|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
403-667 |
2.44e-34 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 136.96 E-value: 2.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 403 LIATCSLDRSIRLWNYETNT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDD-IRSFK--EYSVRGcgeC 477
Cdd:COG2319 134 TLASGSADGTVRLWDLATGKlLRTLTGHSGAVTSVAFSPDGKLLASGSDDGtVRLWDLATGKlLRTLTghTGAVRS---V 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 478 SFS-NGGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCS 556
Cdd:COG2319 211 AFSpDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 557 YNCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEY 634
Cdd:COG2319 291 VNSVAFSPDGKLLASGSDDGTVRlwDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL--WDLATGELLRTL 368
|
250 260 270
....*....|....*....|....*....|...
gi 767902630 635 QAHAGPITKMLLTFDDQFLLTAAEDGCLFTWKV 667
Cdd:COG2319 369 TGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
386-678 |
1.85e-31 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 128.49 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 386 PLHSAPITGLATCIRKPLIATCSLDRSIRLWNYETN-TLELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNL----L 459
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGlLLRTLTGHTGAVRSVAFSPDGKTLASGSADGtVRLWDLatgkL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 460 IDDIRSFKE--YSVrgcgecSFSNGGHLFAAVNG-NVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAV 536
Cdd:COG2319 155 LRTLTGHSGavTSV------AFSPDGKLLASGSDdGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 537 YEWNLSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTS 614
Cdd:COG2319 229 RLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRlwDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSD 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902630 615 VGTIRAmkYPLPLQKEFNEYQAHAGPITKMLLTFDDQFLLTAAEDGclfTWKVFDKDGRGIKRE 678
Cdd:COG2319 309 DGTVRL--WDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDG---TVRLWDLATGELLRT 367
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
388-666 |
2.46e-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: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 388 HSAPITGLATCIRKPLIATCSLDRSIRLWNYETNTLEL-FKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNL----LID 461
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtLKGHTGPVRDVAASADGTYLASGSSDKtIRLWDLetgeCVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 462 DIRSFKEYsVRGcgeCSFSNGGHLFAAVNG-NVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 540
Cdd:cd00200 88 TLTGHTSY-VSS---VAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 541 LSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTI 618
Cdd:cd00200 164 LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKlwDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTI 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767902630 619 RAmkYPLPLQKEFNEYQAHAGPITKMLLTFDDQFLLTAAEDGCLFTWK 666
Cdd:cd00200 244 RV--WDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
341-579 |
6.22e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 111.93 E-value: 6.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 341 VLCLCFSPSEETLvASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWNYET 420
Cdd:COG2319 165 VTSVAFSPDGKLL-ASGSDDG----TVRLWDLATGKLLRT----LTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 421 NT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDDIRSFKEYSVRGCGECSFS-NGGHLFAAVNGNVIHVY 497
Cdd:COG2319 236 GKlLRTLTGHSGSVRSVAFSPDGRLLASGSADGtVRLWDLATGELLRTLTGHSGGVNSVAFSpDGKLLASGSDDGTVRLW 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 498 TTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHT 577
Cdd:COG2319 316 DLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395
|
..
gi 767902630 578 LK 579
Cdd:COG2319 396 VR 397
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
703-1221 |
4.35e-22 |
|
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: 103.18 E-value: 4.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 703 ELKTRVEELKMENEYQLRLKD-MNYSEKIKELTDKFI-----------QEMESLKTKNQVLRTEKEKQDVYHHEHIEDLL 770
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVeLNKLEKQKKENKKNIdkflteikkkeKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 771 DKQSrelqDMECCNNQKLLLEY---------EKYQELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFYEAKLQEKTTL 841
Cdd:TIGR04523 184 NIQK----NIDKIKNKLLKLELllsnlkkkiQKNKSLESQISELKKQ-NNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 842 LEEAQEDVRQ---QLREFEETKKQIEEDEDReIQDIKTKYEkKLRDEKESNL--RLKGETGIMRKKFSSLQKE------- 909
Cdd:TIGR04523 259 KDEQNKIKKQlseKQKELEQNNKKIKELEKQ-LNQLKSEIS-DLNNQKEQDWnkELKSELKNQEKKLEEIQNQisqnnki 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 910 IEERTNDIETLKGEQM-------KLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKE 982
Cdd:TIGR04523 337 ISQLNEQISQLKKELTnsesensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 983 LKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL-------WQKLRATDQEMRRERQkerDLEALVKRFKT 1055
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntreslETQLKVLSRSINKIKQ---NLEQKQKELKS 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1056 DLHNCVAYIQEPRLLKEKVRGLFEKyvqradmveIAGLNTDlQQEYTRQREHLERNLATLKKKVVK-EGELHRTDYVRIM 1134
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKK---------ISSLKEK-IEKLESEKKEKESKISDLEDELNKdDFELKKENLEKEI 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1135 QENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEpsrdMLSTAPTARLNEQEETGRIIEMQRLEIQRL 1214
Cdd:TIGR04523 564 DEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKE----KKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
....*..
gi 767902630 1215 RDQIQEQ 1221
Cdd:TIGR04523 640 KNKLKQE 646
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
338-540 |
1.31e-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: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 338 KQDVLCLCFSPSEeTLVASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:cd00200 93 TSYVSSVAFSPDG-RILSSSSRDK----TIKVWDVETGKCLTT----LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 418 YETNTL-ELFKEYQEEAYSISLHPSGHFIVVGFADKlrlmNLLIDDIRSFKE-YSVRGCGE----CSFSNGGHLFAAVNG 491
Cdd:cd00200 164 LRTGKCvATLTGHTGEVNSVAFSPDGEKLLSSSSDG----TIKLWDLSTGKClGTLRGHENgvnsVAFSPDGYLLASGSE 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767902630 492 -NVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 540
Cdd:cd00200 240 dGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
341-543 |
2.43e-20 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 94.98 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 341 VLCLCFSPSEETLvASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCirkP---LIATCSLDRSIRLWN 417
Cdd:COG2319 207 VRSVAFSPDGKLL-ASGSADG----TVRLWDLATGKLLRT----LTGHSGSVRSVAFS---PdgrLLASGSADGTVRLWD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 418 YETNT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDD-IRSFKEYSVRGCGeCSFS-NGGHLFAAVNGNV 493
Cdd:COG2319 275 LATGElLRTLTGHSGGVNSVAFSPDGKLLASGSDDGtVRLWDLATGKlLRTLTGHTGAVRS-VAFSpDGKTLASGSDDGT 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767902630 494 IHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLST 543
Cdd:COG2319 354 VRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
820-1166 |
3.56e-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: 87.42 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 820 KSQALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNlRLKGETGIM 899
Cdd:TIGR02168 675 RRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYK 979
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 980 IKELKKQIEPRENEIRVMKEQIQ--------------EMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERD 1045
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIEslaaeieeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1046 LEALVKRFKTDLHNCVAYIQEPRL----LKEKVRglfEKYVQRADMVEIAGLNTDLQQEYTRQRehlernLATLKKKVVK 1121
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVridnLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR------LKRLENKIKE 983
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 767902630 1122 EGELhrtdyvrimqeNVSLIKEINELRRELKFTRSQVYDLEAALK 1166
Cdd:TIGR02168 984 LGPV-----------NLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
843-1202 |
2.14e-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: 85.12 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 843 EEAQEDVRQQLREFEETKKQIEEDEdrEIQDIKTKYEKKLRDEKESNLRlkgetgimrkkFSSLQKEIEE-----RTNDI 917
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLD--LIIDEKRQQLERLRREREKAER-----------YQALLKEKREyegyeLLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 918 ETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGkfkfvlDYKIKELKKQIEPRENEIRVM 997
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 998 KEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEprlLKEKVRGL 1077
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE---VDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1078 FEKYVQRADMVEiaglntdlqqEYTRQREHLERNLATL---KKKVVKEGELHRTDYVRIMQ-------ENVSLIKEINEL 1147
Cdd:TIGR02169 384 RDELKDYREKLE----------KLKREINELKRELDRLqeeLQRLSEELADLNAAIAGIEAkineleeEKEDKALEIKKQ 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 767902630 1148 RRELKFTRSQVYDLEAAL-KLTKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGR 1202
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELyDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGG 509
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
504-665 |
3.43e-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: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 504 NISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSYNCVTVSPDAKIIFAVGSDHTLK--EI 581
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRlwDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 582 ADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQAHAGPITKMLLTFDDQFLLTAAEDGC 661
Cdd:cd00200 81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKV--WDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158
|
....
gi 767902630 662 LFTW 665
Cdd:cd00200 159 IKLW 162
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
793-1047 |
4.44e-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: 83.96 E-value: 4.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 793 EKYQELQLKSQRMqEEYE--KQLRDNDETKSQALEELTEFyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIE---EDE 867
Cdd:TIGR02169 211 ERYQALLKEKREY-EGYEllKEKEALERQKEAIERQLASL-EEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 868 DREIQ----DIKTKYEKKLRDEKESNLRLKGETGIMRKKFS---SLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQG 940
Cdd:TIGR02169 289 QLRVKekigELEAEIASLERSIAEKERELEDAEERLAKLEAeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 941 LKREIQERDETIQ-------DKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHK 1013
Cdd:TIGR02169 369 LRAELEEVDKEFAetrdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
250 260 270
....*....|....*....|....*....|....
gi 767902630 1014 QNTQLELNITELWQKLRATDQEMRRERQKERDLE 1047
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
478-669 |
5.04e-16 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 81.88 E-value: 5.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 478 SFSNGGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSY 557
Cdd:COG2319 44 ASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 558 NCVTVSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQ 635
Cdd:COG2319 124 RSVAFSPDGKTLASGSADGTVRlwDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL--WDLATGKLLRTLT 201
|
170 180 190
....*....|....*....|....*....|....
gi 767902630 636 AHAGPITKMLLTFDDQFLLTAAEDGclfTWKVFD 669
Cdd:COG2319 202 GHTGAVRSVAFSPDGKLLASGSADG---TVRLWD 232
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
696-1019 |
1.19e-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: 82.42 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 696 EKAQVMLELKTRVEELkmenEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQdvyhHEHIEDLLDKQSR 775
Cdd:TIGR02169 208 EKAERYQALLKEKREY----EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR----LEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 776 ELQDM---ECCNNQKLLLEYEKYQElqlKSQRMQEEYEKQLRDNDETKSQALEELTefyeaKLQEKTTLLEEAQEDVRQQ 852
Cdd:TIGR02169 280 KIKDLgeeEQLRVKEKIGELEAEIA---SLERSIAEKERELEDAEERLAKLEAEID-----KLLAEIEELEREIEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 853 LREFEEtkkqieededrEIQDIKTKYEK---KLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQG 929
Cdd:TIGR02169 352 RDKLTE-----------EYAELKEELEDlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 930 VIKSLEKDIQGLKREIQERDETIQDKEKRIydlKKKNQELgkfkfvldykiKELKKQIEPRENEIRVMKEQIQEMEAELE 1009
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEI---KKQEWKL-----------EQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
330
....*....|
gi 767902630 1010 NFHKQNTQLE 1019
Cdd:TIGR02169 487 KLQRELAEAE 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
712-1222 |
1.84e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 81.65 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 712 KMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKtkNQVLRTEKEKQDVYHH-EHIEDLLDKQSRELQDMEccnnqKLLL 790
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIE--ELIKEKEKELEEVLREiNEISSELPELREELEKLE-----KEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 791 EYEKYQELQLKSQRMQEEYEKQLRdndetksqaleeltefyeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE----- 865
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKR-------------------KLEEKIRELEERIEELKKEIEELEEKVKELKElkeka 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 866 DEDREIQDIKTKYEKKLRDEKESNLRLKGE-TGIMR--KKFSSLQKEIEERTNDIETLKGEQMKLQG------VIKSLEK 936
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEiNGIEEriKELEEKEERLEELKKKLKELEKRLEELEErhelyeEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 937 DIQGLK-----REIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQI-------------------EPREN 992
Cdd:PRK03918 373 ELERLKkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteEHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 993 EIRVMKEQIQEMEAELENFHKQNTQLELNITELwQKLRATDQEMRRERQKERDLEALVKRFKT-DLHNCVAYIQEPRLLK 1071
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1072 EKVRGLFEkyvqradmvEIAGLNTDLQ--QEYTRQREHLERNLATLKKKVvkeGELHRtdyvRIMQENVSLIKEINELRR 1149
Cdd:PRK03918 532 EKLIKLKG---------EIKSLKKELEklEELKKKLAELEKKLDELEEEL---AELLK----ELEELGFESVEELEERLK 595
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902630 1150 ELKFTRSQVYDLEAAlkltkkvrPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQE 1222
Cdd:PRK03918 596 ELEPFYNEYLELKDA--------EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
829-1170 |
2.04e-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: 78.56 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 829 EFYEAKLQEKTTLLEEA------QEDVRQQLREFEETKKQIEEDED--REI---------QDIKTKYEKKLRDEKEsNLR 891
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAagiskyKERRKETERKLERTRENLDRLEDilNELerqlkslerQAEKAERYKELKAELR-ELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 892 LkgetGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGK 971
Cdd:TIGR02168 227 L----ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 972 FKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVK 1051
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1052 RFKTDLHncvayiqeprLLKEkvrglfEKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEgelHRTDYV 1131
Cdd:TIGR02168 383 TLRSKVA----------QLEL------QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE---LQAELE 443
|
330 340 350
....*....|....*....|....*....|....*....
