLK--------KE--EKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 755 IEDL---LDKQSRELQ------DMECCNNQKLLleyEKYQELQLKSQRMQE--EYEKQLRDNDETKSQALEELTEFYEAK 823
Cdd:pfam01576 231 IAELraqLAKKEEELQaalarlEEETAQKNNAL---KKIRELEAQISELQEdlESERAARNKAEKQRRDLGEELEALKTE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 824 LqEKTTLLEEAQEDVR-QQLREFEETKKQIEED---EDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEI 899
Cdd:pfam01576 308 L-EDTLDTTAAQQELRsKREQEVTELKKALEEEtrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 900 EERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPR 979
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 980 ENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLratDQEMRRERQKERDLEALV-------KRFKTDLHNCVAY 1052
Cdd:pfam01576 467 ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQL---EEEEEAKRNVERQLSTLQaqlsdmkKKLEEDAGTLEAL 543
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 578798459 1053 IQEPRLLKEKVRGLFEKYVQRADMVE-IAGLNTDLQQEY---TRQREHLERNLATLKKK 1107
Cdd:pfam01576 544 EEGKKRLQRELEALTQQLEEKAAAYDkLEKTKNRLQQELddlLVDLDHQRQLVSNLEKK 602
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
778-1017 |
1.02e-06 |
|
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: 52.12 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 778 LLEYEKYQELQLKSQRMQEEYEKQLRD------NDETKSQALEELTEFYEAKLQ----EKTTLLEEAQEdVRQQLREF-- 845
Cdd:pfam15905 58 SLELKKKSQKNLKESKDQKELEKEIRAlvqergEQDKRLQALEEELEKVEAKLNaavrEKTSLSASVAS-LEKQLLELtr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 846 -----------EETKKQIE-------------EDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 901
Cdd:pfam15905 137 vnellkakfseDGTQKKMSslsmelmklrnklEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 902 RTNDIETLKGEQMKLQGVIKSLEKdiqgLKREIQERDETiqdkekriydLKKKNQELGKFKFVLDYKIKELKKQIEPR-- 979
Cdd:pfam15905 217 EKSETEKLLEYITELSCVSEQVEK----YKLDIAQLEEL----------LKEKNDEIESLKQSLEEKEQELSKQIKDLne 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 578798459 980 ---------ENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQK 1017
Cdd:pfam15905 283 kckllesekEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
755-1213 |
1.08e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.37 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 755 IEDLLDKQSRELQDMEccNNQKLLLEYEKYQELQLKS-QRMQEEYEKQLRDNDETKSQ-----ALEELTEFYEAKLQEKT 828
Cdd:PRK01156 185 IDYLEEKLKSSNLELE--NIKKQIADDEKSHSITLKEiERLSIEYNNAMDDYNNLKSAlnelsSLEDMKNRYESEIKTAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 829 TLLEEAQEDVrQQLREFEETKKQIEEDE---DREIQDIKTKYEKKLRDEKESNLRLKGETG----IMRK---------KF 892
Cdd:PRK01156 263 SDLSMELEKN-NYYKELEERHMKIINDPvykNRNYINDYFKYKNDIENKKQILSNIDAEINkyhaIIKKlsvlqkdynDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 893 SSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKdiqgLKREIQERDETIQDKEKRIYDLKKKN----QELGKFKFVLDYK 968
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIES----LKKKIEEYSKNIERMSAFISEILKIQeidpDAIKKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 969 IKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNT----QLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKT 1044
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1045 DLHNCVAyiQEPRLLKEKVRGLFEKYVQRADMVeiAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELH--RTDYVRI 1122
Cdd:PRK01156 498 KIVDLKK--RKEYLESEEINKSINEYNKIESAR--ADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDskRTSWLNA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1123 MQEnVSLI------KEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTaptaRLNEQEETGRIIEMQ 1196
Cdd:PRK01156 574 LAV-ISLIdietnrSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNN----KYNEIQENKILIEKL 648
|
490
....*....|....*..
gi 578798459 1197 RLEIQRLRDQIQEQEQV 1213
Cdd:PRK01156 649 RGKIDNYKKQIAEIDSI 665
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
880-1154 |
1.17e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 880 RLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELG 959
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 960 KFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFhkQNTQLELNITELWQKLRATDQEMRRERQKERDLEALV 1039
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1040 KRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDY 1119
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
250 260 270
....*....|....*....|....*....|....*
gi 578798459 1120 VRIMQENVSLIKEINELRRELKFTRSQVYDLEAAL 1154
Cdd:COG4372 287 ALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
807-1043 |
1.18e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 807 ETKSQALEELTEFYeAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED-----REIQDIktkyEKKLRDEKESNLRL 881
Cdd:COG4913 613 AALEAELAELEEEL-AEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAEL----EAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 882 KGetgimrkkfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI-----YDLKKKNQ 956
Cdd:COG4913 688 AA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 957 ELGKFKFVldykiKELKKQIeprENEIRVMKEQIQEMEAELEN-FHKQNTQLELNITELWQKLRATDQ-EMRRERQKERD 1034
Cdd:COG4913 757 AALGDAVE-----RELRENL---EERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLESLPEyLALLDRLEEDG 828
|
....*....
gi 578798459 1035 LEALVKRFK 1043
Cdd:COG4913 829 LPEYEERFK 837
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
490-529 |
1.57e-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: 1.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 578798459 490 SLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 529
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
861-1082 |
1.98e-06 |
|
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: 51.69 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 861 QDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDET 940
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 941 IQDKEKRIYDLKKKNQELGK---FKFVLD-------YKIKELKKQIEP-RENEIRVMKEQIQEMEAELENFHKQNTQLEL 1009
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRqppLALLLSpedfldaVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578798459 1010 NITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLhncVAYIQEPRLLKEKVRGLFEKYVQRADMVEIAGL 1082
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
786-1064 |
2.52e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 786 ELQLKSQRMQEEYeKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEaQEDVRQQLREFEEtkkqieededreiqDIKT 865
Cdd:pfam07888 77 ELESRVAELKEEL-RQSREKHEELEEKYKELSASSEELSEEKDALLAQ-RAAHEARIRELEE--------------DIKT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 866 KYEKKLrdEKESNL-RLKGETgimrKKFSSLQKEIEErtnDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDK 944
Cdd:pfam07888 141 LTQRVL--ERETELeRMKERA----KKAGAQRKEEEA---ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 945 EKRIYDLKKKNQELGKFKFVLDYKIKELK----------KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL 1014
Cdd:pfam07888 212 QDTITTLTQKLTTAHRKEAENEALLEELRslqerlnaseRKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADA 291
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1015 ----------WQKLRATdqeMRRERQKERDleaLVKRFKTDLHNCVAYIQEPRLLKEKVR 1064
Cdd:pfam07888 292 slalregrarWAQERET---LQQSAEADKD---RIEKLSAELQRLEERLQEERMEREKLE 345
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
701-1141 |
2.57e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.97 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 701 KMENEYQLRLK-----DMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQ 775
Cdd:TIGR00606 605 QNKNHINNELEskeeqLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQ 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 776 KLLLEYEKYQELQLKSQRM-------QEEYEKQLRDNDETKSQALEeLTEFYEAKLQEKTTLLEEAQEDVRQQLREFEET 848
Cdd:TIGR00606 685 RVFQTEAELQEFISDLQSKlrlapdkLKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 849 KKQIEEDEdreiqdiktKYEKKLRDEKESNLRLKGETGIMRKkfssLQKEIEERTNDIETLKGeqmKLQGVikSLEKDIQ 928
Cdd:TIGR00606 764 KNDIEEQE---------TLLGTIMPEEESAKVCLTDVTIMER----FQMELKDVERKIAQQAA---KLQGS--DLDRTVQ 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 929 GLKREIQERDET--------------IQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEME 994
Cdd:TIGR00606 826 QVNQEKQEKQHEldtvvskielnrklIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK 905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 995 AELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRllkekvrglfEKYVQRA 1074
Cdd:TIGR00606 906 DAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK----------DDYLKQK 975
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1075 DmVEIAGLNTDLqQEYTRQREHLERNLATLKKKVVKEGELHrtdyvRIMQENVSLIK---EINELRRELK 1141
Cdd:TIGR00606 976 E-TELNTVNAQL-EECEKHQEKINEDMRLMRQDIDTQKIQE-----RWLQDNLTLRKrenELKEVEEELK 1038
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
839-999 |
2.71e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.70 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 839 RQQLREFEETKKQIEEDEDREIQDIKtkyEKKLRDEKESNLRLKGEtgimrkkfssLQKEIEERtndietlkgeqmklqg 918
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIK---KEALLEAKEEIHKLRNE----------FEKELRER---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 919 vikslEKDIQGLKREIQERDETIqdkEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEpreneirVMKEQIQEMEAELE 998
Cdd:PRK12704 81 -----RNELQKLEKRLLQKEENL---DRKLELLEKREEELEKKEKELEQKQQELEKKEE-------ELEELIEEQLQELE 145
|
.
gi 578798459 999 N 999
Cdd:PRK12704 146 R 146
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
831-995 |
2.89e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.78 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 831 LEEAQEDVRQQLREFEETKKQIEEDEDREIQdikTKYEKKLRdekesnlrlkgetgimrkkfsslqkeieertndietlk 910
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEEREL---TEEEEEIR-------------------------------------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 911 geqmKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK-NQELGKFKFV--LDYKIKELKKQIEPRENEIRVMK 987
Cdd:COG2433 417 ----RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEeRREIRKDREIsrLDREIERLERELEEERERIEELK 492
|
....*...
gi 578798459 988 EQIQEMEA 995
Cdd:COG2433 493 RKLERLKE 500
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
889-1037 |
3.34e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 889 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIqdkEKRIYDLKKKNQELGKFKFVL--- 965
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGSVSYLDVLLgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 966 ---DY-------------------KIKELKKQIEPRENEIRVMKEQIQEMEAELEnfhKQNTQLELNITELWQKLRATDQ 1023
Cdd:COG3883 113 sfsDFldrlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELE---AAKAELEAQQAEQEALLAQLSA 189
|
170
....*....|....
gi 578798459 1024 EMRRERQKERDLEA 1037
Cdd:COG3883 190 EEAAAEAQLAELEA 203
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
821-1064 |
4.21e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 821 EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEK--KLRDEKESNLRLKGEtgiMRKKFSSLQKE 898
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEaqELREKRDELNEKVKE---LKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 899 IEERTNDIETLKGEQMKLQGV---IKSLEKDIQGLKREIQERDETIqDKEKRIYD-LKKKNQELGKFKFVLDY--KIKEL 972
Cdd:COG1340 87 LNELREELDELRKELAELNKAggsIDKLRKEIERLEWRQQTEVLSP-EEEKELVEkIKELEKELEKAKKALEKneKLKEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 973 KKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNcvaY 1052
Cdd:COG1340 166 RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE---L 242
|
250
....*....|..
gi 578798459 1053 IQEPRLLKEKVR 1064
Cdd:COG1340 243 RKELKKLRKKQR 254
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
767-1030 |
4.27e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.28 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 767 QDMECCNNQKLLLEYEKYQELQ-LKSQRMQEEYEKQLRDNDetKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREF 845
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEkMEQERLRQEKEEKAREVE--RRRKLEEAEKARQAEMDRQAAIYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 846 EETKkqiEEDEDREIQDIKTK-----------YEKKLRDEKESNLRLKGETGIMRKKF---SSLQKEIEERTNDIETLKG 911
Cdd:pfam17380 351 ERIR---QEERKRELERIRQEeiameisrmreLERLQMERQQKNERVRQELEAARKVKileEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 912 EQ-----MKLQGVIKSLEKDIQGLKREIQERDETI----QDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENE 982
Cdd:pfam17380 428 EQeearqREVRRLEEERAREMERVRLEEQERQQQVerlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 578798459 983 IRVMKEQIQEMEAELENfhKQNTQLELNITELWQKLRATDQEMRRERQ 1030
Cdd:pfam17380 508 MIEEERKRKLLEKEMEE--RQKAIYEEERRREAEEERRKQQEMEERRR 553
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
667-1212 |
7.52e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 667 EREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQlRLKDMNYSEKIKELTDKFIQEM----------ESLKTK 736
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-KAEDARKAEEARKAEDAKRVEIarkaedarkaEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 737 NQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQL-----KSQRMQEEYEKQLRDNDETKSQ 811
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkKAEEAKKDAEEAKKAEEERNNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 812 ALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIE---EDEDREIQDIKTKYEKKlrdEKESNLRLKGETGim 888
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakkAEEKKKADEAKKKAEEA---KKADEAKKKAEEA-- 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 889 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQErdetiqdKEKRIYDLKKKNQELgkfkfvldYK 968
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-------AKKKADAAKKKAEEK--------KK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 969 IKELKKQIEprenEIRVMKEQIQEMEAELENFHKQNTQLElnitelwQKLRAtdQEMRRERQKERDLEALVKRF--KTDL 1046
Cdd:PTZ00121 1393 ADEAKKKAE----EDKKKADELKKAAAAKKKADEAKKKAE-------EKKKA--DEAKKKAEEAKKADEAKKKAeeAKKA 1459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1047 HNCVAYIQEPRLLKEKVRGLFEKyvQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKvvkeGELHRTDYVRIMQEN 1126
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEA--KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA----EEAKKADEAKKAEEA 1533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1127 vsliKEINELRR-ELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDM-LSTAPTARLNEQEETGRIIEMQRLEIQRLR 1204
Cdd:PTZ00121 1534 ----KKADEAKKaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMaLRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
....*...