gi 767902630 1132 RIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKK 1170
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
692-1222 |
2.54e-14 |
|
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: 78.24 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 692 TDMEEK-AQVMLELK--TRVEELKMEN-EYQLRLKDMNYSEKIKElTDKFIQEMESLKTKNQVLRTekekqDVYHHEHIE 767
Cdd:pfam15921 320 SDLESTvSQLRSELReaKRMYEDKIEElEKQLVLANSELTEARTE-RDQFSQESGNLDDQLQKLLA-----DLHKREKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 768 DLLDKQSRELQDMECCNN-------QKLLLEYEKYQELQLKSQRMQEEYEKQLrdndETKSQALEELTEFYEaKLQEKTT 840
Cdd:pfam15921 394 SLEKEQNKRLWDRDTGNSitidhlrRELDDRNMEVQRLEALLKAMKSECQGQM----ERQMAAIQGKNESLE-KVSSLTA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 841 LLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKESNlrlkgetgimrKKFSSLQKEIEERTNDIETL 920
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSE-RTVSDLTASLQEKERAIEATN-----------AEITKLRSRVDLKLQELQHL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 921 KGEQMKLQGVikslEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRE---NEIRVM 997
Cdd:pfam15921 537 KNEGDHLRNV----QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRlelQEFKIL 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 998 KE----QIQEMEAELENFHKQNTQLelnITELWQKLRATdqemrRERQKERD-LEALVKRFKTDLHNCVayiQEPRLLKE 1072
Cdd:pfam15921 613 KDkkdaKIRELEARVSDLELEKVKL---VNAGSERLRAV-----KDIKQERDqLLNEVKTSRNELNSLS---EDYEVLKR 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1073 KVRGLFEkyvqradmvEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGElhrtdyvrIMQENVSLIKEINELRRELK 1152
Cdd:pfam15921 682 NFRNKSE---------EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH--------AMKVAMGMQKQITAKRGQID 744
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1153 FTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTAPTarlnEQEETGRIIEMQRLEIQRLRDQIQEQE 1222
Cdd:pfam15921 745 ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVAT----EKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
685-1055 |
2.84e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.80 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 685 EEVLVTKTDMEEKAQVMLELKTRVEELKmENEYQLRLKDMNYSEKIKELTDKfIQEMESLKTKNQVLRTEKE-------- 756
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEER-IKELEEKEERLEELKKKLKelekrlee 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 757 -KQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLleyEKYQELQLKSQRMQEEYEK------QLRDNDETKSQALEEL-- 827
Cdd:PRK03918 357 lEERHELYEEAKAKKEELERLKKRLTGLTPEKLE---KELEELEKAKEEIEEEISKitarigELKKEIKELKKAIEELkk 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 828 ------------TEFYEAKLQEKTTLleeaqedvrqQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKE--SNLRLK 893
Cdd:PRK03918 434 akgkcpvcgrelTEEHRKELLEEYTA----------ELKRIEKELKEIEEKE-RKLRKELRELEKVLKKESEliKLKELA 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 894 GETGIMRKKFSSLQKE-IEERTNDIETLKGEQMKLQGVIKSLEKDI---QGLKREIQERDETIQDKEKRIYDLKKKNQEL 969
Cdd:PRK03918 503 EQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELeklEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 970 GkFKFV--LDYKIKEL-------------KKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQ 1034
Cdd:PRK03918 583 G-FESVeeLEERLKELepfyneylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY 661
|
410 420
....*....|....*....|...
gi 767902630 1035 EMRRER--QKERDLEALVKRFKT 1055
Cdd:PRK03918 662 EELREEylELSRELAGLRAELEE 684
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
670-1170 |
3.16e-14 |
|
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: 77.84 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 670 KDGRGIKREReVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEyQLRLKdmnYSEKIKELTDkFIQEMESLKTKNQ 749
Cdd:pfam05483 85 KEAEKIKKWK-VSIEAELKQKENKLQENRKIIEAQRKAIQELQFENE-KVSLK---LEEEIQENKD-LIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 750 VLRT----EKEKQDVYHHEHIE------DL---LDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDN 816
Cdd:pfam05483 159 LLKEtcarSAEKTKKYEYEREEtrqvymDLnnnIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 817 DETKSQALEELTEfYEAKLQEKTTLLEEAQEDVRQ---QLREFEETKKQIEEDED---REIQDIK--------------- 875
Cdd:pfam05483 239 EKQVSLLLIQITE-KENKMKDLTFLLEESRDKANQleeKTKLQDENLKELIEKKDhltKELEDIKmslqrsmstqkalee 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 876 -----TKYEKKLRDEKESNLRlkgETGIMRKKFSSLQKEIEERTNDIETL-KGEQMKLQG---VIKSLEKDIQGLKREIQ 946
Cdd:pfam05483 318 dlqiaTKTICQLTEEKEAQME---ELNKAKAAHSFVVTEFEATTCSLEELlRTEQQRLEKnedQLKIITMELQKKSSELE 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 947 ERDETIQDKEKRIYDLKK----------KNQELGKFKFVLDYKIKELKKQIEPRENEIRVMK--------------EQIQ 1002
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKilaedeklldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqltaiktseehylKEVE 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1003 EMEAELENFHKQNTQLELNITELwqklratDQEMRRERQKERDLEALVKRFKTDLHNCVAyiQEPRLLKEkVRGLFEKYV 1082
Cdd:pfam05483 475 DLKTELEKEKLKNIELTAHCDKL-------LLENKELTQEASDMTLELKKHQEDIINCKK--QEERMLKQ-IENLEEKEM 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1083 QRADMVEiaglntDLQQEYTRQREHLERNLatlkKKVVKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLE 1162
Cdd:pfam05483 545 NLRDELE------SVREEFIQKGDEVKCKL----DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH 614
|
....*...
gi 767902630 1163 AALKLTKK 1170
Cdd:pfam05483 615 QENKALKK 622
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
726-1049 |
5.63e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 77.03 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 726 YSEKIKELTDkfiqEMESLKTKNQVLRTEKEkqdvyhheHIEDLLDKQSRELQDMEccnnqKLLLEYEKYQELQLKSQRM 805
Cdd:TIGR02169 672 EPAELQRLRE----RLEGLKRELSSLQSELR--------RIENRLDELSQELSDAS-----RKIGEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 806 QEEYEKQLRDNDETKSQALEEltefYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDE 885
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIEN----VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 886 KESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK 965
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 966 NQElgkfkfvLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL----WQKLRATDQEMRRERq 1041
Cdd:TIGR02169 891 RDE-------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipEEELSLEDVQAELQR- 962
|
....*...
gi 767902630 1042 KERDLEAL 1049
Cdd:TIGR02169 963 VEEEIRAL 970
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
690-1059 |
8.84e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 76.21 E-value: 8.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 690 TKTDMEEKAQVMLELKTRVEELKME-NEYQLRLKDMNySEKIKELTDKFIQEMESLKTKNQVLRTE---KEKQDVYHHEH 765
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQlNQLKSEISDLN-NQKEQDWNKELKSELKNQEKKLEEIQNQisqNNKIISQLNEQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 766 IEDLldkqSRELQDMECCNNQKLLLEYEKYQELQlKSQRMQEEYEKQLRdNDETKSQALEELTEFYEAKLQEKTTLLEEA 845
Cdd:TIGR04523 344 ISQL----KKELTNSESENSEKQRELEEKQNEIE-KLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 846 QEDVRQQLREFEETKKQIEEDED------REIQDIKTKYE--KKLRDEKESNLR-LKGETGIMRKKFSSLQKEIEERTND 916
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSeikdltNQDSVKELIIKnlDNTRESLETQLKvLSRSINKIKQNLEQKQKELKSKEKE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 917 IETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKK---------KNQELGKFKFVLDYKIKELKKQI 987
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQ 577
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902630 988 EPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHN 1059
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
788-1048 |
1.40e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 788 LLLEYEKYQElQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDE 867
Cdd:COG1196 230 LLLKLRELEA-ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 868 DReiqdiktkyekkLRDEKESNLRLKGETgimrkkfSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQE 947
Cdd:COG1196 309 ER------------RRELEERLEELEEEL-------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 948 RDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQ 1027
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260
....*....|....*....|.
gi 767902630 1028 KLRATDQEMRRERQKERDLEA 1048
Cdd:COG1196 450 EEAELEEEEEALLELLAELLE 470
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
725-1053 |
7.49e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 7.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 725 NYSEKIKELTDKfIQEMESLKTKNQVLRTEKEKQdvyhHEHIEDLLDKQSRELQDMEccnnQKLLLEYEKYQELQLKSQR 804
Cdd:TIGR02168 674 ERRREIEELEEK-IEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 805 mqeeYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLLEEAqEDVRQQLREfeetkkQIEEDEDR--EIQDIKTKYEKKL 882
Cdd:TIGR02168 745 ----LEERIAQLSKELTELEAEIEE-LEERLEEAEEELAEA-EAEIEELEA------QIEQLKEElkALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 883 RDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDL 962
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 963 KKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQ-NTQLELNITELWQKLRATDQEMRRERQ 1041
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARR 972
|
330
....*....|..
gi 767902630 1042 KERDLEALVKRF 1053
Cdd:TIGR02168 973 RLKRLENKIKEL 984
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
676-1066 |
9.05e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 9.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 676 KREREVGFAEEvLVTKTDMEEKAQvmlELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEK 755
Cdd:PTZ00121 1438 KKAEEAKKADE-AKKKAEEAKKAE---EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 756 EKQDVYHHEHIEDLLD-KQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAK 834
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 835 LQEKTTLLEEAQEDVRQQLREFEETKKQIEE-DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEER 913
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 914 TNDIETLKGEQmklqgviKSLEKDIQGLKREIQERDETIQDKeKRIYDLKKKNQELGKFKFVLDYKIKELKKQieprENE 993
Cdd:PTZ00121 1674 KKKAEEAKKAE-------EDEKKAAEALKKEAEEAKKAEELK-KKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEE 1741
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902630 994 IRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEalVKRFKTDLHNCVAYIQE 1066
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIE 1812
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
791-1054 |
1.11e-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: 72.79 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 791 EYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEeltefYEAKLQEKTTLLEEAQEDvRQQLREFEETKKQIEEDEDRE 870
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDE-----LSQELSDASRKIGEIEKE-IEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 871 IQDIktkyEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERtndietlkgEQMKLQGVIKSLEKDIQGLKREIQERDE 950
Cdd:TIGR02169 746 LSSL----EQEIENVKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 951 TIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLR 1030
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
250 260
....*....|....*....|....
gi 767902630 1031 ATDQEMRRERQKERDLEALVKRFK 1054
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKR 916
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
691-1222 |
1.64e-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: 72.08 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 691 KTDMEEKAQVMLELKTRVEELkmenEYQLRLKDMNYSEKIKELTDKfiqeMESLKTKNQVLRtEKEKQDVYHHEhIEDLL 770
Cdd:pfam05557 40 KRQLDRESDRNQELQKRIRLL----EKREAEAEEALREQAELNRLK----KKYLEALNKKLN-EKESQLADARE-VISCL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 771 DKQSRELQDMEccnnqkllleyeKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQE--- 847
Cdd:pfam05557 110 KNELSELRRQI------------QRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElef 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 848 DVRQQLREFEETKKQIEE-----DEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEErtndIETLKG 922
Cdd:pfam05557 178 EIQSQEQDSEIVKNSKSElaripELEKELERLR-EHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREE----AATLEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 923 EQMKLQGVIKSLEKDIQGLKREIQerdeTIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQ 1002
Cdd:pfam05557 253 EKEKLEQELQSWVKLAQDTGLNLR----SPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1003 EMEAELENFHKQNTQLELnitelwQKLRATdqemrrerqKERD-LEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKY 1081
Cdd:pfam05557 329 DLNKKLKRHKALVRRLQR------RVLLLT---------KERDgYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1082 VQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVvkegELHRTDYVRimQENVSLIKEINELRRELKFTRSQVYDL 1161
Cdd:pfam05557 394 AHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQE----SLADPSYSK--EEVDSLRRKLETLELERQRLREQKNEL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902630 1162 EAALKltkKVRPQEVSETEPSRDM-LSTAPTARLNEQeeTGRIIEMQRLEIQRLRDQIQEQE 1222
Cdd:pfam05557 468 EMELE---RRCLQGDYDPKKTKVLhLSMNPAAEAYQQ--RKNQLEKLQAEIERLKRLLKKLE 524
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
692-1010 |
2.00e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.59 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 692 TDMEEKAQVMLELKTRVEELKMENE-YQLRLKDMNYSEKIKELTDKFIQEMESLKTKN-QVLRTEKEKQDvyhhEHIEDL 769
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQsYKQEIKNLESQINDLESKIQNQEKLNQQKDEQiKKLQQEKELLE----KEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 770 LDKQSRELQDMECCNNQKLLLE--------YEKYQELQLKSqrMQEEYEKQLRDNDETKSQALEELTEFyeAKLQEKTTL 841
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKEliiknldnTRESLETQLKV--LSRSINKIKQNLEQKQKELKSKEKEL--KKLNEEKKE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 842 LEEAQEDVRQQLREFEETKKQIEEDE---DREIQDIKTKYEKKLRDEKESNLRlkgetgimrKKFSSLQKEIEERTNDIE 918
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEKkekESKISDLEDELNKDDFELKKENLE---------KEIDEKNKEIEELKQTQK 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 919 TLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMK 998
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
330
....*....|..