gi 578798459 1205 DQIQEQEQ 1212
Cdd:PTZ00121 1610 EEAKKAEE 1617
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
51-409 |
1.06e-05 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 49.52 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 51 ALSISPNRRYLAiseTVQEKPAITIYELSSIPCRKrkVLNNFDFQVQkfiSMAFSPDSKYLLAqTSppESNLVYwLWEKQ 130
Cdd:COG2319 125 SVAFSPDGKTLA---SGSADGTVRLWDLATGKLLR--TLTGHSGAVT---SVAFSPDGKLLAS-GS--DDGTVR-LWDLA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 131 KVMAIVRIDTQNNPVYQVSFSPqDNTQVcVTG--NGMFKLLRFAEGTLKQTSfqRGEPQNYLAHTWVADDK-IVVGTDTG 207
Cdd:COG2319 193 TGKLLRTLTGHTGAVRSVAFSP-DGKLL-ASGsaDGTVRLWDLATGKLLRTL--TGHSGSVRSVAFSPDGRlLASGSADG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 208 KLFLfesgdqrWETsimvkeptNGSKSLDVIQESESliefpPVSSplpsyeqmVAASSHSQMsmpqvfaiaayskgFACS 287
Cdd:COG2319 269 TVRL-------WDL--------ATGELLRTLTGHSG-----GVNS--------VAFSPDGKL--------------LASG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 288 AGPGRVLLFEkmeekdfYRESREIRIPVDPQSndpsqsdkqDVLCLCFSPSEETLVASTSKNqlysiTMSLTEISKGEPA 367
Cdd:COG2319 307 SDDGTVRLWD-------LATGKLLRTLTGHTG---------AVRSVAFSPDGKTLASGSDDG-----TVRLWDLATGELL 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 578798459 368 HFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWNYET 409
Cdd:COG2319 366 RT----LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
753-1041 |
1.11e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 753 EHIEDLLDKQSRElQDMECCNNQKLLLeyekyqelqlKSQRMQEEYEKQLRDNDETKSQALEELtefyeAKLQEKTTLLE 832
Cdd:TIGR00618 594 VRLQDLTEKLSEA-EDMLACEQHALLR----------KLQPEQDLQDVRLHLQQCSQELALKLT-----ALHALQLTLTQ 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 833 EAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKY----------EKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEER 902
Cdd:TIGR00618 658 ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkemlaqcQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 903 TNDIETLKGEQMKLQG-VIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPREN 981
Cdd:TIGR00618 738 EDALNQSLKELMHQARtVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 982 EIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKR 1041
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
871-1011 |
1.17e-05 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 48.82 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 871 LRDEKESNLRLKGEtgIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGV------IKSLEKDIQGLKREIQERDETIQDK 944
Cdd:pfam17060 96 IPASFISALELKED--VKSSPRSEADSLGTPIKVDLLRNLKPQESPETPrrinrkYKSLELRVESMKDELEFKDETIMEK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 945 E-------KRIYDLKKKNQELGK-FKFVLDYK-----------------IKELKKQIEPRENEIRVMKEQIQEMEAELEN 999
Cdd:pfam17060 174 DrelteltSTISKLKDKYDFLSReFEFYKQHHehggnnsiktatkhefiISELKRKLQEQNRLIRILQEQIQFDPGALHD 253
|
170
....*....|..
gi 578798459 1000 FHKQNTQLELNI 1011
Cdd:pfam17060 254 NGPKNLVLNGAI 265
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
680-1101 |
1.65e-05 |
|
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: 49.44 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 680 KTDMEEKAQVMLELKTRVEELKMENEyqlrlkdmNYSEKIKELTdkfiqemESLKTKNQ---VLRTEKEKQDVYHHEHiE 756
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQNS--------DCKQHIEVLK-------ESLTAKEQraaILQTEVDALRLRLEEK-E 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 757 DLLDKQSRELQDMeccNNQKLLLEYE-------------KYQELQLKSQRMQEeyekQLRDNDetksQALEELTEFYEAk 823
Cdd:pfam10174 359 SFLNKKTKQLQDL---TEEKSTLAGEirdlkdmldvkerKINVLQKKIENLQE----QLRDKD----KQLAGLKERVKS- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 824 LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREiqdiktkyEKKLRDEKESnlrLKGETGIMRKKFSSLQKEIEERT 903
Cdd:pfam10174 427 LQTDSSNTDTALTTLEEALSEKERIIERLKEQRERE--------DRERLEELES---LKKENKDLKEKVSALQPELTEKE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 904 NDIETLKGEQ-------MKLQGVIKSLEKDIQgLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQI 976
Cdd:pfam10174 496 SSLIDLKEHAsslassgLKKDSKLKSLEIAVE-QKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEES 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 977 EPRENEIRVMKEQIQEMEAELENFHKQNTQLELNI-------TELWQKLRATDQEMRRERQKERDleaLVKRFKTDLHNC 1049
Cdd:pfam10174 575 GKAQAEVERLLGILREVENEKNDKDKKIAELESLTlrqmkeqNKKVANIKHGQQEMKKKGAQLLE---EARRREDNLADN 651
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 578798459 1050 VAYIQEPRLLK--EKVRGLFEKYVQRADMVEIA-----GLNTDLQQEytrQREHLERNL 1101
Cdd:pfam10174 652 SQQLQLEELMGalEKTRQELDATKARLSSTQQSlaekdGHLTNLRAE---RRKQLEEIL 707
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
717-1088 |
1.73e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.06 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 717 EKIKELTDKFIQEMESLKTKNQVLRTEkekqdvyhhehIEDLLDKQsRELQdmeccnnQKLLLEYEKYQELqlksqrmQE 796
Cdd:PRK04778 115 DLIEEDIEQILEELQELLESEEKNREE-----------VEQLKDLY-RELR-------KSLLANRFSFGPA-------LD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 797 EYEKQLrDNDETKSQALEELTE---FYEA-----KLQEKTTLLEEAQEDVRQQLREFEETKKQieededrEIQDIKTKYe 868
Cdd:PRK04778 169 ELEKQL-ENLEEEFSQFVELTEsgdYVEAreildQLEEELAALEQIMEEIPELLKELQTELPD-------QLQELKAGY- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 869 kklRDEKESNLRLKgETGIMrKKFSSLQKEIEERTNDIETLKGEQMKLQgvIKSLEKDIQGL----------KREIQERD 938
Cdd:PRK04778 240 ---RELVEEGYHLD-HLDIE-KEIQDLKEQIDENLALLEELDLDEAEEK--NEEIQERIDQLydilerevkaRKYVEKNS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 939 ETIQDKEKRiydLKKKNQELG------KFKFVLDYKIKELKKQIEPRENEIRVMKEQIQ-----------EMEAELENFH 1001
Cdd:PRK04778 313 DTLPDFLEH---AKEQNKELKeeidrvKQSYTLNESELESVRQLEKQLESLEKQYDEITeriaeqeiaysELQEELEEIL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1002 KQNTQLELNITELWQKLRATdqemrreRQKERDLEALVKRFKTDLHNCVAYIQeprllKEKVRGLFEKYVQRADMV--EI 1079
Cdd:PRK04778 390 KQLEEIEKEQEKLSEMLQGL-------RKDELEAREKLERYRNKLHEIKRYLE-----KSNLPGLPEDYLEMFFEVsdEI 457
|
....*....
gi 578798459 1080 AGLNTDLQQ 1088
Cdd:PRK04778 458 EALAEELEE 466
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
752-1209 |
1.77e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 752 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQ------LKSQRMQEEYEKQLRDNDETKSQA--LEELTEFYEAK 823
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEkelkhlREALQQTQQSHAYLTQKREAQEEQlkKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 824 LQEKTTL---LEEAQEDV---RQQLREFEETKK--QIEEDEDREIQDIKTKYEK--KLRDEKESNLRLKGETGIMRKKFS 893
Cdd:TIGR00618 269 IEELRAQeavLEETQERInraRKAAPLAAHIKAvtQIEQQAQRIHTELQSKMRSraKLLMKRAAHVKQQSSIEEQRRLLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 894 SLQKEIE--ERTNDIETLKGEQMKLQgviKSLEKDIqglkREIQERDETIQDKEKRIYDLKKKNQelgkfkfvldykikE 971
Cdd:TIGR00618 349 TLHSQEIhiRDAHEVATSIREISCQQ---HTLTQHI----HTLQQQKTTLTQKLQSLCKELDILQ--------------R 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 972 LKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKT------- 1044
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlqetr 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1045 ----DLHNCVAYIQEPRLLKEKVRglfeKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGElHRTDY- 1119
Cdd:TIGR00618 488 kkavVLARLLELQEEPCPLCGSCI----HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK-QRASLk 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1120 ---VRIMQENVSLIKEINELRRELKFTRSQVYDL----EAALKLTKKVRPQ---EVSETEPSRDMLSTAPTARLNEQEET 1189
Cdd:TIGR00618 563 eqmQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqdltEKLSEAEDMLACEqhaLLRKLQPEQDLQDVRLHLQQCSQELA 642
|
490 500
....*....|....*....|
gi 578798459 1190 GRIIEMQRLEIQRLRDQIQE 1209
Cdd:TIGR00618 643 LKLTALHALQLTLTQERVRE 662
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
975-1212 |
2.07e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 975 QIEPRENEIRVmkEQIQEMEAELENFhkqNTQLEL-----NITELWQKLRATDQEMRRERQKERDLEALVKRFK------ 1043
Cdd:COG3206 60 LVEPQSSDVLL--SGLSSLSASDSPL---ETQIEIlksrpVLERVVDKLNLDEDPLGEEASREAAIERLRKNLTvepvkg 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1044 TDLHNcVAYI-QEPRLLKEKVRGLFEKYVQRadmveiaglNTDLQQEYTRQ-REHLERNLATLKKKVVK-EGELH----R 1116
Cdd:COG3206 135 SNVIE-ISYTsPDPELAAAVANALAEAYLEQ---------NLELRREEARKaLEFLEEQLPELRKELEEaEAALEefrqK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1117 TDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALK-LTKKVRPQEVSETEPSRDMLSTAPTARLNEQEetGRIIEM 1195
Cdd:COG3206 205 NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAaLRAQLGSGPDALPELLQSPVIQQLRAQLAELE--AELAEL 282
|
250 260
....*....|....*....|...
gi 578798459 1196 QRL------EIQRLRDQIQEQEQ 1212
Cdd:COG3206 283 SARytpnhpDVIALRAQIAALRA 305
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
698-938 |
2.29e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 698 EELKMENEYQLRLKDMNySEKIKELTDKF---IQEMESLKT-----KNQVLRTEKEKQDVyhHEHIEDLLDKQSRELQDM 769
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKN-GENIARKQNKYdelVEEAKTIKAeieelTDELLNLVMDIEDP--SAALNKLNTAAAKIKSKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 770 ECCnnQKLLLEYEKYQELQLKSQrmqeeyekQLRDNDETKSQALEELTEfyeakLQEKTTLLEEAQEDVRQQLREFEETK 849
Cdd:PHA02562 272 EQF--QKVIKMYEKGGVCPTCTQ--------QISEGPDRITKIKDKLKE-----LQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 850 KqieededrEIQDIKTKYEKKLRDekesnlrLKGEtgimRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQG 929
Cdd:PHA02562 337 K--------KLLELKNKISTNKQS-------LITL----VDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
....*....
gi 578798459 930 LKREIQERD 938
Cdd:PHA02562 398 LVKEKYHRG 406
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
492-529 |
2.32e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 42.33 E-value: 2.32e-05
10 20 30
....*....|....*....|....*....|....*...
gi 578798459 492 ENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 529
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
795-1021 |
2.80e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 795 QEEYEKQLRDNDETKSQALEELtefyeAKLQEKttlLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYEKKlRDE 874
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAEL-----DALQAE---LEELNEEYNELQAELEALQAEIDKLQ-AEIAEAEAEIEER-REE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 875 KESNLRLKGETGIMRKKFSSL--QKEIEERTNDIETLKgeqmKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 952
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLlgSESFSDFLDRLSALS----KIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578798459 953 KKNQElgkfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRAT 1021
Cdd:COG3883 164 AELEA----------AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
662-962 |
2.95e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 662 RGIKREREVGFAEEVlvTKTDMEEKAQVMLELktrvEELKMENEYQLrlkdmnysEKIKEltdkfiqemESLKTKNQVLR 741
Cdd:pfam17380 310 REVERRRKLEEAEKA--RQAEMDRQAAIYAEQ----ERMAMEREREL--------ERIRQ---------EERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 742 TEKEKQDVYHHEHIEDLL----DKQSRELQDMECCNNQKLLLEyekyqELQLKSQRMQEEYEKQLRDNDETKSQALEELT 817
Cdd:pfam17380 367 QEEIAMEISRMRELERLQmerqQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQIRAEQEEARQREVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 818 EFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQ--IEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKkfsSL 895
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKklELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK---LL 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578798459 896 QKEIEERTNDIetLKGEQMKLQGVIKSLEKDIQGlKREIQERDETIQDKEKRIYDLKKKNQELGKFK 962
Cdd:pfam17380 519 EKEMEERQKAI--YEEERRREAEEERRKQQEMEE-RRRIQEQMRKATEERSRLEAMEREREMMRQIV 582
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
889-1044 |
3.04e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 889 RKKFSSLQKEIEERTnDIETLKGEQMK---LQGVIKSLEKDIQGLK-----REIQERDETIQDKEKRIYDLKKKNQELGK 960
Cdd:COG2433 349 KNKFERVEKKVPPDV-DRDEVKARVIRglsIEEALEELIEKELPEEepeaeREKEHEERELTEEEEEIRRLEEQVERLEA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 961 FKFVLDYKIKELKKQIEPRENEIRVMKEQIQE---MEAELENFHKQNTQLElnitelwqklratdQEMRRERQKERDLEA 1037
Cdd:COG2433 428 EVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDREIERLE--------------RELEEERERIEELKR 493
|
....*..
gi 578798459 1038 LVKRFKT 1044
Cdd:COG2433 494 KLERLKE 500
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
822-1048 |
3.80e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.93 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 822 AKLQEKTTLLEEAQEDVRQQLREFEETKKQiEEDEDREIQDIKTKYEKkLRDEKESNlrlkgetgimRKKFSSLQKEIEE 901
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLES-EEKNREEVEELKDKYRE-LRKTLLAN----------RFSYGPAIDELEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 902 RTNDIE---------TLKGEQMKLQGVIKSLEKDIQGLKR---EIQERDETIQDK-EKRIYDLKKKNQELGKFKFVLDY- 967
Cdd:pfam06160 154 QLAEIEeefsqfeelTESGDYLEAREVLEKLEEETDALEElmeDIPPLYEELKTElPDQLEELKEGYREMEEEGYALEHl 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 968 ----KIKELKKQIEPR------------ENEIRVMKEQIQE----MEAELENFH-----------------KQNTQLELN 1010
Cdd:pfam06160 234 nvdkEIQQLEEQLEENlallenleldeaEEALEEIEERIDQlydlLEKEVDAKKyveknlpeiedylehaeEQNKELKEE 313
|
250 260 270
....*....|....*....|....*....|....*...
gi 578798459 1011 ITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHN 1048
Cdd:pfam06160 314 LERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVER 351
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
692-1215 |
3.95e-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: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 692 ELKTRVEELKmeneyQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLR------TEKEKQDVYHHEHIE--DLLDKQS 763
Cdd:TIGR00606 249 PLKNRLKEIE-----HNLSKIMKLDNEIKAL-KSRKKQMEKDNSELELKMekvfqgTDEQLNDLYHNHQRTvrEKERELV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 764 RELQDMECCNNQKLLLEYEKYQ------ELQLKSQRMQEEYEKqlRDNDETKSQALEELTEFyeaklqekttlleEAQED 837
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTEllveqgRLQLQADRHQEHIRA--RDSLIQSLATRLELDGF-------------ERGPF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 838 VRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKES----NLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQ 913
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQadeiRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 914 MKLQGVIKsLEKDIQGLKREIQERDE--TIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQ 991
Cdd:TIGR00606 468 GSSDRILE-LDQELRKAERELSKAEKnsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 992 EMEAELENFHKQNTQLE------LNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNcvaYIQEPRLLKEKVRG 1065
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTsllgyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNH---INNELESKEEQLSS 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1066 LFEKyvqradMVEIAGlNTDLQQEYTRQREHLER---NLATLKKKV------VKEGELHRTDYVRIMQENVSLIKEINEL 1136
Cdd:TIGR00606 624 YEDK------LFDVCG-SQDEESDLERLKEEIEKsskQRAMLAGATavysqfITQLTDENQSCCPVCQRVFQTEAELQEF 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1137 RRELK-FTRSQVYDLEAALKLTKKV--RPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMqrlEIQRLRDQIQEQEQV 1213
Cdd:TIGR00606 697 ISDLQsKLRLAPDKLKSTESELKKKekRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNR---DIQRLKNDIEEQETL 773
|
..
gi 578798459 1214 TG 1215
Cdd:TIGR00606 774 LG 775
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
847-1020 |
5.12e-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: 47.71 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 847 ETKKQIEEDEDREIQ-DIKTKyEKKLRD-EKESNLRlkgetgimRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLE 924
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKnELKNK-EKELKNlDKNLNKD--------EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 925 KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN 1004
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170
....*....|....*.
gi 578798459 1005 TQLELNITELWQKLRA 1020
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLK 198
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
866-1150 |
5.49e-05 |
|
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: 47.53 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 866 KYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIeerTNDIETLKGEQMKLQgvikSLEKDIQGLKREIQE-RDETIQDK 944
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKASREE---TFARTALKNARLDLR----RLFDEKQSEKDKKNKaLAERKDSA 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 945 EKRIYDLKKKnqelgkfKFVLDYKIKELKKQIEPRENEIRV-MKEQIQEMEAELENFHKQ-NTQLELNITELWQKLRATD 1022
Cdd:pfam12128 681 NERLNSLEAQ-------LKQLDKKHQAWLEEQKEQKREARTeKQAYWQVVEGALDAQLALlKAAIAARRSGAKAELKALE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1023 QEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLF----EKYVQRADMVEIAGLNT-----DLQQEYTRQ 1093
Cdd:pfam12128 754 TWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFdwyqETWLQRRPRLATQLSNIeraisELQQQLARL 833
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578798459 1094 -------REHLERNLATLKKKVVKEGELHRTdyVRIMQENVSLIKE---INELRRELKFTRSQVYDL 1150
Cdd:pfam12128 834 iadtklrRAKLEMERKASEKQQVRLSENLRG--LRCEMSKLATLKEdanSEQAQGSIGERLAQLEDL 898
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
838-1214 |
5.58e-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: 47.32 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 838 VRQQLREFEETKKQIEEDEDrEIQDIKTKYEKKLRDEKESNLRLKgetgIMRKKFSSLQKEIEERTNDIETLKGEQMKLQ 917
Cdd:TIGR04523 35 EKQLEKKLKTIKNELKNKEK-ELKNLDKNLNKDEEKINNSNNKIK----ILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 918 GVIKS-------LEKDIQGLKREIQERDETIQD-------KEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEI 983
Cdd:TIGR04523 110 SEIKNdkeqknkLEVELNKLEKQKKENKKNIDKflteikkKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 984 RVMKEQI-----------------QEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDL 1046
Cdd:TIGR04523 190 DKIKNKLlklelllsnlkkkiqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1047 HNCVAYI-QEPRLLKEKvrglfEKYVQRADMvEIAGLNTDLQQEYTRQrehLERNLATLKKKVvkegELHRTDYVRIMQE 1125
Cdd:TIGR04523 270 SEKQKELeQNNKKIKEL-----EKQLNQLKS-EISDLNNQKEQDWNKE---LKSELKNQEKKL----EEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1126 NVSLIKEINELRRELKFTRSQvyDLEAALKLTKKVRPQEVSEtepsrdmlstaptarlNEQEETGRIIEMQRLEIQRLRD 1205
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESE--NSEKQRELEEKQNEIEKLK----------------KENQSYKQEIKNLESQINDLES 398
|
....*....
gi 578798459 1206 QIQEQEQVT 1214
Cdd:TIGR04523 399 KIQNQEKLN 407
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
826-1111 |
5.94e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.90 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 826 EKTTLLEEAQEDVRQQLREFEETKKQIEE---DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIM-------------- 888
Cdd:PTZ00440 404 KYTNIISLSEHTLKAAEDVLKENSQKIADyalYSNLEIIEIKKKYDEKINELKKSINQLKTLISIMksfydliisekdsm 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 889 ------RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLE---KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELG 959
Cdd:PTZ00440 484 dskekkESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEdyyITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKR 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 960 KFKFVLDYKIKELKKQIEpRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKeRDLEALV 1039
Cdd:PTZ00440 564 SMKNDIKNKIKYIEENVD-HIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYK-GDLQELL 641
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578798459 1040 KRFKTDLHNCVAYIQEPRlLKEKVRGLFEKYVQRADmvEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKE 1111
Cdd:PTZ00440 642 DELSHFLDDHKYLYHEAK-SKEDLQTLLNTSKNEYE--KLEFMKSDNIDNIIKNLKKELQNLLSLKENIIKK 710
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
714-941 |
6.32e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 46.59 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 714 NYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDvyHHEHIEDLLDKQSRELQdmeccnnqkllleyekyqELQLKSQR 793
Cdd:cd22656 80 NYAQNAGGTIDSYYAEILELIDDLADATDDEELEE--AKKTIKALLDDLLKEAK------------------KYQDKAAK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 794 MQEEYeKQLRDNDETKSQALEELTEFYEAKLQEKttLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKkLRD 873
Cdd:cd22656 140 VVDKL-TDFENQTEKDQTALETLEKALKDLLTDE--GGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIAD-DEA 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578798459 874 EKESNLRLKGETGIMRKKFSSLQKEIEERTNDIEtlkgeqmKLQGVIKSLEKDIQGLKREIQERDETI 941
Cdd:cd22656 216 KLAAALRLIADLTAADTDLDNLLALIGPAIPALE-------KLQGAWQAIATDLDSLKDLLEDDISKI 276
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
753-949 |
6.46e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 753 EHIEDLLDKQS------------REL-QDMECCNNQKLLLE-----YEKYQELQLKS-----QRMQEEYEKQL---RDND 806
Cdd:PHA02562 154 KLVEDLLDISVlsemdklnkdkiRELnQQIQTLDMKIDHIQqqiktYNKNIEEQRKKngeniARKQNKYDELVeeaKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 807 ETKSQALEELTEF------YEAKLQEKTTLLEEAQEDVRQQLRE---FEE-----TKKQIEEDEDREIQDIKTK---YEK 869
Cdd:PHA02562 234 AEIEELTDELLNLvmdiedPSAALNKLNTAAAKIKSKIEQFQKVikmYEKggvcpTCTQQISEGPDRITKIKDKlkeLQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 870 KLRDEKESNLRLKG---ETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKD-------IQGLKREIQERDE 939
Cdd:PHA02562 314 SLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdnaeeLAKLQDELDKIVK 393
|
250
....*....|
gi 578798459 940 TIQDKEKRIY 949
Cdd:PHA02562 394 TKSELVKEKY 403
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
690-1116 |
7.03e-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: 47.25 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 690 MLELKTR----VEELKMENEyqlrlKDMNYSEKIkeltDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedlLDKQSRE 765
Cdd:pfam15818 2 LLDFKTSlleaLEELRMRRE-----AETQYEEQI----GKIIVETQELKWQKETLQNQKET------------LAKQHKE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 766 LqdMECCNNQkllleyekyqeLQLKSQRMQEEYEK-QLRDndETKSQALEELTEFYEAKLQEKTTL---LEEAQEDVRQQ 841
Cdd:pfam15818 61 A--MAVFKKQ-----------LQMKMCALEEEKGKyQLAT--EIKEKEIEGLKETLKALQVSKYSLqkkVSEMEQKLQLH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 842 LREFEETKKQIEEDEdreiqdiktKYEKKLrdekesnlrlKGETGIMRKKFSSLQKEIEERtndIETLKgeqmKLQGVIK 921
Cdd:pfam15818 126 LLAKEDHHKQLNEIE---------KYYATI----------TGQFGLVKENHGKLEQNVQEA---IQLNK----RLSALNK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 922 SLEKDIQGLKREiqerdetiqdkekriydLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQeMEAEL---- 997
Cdd:pfam15818 180 KQESEICSLKKE-----------------LKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLN-MELELnkki 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 998 --ENFHKQNTQLELNITelwqkLRATDQEMRRERQKERDLEALVKRFKtdlHNCVAYIQEPRLLKEKVRGLFEKYVQRAD 1075
Cdd:pfam15818 242 neEITHIQEEKQDIIIS-----FQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQREKVKENEEKFLNLQN 313
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 578798459 1076 MVEIAglntdlQQEYTRQREHLERNLATLKKKVVKEGELHR 1116
Cdd:pfam15818 314 EHEKA------LGTWKKHVEELNGEINEIKNELSSLKETHI 348
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
780-1046 |
7.74e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 780 EYEKYQELQLKSQRmQEEYEKQLRDNDETKSQALEELTE-------------FYEAKLQEKTT--LLEEAQEDVRQQLRE 844
Cdd:PRK04778 49 ELEKVKKLNLTGQS-EEKFEEWRQKWDEIVTNSLPDIEEqlfeaeelndkfrFRKAKHEINEIesLLDLIEEDIEQILEE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 845 FEETKKQiEEDEDREIQDIKTKYEKkLRDEKESNlrlkgetgimRKKFSSLQKEIEERTNDIETL---------KGEQMK 915
Cdd:PRK04778 128 LQELLES-EEKNREEVEQLKDLYRE-LRKSLLAN----------RFSFGPALDELEKQLENLEEEfsqfvelteSGDYVE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 916 LQGVIKSLEKDIQGLKREIQERDETIQDKEK----RIYDLKKKNQELGKFKFVLDYK-----IKELKKQI---------- 976
Cdd:PRK04778 196 AREILDQLEEELAALEQIMEEIPELLKELQTelpdQLQELKAGYRELVEEGYHLDHLdiekeIQDLKEQIdenlalleel 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 977 --EPRENEIRVMKEQIQEM----EAE-----------------LENFHKQNTQLELNITELWQKLRATDQEMRRERQKER 1033
Cdd:PRK04778 276 dlDEAEEKNEEIQERIDQLydilEREvkarkyveknsdtlpdfLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEK 355
|
330
....*....|...