gi 767902630 999 EQIQEMEAELEN 1010
Cdd:TIGR04523 659 NKWPEIIKKIKE 670
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
691-1225 |
1.36e-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: 69.23 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 691 KTDMEEKAQVMLELKTRVEELK--MENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDV------YH 762
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKklIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLlyldylKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 763 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKyQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLL 842
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEK-LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 843 EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKgetgimrkkfssLQKEIEERTNDIETLKG 922
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL------------QEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 923 EQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVM--KEQ 1000
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1001 IQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRR--ERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLF 1078
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSqkESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1079 EKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDYVRImQENVSLIKEINELRRELKFTRSQV 1158
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV-LEIDPILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902630 1159 YDLEAA--LKLTKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQVT 1225
Cdd:pfam02463 621 RAKVVEgiLKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
807-1139 |
1.91e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 807 EEYEKQLRDNDETKSQ---ALEELTEFYEaKLQEKTTLLEEAQEdVRQQLREFEET----KKQIEEDEDREIQDIKTKYE 879
Cdd:TIGR02168 175 KETERKLERTRENLDRledILNELERQLK-SLERQAEKAERYKE-LKAELRELELAllvlRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 880 KKlRDEKESNLRLKGEtgimrkKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI 959
Cdd:TIGR02168 253 EE-LEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 960 YDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRE 1039
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1040 RQKERDLEALVKRFKTDLHNCVAYIQEPRlLKEKVRGLFEKyvqRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKV 1119
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEEL---EEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
330 340
....*....|....*....|.
gi 767902630 1120 VKEGELH-RTDYVRIMQENVS 1139
Cdd:TIGR02168 482 RELAQLQaRLDSLERLQENLE 502
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
794-1233 |
1.96e-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: 68.23 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 794 KYQELQLKSQRMQEEYE-KQLRDNDETKSQALEELTEFYEAKLQEKTTlleeaqedvRQQLREFEETKKQIEEDEDREIQ 872
Cdd:pfam05557 8 KARLSQLQNEKKQMELEhKRARIELEKKASALKRQLDRESDRNQELQK---------RIRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 873 DIKTKYEK---KLRDEKESNLRLKGETgimrkkFSSLQKEIEErtndietLKGEQMKLQGVIKSLEKDIQGLKREIQERD 949
Cdd:pfam05557 79 RLKKKYLEalnKKLNEKESQLADAREV------ISCLKNELSE-------LRRQIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 950 ETIQDKEKRIYDLKKKNQELGkfkfVLDYKIKELKKQIEPRENEIRVMK------EQIQEMEAELENFHKQNTQL-ELNI 1022
Cdd:pfam05557 146 AKASEAEQLRQNLEKQQSSLA----EAEQRIKELEFEIQSQEQDSEIVKnskselARIPELEKELERLREHNKHLnENIE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1023 TELWQKLRATDQEMRRERQKER-----DLEALVKRFKTDLHNCVAYIQEPRL---LKEKVRGLFEKYVQR--ADMVEIAG 1092
Cdd:pfam05557 222 NKLLLKEEVEDLKRKLEREEKYreeaaTLELEKEKLEQELQSWVKLAQDTGLnlrSPEDLSRRIEQLQQReiVLKEENSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1093 LNTDLQQEYTRQREhLERNLATLKKKVVKEG-ELHRTD-YVRIMQENVSLI-KEINELRRELKFTRSQVYDLEAALKLTK 1169
Cdd:pfam05557 302 LTSSARQLEKARRE-LEQELAQYLKKIEDLNkKLKRHKaLVRRLQRRVLLLtKERDGYRAILESYDKELTMSNYSPQLLE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1170 KVRP-----QEV---------------SETEPSRDMLSTA---------------PTARLNEQEETGRIIEMQRLEIQRL 1214
Cdd:pfam05557 381 RIEEaedmtQKMqahneemeaqlsvaeEELGGYKQQAQTLerelqalrqqesladPSYSKEEVDSLRRKLETLELERQRL 460
|
490
....*....|....*....
gi 767902630 1215 RDQIQEQEQVTGFHTLAGV 1233
Cdd:pfam05557 461 REQKNELEMELERRCLQGD 479
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
793-1122 |
2.38e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 793 EKYQELQLKsqrmQEEYEKQLRdndetkSQALEELtefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEdedreiq 872
Cdd:COG1196 213 ERYRELKEE----LKELEAELL------LLKLREL----EAELEELEAELEELEAELEELEAELAELEAELEE------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 873 diktkyekklrdekesnlrlkgetgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETI 952
Cdd:COG1196 272 --------------------------LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 953 QDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL-WQKLRA 1031
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELaAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1032 TDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRAdmvEIAGLNTDLQQEYTRQREHLERN 1111
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE---ALLELLAELLEEAALLEAALAEL 482
|
330
....*....|.
gi 767902630 1112 LATLKKKVVKE 1122
Cdd:COG1196 483 LEELAEAAARL 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-1021 |
8.32e-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: 66.62 E-value: 8.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 696 EKAQVMLELKTRVEELKMEnEYQLRLKDMNYS-EKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHIEDLLDKQS 774
Cdd:TIGR02168 210 EKAERYKELKAELRELELA-LLVLRLEELREElEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 775 R------ELQDMEccnNQKllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELtefyeAKLQEKTTLLEEAQED 848
Cdd:TIGR02168 289 ElyalanEISRLE---QQK-----QILRERLANLERQLEELEAQLEELESKLDELAEEL-----AELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 849 VRQQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETL--KGEQMK 926
Cdd:TIGR02168 356 LEAELEELEAELEELESRL-EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 927 LQGVIKSLEKDIQGLKrEIQERDETIQDKEKRIYDLKKKNQElgkfkfvldyKIKELKKQieprENEIRVMKEQIQEMEA 1006
Cdd:TIGR02168 435 LKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQ----------ALDAAERE----LAQLQARLDSLERLQE 499
|
330
....*....|....*
gi 767902630 1007 ELENFHKQNTQLELN 1021
Cdd:TIGR02168 500 NLEGFSEGVKALLKN 514
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
794-1117 |
8.90e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 66.74 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 794 KYQELQlKSQRMQEEYEKQLRDNDETKSQALEELTEFYEaKLQEKTTLLEEAQEdvrqqLREFEETKKQieededrEIQD 873
Cdd:pfam01576 10 KEEELQ-KVKERQQKAESELKELEKKHQQLCEEKNALQE-QLQAETELCAEAEE-----MRARLAARKQ-------ELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 874 IKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGL----------KR 943
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLedqnsklskeRK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 944 EIQER-------------------------DETIQDKEKRIYDLKKKNQELGKFKFVLD--------------YKIKELK 984
Cdd:pfam01576 156 LLEERiseftsnlaeeeekakslsklknkhEAMISDLEERLKKEEKGRQELEKAKRKLEgestdlqeqiaelqAQIAELR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 985 KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCV--- 1061
Cdd:pfam01576 236 AQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLdtt 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902630 1062 AYIQEPRLLKEKVRGLF------EKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKK 1117
Cdd:pfam01576 316 AAQQELRSKREQEVTELkkaleeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
699-1226 |
1.96e-10 |
|
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: 65.52 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 699 QVMLELKTRVEELKMENE--YQLRLKDMNYSEKIKELTDKFIQEMESLK-----------TKNQVLRT------------ 753
Cdd:pfam15921 110 QSVIDLQTKLQEMQMERDamADIRRRESQSQEDLRNQLQNTVHELEAAKclkedmledsnTQIEQLRKmmlshegvlqei 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 754 --------EKEKQDVYHHEHIEDL--------LDKQSRELQ--------------------DMECCNNQKLLLEYEKYQE 797
Cdd:pfam15921 190 rsilvdfeEASGKKIYEHDSMSTMhfrslgsaISKILRELDteisylkgrifpvedqlealKSESQNKIELLLQQHQDRI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 798 LQLKSQR---------------------------MQEE-------YEKQLRDNDETKSQALEELTE---FYEAKLQ--EK 838
Cdd:pfam15921 270 EQLISEHeveitgltekassarsqansiqsqleiIQEQarnqnsmYMRQLSDLESTVSQLRSELREakrMYEDKIEelEK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 839 TTLLEEAQ-EDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDI 917
Cdd:pfam15921 350 QLVLANSElTEARTERDQFSQESGNLDDQLQKLLADLH-KREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 918 EtlkgeqmKLQGVIKSLEKDIQGlkrEIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKEL---KKQIEPRENEI 994
Cdd:pfam15921 429 Q-------RLEALLKAMKSECQG---QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTV 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 995 RVMKEQIQEMEAELENFHKQNTQLELNITELWQKLratdQEMRRERQKERDLEALVKRFKTDLHNCVAYIQeprLLKEKV 1074
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL----QHLKNEGDHLRNVQTECEALKLQMAEKDKVIE---ILRQQI 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1075 RGLFEKYVQR-----ADMVEIAGLNTDLQ------QEYTRQREHLERNLATLKKKvVKEGELHRTDYVRIMQENVSLIKE 1143
Cdd:pfam15921 572 ENMTQLVGQHgrtagAMQVEKAQLEKEINdrrlelQEFKILKDKKDAKIRELEAR-VSDLELEKVKLVNAGSERLRAVKD 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1144 I----NELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIE-MQRLEIQRLRDQI 1218
Cdd:pfam15921 651 IkqerDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKsMEGSDGHAMKVAM 730
|
....*...
gi 767902630 1219 QEQEQVTG 1226
Cdd:pfam15921 731 GMQKQITA 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-1151 |
3.59e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 675 IKREREVGFAEEVLVTKTDMEEKAQVMLELKtRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTE 754
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 755 KEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQAleeltefYEAK 834
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA-------EEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 835 LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlrlkgetgimRKKFSSLQKEIEERT 914
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE------------KKKIAHLKKEEEKKA 1770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 915 NDIETLKgeqmklQGVIKslekdiQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfvldykikelkkqieprENEI 994
Cdd:PTZ00121 1771 EEIRKEK------EAVIE------EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK-------------------EGNL 1819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 995 RVMKEQIQEMEAELENFHKQNTQLElNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNcvayIQEPRLLKEKV 1074
Cdd:PTZ00121 1820 VINDSKEMEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE----IEEADEIEKID 1894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1075 RGLFEKYVQRADMveiAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELH------RTDYVRIMQENVSLIKEINELR 1148
Cdd:PTZ00121 1895 KDDIEREIPNNNM---AGKNNDIIDDKLDKDEYIKRDAEETREEIIKISKKDmcindfSSKFCDYMKDNISSGNCSDEER 1971
|
...