gi 578798459 1034 DLEALVKRFKTDL 1046
Cdd:PRK04778 356 QLESLEKQYDEIT 368
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
717-1177 |
7.82e-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: 47.35 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 717 EKIKELTDKFIQEMESLKTKNQVLRTEKEKQdvyhhEHIEDLLdkQSRELQdMECcnnqkllleyekyqelqlkSQRMQE 796
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKA-----CEIRDQI--TSKEAQ-LES-------------------SREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 797 EYEKQLRDNDETKSQALEELTEFYeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE 876
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIM--KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKER 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 877 SNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQ----ERDETIQDKEKRIYDLK 952
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfERGPFSERQIKNFHTLV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 953 KKNQElGKFKFV----LDYKIKELKKQIEPRENEIRvMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRE 1028
Cdd:TIGR00606 400 IERQE-DEAKTAaqlcADLQSKERLKQEQADEIRDE-KKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELD 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1029 ---RQKERDLEALVKRFKTD-LHNCVAYIQEPRL-LKEKVRGLFEKYVQRadmveiaglntDLQQEYTRQREHLERNLAT 1103
Cdd:TIGR00606 478 qelRKAERELSKAEKNSLTEtLKKEVKSLQNEKAdLDRKLRKLDQEMEQL-----------NHHTTTRTQMEMLTKDKMD 546
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578798459 1104 LKKKVVKEGELHRTDYVRIMQE---NVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLST 1177
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS 623
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
684-1141 |
8.81e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 684 EEKAQVMLELK-----TRVEELKMENEYQLRLKDMNYSEKIKELTDKfiqEMESLKTKNQVLRTEKEKQDVyhHEHIEDL 758
Cdd:COG5022 902 LELESEIIELKkslssDLIENLEFKTELIARLKKLLNNIDLEEGPSI---EYVKLPELNKLHEVESKLKET--SEEYEDL 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 759 LDKQS---RELQDMeccnNQKLLLEYEKYQELQLKSQRMQEEyEKQLRDNDeTKSQALEELTEFY---------EAKLQE 826
Cdd:COG5022 977 LKKSTilvREGNKA----NSELKNFKKELAELSKQYGALQES-TKQLKELP-VEVAELQSASKIIssestelsiLKPLQK 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 827 KTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKK---LRDEKESNLRLKGETGIMR------KKFSSLQK 897
Cdd:COG5022 1051 LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKtinVKDLEVTNRNLVKPANVLQfivaqmIKLNLLQE 1130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 898 EIEERTNDIETLKGEQMKLqgviKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFvldykiKELKKQIE 977
Cdd:COG5022 1131 ISKFLSQLVNTLEPVFQKL----SVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKS------KLSSSEVN 1200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 978 PRENEIRVMKEQIQEmEAELENFHKQNTQLELNITELWQKLRAT-DQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEP 1056
Cdd:COG5022 1201 DLKNELIALFSKIFS-GWPRGDKLKKLISEGWVPTEYSTSLKGFnNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEE 1279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1057 RLLKEKVRGLFEKYVQRADMVEIAGLNT-------------------DLQQEYTRQREHLERNLATLKKKVVKEGELHRT 1117
Cdd:COG5022 1280 EVLPATINSLLQYINVGLFNALRTKASSlrwksatevnynseelddwCREFEISDVDEELEELIQAVKVLQLLKDDLNKL 1359
|
490 500
....*....|....*....|....
gi 578798459 1118 DYVRIMQENVSLIkEINELRRELK 1141
Cdd:COG5022 1360 DELLDACYSLNPA-EIQNLKSRYD 1382
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
728-989 |
1.02e-04 |
|
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: 45.71 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 728 QEMESLKTKNQVLRTEKEKQDVYHHEHIE--DLLDKQSRELQ----DMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQ 801
Cdd:pfam09728 39 KDLKKLKKKQDQLQKEKDQLQSELSKAILakSKLEKLCRELQkqnkKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 802 LRDNDETKSQALEELTEFYE--AKLQEKTTLLEE------AQEDVRQQLRE------FEETKKQIEEDEDREIQDIKTKY 867
Cdd:pfam09728 119 MEEKSEKNNKLREENEELREklKSLIEQYELRELhfekllKTKELEVQLAEaklqqaTEEEEKKAQEKEVAKARELKAQV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 868 EKKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDetiqdkeKR 947
Cdd:pfam09728 199 QTLSETEKE----LREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSN-------KA 267
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 578798459 948 IYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQ 989
Cdd:pfam09728 268 LLEMAEERQKLKE-------ELEKLQKKLEKLENLCRALQAE 302
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
915-1212 |
1.36e-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: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 915 KLQGVIKSLEKDIQGLKREiqerdetiqdKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEME 994
Cdd:TIGR02168 190 RLEDILNELERQLKSLERQ----------AEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 995 AELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEalvkrfktdlhncvayiQEPRLLKEKVRGLFEKYVQra 1074
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE-----------------QQKQILRERLANLERQLEE-- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1075 dmveiagLNTDLQQEyTRQREHLERNLATLKKKVVkegelhrtdyvrimqenvSLIKEINELRRELKFTRSQVYDLEAAL 1154
Cdd:TIGR02168 321 -------LEAQLEEL-ESKLDELAEELAELEEKLE------------------ELKEELESLEAELEELEAELEELESRL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 578798459 1155 KLTKKVRPQEVSETepsrdmlstaptARLNEQEETgriiemQRLEIQRLRDQIQEQEQ 1212
Cdd:TIGR02168 375 EELEEQLETLRSKV------------AQLELQIAS------LNNEIERLEARLERLED 414
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
965-1149 |
1.64e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 965 LDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN--TQLELNITELWQKLRATDQEMRRERQKERDLEALVKRF 1042
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1043 KTDL---HNCVAYIQEPRLLKEKVRGLFEKYVQRADMV---------------EIAGLNTDLQQEYTRQREHLERNLATL 1104
Cdd:COG3206 246 RAQLgsgPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvialraQIAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578798459 1105 KKkvvKEGELHRT--DYVRIMQENVSLIKEINELRRELKFTRsQVYD 1149
Cdd:COG3206 326 QA---REASLQAQlaQLEARLAELPELEAELRRLEREVEVAR-ELYE 368
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
738-1197 |
1.69e-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: 46.20 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 738 QVLRTEKEKQDV-----YHHEHIEDLLDKQSRELQdmECCNNQKLLLEYekyqelqLKSQRMQEEYEKQLRdndETKSQA 812
Cdd:TIGR01612 328 KILESEGEQGHIinkliFLEKEFEDTIHKSDIYKD--ECLSNHLFMEDY-------LKDDKISPYYYEFLE---EIKKIA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 813 LEELTEFYEAKLQEKTTLLEEAQEDVrqqLREFEETKKQ--IEEDEDREIQDIKTKYEKKLRDEKESNLRL--KGETGIM 888
Cdd:TIGR01612 396 KQRAIFFYNAKKLKHLEILYKHQEDI---LNNFHKTIERliFEKPDPNNNNIFKDDFDEFNKPIPKSKLKAleKRFFEIF 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 889 RKKFSS--LQKEIEERTNDIETLKG--EQMK-LQGVIKSLEkdiQGLKREIQERDETIQDKEKRIYDLKKKNQELGkfkf 963
Cdd:TIGR01612 473 EEEWGSydIKKDIDENSKQDNTVKLilMRMKdFKDIIDFME---LYKPDEVPSKNIIGFDIDQNIKAKLYKEIEAG---- 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 964 vldykikeLKKQIEPRENeirvMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEmrrerqkerdlealvkrfk 1043
Cdd:TIGR01612 546 --------LKESYELAKN----WKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDE------------------- 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1044 tdlhncVAYIQEPRL-LKEKVRGLFEK--YVQRA-DMVEIAGLNTDLQQEYTRQR-----EHLERN---LATLKKKVVKe 1111
Cdd:TIGR01612 595 ------IIYINKLKLeLKEKIKNISDKneYIKKAiDLKKIIENNNAYIDELAKISpyqvpEHLKNKdkiYSTIKSELSK- 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1112 geLHRTDYVRIMQENVSLIKEINELRRELKftrSQVYDLEAalKLTKKVRPQEVSETEPSRDMLSTAPTarlNEQEETGR 1191
Cdd:TIGR01612 668 --IYEDDIDALYNELSSIVKENAIDNTEDK---AKLDDLKS--KIDKEYDKIQNMETATVELHLSNIEN---KKNELLDI 737
|
....*.
gi 578798459 1192 IIEMQR 1197
Cdd:TIGR01612 738 IVEIKK 743
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
672-947 |
1.81e-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: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 672 FAEEVLvTKTDMEEKAQVMLELktrVEELkmeNEYQLRLKDMnySEKIKELTD--KFIQEMESLKTKNQVLRTEKEKQDV 749
Cdd:COG4913 213 VREYML-EEPDTFEAADALVEH---FDDL---ERAHEALEDA--REQIELLEPirELAERYAAARERLAELEYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 750 YHHEHIEDLLDKQSRELQdmeccnnqkllleyEKYQELqlksqrmqeeyEKQLRDNDETKSQALEELTEFYEAKLQEKTT 829
Cdd:COG4913 284 WFAQRRLELLEAELEELR--------------AELARL-----------EAELERLEARLDALREELDELEAQIRGNGGD 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 830 LLEEAQEDVRQQlrefEETKKQIEEDEDReiqdiktkYEKKLRDekesnLRLKGETGimRKKFSSLQKEIEERtndIETL 909
Cdd:COG4913 339 RLEQLEREIERL----ERELEERERRRAR--------LEALLAA-----LGLPLPAS--AEEFAALRAEAAAL---LEAL 396
|
250 260 270
....*....|....*....|....*....|....*...