gi 767902630 1149 REL 1151
Cdd:PTZ00121 1972 KEL 1974
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
685-1049 |
5.47e-10 |
|
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: 63.98 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 685 EEVLVTKTDMEEKAQVMLELKTRVEElkmeneyQLRLKDMNYSE--KIKELTDKFIQEMESLKTKNQVLR---TEKE--K 757
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASLQE-------KERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRnvqTECEalK 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 758 QDVYHHEHIEDLLDKQSRELQDMECCNNQKL-LLEYEKYQ-ELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAkl 835
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTAgAMQVEKAQlEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL-- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 836 qEKTTLLEEAQEDVRQqLREFEETKKQI--EEDEDR-EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 912
Cdd:pfam15921 633 -EKVKLVNAGSERLRA-VKDIKQERDQLlnEVKTSRnELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 913 RTNDIETLKGEQ-------MKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKK 985
Cdd:pfam15921 711 TRNTLKSMEGSDghamkvaMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902630 986 QIEPRENEIRVMKEQIQEMEAELEnfhkqntQLELNITELWQKLRATDQE-MRRERQKERDLEAL 1049
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEVALD-------KASLQFAECQDIIQRQEQEsVRLKLQHTLDVKEL 848
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
863-1231 |
5.70e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 863 IEEDEDRE--------IQDIKTKYEKKLRDEKESNLRLKG-ETGIMRKkfSSLQKEIEERTNDIETLKGEQMKLQGVIKS 933
Cdd:PRK03918 141 LESDESREkvvrqilgLDDYENAYKNLGEVIKEIKRRIERlEKFIKRT--ENIEELIKEKEKELEEVLREINEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 934 LEKDIQGLKREIQERDETiqdKEKrIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEaELENFHK 1013
Cdd:PRK03918 219 LREELEKLEKEVKELEEL---KEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1014 QNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKrfktDLHNCVAYIQEprlLKEKVRGLFEKYvqrADMVEIAGL 1093
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEE---LKKKLKELEKRL---EELEERHEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1094 NTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAAlKLTKKVRP 1173
Cdd:PRK03918 364 YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA-KGKCPVCG 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1174 QEVSETEPSRDMLS-TAPTARL-NEQEETGRIIEMQRLEIQRLRDQIQEQEQVTGFHTLA 1231
Cdd:PRK03918 443 RELTEEHRKELLEEyTAELKRIeKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA 502
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
736-1223 |
6.34e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 736 KFIQEM--ESLKTKNQVLRTEKEKQDVYHHEHIEDLlDKQSRELQDmeccnnqklllEYEKYQELQLKSQRMQEEYE--K 811
Cdd:COG4717 41 AFIRAMllERLEKEADELFKPQGRKPELNLKELKEL-EEELKEAEE-----------KEEEYAELQEELEELEEELEelE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 812 QLRDNDETKSQALEELTEFYEA-----KLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDrEIQDIKTKYEKKLRDek 886
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLyqeleALEAELAELPERLEELEERLEELRELEEELEELEA-ELAELQEELEELLEQ-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 887 eSNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKD--IQGLKREIQERDET---------IQDK 955
Cdd:COG4717 186 -LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEleAAALEERLKEARLLlliaaallaLLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 956 EKRIYDLKKKNQELGK--------FKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQ 1027
Cdd:COG4717 265 GGSLLSLILTIAGVLFlvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1028 KLRATDQEMR--RERQKERDLEALVKRFKTDLHNCVAyiqeprllkekvrGLFEKYVQRADMVEIaglntdlQQEYTRQR 1105
Cdd:COG4717 345 RIEELQELLReaEELEEELQLEELEQEIAALLAEAGV-------------EDEEELRAALEQAEE-------YQELKEEL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1106 EHLERNLATLKKKVvkEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALkltkkvrpqevsetepsrdm 1185
Cdd:COG4717 405 EELEEQLEELLGEL--EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-------------------- 462
|
490 500 510
....*....|....*....|....*....|....*...
gi 767902630 1186 lstaptarlnEQEETGRIIEMQRLEIQRLRDQIQEQEQ 1223
Cdd:COG4717 463 ----------EQLEEDGELAELLQELEELKAELRELAE 490
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
728-1066 |
6.69e-10 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 63.44 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 728 EKIKELTDKFIQEMESLKTKN-QVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQ 806
Cdd:COG5185 159 GIIKDIFGKLTQELNQNLKKLeIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGF 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 807 EEYEKQLRDNDETK---SQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLR 883
Cdd:COG5185 239 QDPESELEDLAQTSdklEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 884 DEKESN-----LRLKGETGIMR------KKFSSLQKEIEERTNDIETLKGEQM--KLQGVIKSLEKDIQGLKREIQERDE 950
Cdd:COG5185 319 AAAEAEqeleeSKRETETGIQNltaeieQGQESLTENLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 951 TIQDKEKRIydlkkkNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELE-NFHKQNTQLELNITELWQKL 1029
Cdd:COG5185 399 NQRGYAQEI------LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNkVMREADEESQSRLEEAYDEI 472
|
330 340 350
....*....|....*....|....*....|....*...
gi 767902630 1030 RATDQEMRRERQKER-DLEALVKRFKTDLHNCVAYIQE 1066
Cdd:COG5185 473 NRSVRSKKEDLNEELtQIESRVSTLKATLEKLRAKLER 510
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
736-1223 |
8.06e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 736 KFIQEMESLKTKNQVLRTEKEKQDVYHHehIEDLLDKQSRELQDMEccnnqkllleyEKYQELQLKSQRMqeEYEKQLRD 815
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAE--LQEELEELEEELEELE-----------AELEELREELEKL--EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 816 NDETKSQALEELTEFYE--AKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEdedrEIQDIKTKYEKKLRDEKESNLRLK 893
Cdd:COG4717 130 LYQELEALEAELAELPErlEELEERLEELRELEEELEELEAELAELQEELEE----LLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 894 GETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQgVIKSLEK------------DIQGLKREIQERDETIQDKEKRIYD 961
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEarlllliaaallALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 962 LkkknqeLGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMR--RE 1039
Cdd:COG4717 285 L------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLReaEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1040 RQKERDLEALVKRFKTDLHNCVAyiqeprllkekvrGLFEKYVQRADMVEIaglntdlQQEYTRQREHLERNLATLKKKV 1119
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGV-------------EDEEELRAALEQAEE-------YQELKEELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1120 vkEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRpqEVSETEPSRDMLStaptARLNEQEE 1199
Cdd:COG4717 419 --EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG--ELAELLQELEELK----AELRELAE 490
|
490 500
....*....|....*....|....
gi 767902630 1200 TGRIIEMQRLEIQRLRDQIQEQEQ 1223
Cdd:COG4717 491 EWAALKLALELLEEAREEYREERL 514
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
807-1220 |
1.36e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 807 EEYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLlEEAQEDVRQQLREFEETKkqieEDEDREIQDIKTKYEKkLRDEK 886
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEE-HEERREELETL-EAEIEDLRETIAETERER----EELAEEVRDLRERLEE-LEEER 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 887 ESnlrLKGETGimrkkFSSLqkeieertnDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKN 966
Cdd:PRK02224 296 DD---LLAEAG-----LDDA---------DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 967 QELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENfhkQNTQLElNITELWQKLRATDQEMrreRQKERDL 1046
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD---APVDLG-NAEDFLEELREERDEL---REREAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1047 EAlvkrfktDLHNCVAYIQEPRLLKEK---------------VRGLFEKYVQRADmveiagLNTDLQQEYTrQREHLERN 1111
Cdd:PRK02224 432 EA-------TLRTARERVEEAEALLEAgkcpecgqpvegsphVETIEEDRERVEE------LEAELEDLEE-EVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1112 LATLKKKVVKEGELHRtdyvriMQENVSLIKE--------INELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSR 1183
Cdd:PRK02224 498 LERAEDLVEAEDRIER------LEERREDLEEliaerretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430
....*....|....*....|....*....|....*....
gi 767902630 1184 DMLSTAPTAR--LNEQEETGRIIEMQRLEIQRLRDQIQE 1220
Cdd:PRK02224 572 EEVAELNSKLaeLKERIESLERIRTLLAAIADAEDEIER 610
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
684-1163 |
1.66e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 684 AEEVLvtkTDMEEKAQVMLELKTRVEELKMENEYQLRLKDmNYSEKIKELTDkfiqEMESLKTKNQVLRTEKEKQDVyHH 763
Cdd:PRK02224 239 ADEVL---EEHEERREELETLEAEIEDLRETIAETERERE-ELAEEVRDLRE----RLEELEEERDDLLAEAGLDDA-DA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 764 EHIEDLLDKQSRELQDMEccnnqkllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQAlEELTEfyEAKLQEKTtlLE 843
Cdd:PRK02224 310 EAVEARREELEDRDEELR-----------DRLEECRVAAQAHNEEAESLREDADDLEERA-EELRE--EAAELESE--LE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 844 EAQEDVRQQLREFEETKKQIEEDEDReIQDIKTKYEK--KLRDEKESNL-RLKGETGIMRKKFSSLQK------------ 908
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRER-FGDAPVDLGNaeDFLEELREERdELREREAELEATLRTARErveeaealleag 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 909 ----------------EIEERTNDIETLKGEQMKLQGVIKSLEKDIqglkreiqERDETIQDKEKRIYDLKKKNQELGKf 972
Cdd:PRK02224 453 kcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERL--------ERAEDLVEAEDRIERLEERREDLEE- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 973 kfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQemRRERQKERdLEALvKR 1052
Cdd:PRK02224 524 ------LIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKER-IESL-ER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1053 FKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADMVE-----IAGLN--------TDLQQEYTRQREHLERNLATLKKKV 1119
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrerKRELEaefdeariEEAREDKERAEEYLEQVEEKLDELR 673
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 767902630 1120 VKEGELHRtdyvRI-MQENVslIKEINELRRELKFTRSQVYDLEA 1163
Cdd:PRK02224 674 EERDDLQA----EIgAVENE--LEELEELRERREALENRVEALEA 712
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
797-1081 |
1.70e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 60.69 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 797 ELQLKSQRMQEEYEkQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEdVRQQLREFEETKKQIEEDEDREIQDIKT 876
Cdd:COG1340 12 ELEEKIEELREEIE-ELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 877 KYEK--KLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIEtlkgEQMKLQGVIKSLEKDIQGLKREIQERDEtIQD 954
Cdd:COG1340 90 LREEldELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPE----EEKELVEKIKELEKELEKAKKALEKNEK-LKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 955 KEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQ 1034
Cdd:COG1340 165 LRAELKELRKEAEEIHK-------KIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767902630 1035 EMRRERQKERDLEALVKRFKTDlhncvayiQEPRLLKEKVRGLFEKY 1081
Cdd:COG1340 238 ELRELRKELKKLRKKQRALKRE--------KEKEELEEKAEEIFEKL 276
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
675-1185 |
2.98e-09 |
|
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: 61.60 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 675 IKREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQ------EMESLKTKN 748
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKElqqlegSSDRILELD 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 749 QVLRTE---------------KEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEyekyQELQLKSQRMQEEyeKQL 813
Cdd:TIGR00606 478 QELRKAerelskaeknsltetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT----QMEMLTKDKMDKD--EQI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 814 RDNDETKSQALEELTEFYEAKLQEKTTL---------LEEAQEDVRQQLREFEETKKQIEEDEDREIQDIkTKYEKKLRD 884
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYFPNKKQLEDWLhskskeinqTRDRLAKLNKELASLEQNKNHINNELESKEEQL-SSYEDKLFD 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 885 -----EKESNL-RLKGETGIMRKKFSSLQKEIEERTNDIETLKGE--------------QMKLQGVIKSLEKDIQGLKRE 944
Cdd:TIGR00606 631 vcgsqDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcqrvfqtEAELQEFISDLQSKLRLAPDK 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 945 IQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITE 1024
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTD 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1025 LwqklRATDQEMRRERQKERDLEALVKrfKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADmveiagLNTDLQQEYTRQ 1104
Cdd:TIGR00606 791 V----TIMERFQMELKDVERKIAQQAA--KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIE------LNRKLIQDQQEQ 858
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1105 REHLERNLATLKKKVVKEGE-LHRTDyvRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSR 1183
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTnLQRRQ--QFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN 936
|
..
gi 767902630 1184 DM 1185
Cdd:TIGR00606 937 KK 938
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
813-1055 |
4.80e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.80 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 813 LRDNDETKSQA-LEELTEFY-EAKLQEKTTLLEEAQEDVRQQLrefEETKKQIEEDEdREIQDIKTKYekklrdekeSNL 890
Cdd:COG3206 142 YTSPDPELAAAvANALAEAYlEQNLELRREEARKALEFLEEQL---PELRKELEEAE-AALEEFRQKN---------GLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 891 RLKGETGIMRKKFSSLQKEIEErtndietLKGEQMKLQGVIKSLEKDIQGLKREIQE--RDETIQDKEKRIYDLKKKNQE 968
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAE-------ARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 969 LGKfKFVLDY-KIKELKKQIEPRENEIRVMKEQI-QEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDL 1046
Cdd:COG3206 282 LSA-RYTPNHpDVIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
....*....
gi 767902630 1047 EALVKRFKT 1055
Cdd:COG3206 361 EVARELYES 369
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
677-1009 |
7.33e-09 |
|
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: 60.12 E-value: 7.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 677 REREVGFAE-EVLVTKTDMEEKAQVMLELKTRVEELKMENeyqlrLKDMNYSEKIKELTDKFIQEmeslkTKNQVLRTEK 755
Cdd:pfam05483 448 REKEIHDLEiQLTAIKTSEEHYLKEVEDLKTELEKEKLKN-----IELTAHCDKLLLENKELTQE-----ASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 756 EKQDVYHHEHIEDLLDKQSRELQdmeccnnqkllleyEKYQELQLKSQRMQEEYeKQLRDNDETKSQALEELTEFYEAKL 835
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLE--------------EKEMNLRDELESVREEF-IQKGDEVKCKLDKSEENARSIEYEV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 836 QEKTTLLEEAQEDVRQQLREFEETKKQIEE--DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSL----QKE 909
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEElhQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIidnyQKE 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 910 IEERTNDIETLKGEQMKLQGVIKS---LEKDIQG------------LKREIQERDETIQDKEKRIYDLKKKNQELGKFKF 974
Cdd:pfam05483 663 IEDKKISEEKLLEEVEKAKAIADEavkLQKEIDKrcqhkiaemvalMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKA 742
|
330 340 350
....*....|....*....|....*....|....*
gi 767902630 975 VLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELE 1009
Cdd:pfam05483 743 ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
900-1057 |
7.42e-09 |
|
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: 57.63 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIyDLKKKNQELGkfkfVLDYK 979
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-GNVRNNKEYE----ALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902630 980 IKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQK-ERDLEALVKRFKTDL 1057
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEElEAEREELAAKIPPEL 176
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
703-1114 |
7.48e-09 |
|
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: 60.45 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 703 ELKTRVEELKMENEYQLRLKDMNYSEkikelTDKFIQEMESLKTKNQVLRTE--KEKQDVyhhEHIEDLLDKQSRELQDM 780
Cdd:TIGR00606 713 STESELKKKEKRRDEMLGLAPGRQSI-----IDLKEKEIPELRNKLQKVNRDiqRLKNDI---EEQETLLGTIMPEEESA 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 781 ECCnnqklLLEYEKYQELQLKSQRMQEEYEKQLRDNDETksqaleELTEFYEAKLQEKttllEEAQEDVRQQLREFEETK 860
Cdd:TIGR00606 785 KVC-----LTDVTIMERFQMELKDVERKIAQQAAKLQGS------DLDRTVQQVNQEK----QEKQHELDTVVSKIELNR 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 861 KQIEeDEDREIQDIKTKYeKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQgviKSLEKDIQG 940
Cdd:TIGR00606 850 KLIQ-DQQEQIQHLKSKT-NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLE---TFLEKDQQE 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 941 LKREIQERDETIQDKEKRIYDLKKK-NQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLE 1019
Cdd:TIGR00606 925 KEELISSKETSNKKAQDKVNDIKEKvKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMR 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1020 LNITELWQKLR-ATDQEMRRERQKErdlealVKRFKTDLHNCVAYIQEPRLLKEKvrglfEKYVQRADMVEIAGLNTDL- 1097
Cdd:TIGR00606 1005 QDIDTQKIQERwLQDNLTLRKRENE------LKEVEEELKQHLKEMGQMQVLQMK-----QEHQKLEENIDLIKRNHVLa 1073
|
410 420
....*....|....*....|
gi 767902630 1098 ---QQEYTRQREHLERNLAT 1114
Cdd:TIGR00606 1074 lgrQKGYEKEIKHFKKELRE 1093
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
796-993 |
9.11e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 9.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 796 QELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIK 875
Cdd:COG4942 27 AELEQLQQEIAEL-EKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAELAELEKEIAELR-AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 876 TKYEKKLR--------------------DEKESNLR-LKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSL 934
Cdd:COG4942 104 EELAELLRalyrlgrqpplalllspedfLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902630 935 EKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENE 993
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
900-1057 |
9.35e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfVLDYK 979
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA---ELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 980 IKELKKQI-------------------EPRENEIRVM---------KEQIQEMEAELENFHKQNTQLELNITELWQKLRA 1031
Cdd:COG4942 103 KEELAELLralyrlgrqpplalllspeDFLDAVRRLQylkylaparREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180
....*....|....*....|....*.
gi 767902630 1032 TDQEMRRERQKERDLEALVKRFKTDL 1057
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKEL 208
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
695-1021 |
1.87e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 695 EEKAQVMLELKTRVEELkMENEYQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLRTEKEKqdvyhhEHIEDLLDKQS 774
Cdd:PRK03918 387 EKLEKELEELEKAKEEI-EEEISKITARIGELKKEIKEL-KKAIEELKKAKGKCPVCGRELTE------EHRKELLEEYT 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 775 RELQDMEccNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQ---ALEELTEFYEAKLQEKTTLLEEAQEDVRQ 851
Cdd:PRK03918 459 AELKRIE--KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkeLEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 852 QLREFEETKKQIEEDEdrEIQDIKTKYEKKLRDEKESNLRLKGEtgIMRKKFSSLqKEIEERTNDIETLKGEQMKLQGV- 930
Cdd:PRK03918 537 LKGEIKSLKKELEKLE--ELKKKLAELEKKLDELEEELAELLKE--LEELGFESV-EELEERLKELEPFYNEYLELKDAe 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 931 --IKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDY------------------------------ 978
Cdd:PRK03918 612 keLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYeelreeylelsrelaglraeleelekrree 691
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 767902630 979 ------KIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELN 1021
Cdd:PRK03918 692 ikktleKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
950-1166 |
2.76e-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: 57.47 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 950 ETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKL 1029
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1030 ratdqemrrERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGL-FEKYVQRADMVEIAGLNTDlQQEYTRQREHL 1108
Cdd:COG4942 100 ---------EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqYLKYLAPARREQAEELRAD-LAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902630 1109 ERNLATLkKKVVKEGELHRTDYVRIMQENVSLI----KEINELRRELKFTRSQVYDLEAALK 1166
Cdd:COG4942 170 EAERAEL-EALLAELEEERAALEALKAERQKLLarleKELAELAAELAELQQEAEELEALIA 230
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
707-1223 |
5.18e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 707 RVEELKMENEYQLRLKDMNysEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHhEHIEDLLDKQSRELQDMECCNNQ 786
Cdd:TIGR02168 325 LEELESKLDELAEELAELE--EKLEELKEELESLEAELEELEAELEELESRLEELE-EQLETLRSKVAQLELQIASLNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 787 KLLLEYEKyQELQLKSQRMQEEYEKQLRDNDETKSQALE---ELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQI 863
Cdd:TIGR02168 402 IERLEARL-ERLEDRRERLQQEIEELLKKLEEAELKELQaelEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 864 EEDEDR------EIQDIKTKYEKKLRDEKE---SNLRLKGETGIMRKKFS---SLQKEIE----ERTNDIETlKGEQMKL 927
Cdd:TIGR02168 481 ERELAQlqarldSLERLQENLEGFSEGVKAllkNQSGLSGILGVLSELISvdeGYEAAIEaalgGRLQAVVV-ENLNAAK 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 928 QGvIKSLEK-----------------DIQGLKREIQERDETIQDKEKRIY---------------------------DLK 963
Cdd:TIGR02168 560 KA-IAFLKQnelgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVkfdpklrkalsyllggvlvvddldnalELA 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 964 KKNQELGKFkFVLD------------------YKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNIT-- 1023
Cdd:TIGR02168 639 KKLRPGYRI-VTLDgdlvrpggvitggsaktnSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEql 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1024 -----ELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEkyvqrADMVEIAGLNTDLQ 1098
Cdd:TIGR02168 718 rkeleELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----EAEAEIEELEAQIE 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1099 QeYTRQREHLERNLATLKKKVvkegELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKvrpqEVSE 1178
Cdd:TIGR02168 793 Q-LKEELKALREALDELRAEL----TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA----EIEE 863
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 767902630 1179 TEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQ 1223
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
832-1222 |
5.37e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 832 EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReiqdiKTKYEkKLRDEKESNLRLKgetgimrkkfsSLQKEIE 911
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-----REALQ-RLAEYSWDEIDVA-----------SAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 912 ERTNDIETLKGEQmklqgviksleKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELgkfkfvldykikelkkqieprE 991
Cdd:COG4913 672 ELEAELERLDASS-----------DDLAALEEQLEELEAELEELEEELDELKGEIGRL---------------------E 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 992 NEIRVMKEQIQEMEAELENF-HKQNTQLELNITELWQKLRATdqemRRERQKERDLEALVKRFKTDLHNcvayiqeprlL 1070
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALGD----AVERELRENLEERIDALRARLNR----------A 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1071 KEKVRGLFEKYVQRADMvEIAGLNTDL------QQEYTR-QREHLERNLATLKKKVVKEGELHRTDYVRIMQENVSLIKE 1143
Cdd:COG4913 786 EEELERAMRAFNREWPA-ETADLDADLeslpeyLALLDRlEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKE 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1144 ----INELRRELKFTRSQVYDLEAalkltKKVRPQEVSETepsRDMLStapTARLNEQEETGRIIEMQRLEIQRLRDQIQ 1219
Cdd:COG4913 865 ridpLNDSLKRIPFGPGRYLRLEA-----RPRPDPEVREF---RQELR---AVTSGASLFDEELSEARFAALKRLIERLR 933
|
...
gi 767902630 1220 EQE 1222
Cdd:COG4913 934 SEE 936
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
676-1220 |
6.33e-08 |
|
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: 57.39 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 676 KREREVGFAEEVL--VTKTDMEEKAQVMLELKTRVEELKME--------NEYQLRLKDM-NYSEKIKELTDKFIQEMESL 744
Cdd:TIGR02169 262 ELEKRLEEIEQLLeeLNKKIKDLGEEEQLRVKEKIGELEAEiaslersiAEKERELEDAeERLAKLEAEIDKLLAEIEEL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 745 KTKNQVLRTEKEK-QDVYhhEHIEDLLDKQSRELQDMECcNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQA 823
Cdd:TIGR02169 342 EREIEEERKRRDKlTEEY--AELKEELEDLRAELEEVDK-EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 824 LEELTEFY------EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEeDEDREIQDIKTKY---EKKLRDEKESNLRLKG 894
Cdd:TIGR02169 419 SEELADLNaaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLS-KYEQELYDLKEEYdrvEKELSKLQRELAEAEA 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 895 ETGIMRKK---FSSLQKEIEERTNDIETLKGEQMK----------------LQGVIKSLEKD----IQGLKRE------- 944
Cdd:TIGR02169 498 QARASEERvrgGRAVEEVLKASIQGVHGTVAQLGSvgeryataievaagnrLNNVVVEDDAVakeaIELLKRRkagratf 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 945 -------IQERDETIQDKEKRI--------YDLKKKN-------------------QELGKFKFV--------------- 975
Cdd:TIGR02169 578 lplnkmrDERRDLSILSEDGVIgfavdlveFDPKYEPafkyvfgdtlvvedieaarRLMGKYRMVtlegelfeksgamtg 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 976 ---------------------LDYKIKELKKQ----------IEPRENE----IRVMKEQIQEMEAELENFHKQNTQLEL 1020
Cdd:TIGR02169 658 gsraprggilfsrsepaelqrLRERLEGLKRElsslqselrrIENRLDElsqeLSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1021 NITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEP--RLLKEKVRGLFEKY-VQRADMVEIAGLNTDL 1097
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELsKLEEEVSRIEARLREI 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1098 QQEYtrQREHLERNLATLKKKVVKEGELHRTDY-VRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQ-- 1174
Cdd:TIGR02169 818 EQKL--NRLTLEKEYLEKEIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEle 895
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 767902630 1175 -EVSETEPSRDMLSTA---PTARLNEQEETGRIIEMQRLEIQRLRDQIQE 1220
Cdd:TIGR02169 896 aQLRELERKIEELEAQiekKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
703-1178 |
8.65e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 703 ELKTRVEELKmeneyQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLRTEKEK--QDVYHHEHIEDLLDKQsRELQDM 780
Cdd:COG4717 72 ELKELEEELK-----EAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKleKLLQLLPLYQELEALE-AELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 781 EccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEdVRQQLREFEETK 860
Cdd:COG4717 145 P--------ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE-LQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 861 KQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVI-KSLEKDIQ 939
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLaLLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 940 GLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEpRENEIRVMKEQIQEMEAELenfhkQNTQLE 1019
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD-RIEELQELLREAEELEEEL-----QLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1020 LNITELWQKLRATDQEMRRERQKE-RDLEALVKRFktdlhncvayiqepRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQ 1098
Cdd:COG4717 370 QEIAALLAEAGVEDEEELRAALEQaEEYQELKEEL--------------EELEEQLEELLGELEELLEALDEEELEEELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1099 Q------EYTRQREHLERNLATLKKKVvkEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVR 1172
Cdd:COG4717 436 EleeeleELEEELEELREELAELEAEL--EQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
....*.
gi 767902630 1173 PQEVSE 1178
Cdd:COG4717 514 LPPVLE 519
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
833-990 |
1.11e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 833 AKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKL---RDEKESNlRLKGETGIMRKKFSSLQKE 909
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLgnvRNNKEYE-ALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 910 IEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDlkkknqelgkfkfvldyKIKELKKQIEP 989
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA-----------------EREELAAKIPP 174
|
.
gi 767902630 990 R 990
Cdd:COG1579 175 E 175
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
482-669 |
1.24e-07 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 55.69 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 482 GGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWNLSTGKRETECVLKSCSYNCVT 561
Cdd:COG2319 6 GAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 562 VSPDAKIIFAVGSDHTLK--EIADSLILREISAFDVTYTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQAHAG 639
Cdd:COG2319 86 FSPDGRLLASASADGTVRlwDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRL--WDLATGKLLRTLTGHSG 163
|
170 180 190
....*....|....*....|....*....|..