gi 578798459 910 KGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKR 947
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
780-1199 |
1.88e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 780 EYEKYQELQLKSQRMQEEYEK-QLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE--DE 856
Cdd:COG5022 811 EYRSYLACIIKLQKTIKREKKlRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQElkID 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 857 DREIQDIKTKYEK------KLRDEKESNLRLKGEtgIMRKKFSSLQKEIEERtnDIETLKGEQMKLQGVIKSLEKDIQGL 930
Cdd:COG5022 891 VKSISSLKLVNLEleseiiELKKSLSSDLIENLE--FKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLHEVESKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 931 KREIQERDETIQDKEKRIYDLKKKNQELGKFKfvldYKIKELKKQIEPRENEIRVMKEQIQEMEaelenFHKQNTQLELN 1010
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFK----KELAELSKQYGALQESTKQLKELPVEVA-----ELQSASKIISS 1037
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1011 ITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYiqeprllkekvrgLFEKYVQRADMVEIAGLNTDLQQEY 1090
Cdd:COG5022 1038 ESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLD-------------DKQLYQLESTENLLKTINVKDLEVT 1104
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1091 TRQREHLERNLATLKKKVVKEGELHRTDyvRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEP 1170
Cdd:COG5022 1105 NRNLVKPANVLQFIVAQMIKLNLLQEIS--KFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRL 1182
|
410 420 430
....*....|....*....|....*....|.
gi 578798459 1171 SRD-MLSTAPTARLNEQEE-TGRIIEMQRLE 1199
Cdd:COG5022 1183 YQSaLYDEKSKLSSSEVNDlKNELIALFSKI 1213
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
717-1045 |
2.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 717 EKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHH--EHIEDLLDKQS--RELQDMEccnnqkllleyEKYQELQLKSQ 792
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASaeREIAELE-----------AELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 793 RMQEeyekqLRDNDETKSQALEELTEFYEAkLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDRE-IQDIKTKYEKKL 871
Cdd:COG4913 686 DLAA-----LEEQLEELEAELEELEEELDE-LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 872 RDEKESNLR--LKGETGIMRKKFSSLQKEIEERTND-IETLKGEQMKLQGVIKSLEkDIQGLKREIQERDetIQDKEKRI 948
Cdd:COG4913 760 GDAVERELRenLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLP-EYLALLDRLEEDG--LPEYEERF 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 949 YDLKKKNQElgkfkfvldYKIKELKKQIeprENEIRVMKEQIQEMEAELEN----------FHKQNTQLElNITELWQKL 1018
Cdd:COG4913 837 KELLNENSI---------EFVADLLSKL---RRAIREIKERIDPLNDSLKRipfgpgrylrLEARPRPDP-EVREFRQEL 903
|
330 340 350
....*....|....*....|....*....|...
gi 578798459 1019 RA------TDQEMRRERQKERdLEALVKRFKTD 1045
Cdd:COG4913 904 RAvtsgasLFDEELSEARFAA-LKRLIERLRSE 935
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
938-1190 |
2.15e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 938 DETIQDKEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQK 1017
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1018 LRATDQEMRRERQKERDLEALVKrfKTDlhncvayiqeprllkekvrglFEKYVQRADMVE-IAGLNTDLQQEYTRQREH 1096
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLG--SES---------------------FSDFLDRLSALSkIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1097 LERNLATLKKKvVKEGELHRTDYVRIMQENVSLIKE----INELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSR 1172
Cdd:COG3883 145 LEAKKAELEAK-LAELEALKAELEAAKAELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250
....*....|....*...
gi 578798459 1173 DMLSTAPTARLNEQEETG 1190
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAA 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
957-1159 |
2.58e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 957 ELGK---FKFVLDYKIKELKKQIE----PRENEIRVMKEQIQEMEAELENFHKQNTQLElnitELWQKLRATDQEMRRER 1029
Cdd:COG4717 33 EAGKstlLAFIRAMLLERLEKEADelfkPQGRKPELNLKELKELEEELKEAEEKEEEYA----ELQEELEELEEELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1030 QKERDLEALVKRFKtDLHNCVAYIQEPRLLKEKVRGLFEKYVQ-RADMVEIAglntDLQQEYTRQREHLERNLATLKKKV 1108
Cdd:COG4717 109 AELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERLEElEERLEELR----ELEEELEELEAELAELQEELEELL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578798459 1109 VKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKK 1159
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
773-873 |
3.13e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 42.18 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 773 NNQKLLLEYEKYQELQLKSQRMQEEYEKQLrdndETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQI 852
Cdd:pfam03938 6 DMQKILEESPEGKAAQAQLEKKFKKRQAEL----EAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKA 81
|
90 100
....*....|....*....|.
gi 578798459 853 EEDEDREIQDIKTKYEKKLRD 873
Cdd:pfam03938 82 QQELQKKQQELLQPIQDKINK 102
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
674-1007 |
3.34e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 674 EEVLVTKTDMEE------KAQVML-----ELKTRVEELKMENEYqlrLKDMNYSEKIKELTDKfIQEMESLKTKNQVLRT 742
Cdd:PRK04778 205 EELAALEQIMEEipellkELQTELpdqlqELKAGYRELVEEGYH---LDHLDIEKEIQDLKEQ-IDENLALLEELDLDEA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 743 EKEKQDVyhHEHIEDLLDKqsrelqdMEccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKsqalEELTEfyea 822
Cdd:PRK04778 281 EEKNEEI--QERIDQLYDI-------LE--------REVKARKYVEKNSDTLPDFLEHAKEQNKELK----EEIDR---- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 823 kLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTkyekklrdekesnlrlkgetgimrkkFSSLQKEIEER 902
Cdd:PRK04778 336 -VKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIA--------------------------YSELQEELEEI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 903 TNDIETLKGEQMKLQGVIKSLEKDiqglkrEIQERdETIQDKEKRIYDLK----KKN-----QELGKFKFVLDYKIKELK 973
Cdd:PRK04778 389 LKQLEEIEKEQEKLSEMLQGLRKD------ELEAR-EKLERYRNKLHEIKryleKSNlpglpEDYLEMFFEVSDEIEALA 461
|
330 340 350
....*....|....*....|....*....|....
gi 578798459 974 KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQL 1007
Cdd:PRK04778 462 EELEEKPINMEAVNRLLEEATEDVETLEEETEEL 495
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
832-1003 |
3.73e-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: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 832 EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFsslqKEIEERTNDIEtlkg 911
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESSIK-QVEEELEELKEQNEELEKQYKVKKKTL----DLLPDAEENIA---- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 912 eqmKLQGVIKSLEKDIQGLKREIQERDETIQdKEKRIYDLKKKNQELgKFKFVLDyKIKELKKQIEPRENEIRVMKEQIQ 991
Cdd:pfam05667 405 ---KLQALVDASAQRLVELAGQWEKHRVPLI-EEYRALKEAKSNKED-ESQRKLE-EIKELREKIKEVAEEAKQKEELYK 478
|
170
....*....|..
gi 578798459 992 EMEAELENFHKQ 1003
Cdd:pfam05667 479 QLVAEYERLPKD 490
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
691-1140 |
3.95e-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: 45.04 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 691 LELKTRVEELKMENEYQLRLKDMnysEKIKELTDKFIQEM---------ESLKTKNQVLRTEK-EKQDVYhhehiEDLLD 760
Cdd:TIGR01612 603 LELKEKIKNISDKNEYIKKAIDL---KKIIENNNAYIDELakispyqvpEHLKNKDKIYSTIKsELSKIY-----EDDID 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 761 KQSRELQDMECCNNQKLLLEYEKYQELQLKSqrmqeeyekqlrDNDETKSQALEelTEFYEAKLqektTLLEEAQEDVRQ 840
Cdd:TIGR01612 675 ALYNELSSIVKENAIDNTEDKAKLDDLKSKI------------DKEYDKIQNME--TATVELHL----SNIENKKNELLD 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 841 QLREFEE-TKKQIEEDEDREIQDIKTKyEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNdIETLKGEQMKlQGV 919
Cdd:TIGR01612 737 IIVEIKKhIHGEINKDLNKILEDFKNK-EKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQIN-IDNIKDEDAK-QNY 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 920 IKSlekdiqglkreiQERDETIQDKEKRIydlkkknqelgkFKFVldykikelkkqiepreNEIRVMKEQIQ---EMEAE 996
Cdd:TIGR01612 814 DKS------------KEYIKTISIKEDEI------------FKII----------------NEMKFMKDDFLnkvDKFIN 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 997 LENFHKQNTQLE-LNITELWQKLRA--TDQEMRRERQKERDLEALV-----------------KRFKTDLHNCVAYIQEP 1056
Cdd:TIGR01612 854 FENNCKEKIDSEhEQFAELTNKIKAeiSDDKLNDYEKKFNDSKSLIneinksieeeyqnintlKKVDEYIKICENTKESI 933
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1057 RLLKEKVRGLFEKYVQRADMVEIAGLntdLQQEYTRQREHLERNLATLKKKVVKEGELhrTDYvriMQENVSLIKEINEL 1136
Cdd:TIGR01612 934 EKFHNKQNILKEILNKNIDTIKESNL---IEKSYKDKFDNTLIDKINELDKAFKDASL--NDY---EAKNNELIKYFNDL 1005
|
....
gi 578798459 1137 RREL 1140
Cdd:TIGR01612 1006 KANL 1009
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
377-406 |
4.18e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.87 E-value: 4.18e-04
10 20 30
....*....|....*....|....*....|
gi 578798459 377 HSAPITGLATCIRKPLIATCSLDRSIRLWN 406
Cdd:pfam00400 10 HTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
778-1063 |
5.02e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 778 LLEYEKYQELQlKSQRMQEEYEKQlRDNDETKSQALEELTEfyeaklQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED 857
Cdd:pfam02029 64 FLDRTAKREER-RQKRLQEALERQ-KEFDPTIADEKESVAE------RKENNEEEENSSWEKEEKRDSRLGRYKEEETEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 858 REIQDIKTKYEKKLRDEKEsnlrlKGEtgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQER 937
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEE-----EGE---EEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 938 deTIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPrENEIRVMKEQIQEME-AELENFHKQNTQLELNITELwQ 1016
Cdd:pfam02029 208 --KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEA-EQKLEELRRRRQEKEsEEFEKLRQKQQEAELELEEL-K 283
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 578798459 1017 KLRATDQEMRRERQKERDLEALVKRFKTDlhncvayiQEPRLLKEKV 1063
Cdd:pfam02029 284 KKREERRKLLEEEEQRRKQEEAERKLREE--------EEKRRMKEEI 322
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
374-406 |
5.27e-04 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 38.83 E-value: 5.27e-04
10 20 30
....*....|....*....|....*....|...
gi 578798459 374 YPLHSAPITGLATCIRKPLIATCSLDRSIRLWN 406
Cdd:smart00320 8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
46-168 |
5.47e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.75 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 46 SQGMLALSISPNRRYLAiseTVQEKPAITIYELSSipcrkRKVLNNFDFQVQKFISMAFSPDSKYLLAQTSppeSNLVYw 125
Cdd:COG2319 288 SGGVNSVAFSPDGKLLA---SGSDDGTVRLWDLAT-----GKLLRTLTGHTGAVRSVAFSPDGKTLASGSD---DGTVR- 355
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578798459 126 LWEKQKVMAIVRIDTQNNPVYQVSFSPQDNTQVCVTGNGMFKL 168
Cdd:COG2319 356 LWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
680-958 |
5.60e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 44.07 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 680 KTDMEEKAQVMLELKTRVEELkmeneyqlrlkdMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedll 759
Cdd:pfam09726 408 KAELQASRQTEQELRSQISSL------------TSLERSLKSELGQLRQENDLLQTKLHNAVSAKQK------------- 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 760 DKQSreLQDMEccnnQKLLLEyekyqelqlksQRMQEEYEKQLrdNDETKSQALEELTEFYEAKLQEKTTllEEAQEDVR 839
Cdd:pfam09726 463 DKQT--VQQLE----KRLKAE-----------QEARASAEKQL--AEEKKRKKEEEATAARAVALAAASR--GECTESLK 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 840 QQLREFEETKKQIEED---EDREIQDIKTKyEKKLRDEKESnlrlKGETGIMRKKFSSLQKEIEERTNDI--ETlkgeQM 914
Cdd:pfam09726 522 QRKRELESEIKKLTHDiklKEEQIRELEIK-VQELRKYKES----EKDTEVLMSALSAMQDKNQHLENSLsaET----RI 592
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 578798459 915 KLqgvikSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQEL 958
Cdd:pfam09726 593 KL-----DLFSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEV 631
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
670-878 |
6.90e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 670 VGFAEEVLVTKTDMEEKAQVMLEL-KTRVEELKMENEYQLRLKDMNYSEKIKELTDKFiqEMESLKTKNQVLRTEKEKQD 748
Cdd:PRK12704 16 VGAVIGYFVRKKIAEAKIKEAEEEaKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF--EKELRERRNELQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 749 VyhhehiEDLLDKQSRELQDMEccnnqkllleyekyQELQLKsqrmQEEYEKQLRDndetksqaLEELTEFYEAKLQEKT 828
Cdd:PRK12704 94 K------EENLDRKLELLEKRE--------------EELEKK----EKELEQKQQE--------LEKKEEELEELIEEQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578798459 829 TLLEEA----QEDVRQQLreFEETKKQIEEDEDREIQDIKTKYekKLRDEKESN 878
Cdd:PRK12704 142 QELERIsgltAEEAKEIL--LEKVEEEARHEAAVLIKEIEEEA--KEEADKKAK 191
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
806-1212 |
1.01e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.46 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 806 DETKSQALEELTEFYEAKLQEKTTLLEEaqedvRQQLREFEETKKqieededreIQDIKTKY-------EKKLRDEKESN 878
Cdd:NF033838 53 NESQKEHAKEVESHLEKILSEIQKSLDK-----RKHTQNVALNKK---------LSDIKTEYlyelnvlKEKSEAELTSK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 879 LR---------LKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVI--KSLEKDIQGLKREIQERD-ETIQDKEK 946
Cdd:NF033838 119 TKkeldaafeqFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNtyKTLELEIAESDVEVKKAElELVKEEAK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 947 RIYDLKKKNQELGKFkfvldykikELKKQIEPRENEIRVMKEQIQE-----MEAELENFHKQNTQLELNITELWQKLRAT 1021
Cdd:NF033838 199 EPRDEEKIKQAKAKV---------ESKKAEATRLEKIKTDREKAEEeakrrADAKLKEAVEKNVATSEQDKPKRRAKRGV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1022 DQEMRRERQKERDLEAlvkrfkTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRAdmveiaglntdlQQEYTRQREHLERNL 1101
Cdd:NF033838 270 LGEPATPDKKENDAKS------SDSSVGEETLPSPSLKPEKKVAEAEKKVEEA------------KKKAKDQKEEDRRNY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1102 ATLKKKVVkEGELHRTDyVRIMQENVSLIKEI-NELRRELKFTRSQvydleaalkltKKVrpqEVSETEPSRdmLSTAPT 1180
Cdd:NF033838 332 PTNTYKTL-ELEIAESD-VKVKEAELELVKEEaKEPRNEEKIKQAK-----------AKV---ESKKAEATR--LEKIKT 393
|
410 420 430
....*....|....*....|....*....|..
gi 578798459 1181 ARLNEQEETGRIIEmqrlEIQRLRDQIQEQEQ 1212
Cdd:NF033838 394 DRKKAEEEAKRKAA----EEDKVKEKPAEQPQ 421
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
785-865 |
1.10e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.50 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 785 QELQLKSQRMQEEYEKQLRdndETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLrefEETKKQIEEDEDREIQDIK 864
Cdd:cd06503 43 EKAKEEAEELLAEYEEKLA---EARAEAQEIIEEARKEAEKIKEEILAEAKEEAERIL---EQAKAEIEQEKEKALAELR 116
|
.
gi 578798459 865 T 865
Cdd:cd06503 117 K 117
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
814-952 |
1.14e-03 |
|
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: 41.07 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 814 EELTEFYeAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYE---KKLRDEKESNLRLKGEtgimrk 890
Cdd:pfam08614 3 LELIDAY-NRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllAQLREELAELYRSRGE------ 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578798459 891 kfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 952
Cdd:pfam08614 76 ----LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQ 133
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
825-1014 |
1.17e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 825 QEKTTLLEEAQEdvrQQLREFEETKKQIEEDEDREIQDIKTKYEK---KLRDEKESNLRLKGETGIMRKK---------- 891
Cdd:PRK05771 16 SYKDEVLEALHE---LGVVHIEDLKEELSNERLRKLRSLLTKLSEaldKLRSYLPKLNPLREEKKKVSVKsleelikdve 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 892 --FSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEK------DIQ-------------GLKREIQERDETI--------- 941
Cdd:PRK05771 93 eeLEKIEKEIKELEEEISELENEIKELEQEIERLEPwgnfdlDLSlllgfkyvsvfvgTVPEDKLEELKLEsdvenveyi 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 942 -QDKEKRIY-------DLKKKNQELGKF---KFVLDYK--IKELKKQIEPRENEIrvmKEQIQEMEAELENFHKQNTQLE 1008
Cdd:PRK05771 173 sTDKGYVYVvvvvlkeLSDEVEEELKKLgfeRLELEEEgtPSELIREIKEELEEI---EKERESLLEELKELAKKYLEEL 249
|
....*.
gi 578798459 1009 LNITEL 1014
Cdd:PRK05771 250 LALYEY 255
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
919-1212 |
1.31e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 919 VIKSLEKDIQGLKR--EIQERDETIQDKEKRiydlkKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAE 996
Cdd:COG1196 194 ILGELERQLEPLERqaEKAERYRELKEELKE-----LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 997 LENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLhncvayiqeprllkekvrglfekyvqradm 1076
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1077 veiaglntdlqQEYTRQREHLERNLATLKkkvvkegelhrtdyvrimQENVSLIKEINELRRELKFTRSQVYDLEAALKL 1156
Cdd:COG1196 319 -----------EELEEELAELEEELEELE------------------EELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 578798459 1157 TKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQ 1212
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
838-1034 |
1.38e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 838 VRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQ 917
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKT----IKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 918 GVIKSLEKDI-------------QGLKREiQERDETIQDK----EKRIYDLKKKNQELGKFKFVLD---YKIKELKKQIE 977
Cdd:PHA02562 269 SKIEQFQKVIkmyekggvcptctQQISEG-PDRITKIKDKlkelQHSLEKLDTAIDELEEIMDEFNeqsKKLLELKNKIS 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578798459 978 PRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEmRRERQKERD 1034
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT-KSELVKEKY 403
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
665-943 |
1.42e-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: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 665 KREREVGFAEEVLVTKTDMEEKAQVMLE----LKTRVEELKME-----NEYQLRLKDMNYSEKIKELTDKFIQEMESLKT 735
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEelkaLREALDELRAEltllnEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 736 KNQVLRTEKEKQdvyhHEHIEDLLDKQSRELQdmeccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEE 815
Cdd:TIGR02168 849 ELSEDIESLAAE----IEELEELIEELESELE-----------ALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 816 ltefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGetgiMRKKFSSL 895
Cdd:TIGR02168 914 -----RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR----LENKIKEL 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 578798459 896 Q----------KEIEERtndIETLKGEQMKLQGVIKSLEKDIQGLKREIQER-DETIQD 943
Cdd:TIGR02168 985 GpvnlaaieeyEELKER---YDFLTAQKEDLTEAKETLEEAIEEIDREARERfKDTFDQ 1040
|
|
| PTZ00332 |
PTZ00332 |
paraflagellar rod protein; Provisional |
764-1161 |
1.48e-03 |
|
paraflagellar rod protein; Provisional
Pssm-ID: 240364 [Multi-domain] Cd Length: 589 Bit Score: 42.64 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 764 RELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRD-------------NDETKSQALEELTEFyeakLQEKTTL 830
Cdd:PTZ00332 162 ATLKNIEDIMNVTQIQNALASTDDQIKTQLAQLEKTNEIQNvamhdgemqvaeeQMWTKVQLQERLIEL----VADKFRL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 831 LEEAqEDVRQQLREFEETKKQIEEdEDREIQDIKtkyeKKLRDEKESNLRlkgetgimrkkfsSLQKEIEERtnDIEtlK 910
Cdd:PTZ00332 238 IGKC-EEENKSFSKIHEVQKQANQ-ETSQMKDAK----RRLKQRCETDLK-------------HIHDAIQKA--DLE--D 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 911 GEQMKLQGVIKslEKDiqglKREIQERDETIQDKEKRIYDLKKKNQELGKFKFvldykiKELKKQIEP--RENEIRVMKE 988
Cdd:PTZ00332 295 AEAMKRYATNK--EKS----ERFIRENEDRQEEAWNKIQDLERQLQRLGTERF------EEVKRRIEEndREEKRRVEYQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 989 QIQEMEAElenfHKQ-------NTQLELNITELWQKLRA------------TDQEM---RRERQKERdLEALVKRFKTdl 1046
Cdd:PTZ00332 363 QFLEVAGQ----HKKlleltvyNCDLALRCTGLVEELVSegcaavkarhdkTNQDLaalRLQVHKEH-LEYFRMLYLT-- 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1047 HNCVAYIQEPRLlKEKVRGLFEKYVQRADMVEI----AGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDYVRI 1122
Cdd:PTZ00332 436 LGSLIYKKEKRL-EEIDRNIRTTHIQLEFCVETfdpnAKKHADMKKELYKLRQGVEEELAMLKEKQAQALEMFKESEEAL 514
|
410 420 430
....*....|....*....|....*....|....*....
gi 578798459 1123 MQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVR 1161
Cdd:PTZ00332 515 DAAGIEFVHPVDENNEEVLTRRSKMVEYRSHLAKQEEVK 553
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
692-958 |
1.63e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 692 ELKTRVEELKMENEYQLRLKDMNYsEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHIEdlLDKQSRELQDME- 770
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELN-EKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS--IDKLRKEIERLEw 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 771 CCNNQKLLLEYEKyqELQLKSQRMQEEYEKqLRDNDETKSQALEELTEFYEAKLQekttlleeaQEDVRQQLREFEETKK 850
Cdd:COG1340 124 RQQTEVLSPEEEK--ELVEKIKELEKELEK-AKKALEKNEKLKELRAELKELRKE---------AEEIHKKIKELAEEAQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 851 QIEEdedrEIQDIKTKYEKkLRDEKESnlrlkgetgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGL 930
Cdd:COG1340 192 ELHE----EMIELYKEADE-LRKEADE----------LHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
250 260
....*....|....*....|....*...
gi 578798459 931 KREiqERDETIQDKEKRIYDLKKKNQEL 958
Cdd:COG1340 257 KRE--KEKEELEEKAEEIFEKLKKGEKL 282
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
737-1034 |
1.72e-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: 42.21 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 737 NQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQ----ELQLKSQRMQEEYEKQLRDNDETKSQA 812
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEeqieEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 813 LEELTEFYEAKLQEKTTLLEEAQEDVRQQlREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKF 892
Cdd:pfam13868 111 QEEDQAEAEEKLEKQRQLREEIDEFNEEQ-AEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 893 SSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIydlkkknqelgkfkfvldyKIKEL 972
Cdd:pfam13868 190 RAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI-------------------ELKER 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578798459 973 KKQIEPRENE---IRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERD 1034
Cdd:pfam13868 251 RLAEEAEREEeefERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELE 315
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
816-1047 |
1.94e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 816 LTEFYEAKLQEKTTLLEEAqEDVRQQLREFEETKKQIEEDEDR-----EIQDIKTKYEKKLRDEKESN-LRLKGETGIMR 889
Cdd:COG4913 209 LDDFVREYMLEEPDTFEAA-DALVEHFDDLERAHEALEDAREQiellePIRELAERYAAARERLAELEyLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 890 KKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDetiqdkekriydlkkknqelGKfkfvldyki 969
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG--------------------GD--------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 970 kelkkQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLEL-----------NITELWQKLRATDQEMRRERQKERDLEAL 1038
Cdd:COG4913 339 -----RLEQLEREIERLERELEERERRRARLEALLAALGLplpasaeefaaLRAEAAALLEALEEELEALEEALAEAEAA 413
|
....*....
gi 578798459 1039 VKRFKTDLH 1047
Cdd:COG4913 414 LRDLRRELR 422
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
941-1099 |
2.18e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.67 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 941 IQDKEKRIYDLKK-KNQELGKFKFVLDYKIKELKK-------QIEPRENEIRVMKEQIQEMEA----ELENFHKQNTQLE 1008
Cdd:pfam09787 20 LQSKEKLIASLKEgSGVEGLDSSTALTLELEELRQerdllreEIQKLRGQIQQLRTELQELEAqqqeEAESSREQLQELE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1009 LNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCV----AYIQEPRL--------------LKEKVRGLFEKY 1070
Cdd:pfam09787 100 EQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIkdreAEIEKLRNqltsksqssssqseLENRLHQLTETL 179
|
170 180
....*....|....*....|....*....