gi 767902630 640 PITkmLLTF--DDQFLLTAAEDGclfTWKVFD 669
Cdd:COG2319 164 AVT--SVAFspDGKLLASGSDDG---TVRLWD 190
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
816-1013 |
1.41e-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: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 816 NDETKSQALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEetkKQIEEDEDrEIQDIKTKYEKKLRDEKESnlrlkge 895
Cdd:cd22656 108 DDEELEEAKKTIKALLD-DLLKEAKKYQDKAAKVVDKLTDFE---NQTEKDQT-ALETLEKALKDLLTDEGGA------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 896 tgIMRKKFSSLQKEIEERTNDIetlkgeqmklqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKknqelgkfkfv 975
Cdd:cd22656 176 --IARKEIKDLQKELEKLNEEY-------------AAKLKAKIDELKALIADDEAKLAAALRLIADLTA----------- 229
|
170 180 190
....*....|....*....|....*....|....*...
gi 767902630 976 LDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHK 1013
Cdd:cd22656 230 ADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKD 267
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
803-1054 |
1.56e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 803 QRMQEEYekqLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQedvrQQLREFEETKKQIEEDEDREIqdiktkYEKKL 882
Cdd:COG3206 155 NALAEAY---LEQNLELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQKNGLVDLSEEAKL------LLQQL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 883 RDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQmklqgVIKSLEKDIQGLKREIQERDETIQDKEKRIYDL 962
Cdd:COG3206 222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 963 KKKNQELGKFKFvldykiKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLelnitelwQKLRATDQEMRRERQK 1042
Cdd:COG3206 297 RAQIAALRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL--------PELEAELRRLEREVEV 362
|
250
....*....|...
gi 767902630 1043 ERDL-EALVKRFK 1054
Cdd:COG3206 363 ARELyESLLQRLE 375
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
686-1118 |
1.90e-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: 55.57 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 686 EVLVTKTDMEEKAQVMLELKTRVEelKMENEYQLRLKdmnysekiKEltDKFIQEMESLKTKNQVLRTEKEKQDVYHHEH 765
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHE--AMISDLEERLK--------KE--EKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 766 IEDL---LDKQSRELQ------DMECCNNQKLLleyEKYQELQLKSQRMQE--EYEKQLRDNDETKSQALEELTEFYEAK 834
Cdd:pfam01576 231 IAELraqLAKKEEELQaalarlEEETAQKNNAL---KKIRELEAQISELQEdlESERAARNKAEKQRRDLGEELEALKTE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 835 LqEKTTLLEEAQEDVR-QQLREFEETKKQIEED---EDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEI 910
Cdd:pfam01576 308 L-EDTLDTTAAQQELRsKREQEVTELKKALEEEtrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 911 EERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPR 990
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 991 ENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLratDQEMRRERQKERDLEALV-------KRFKTDLHNCVAY 1063
Cdd:pfam01576 467 ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQL---EEEEEAKRNVERQLSTLQaqlsdmkKKLEEDAGTLEAL 543
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902630 1064 IQEPRLLKEKVRGLFEKYVQRADMVE-IAGLNTDLQQEY---TRQREHLERNLATLKKK 1118
Cdd:pfam01576 544 EEGKKRLQRELEALTQQLEEKAAAYDkLEKTKNRLQQELddlLVDLDHQRQLVSNLEKK 602
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
821-1052 |
2.56e-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: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 821 SQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIktkyEKKLRDekesnlrLKGETGIMR 900
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-RRIAAL----ARRIRA-------LEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 901 KKFSSLQKEIEERTNDIETLKGEqmkLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKI 980
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902630 981 KELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKR 1052
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
789-1028 |
3.55e-07 |
|
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: 53.66 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 789 LLEYEKYQELQLKSQRMQEEYEKQLRD------NDETKSQALEELTEFYEAKLQ----EKTTLLEEAQEdVRQQLREF-- 856
Cdd:pfam15905 58 SLELKKKSQKNLKESKDQKELEKEIRAlvqergEQDKRLQALEEELEKVEAKLNaavrEKTSLSASVAS-LEKQLLELtr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 857 -----------EETKKQIE-------------EDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 912
Cdd:pfam15905 137 vnellkakfseDGTQKKMSslsmelmklrnklEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 913 RTNDIETLKGEQMKLQGVIKSLEKdiqgLKREIQERDETiqdkekriydLKKKNQELGKFKFVLDYKIKELKKQIEPR-- 990
Cdd:pfam15905 217 EKSETEKLLEYITELSCVSEQVEK----YKLDIAQLEEL----------LKEKNDEIESLKQSLEEKEQELSKQIKDLne 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767902630 991 ---------ENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQK 1028
Cdd:pfam15905 283 kckllesekEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
766-1224 |
5.15e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.14 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 766 IEDLLDKQSRELQDMEccNNQKLLLEYEKYQELQLKS-QRMQEEYEKQLRDNDETKSQ-----ALEELTEFYEAKLQEKT 839
Cdd:PRK01156 185 IDYLEEKLKSSNLELE--NIKKQIADDEKSHSITLKEiERLSIEYNNAMDDYNNLKSAlnelsSLEDMKNRYESEIKTAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 840 TLLEEAQEDVrQQLREFEETKKQIEEDE---DREIQDIKTKYEKKLRDEKESNLRLKGETG----IMRK---------KF 903
Cdd:PRK01156 263 SDLSMELEKN-NYYKELEERHMKIINDPvykNRNYINDYFKYKNDIENKKQILSNIDAEINkyhaIIKKlsvlqkdynDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 904 SSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKdiqgLKREIQERDETIQDKEKRIYDLKKKN----QELGKFKFVLDYK 979
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIES----LKKKIEEYSKNIERMSAFISEILKIQeidpDAIKKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 980 IKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN------TQLELNITE------------LWQKLRATDQEMRRERQ 1041
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNhiinhynekksrLEEKIREIEIEVKDIDE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1042 KERDLEALvkrfktdlhncvayiqEPRLLKEKVRGLFEKYVQRADMVeiAGLNTDLQQEYTRQREHLERNLATLKKKVVK 1121
Cdd:PRK01156 498 KIVDLKKR----------------KEYLESEEINKSINEYNKIESAR--ADLEDIKIKINELKDKHDKYEEIKNRYKSLK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1122 EGELH--RTDYVRIMQEnVSLI------KEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTaptaR 1193
Cdd:PRK01156 560 LEDLDskRTSWLNALAV-ISLIdietnrSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNN----K 634
|
490 500 510
....*....|....*....|....*....|.
gi 767902630 1194 LNEQEETGRIIEMQRLEIQRLRDQIQEQEQV 1224
Cdd:PRK01156 635 YNEIQENKILIEKLRGKIDNYKKQIAEIDSI 665
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
891-1165 |
5.77e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.37 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 891 RLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELG 970
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 971 KFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFhkQNTQLELNITELWQKLRATDQEMRRERQKERDLEALV 1050
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1051 KRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDY 1130
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
250 260 270
....*....|....*....|....*....|....*
gi 767902630 1131 VRIMQENVSLIKEINELRRELKFTRSQVYDLEAAL 1165
Cdd:COG4372 287 ALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
712-1152 |
6.23e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.28 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 712 KMENEYQLRLK-----DMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKE------KQDVYHhEHIEDLLDKQSrelqdm 780
Cdd:TIGR00606 605 QNKNHINNELEskeeqLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQramlagATAVYS-QFITQLTDENQ------ 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 781 ECCNNQKLLLEYEK-YQELQLKSQRM-------QEEYEKQLRDNDETKSQALEeLTEFYEAKLQEKTTLLEEAQEDVRQQ 852
Cdd:TIGR00606 678 SCCPVCQRVFQTEAeLQEFISDLQSKlrlapdkLKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKV 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 853 LREFEETKKQIEEDEdreiqdiktKYEKKLRDEKESNLRLKGETGIMRKkfssLQKEIEERTNDIETLKGeqmKLQGVik 932
Cdd:TIGR00606 757 NRDIQRLKNDIEEQE---------TLLGTIMPEEESAKVCLTDVTIMER----FQMELKDVERKIAQQAA---KLQGS-- 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 933 SLEKDIQGLKREIQERDET--------------IQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMK 998
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHEldtvvskielnrklIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ 898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 999 EQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRllkekvrglf 1078
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK---------- 968
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902630 1079 EKYVQRADmVEIAGLNTDLqQEYTRQREHLERNLATLKKKVVKEGELHrtdyvRIMQENVSLIK---EINELRRELK 1152
Cdd:TIGR00606 969 DDYLKQKE-TELNTVNAQL-EECEKHQEKINEDMRLMRQDIDTQKIQE-----RWLQDNLTLRKrenELKEVEEELK 1038
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
797-1075 |
7.70e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 53.36 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 797 ELQLKSQRMQEEYeKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEaQEDVRQQLREFEEtkkqieededreiqDIKT 876
Cdd:pfam07888 77 ELESRVAELKEEL-RQSREKHEELEEKYKELSASSEELSEEKDALLAQ-RAAHEARIRELEE--------------DIKT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 877 KYEKKLrdEKESNL-RLKGETgimrKKFSSLQKEIEErtnDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDK 955
Cdd:pfam07888 141 LTQRVL--ERETELeRMKERA----KKAGAQRKEEEA---ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 956 EKRIYDLKKKNQELGKFKFVLDYKIKELK----------KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL 1025
Cdd:pfam07888 212 QDTITTLTQKLTTAHRKEAENEALLEELRslqerlnaseRKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADA 291
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1026 ----------WQKLRATdqeMRRERQKERDleaLVKRFKTDLHNCVAYIQEPRLLKEKVR 1075
Cdd:pfam07888 292 slalregrarWAQERET---LQQSAEADKD---RIEKLSAELQRLEERLQEERMEREKLE 345
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
818-1054 |
7.86e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 818 ETKSQALEELTEFYeAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED-----REIQDIktkyEKKLRDEKESNLRL 892
Cdd:COG4913 613 AALEAELAELEEEL-AEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAEL----EAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 893 KGetgimrkkfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI-----YDLKKKNQ 967
Cdd:COG4913 688 AA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 968 ELGKFKFVldykiKELKKQIeprENEIRVMKEQIQEMEAELEN-FHKQNTQLELNITELWQKLRATDQ-EMRRERQKERD 1045
Cdd:COG4913 757 AALGDAVE-----RELRENL---EERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLESLPEyLALLDRLEEDG 828
|
....*....
gi 767902630 1046 LEALVKRFK 1054
Cdd:COG4913 829 LPEYEERFK 837
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
832-1075 |
1.55e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 832 EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEK--KLRDEKESNLRLKGEtgiMRKKFSSLQKE 909
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEaqELREKRDELNEKVKE---LKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 910 IEERTNDIETLKGEQMKLQGV---IKSLEKDIQGLKREIQERDETIqDKEKRIYD-LKKKNQELGKFKFVLDY--KIKEL 983
Cdd:COG1340 87 LNELREELDELRKELAELNKAggsIDKLRKEIERLEWRQQTEVLSP-EEEKELVEkIKELEKELEKAKKALEKneKLKEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 984 KKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNcvaY 1063
Cdd:COG1340 166 RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE---L 242
|
250
....*....|..
gi 767902630 1064 IQEPRLLKEKVR 1075
Cdd:COG1340 243 RKELKKLRKKQR 254
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
501-540 |
1.59e-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: 1.59e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 767902630 501 SLENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 540
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
872-1093 |
1.62e-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: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 872 QDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDET 951
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 952 IQDKEKRIYDLKKKNQELGK---FKFVLD-------YKIKELKKQIEP-RENEIRVMKEQIQEMEAELENFHKQNTQLEL 1020
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRqppLALLLSpedfldaVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902630 1021 NITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLhncVAYIQEPRLLKEKVRGLFEKYVQRADMVEIAGL 1093
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
778-1041 |
1.66e-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: 52.43 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 778 QDMECCNNQKLLLEYEKYQELQ-LKSQRMQEEYEKQLRDNDetKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREF 856
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEkMEQERLRQEKEEKAREVE--RRRKLEEAEKARQAEMDRQAAIYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 857 EETKkqiEEDEDREIQDIKTK-----------YEKKLRDEKESNLRLKGETGIMRKKF---SSLQKEIEERTNDIETLKG 922
Cdd:pfam17380 351 ERIR---QEERKRELERIRQEeiameisrmreLERLQMERQQKNERVRQELEAARKVKileEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 923 EQ-----MKLQGVIKSLEKDIQGLKREIQERDETI----QDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENE 993
Cdd:pfam17380 428 EQeearqREVRRLEEERAREMERVRLEEQERQQQVerlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767902630 994 IRVMKEQIQEMEAELENfhKQNTQLELNITELWQKLRATDQEMRRERQ 1041
Cdd:pfam17380 508 MIEEERKRKLLEKEMEE--RQKAIYEEERRREAEEERRKQQEMEERRR 553
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
678-1223 |
2.18e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 678 EREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQlRLKDMNYSEKIKELTDKFIQEM----------ESLKTK 747
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-KAEDARKAEEARKAEDAKRVEIarkaedarkaEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 748 NQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQL-----KSQRMQEEYEKQLRDNDETKSQ 822
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkKAEEAKKDAEEAKKAEEERNNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 823 ALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIE---EDEDREIQDIKTKYEKKlrdEKESNLRLKGETGim 899
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakkAEEKKKADEAKKKAEEA---KKADEAKKKAEEA-- 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQErdetiqdKEKRIYDLKKKNQELgkfkfvldYK 979
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-------AKKKADAAKKKAEEK--------KK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 980 IKELKKQIEprenEIRVMKEQIQEMEAELENFHKQNTQLElnitelwQKLRAtdQEMRRERQKERDLEALVKRF--KTDL 1057
Cdd:PTZ00121 1393 ADEAKKKAE----EDKKKADELKKAAAAKKKADEAKKKAE-------EKKKA--DEAKKKAEEAKKADEAKKKAeeAKKA 1459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1058 HNCVAYIQEPRLLKEKVRGLFEKyvQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKvvkeGELHRTDYVRIMQEN 1137
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEA--KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA----EEAKKADEAKKAEEA 1533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1138 vsliKEINELRR-ELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDM-LSTAPTARLNEQEETGRIIEMQRLEIQRLR 1215
Cdd:PTZ00121 1534 ----KKADEAKKaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMaLRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
....*...
gi 767902630 1216 DQIQEQEQ 1223
Cdd:PTZ00121 1610 EEAKKAEE 1617
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
850-1010 |
2.35e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.70 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 850 RQQLREFEETKKQIEEDEDREIQDIKtkyEKKLRDEKESNLRLKGEtgimrkkfssLQKEIEERtndietlkgeqmklqg 929
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIK---KEALLEAKEEIHKLRNE----------FEKELRER---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 930 vikslEKDIQGLKREIQERDETIqdkEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEpreneirVMKEQIQEMEAELE 1009
Cdd:PRK12704 81 -----RNELQKLEKRLLQKEENL---DRKLELLEKREEELEKKEKELEQKQQELEKKEE-------ELEELIEEQLQELE 145
|
.
gi 767902630 1010 N 1010
Cdd:PRK12704 146 R 146
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
842-1006 |
2.40e-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: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 842 LEEAQEDVRQQLREFEETKKQIEEDEDREIQdikTKYEKKLRdekesnlrlkgetgimrkkfsslqkeieertndietlk 921
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEEREL---TEEEEEIR-------------------------------------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 922 geqmKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK-NQELGKFKFV--LDYKIKELKKQIEPRENEIRVMK 998
Cdd:COG2433 417 ----RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEeRREIRKDREIsrLDREIERLERELEEERERIEELK 492
|
....*...
gi 767902630 999 EQIQEMEA 1006
Cdd:COG2433 493 RKLERLKE 500
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
900-1048 |
3.29e-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: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 900 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIqdkEKRIYDLKKKNQELGKFKFVL--- 976
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGSVSYLDVLLgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 977 ---DY-------------------KIKELKKQIEPRENEIRVMKEQIQEMEAELEnfhKQNTQLELNITELWQKLRATDQ 1034
Cdd:COG3883 113 sfsDFldrlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELE---AAKAELEAQQAEQEALLAQLSA 189
|
170
....*....|....
gi 767902630 1035 EMRRERQKERDLEA 1048
Cdd:COG3883 190 EEAAAEAQLAELEA 203
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
691-1112 |
3.77e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.36 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 691 KTDMEEKAQVMLELKTRVEELKMENEyqlrlkdmNYSEKIKELTdkfiqemESLKTKNQ---VLRTEKEKQDVYHHEHiE 767
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQNS--------DCKQHIEVLK-------ESLTAKEQraaILQTEVDALRLRLEEK-E 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 768 DLLDKQSRELQDMeccNNQKLLLEYE-------------KYQELQLKSQRMQEeyekQLRDNDetksQALEELTEFYEAk 834
Cdd:pfam10174 359 SFLNKKTKQLQDL---TEEKSTLAGEirdlkdmldvkerKINVLQKKIENLQE----QLRDKD----KQLAGLKERVKS- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 835 LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREiqdiktkyEKKLRDEKESnlrLKGETGIMRKKFSSLQKEIEERT 914
Cdd:pfam10174 427 LQTDSSNTDTALTTLEEALSEKERIIERLKEQRERE--------DRERLEELES---LKKENKDLKEKVSALQPELTEKE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 915 NDIETLKGEQ-------MKLQGVIKSLEKDIQgLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQI 987
Cdd:pfam10174 496 SSLIDLKEHAsslassgLKKDSKLKSLEIAVE-QKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEES 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 988 EPRENEIRVMKEQIQEMEAELENFHKQNTQLELNI-------TELWQKLRATDQEMRRERQKERDleaLVKRFKTDLHNC 1060
Cdd:pfam10174 575 GKAQAEVERLLGILREVENEKNDKDKKIAELESLTlrqmkeqNKKVANIKHGQQEMKKKGAQLLE---EARRREDNLADN 651
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902630 1061 VAYIQEPRLLK--EKVRGLFEKYVQRADMVEIA-----GLNTDLQQEytrQREHLERNL 1112
Cdd:pfam10174 652 SQQLQLEELMGalEKTRQELDATKARLSSTQQSlaekdGHLTNLRAE---RRKQLEEIL 707
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
764-1052 |
6.15e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.74 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 764 EHIEDLLDKQSRElQDMECCNNQKLLLeyekyqelqlKSQRMQEEYEKQLRDNDETKSQALEELtefyeAKLQEKTTLLE 843
Cdd:TIGR00618 594 VRLQDLTEKLSEA-EDMLACEQHALLR----------KLQPEQDLQDVRLHLQQCSQELALKLT-----ALHALQLTLTQ 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 844 EAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKY----------EKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEER 913
Cdd:TIGR00618 658 ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkemlaqcQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 914 TNDIETLKGEQMKLQG-VIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPREN 992
Cdd:TIGR00618 738 EDALNQSLKELMHQARtVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 993 EIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKR 1052
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
763-1220 |
6.20e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.74 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 763 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQ------LKSQRMQEEYEKQLRDNDETKSQA--LEELTEFYEAK 834
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEkelkhlREALQQTQQSHAYLTQKREAQEEQlkKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 835 LQEKTTL---LEEAQEDV---RQQLREFEETKK--QIEEDEDREIQDIKTKYEK--KLRDEKESNLRLKGETGIMRKKFS 904
Cdd:TIGR00618 269 IEELRAQeavLEETQERInraRKAAPLAAHIKAvtQIEQQAQRIHTELQSKMRSraKLLMKRAAHVKQQSSIEEQRRLLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 905 SLQKEIE--ERTNDIETLKGEQMKLQgviKSLEKDIqglkREIQERDETIQDKEKRIYDLKKKNQelgkfkfvldykikE 982
Cdd:TIGR00618 349 TLHSQEIhiRDAHEVATSIREISCQQ---HTLTQHI----HTLQQQKTTLTQKLQSLCKELDILQ--------------R 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 983 LKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKT------- 1055
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlqetr 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1056 ----DLHNCVAYIQEPRLLKEKVRglfeKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGElHRTDY- 1130
Cdd:TIGR00618 488 kkavVLARLLELQEEPCPLCGSCI----HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK-QRASLk 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1131 ---VRIMQENVSLIKEINELRRELKFTRSQVYDL----EAALKLTKKVRPQ---EVSETEPSRDMLSTAPTARLNEQEET 1200
Cdd:TIGR00618 563 eqmQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqdltEKLSEAEDMLACEqhaLLRKLQPEQDLQDVRLHLQQCSQELA 642
|
490 500
....*....|....*....|
gi 767902630 1201 GRIIEMQRLEIQRLRDQIQE 1220
Cdd:TIGR00618 643 LKLTALHALQLTLTQERVRE 662
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
703-1226 |
7.61e-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: 50.43 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 703 ELKTRVEELKmeneyQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLR------TEKEKQDVYHHEHIE--DLLDKQS 774
Cdd:TIGR00606 249 PLKNRLKEIE-----HNLSKIMKLDNEIKAL-KSRKKQMEKDNSELELKMekvfqgTDEQLNDLYHNHQRTvrEKERELV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 775 RELQDMECCNNQKLLLEYEKYQ------ELQLKSQRMQEEYEKqlRDNDETKSQALEELTEFyeaklqekttlleEAQED 848
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTEllveqgRLQLQADRHQEHIRA--RDSLIQSLATRLELDGF-------------ERGPF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 849 VRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKES----NLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQ 924
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQadeiRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 925 MKLQGVIKsLEKDIQGLKREIQERDE--TIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQ 1002
Cdd:TIGR00606 468 GSSDRILE-LDQELRKAERELSKAEKnsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1003 EMEAELENFHKQNTQLE------LNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNcvaYIQEPRLLKEKVRG 1076
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTsllgyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNH---INNELESKEEQLSS 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1077 LFEKyvqradMVEIAGlNTDLQQEYTRQREHLER---NLATLKKKV------VKEGELHRTDYVRIMQENVSLIKEINEL 1147
Cdd:TIGR00606 624 YEDK------LFDVCG-SQDEESDLERLKEEIEKsskQRAMLAGATavysqfITQLTDENQSCCPVCQRVFQTEAELQEF 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1148 RRELK-FTRSQVYDLEAALKLTKKV--RPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMqrlEIQRLRDQIQEQEQV 1224
Cdd:TIGR00606 697 ISDLQsKLRLAPDKLKSTESELKKKekRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNR---DIQRLKNDIEEQETL 773
|
..
gi 767902630 1225 TG 1226
Cdd:TIGR00606 774 LG 775
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
882-1022 |
9.58e-06 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 49.20 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 882 LRDEKESNLRLKGEtgIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGV------IKSLEKDIQGLKREIQERDETIQDK 955
Cdd:pfam17060 96 IPASFISALELKED--VKSSPRSEADSLGTPIKVDLLRNLKPQESPETPrrinrkYKSLELRVESMKDELEFKDETIMEK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 956 E-------KRIYDLKKKNQELGK-FKFVLDYK-----------------IKELKKQIEPRENEIRVMKEQIQEMEAELEN 1010
Cdd:pfam17060 174 DrelteltSTISKLKDKYDFLSReFEFYKQHHehggnnsiktatkhefiISELKRKLQEQNRLIRILQEQIQFDPGALHD 253
|
170
....*....|..
gi 767902630 1011 FHKQNTQLELNI 1022
Cdd:pfam17060 254 NGPKNLVLNGAI 265
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
62-420 |
1.07e-05 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 49.52 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 62 ALSISPNRRYLAiseTVQEKPAITIYELSSIPCRKrkVLNNFDFQVQkfiSMAFSPDSKYLLAqTSppESNLVYwLWEKQ 141
Cdd:COG2319 125 SVAFSPDGKTLA---SGSADGTVRLWDLATGKLLR--TLTGHSGAVT---SVAFSPDGKLLAS-GS--DDGTVR-LWDLA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 142 KVMAIVRIDTQNNPVYQVSFSPqDNTQVcVTG--NGMFKLLRFAEGTLKQTSfqRGEPQNYLAHTWVADDK-IVVGTDTG 218
Cdd:COG2319 193 TGKLLRTLTGHTGAVRSVAFSP-DGKLL-ASGsaDGTVRLWDLATGKLLRTL--TGHSGSVRSVAFSPDGRlLASGSADG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 219 KLFLfesgdqrWETsimvkeptNGSKSLDVIQESESliefpPVSSplpsyeqmVAASSHSQMsmpqvfaiaayskgFACS 298
Cdd:COG2319 269 TVRL-------WDL--------ATGELLRTLTGHSG-----GVNS--------VAFSPDGKL--------------LASG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 299 AGPGRVLLFEkmeekdfYRESREIRIPVDPQSndpsqsdkqDVLCLCFSPSEETLVASTSKNqlysiTMSLTEISKGEPA 378
Cdd:COG2319 307 SDDGTVRLWD-------LATGKLLRTLTGHTG---------AVRSVAFSPDGKTLASGSDDG-----TVRLWDLATGELL 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 767902630 379 HFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWNYET 420
Cdd:COG2319 366 RT----LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
728-1099 |
1.08e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.83 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 728 EKIKELTDKFIQEMESLKTKNQVLRTEkekqdvyhhehIEDLLDKQsRELQdmeccnnQKLLLEYEKYQELqlksqrmQE 807
Cdd:PRK04778 115 DLIEEDIEQILEELQELLESEEKNREE-----------VEQLKDLY-RELR-------KSLLANRFSFGPA-------LD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 808 EYEKQLrDNDETKSQALEELTE---FYEA-----KLQEKTTLLEEAQEDVRQQLREFEETKKQieededrEIQDIKTKYe 879
Cdd:PRK04778 169 ELEKQL-ENLEEEFSQFVELTEsgdYVEAreildQLEEELAALEQIMEEIPELLKELQTELPD-------QLQELKAGY- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 880 kklRDEKESNLRLKgETGIMrKKFSSLQKEIEERTNDIETLKGEQMKLQgvIKSLEKDIQGL----------KREIQERD 949
Cdd:PRK04778 240 ---RELVEEGYHLD-HLDIE-KEIQDLKEQIDENLALLEELDLDEAEEK--NEEIQERIDQLydilerevkaRKYVEKNS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 950 ETIQDKEKRiydLKKKNQELG------KFKFVLDYKIKELKKQIEPRENEIRVMKEQIQ-----------EMEAELENFH 1012
Cdd:PRK04778 313 DTLPDFLEH---AKEQNKELKeeidrvKQSYTLNESELESVRQLEKQLESLEKQYDEITeriaeqeiaysELQEELEEIL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1013 KQNTQLELNITELWQKLRATdqemrreRQKERDLEALVKRFKTDLHNCVAYIQeprllKEKVRGLFEKYVQRADMV--EI 1090
Cdd:PRK04778 390 KQLEEIEKEQEKLSEMLQGL-------RKDELEAREKLERYRNKLHEIKRYLE-----KSNLPGLPEDYLEMFFEVsdEI 457
|
....*....