gi 578798459 1071 VQRADMVEiaglntDLQQEYTRQREHLER 1099
Cdd:pfam09787 180 IQKQTMLE------ALSTEKNSLVLQLER 202
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
782-1010 |
2.37e-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: 42.36 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 782 EKYQELQLKSQRMQEEYEKQlrdndetKSQALEELTEfyeakLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReiq 861
Cdd:pfam13166 279 DEFTEFQNRLQKLIEKVESA-------ISSLLAQLPA-----VSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRA--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 862 diktKYEKKLRDEKESNL-RLKGETGIMRKKFSSLQKEIE---ERTNDIETLKGEQMKL--QGVIKSLEKDIQGLKREIQ 935
Cdd:pfam13166 344 ----LEAKRKDPFKSIELdSVDAKIESINDLVASINELIAkhnEITDNFEEEKNKAKKKlrLHLVEEFKSEIDEYKDKYA 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578798459 936 ERDETIQDKEKRIYDLKKKNQELGKfkfvldyKIKELkkqieprENEIRVMKEQIQEMEAELENFHKQNTQLELN 1010
Cdd:pfam13166 420 GLEKAINSLEKEIKNLEAEIKKLRE-------EIKEL-------EAQLRDHKPGADEINKLLKAFGFGELELSFN 480
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
891-1045 |
2.38e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 891 KFSSLQKEIEERTNDIETL----KGEQMKLQGVIKSLEKDIQGLKREIQERDETI----QDKEKRIYDLKKKNQELGKFK 962
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQrkknGENIARKQNKYDELVEEAKTIKAEIEELTDELlnlvMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 963 FVLDYKIKELK------------KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLEL----------NITELWQKLRA 1020
Cdd:PHA02562 269 SKIEQFQKVIKmyekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdefneqskKLLELKNKIST 348
|
170 180
....*....|....*....|....*
gi 578798459 1021 TDQEMRRERQKERDLEALVKRFKTD 1045
Cdd:PHA02562 349 NKQSLITLVDKAKKVKAAIEELQAE 373
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
789-963 |
2.50e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 789 LKSQRMQEEYEKQLRDNDEtksqalEELTEFYEAKLQEKTTLLEEAQE--DVRQQLRE-FEETKKQIEEdedreiqdikt 865
Cdd:smart00787 128 LEAKKMWYEWRMKLLEGLK------EGLDENLEGLKEDYKLLMKELELlnSIKPKLRDrKDALEEELRQ----------- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 866 kyEKKLRDEKESNLrlKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIqdKE 945
Cdd:smart00787 191 --LKQLEDELEDCD--PTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL--EQ 264
|
170
....*....|....*...
gi 578798459 946 KRIYDLKKKNQELGKFKF 963
Cdd:smart00787 265 CRGFTFKEIEKLKEQLKL 282
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
684-863 |
2.62e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 684 EEKAQVMLELKTRVEELKMENEYQLRLKDmnysEKIKELTDKFIQEMESLKTKnqvlrtekekqdvyhhehiEDLLDKQS 763
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERR----NELQKLEKRLLQKEENLDRK-------------------LELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 764 RELQDMECCNNQKLlleyekyQELQLKSQRMQEEYEKQLrdndetksQALEE---LTEFyEAKLQEKTTLLEEAQEDVRQ 840
Cdd:PRK12704 110 EELEKKEKELEQKQ-------QELEKKEEELEELIEEQL--------QELERisgLTAE-EAKEILLEKVEEEARHEAAV 173
|
170 180
....*....|....*....|...
gi 578798459 841 QLREFEEtkkQIEEDEDREIQDI 863
Cdd:PRK12704 174 LIKEIEE---EAKEEADKKAKEI 193
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
778-1037 |
2.73e-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: 42.08 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 778 LLEYEKYQELQLKSQRMQEEYEK-----QLRDNDETKSQALEELTEF------YEAKLQEKTTLLEEAQEDVRQQLREFE 846
Cdd:pfam01576 476 LLQEETRQKLNLSTRLRQLEDERnslqeQLEEEEEAKRNVERQLSTLqaqlsdMKKKLEEDAGTLEALEEGKKRLQRELE 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 847 ETKKQIEEDEDR--EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLE 924
Cdd:pfam01576 556 ALTQQLEEKAAAydKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKE 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 925 KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN 1004
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAK 715
|
250 260 270
....*....|....*....|....*....|...
gi 578798459 1005 TQLELNItelwQKLRAtdqemrrerQKERDLEA 1037
Cdd:pfam01576 716 LRLEVNM----QALKA---------QFERDLQA 735
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
857-1141 |
3.15e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 857 DREIQDIKTKYEKKLRD-EKESNLRLKGETGIMR---KKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQ---- 928
Cdd:PLN02939 105 DEAIAAIDNEQQTNSKDgEQLSDFQLEDLVGMIQnaeKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSetda 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 929 --GLKREIQERDETIQDK-EKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQ---IQEMEAELENFHK 1002
Cdd:PLN02939 185 riKLAAQEKIHVEILEEQlEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAElieVAETEERVFKLEK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1003 QNTQLELNITELWQKLRATDQEMRRER--------QKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLfEKYVQRA 1074
Cdd:PLN02939 265 ERSLLDASLRELESKFIVAQEDVSKLSplqydcwwEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKL-EASLKEA 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578798459 1075 DMVEIAGLNTDL-QQEYTRQREHLERNlatlkkkvvkEGELHrtDYVRIMQEnvsLIKEINELRRELK 1141
Cdd:PLN02939 344 NVSKFSSYKVELlQQKLKLLEERLQAS----------DHEIH--SYIQLYQE---SIKEFQDTLSKLK 396
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
691-876 |
3.24e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 691 LELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRT-EKEKQDVYHHEHIEDLLDK-QSRELQD 768
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAALLAEaGVEDEEE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 769 MEccnnqKLLLEYEKYQELQLKsqrmQEEYEKQLRDNDETKSQALEELT-EFYEAKLQEKTTLLEEAQEDVRQQLREFEE 847
Cdd:COG4717 387 LR-----AALEQAEEYQELKEE----LEELEEQLEELLGELEELLEALDeEELEEELEELEEELEELEEELEELREELAE 457
|
170 180 190
....*....|....*....|....*....|
gi 578798459 848 TKKQIEE-DEDREIQDIKTKYEKKLRDEKE 876
Cdd:COG4717 458 LEAELEQlEEDGELAELLQELEELKAELRE 487
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
799-1213 |
3.29e-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: 41.73 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 799 EKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQlREFEETKKQIEEDEDREIQDIKTKYEKklrdEKESN 878
Cdd:pfam10174 44 ERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQ-RDLNQLLQQDFTTSPVDGEDKFSTPEL----TEENF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 879 LRLKGETGIMRKKFSSLQKEIEERTNDIETLKG-------------EQMKLQGVIKSLEKDIQGLKREIQERDETIQDKE 945
Cdd:pfam10174 119 RRLQSEHERQAKELFLLRKTLEEMELRIETQKQtlgardesikkllEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 946 KRiydLKKKNQELGKFKFVLDY---------KIKELKKQIEPRENEIRVMKEQIQEMEAELEN------FHKQNTQLELN 1010
Cdd:pfam10174 199 VL---LDQKEKENIHLREELHRrnqlqpdpaKTKALQTVIEMKDTKISSLERNIRDLEDEVQMlktnglLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1011 ITELWQ--------KLRATDQEMRRerqKERDLEALVKRFKTdLHN----CVAYIQeprLLKEKvrgLFEKYvQRADMve 1078
Cdd:pfam10174 276 QMEVYKshskfmknKIDQLKQELSK---KESELLALQTKLET-LTNqnsdCKQHIE---VLKES---LTAKE-QRAAI-- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1079 iaglntdLQQEYTRQREHLERNLATLKKKvvkegelhrTDYVRIMQENVSL-------------IKE--INELRRELKFT 1143
Cdd:pfam10174 343 -------LQTEVDALRLRLEEKESFLNKK---------TKQLQDLTEEKSTlageirdlkdmldVKErkINVLQKKIENL 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1144 RSQVYDLEAALKlTKKVRPQEVSETEPSRDMLSTAPTARLNEQEetgRIIEmqRLEIQRLRDQIQEQEQV 1213
Cdd:pfam10174 407 QEQLRDKDKQLA-GLKERVKSLQTDSSNTDTALTTLEEALSEKE---RIIE--RLKEQREREDRERLEEL 470
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
713-886 |
3.34e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 713 MNYSEKIKELTDKfiqEMESLKTKNQVLRTEKEKQDVYHHEhIEDLLDKQSRELQDMeccnnQKLLLEYEKYQELQLKSQ 792
Cdd:smart00787 139 MKLLEGLKEGLDE---NLEGLKEDYKLLMKELELLNSIKPK-LRDRKDALEEELRQL-----KQLEDELEDCDPTELDRA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 793 RmqEEYEKQLRDNDEtKSQALEELTEfyeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLR 872
Cdd:smart00787 210 K--EKLKKLLQEIMI-KVKKLEELEE----ELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKL 282
|
170
....*....|....
gi 578798459 873 DEKESNLRLKGETG 886
Cdd:smart00787 283 LQSLTGWKITKLSG 296
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
898-1163 |
3.64e-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: 41.75 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 898 EIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIY----DLKKKNQELGKFKFVLDYKIKELK 973
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRtlddQWKEKRDELNGELSAADAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 974 KQIEPRENEIRV-MKEQIQEMEAELENFHKQNTQLEL---NITELWQKLRATDQEMRRERQKeRDLEalVKRFKTDLHNC 1049
Cdd:pfam12128 322 SELEALEDQHGAfLDADIETAAADQEQLPSWQSELENleeRLKALTGKHQDVTAKYNRRRSK-IKEQ--NNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1050 VAYIQEprllkEKVRGLfekyvqradmveiAGLNTDLQQEYTRQREHLERNLATLK--KKVVKE--GELH-RTDYVRIMQ 1124
Cdd:pfam12128 399 LAKIRE-----ARDRQL-------------AVAEDDLQALESELREQLEAGKLEFNeeEYRLKSrlGELKlRLNQATATP 460
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 578798459 1125 ENVSLIK----EINELRRELKFTRSQVYDLEAALKLTKKVRPQ 1163
Cdd:pfam12128 461 ELLLQLEnfdeRIERAREEQEAANAEVERLQSELRQARKRRDQ 503
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
831-1178 |
3.98e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 831 LEEAQEDVRQQLREFEETKKQIEEDEDR--EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKfsslQKEIEERTNDIET 908
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKacEIRDQITSKEAQLESSREIVKSYENELDPLKNR----LKEIEHNLSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 909 LKGEQMKLQGVIKSLEKDIQGLK----------------------REIQERDETIQDKEKRIYDLKKKNQELGKFKFVLD 966
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELElkmekvfqgtdeqlndlyhnhqRTVREKERELVDCQRELEKLNKERRLLNQEKTELL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 967 YKIKELKKQIEPRENEIRVMKEQIQEMEaelenfhkqnTQLELNITElwqklRATDQEMRRERQKERDLEALVKRFKTDL 1046
Cdd:TIGR00606 347 VEQGRLQLQADRHQEHIRARDSLIQSLA----------TRLELDGFE-----RGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1047 HNCVAYIQEPRLLKEKVRGLfekyvqradMVEIAGLNTDLQQEytrqREHLERNLATLKKKvVKEGELHRTDYVRIMQEN 1126
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEI---------RDEKKGLGRTIELK----KEILEKKQEELKFV-IKELQQLEGSSDRILELD 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578798459 1127 VSLIKEINEL------------RRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTA 1178
Cdd:TIGR00606 478 QELRKAERELskaeknsltetlKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT 541
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
50-179 |
4.13e-03 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 41.05 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 50 LALSISPNRRYLAiseTVQEKPAITIYELSSipcrkRKVLNNFDFQVQKFISMAFSPDSKYLLAQTsppESNLVyWLWEK 129
Cdd:COG2319 250 RSVAFSPDGRLLA---SGSADGTVRLWDLAT-----GELLRTLTGHSGGVNSVAFSPDGKLLASGS---DDGTV-RLWDL 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 578798459 130 QKVMAIVRIDTQNNPVYQVSFSPQDNTQVCVTGNGMFKLLRFAEGTLKQT 179
Cdd:COG2319 318 ATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT 367
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
697-1024 |
4.35e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 697 VEELKMENEYQLRLKDMNYS-EKIKELTDKFIQEMESLKT--KNQvlrTEKEKQDVYHHEHIEDLLDKQSRELQDMECCN 773
Cdd:TIGR01612 1401 LEECKSKIESTLDDKDIDECiKKIKELKNHILSEESNIDTyfKNA---DENNENVLLLFKNIEMADNKSQHILKIKKDNA 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 774 NQKLLLEYEKYQELQLKSQRMQEEYEK---QLRDNDETKSQALEELTE----FYEAKLQEKttlLEEAQEDVRQQLREFE 846
Cdd:TIGR01612 1478 TNDHDFNINELKEHIDKSKGCKDEADKnakAIEKNKELFEQYKKDVTEllnkYSALAIKNK---FAKTKKDSEIIIKEIK 1554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 847 ETKKQIEEDEDREIQDIKTKYEKKLRDEKE---SNLRLKGETGI------MRKKFSSLQkEIEERTNDIETlkgEQMKLQ 917
Cdd:TIGR01612 1555 DAHKKFILEAEKSEQKIKEIKKEKFRIEDDaakNDKSNKAAIDIqlslenFENKFLKIS-DIKKKINDCLK---ETESIE 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 918 GVIKSLEKDIQGLK--------REIQERDETIQDKEKRIYDLKKKNQElgkfkfvLDYKIKELKKQIEPREN--EIRVMk 987
Cdd:TIGR01612 1631 KKISSFSIDSQDTElkengdnlNSLQEFLESLKDQKKNIEDKKKELDE-------LDSEIEKIEIDVDQHKKnyEIGII- 1702
|
330 340 350
....*....|....*....|....*....|....*...
gi 578798459 988 EQIQEM-EAELENFHKQNTQLELNITELWQKLRATDQE 1024
Cdd:TIGR01612 1703 EKIKEIaIANKEEIESIKELIEPTIENLISSFNTNDLE 1740
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
790-1063 |
4.38e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 790 KSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQL---REFEETKKQIEEDEDR--EIQDIK 864
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSIneyNKIESARADLEDIKIKinELKDKH 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 865 TKYEKKlrDEKESNLRLkgetGIMRKKFSSLQKEIEERTN-DIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQD 943
Cdd:PRK01156 546 DKYEEI--KNRYKSLKL----EDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 944 KEKRIYDlkKKNQELGKFKfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLeLNITELWQKLRATDQ 1023
Cdd:PRK01156 620 SIREIEN--EANNLNNKYN-----EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRI-NDIEDNLKKSRKALD 691
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 578798459 1024 EMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKV 1063
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDINETLESMKKI 731
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
717-934 |
4.55e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 717 EKIKELTD--KFIQE----MESLKTKNQVLRTEKE-----KQDVYHHEHIEDLLDKQSRELQDMeccNNQKLLLEYEKYQ 785
Cdd:PRK04863 901 EQLDEAEEakRFVQQhgnaLAQLEPIVSVLQSDPEqfeqlKQDYQQAQQTQRDAKQQAFALTEV---VQRRAHFSYEDAA 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 786 ELQLKSQRMQEEYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLLEEAQE--DV-RQQLREFEetkkqieededREIQD 862
Cdd:PRK04863 978 EMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQ-AQAQLAQYNQVLASLKSsyDAkRQMLQELK-----------QELQD 1045
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578798459 863 IKTKY----EKKLRDEKEsnlRLKGETGIMRKKFSSLQKEIEERTNDIETLkgeqmklQGVIKSLEKDIQGLKREI 934
Cdd:PRK04863 1046 LGVPAdsgaEERARARRD---ELHARLSANRSRRNQLEKQLTFCEAEMDNL-------TKKLRKLERDYHEMREQV 1111
|
|
| WDR74 |
cd22857 |
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ... |
332-409 |
4.91e-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: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 332 CLCFSPSEETLVASTSKNQLYSI---TMSLTEISKGepahfeylmypLHSAPITGLATCIRKPLIATCSLDRSIRLWNYE 408
Cdd:cd22857 228 AVAEDPDGHTVYVGDTSGDLASIdlrTGKLLGCFKG-----------KCGGSIRSIARHPELPLIASCGLDRYLRIWDTE 296
|
.
gi 578798459 409 T 409
Cdd:cd22857 297 T 297
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
747-987 |
5.94e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 747 QDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQElQLKSQRMQ----EEYEKQLRDNDETKSQALEELTEFYEA 822
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYN-KIESARADlediKIKINELKDKHDKYEEIKNRYKSLKLE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 823 KLQEKTTLLEEAQE-----DVRQQLREFEETKKQIEEDEDR------EIQDIKTKYEKKLR--DEKESNLRLKgetgimR 889
Cdd:PRK01156 562 DLDSKRTSWLNALAvisliDIETNRSRSNEIKKQLNDLESRlqeieiGFPDDKSYIDKSIReiENEANNLNNK------Y 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 890 KKFSSLQKEIEERTNDIETLKGEQMKlqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKI 969
Cdd:PRK01156 636 NEIQENKILIEKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
250
....*....|....*...
gi 578798459 970 KELKKQIEPRENEIRVMK 987
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
896-1208 |
6.86e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 896 QKEIEERTNDIETLKGEQMKLQGVIKSLE---KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfvldyKIKEL 972
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRaeiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLK-------EIERL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 973 KKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQlelnitelwqkLRATDQEMRRERQKERDLEALVKRFKtDLHNCVAY 1052
Cdd:PRK01156 224 SIEYNNAMDDYNNLKSALNELSSLEDMKNRYESE-----------IKTAESDLSMELEKNNYYKELEERHM-KIINDPVY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1053 IQeprllKEKVRGLFEKYVQRADMVEI-AGLNTDLQqeytrQREHLERNLATLKKkvvkegelHRTDYVRIMQENVSLIK 1131
Cdd:PRK01156 292 KN-----RNYINDYFKYKNDIENKKQIlSNIDAEIN-----KYHAIIKKLSVLQK--------DYNDYIKKKSRYDDLNN 353
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578798459 1132 EINELRRELKFTRSQVYDLEaalKLTKKVRpqevsETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQ 1208
Cdd:PRK01156 354 QILELEGYEMDYNSYLKSIE---SLKKKIE-----EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
811-921 |
6.87e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 811 QALEELtefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE---------SNLRL 881
Cdd:PRK00409 523 ASLEEL----ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikelRQLQK 598
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 578798459 882 KGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIK 921
Cdd:PRK00409 599 GGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
781-898 |
6.91e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.
Pssm-ID: 214016 [Multi-domain] Cd Length: 152 Bit Score: 38.36 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 781 YEKYQELQLKS---QRMQEEYEKqLRDNDETKSQALE---ELTEFYEAKLQEKTTLLEEAQEDVRQQLRE-FEETKKQIE 853
Cdd:cd12923 11 KEINKEYLDKSreyDELYEKYNK-LSQEIQLKRQALEafeEAVKMFEEQLRTQEKFQKEAQPHEKQRLMEnNELLKSRLK 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578798459 854 ededrEIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKE 898
Cdd:cd12923 90 -----ELEESKEQLEEDLRKQVAYNRELEREMNSLKPELMQLRKQ 129
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
674-884 |
8.40e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 674 EEVLVTKTDMEEKaqvMLELKTRVEELKMENEYQLrlkdmnySEKIKELtDKFIQEMESLKTKNQVLRTEKEKQDVYHHE 753
Cdd:PRK03918 559 AELEKKLDELEEE---LAELLKELEELGFESVEEL-------EERLKEL-EPFYNEYLELKDAEKELEREEKELKKLEEE 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 754 hIEDLLDKQSRELQDMECCNNQ--KLLLEY--EKYQELQLKSQRMQEEYE------KQLRDNDETKSQALEELTEFYEA- 822
Cdd:PRK03918 628 -LDKAFEELAETEKRLEELRKEleELEKKYseEEYEELREEYLELSRELAglraelEELEKRREEIKKTLEKLKEELEEr 706
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578798459 823 -KLQEKTTLLEEAQEDVrQQLRE-FEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGE 884
Cdd:PRK03918 707 eKAKKELEKLEKALERV-EELREkVKKYKALLKERALSKVGEIASEIFEELTEGKYSGVRVKAE 769
|
|
| PHA01351 |
PHA01351 |
putative minor structural protein |
710-1016 |
8.72e-03 |
|
putative minor structural protein
Pssm-ID: 107029 Cd Length: 1070 Bit Score: 40.31 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 710 LKDMNYSEKIKELTDKFIqemeslkTKNQVLRTEKekqdvyhhehiedLLDKQSRELQDMECCNNQKLLLEyekyqelqL 789
Cdd:PHA01351 455 FKDLGYPEEVRTVFDTMI-------TQSQLIQTNQ-------------LLLRQLQQIVSLGIFDQKKIKEE--------L 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 790 KSQRMQEEYEKQLRDNDETKSQALEELTEfYEAKLqeKTTLLeeAQEDVRQQLREFEETKKQIEededreiQDIKTKYEK 869
Cdd:PHA01351 507 KANKFNEQVALQILESELQFAQLQNQLKE-YQFKL--NNFLI--SPQDLEKDLKHLGFDSAIIS-------ALIYENQVE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 870 KLRDEKESNLRlkgetGIMRKKFSSLqKEIEERTNDIETLKGEQMKLQGVIkSLEKDIQGLKREIQERDETIQ-DKEKRI 948
Cdd:PHA01351 575 QLIKFQLNNIE-----SLAKKGYLSL-DEIKKQFKAIGIIKEYEDAFINFY-NQELQISAFLTILKSQLRQFQiDPKEAE 647
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 949 YDLKKK--NQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQ 1016
Cdd:PHA01351 648 TELKKLniNEYLANQIIQEEYNINIAKLQLSVLETIAKTLYYDQQQLSGELKKIHKDKTALELYITKFYY 717
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
810-1096 |
9.14e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 39.68 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 810 SQALEEL------TEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKkLRDEKESNLRLKG 883
Cdd:pfam04108 20 RSLLEELvvllakIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDK-LRNTPVEPALPPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 884 ETG-------IMRKKFSSLQKEIEErtnDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDEtIQDKEKRIYDLKKKNQ 956
Cdd:pfam04108 99 EEKqktlldfIDEDSVEILRDALKE---LIDELQAAQESLDSDLKRFDDDLRDLQKELESLSS-PSESISLIPTLLKELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 957 EL-----GKF-KFVLDY-KIKELKKQIEPRENE---------------IRVMKEQIQEMEAELENFHKQNTQLELNITEL 1014
Cdd:pfam04108 175 SLeeemaSLLeSLTNHYdQCVTAVKLTEGGRAEmlevlendarelddvVPELQDRLDEMENNYERLQKLLEQKNSLIDEL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1015 ---WQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYV-----QRADMVEIAGLNTDL 1086
Cdd:pfam04108 255 lsaLQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREFYEGFPSAYGSLLleverRREWAEKMKKILRKL 334
|
330
....*....|
gi 578798459 1087 QQEYTRQREH 1096
Cdd:pfam04108 335 AEELDRLQEE 344
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
665-1140 |
9.70e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 665 KREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEyQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEK 744
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 745 EKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKS----QRMQEEYEKQLRDNDETKSQALEELTEFY 820
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAllerLERLEEELEELEEALAELEEEEEEEEEAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 821 EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKK--------- 891
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLlaglrglag 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 892 -FSSLQKEIEERTNDIETLKGEQMKLQGV--IKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGK-------- 960
Cdd:COG1196 525 aVAVLIGVEAAYEAALEAALAAALQNIVVedDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAigaavdlv 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 961 ---------FKFVLDYKIKELKKQIEPRENEIRVMK-------EQIQEMEAELENFHKQNTQLELNITELWQKLRATDQE 1024
Cdd:COG1196 605 asdlreadaRYYVLGDTLLGRTLVAARLEAALRRAVtlagrlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798459 1025 MRRERQKERDLEALVKRFKTDLHNcvayIQEPRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQQEYTRQ----------- 1093
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERE----LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEeealeelpepp 760
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578798459 1094 -REHLERNLATLKKKV----------------VKE--GELH--RTDYVRIMQENVSLIKEINELRREL 1140
Cdd:COG1196 761 dLEELERELERLEREIealgpvnllaieeyeeLEEryDFLSeqREDLEEARETLEEAIEEIDRETRER 828
|
|
| |