gi 767902630 1091 AGLNTDLQQ 1099
Cdd:PRK04778 458 EALAEELEE 466
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
673-973 |
1.10e-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: 49.74 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 673 RGIKREREVGFAEEVlvTKTDMEEKAQVMLELktrvEELKMENEYQLrlkdmnysEKIKEltdkfiqemESLKTKNQVLR 752
Cdd:pfam17380 310 REVERRRKLEEAEKA--RQAEMDRQAAIYAEQ----ERMAMEREREL--------ERIRQ---------EERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 753 TEKEKQDVYHHEHIEDLL----DKQSRELQDMECCNNQKLLLEyekyqELQLKSQRMQEEYEKQLRDNDETKSQALEELT 828
Cdd:pfam17380 367 QEEIAMEISRMRELERLQmerqQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQIRAEQEEARQREVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 829 EFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQ--IEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKkfsSL 906
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKklELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK---LL 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902630 907 QKEIEERTNDIetLKGEQMKLQGVIKSLEKDIQGlKREIQERDETIQDKEKRIYDLKKKNQELGKFK 973
Cdd:pfam17380 519 EKEMEERQKAI--YEEERRREAEEERRKQQEMEE-RRRIQEQMRKATEERSRLEAMEREREMMRQIV 582
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
709-949 |
1.94e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 709 EELKMENEYQLRLKDMNySEKIKELTDKF---IQEMESLKT-----KNQVLRTEKEKQDVyhHEHIEDLLDKQSRELQDM 780
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKN-GENIARKQNKYdelVEEAKTIKAeieelTDELLNLVMDIEDP--SAALNKLNTAAAKIKSKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 781 ECCnnQKLLLEYEKYQELQLKSQrmqeeyekQLRDNDETKSQALEELTEfyeakLQEKTTLLEEAQEDVRQQLREFEETK 860
Cdd:PHA02562 272 EQF--QKVIKMYEKGGVCPTCTQ--------QISEGPDRITKIKDKLKE-----LQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 861 KqieededrEIQDIKTKYEKKLRDekesnlrLKGEtgimRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQG 940
Cdd:PHA02562 337 K--------KLLELKNKISTNKQS-------LITL----VDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
....*....
gi 767902630 941 LKREIQERD 949
Cdd:PHA02562 398 LVKEKYHRG 406
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
849-1225 |
1.96e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 849 VRQQLREFEETKKQIEEDEDrEIQDIKTKYEKKLRDEKESNLRLKgetgIMRKKFSSLQKEIEERTNDIETLKGEQMKLQ 928
Cdd:TIGR04523 35 EKQLEKKLKTIKNELKNKEK-ELKNLDKNLNKDEEKINNSNNKIK----ILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 929 GVIKS-------LEKDIQGLKREIQERDETIQD-------KEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEI 994
Cdd:TIGR04523 110 SEIKNdkeqknkLEVELNKLEKQKKENKKNIDKflteikkKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 995 RVMKEQI-----------------QEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDL 1057
Cdd:TIGR04523 190 DKIKNKLlklelllsnlkkkiqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1058 HNCVAYI-QEPRLLKEKvrglfEKYVQRADMvEIAGLNTDLQQEYTRQrehLERNLATLKKKVvkegELHRTDYVRIMQE 1136
Cdd:TIGR04523 270 SEKQKELeQNNKKIKEL-----EKQLNQLKS-EISDLNNQKEQDWNKE---LKSELKNQEKKL----EEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1137 NVSLIKEINELRRELKFTRSQvyDLEAALKLTKKVRPQEVSEtepsrdmlstaptarlNEQEETGRIIEMQRLEIQRLRD 1216
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESE--NSEKQRELEEKQNEIEKLK----------------KENQSYKQEIKNLESQINDLES 398
|
....*....
gi 767902630 1217 QIQEQEQVT 1225
Cdd:TIGR04523 399 KIQNQEKLN 407
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
728-1188 |
2.01e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 728 EKIKELTDKFIQEMESLKTKNQVLRTEKEKQdvyhhEHIEDLLdkQSRELQdMECcnnqkllleyekyqelqlkSQRMQE 807
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKA-----CEIRDQI--TSKEAQ-LES-------------------SREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 808 EYEKQLRDNDETKSQALEELTEFYeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE 887
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIM--KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKER 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 888 SNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQ----ERDETIQDKEKRIYDLK 963
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfERGPFSERQIKNFHTLV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 964 KKNQElGKFKFV----LDYKIKELKKQIEPRENEIRvMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRE 1039
Cdd:TIGR00606 400 IERQE-DEAKTAaqlcADLQSKERLKQEQADEIRDE-KKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELD 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1040 ---RQKERDLEALVKRFKTD-LHNCVAYIQEPRL-LKEKVRGLFEKYVQRadmveiaglntDLQQEYTRQREHLERNLAT 1114
Cdd:TIGR00606 478 qelRKAERELSKAEKNSLTEtLKKEVKSLQNEKAdLDRKLRKLDQEMEQL-----------NHHTTTRTQMEMLTKDKMD 546
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902630 1115 LKKKVVKEGELHRTDYVRIMQE---NVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLST 1188
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS 623
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
503-540 |
2.34e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 42.33 E-value: 2.34e-05
10 20 30
....*....|....*....|....*....|....*...
gi 767902630 503 ENISSLKGHTGKIRSIVWNADDSKLISGGTDGAVYEWN 540
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
900-1055 |
2.51e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.70 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 900 RKKFSSLQKEIEERTnDIETLKGEQMK---LQGVIKSLEKDIQGLKREIQERDET-----IQDKEKRIYDLKKKNQELGK 971
Cdd:COG2433 349 KNKFERVEKKVPPDV-DRDEVKARVIRglsIEEALEELIEKELPEEEPEAEREKEheereLTEEEEEIRRLEEQVERLEA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 972 FKFVLDYKIKELKKQIEPRENEIRVMKEQIQE---MEAELENFHKQNTQLElnitelwqklratdQEMRRERQKERDLEA 1048
Cdd:COG2433 428 EVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDREIERLE--------------RELEEERERIEELKR 493
|
....*..
gi 767902630 1049 LVKRFKT 1055
Cdd:COG2433 494 KLERLKE 500
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
833-1059 |
2.61e-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: 48.31 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 833 AKLQEKTTLLEEAQEDVRQQLREFEETKKQiEEDEDREIQDIKTKYEKkLRDEKESNlrlkgetgimRKKFSSLQKEIEE 912
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLES-EEKNREEVEELKDKYRE-LRKTLLAN----------RFSYGPAIDELEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 913 RTNDIE---------TLKGEQMKLQGVIKSLEKDIQGLKR---EIQERDETIQDK-EKRIYDLKKKNQELGKFKFVLDY- 978
Cdd:pfam06160 154 QLAEIEeefsqfeelTESGDYLEAREVLEKLEEETDALEElmeDIPPLYEELKTElPDQLEELKEGYREMEEEGYALEHl 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 979 ----KIKELKKQIEPR------------ENEIRVMKEQIQE----MEAELENFH-----------------KQNTQLELN 1021
Cdd:pfam06160 234 nvdkEIQQLEEQLEENlallenleldeaEEALEEIEERIDQlydlLEKEVDAKKyveknlpeiedylehaeEQNKELKEE 313
|
250 260 270
....*....|....*....|....*....|....*...
gi 767902630 1022 ITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHN 1059
Cdd:pfam06160 314 LERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVER 351
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
806-1032 |
2.78e-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: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 806 QEEYEKQLRDNDETKSQALEELtefyeAKLQEKttlLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYEKKlRDE 885
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAEL-----DALQAE---LEELNEEYNELQAELEALQAEIDKLQ-AEIAEAEAEIEER-REE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 886 KESNLRLKGETGIMRKKFSSL--QKEIEERTNDIETLKgeqmKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 963
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLlgSESFSDFLDRLSALS----KIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902630 964 KKNQElgkfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRAT 1032
Cdd:COG3883 164 AELEA----------AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
986-1223 |
2.79e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 986 QIEPRENEIRVmkEQIQEMEAELENFhkqNTQLEL-----NITELWQKLRATDQEMRRERQKERDLEALVKRFK------ 1054
Cdd:COG3206 60 LVEPQSSDVLL--SGLSSLSASDSPL---ETQIEIlksrpVLERVVDKLNLDEDPLGEEASREAAIERLRKNLTvepvkg 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1055 TDLHNcVAYI-QEPRLLKEKVRGLFEKYVQRadmveiaglNTDLQQEYTRQ-REHLERNLATLKKKVVK-EGELH----R 1127
Cdd:COG3206 135 SNVIE-ISYTsPDPELAAAVANALAEAYLEQ---------NLELRREEARKaLEFLEEQLPELRKELEEaEAALEefrqK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1128 TDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALK-LTKKVRPQEVSETEPSRDMLSTAPTARLNEQEetGRIIEM 1206
Cdd:COG3206 205 NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAaLRAQLGSGPDALPELLQSPVIQQLRAQLAELE--AELAEL 282
|
250 260
....*....|....*....|...
gi 767902630 1207 QRL------EIQRLRDQIQEQEQ 1223
Cdd:COG3206 283 SARytpnhpDVIALRAQIAALRA 305
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
858-1031 |
2.98e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 858 ETKKQIEEDEDREIQ-DIKTKyEKKLRD-EKESNLRlkgetgimRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLE 935
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKnELKNK-EKELKNlDKNLNKD--------EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 936 KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN 1015
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170
....*....|....*.
gi 767902630 1016 TQLELNITELWQKLRA 1031
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLK 198
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
701-1127 |
3.15e-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: 48.40 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 701 MLELKTR----VEELKMENEyqlrlKDMNYSEKIkeltDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedlLDKQSRE 776
Cdd:pfam15818 2 LLDFKTSlleaLEELRMRRE-----AETQYEEQI----GKIIVETQELKWQKETLQNQKET------------LAKQHKE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 777 LqdMECCNNQkllleyekyqeLQLKSQRMQEEYEK-QLRDndETKSQALEELTEFYEAKLQEKTTL---LEEAQEDVRQQ 852
Cdd:pfam15818 61 A--MAVFKKQ-----------LQMKMCALEEEKGKyQLAT--EIKEKEIEGLKETLKALQVSKYSLqkkVSEMEQKLQLH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 853 LREFEETKKQIEEDEdreiqdiktKYEKKLrdekesnlrlKGETGIMRKKFSSLQKEIEERtndIETLKgeqmKLQGVIK 932
Cdd:pfam15818 126 LLAKEDHHKQLNEIE---------KYYATI----------TGQFGLVKENHGKLEQNVQEA---IQLNK----RLSALNK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 933 SLEKDIQGLKREiqerdetiqdkekriydLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQeMEAEL---- 1008
Cdd:pfam15818 180 KQESEICSLKKE-----------------LKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLN-MELELnkki 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1009 --ENFHKQNTQLELNITelwqkLRATDQEMRRERQKERDLEALVKRFKtdlHNCVAYIQEPRLLKEKVRGLFEKYVQRAD 1086
Cdd:pfam15818 242 neEITHIQEEKQDIIIS-----FQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQREKVKENEEKFLNLQN 313
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 767902630 1087 MVEIAglntdlQQEYTRQREHLERNLATLKKKVVKEGELHR 1127
Cdd:pfam15818 314 EHEKA------LGTWKKHVEELNGEINEIKNELSSLKETHI 348
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
877-1161 |
3.37e-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: 48.30 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 877 KYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIeerTNDIETLKGEQMKLQgvikSLEKDIQGLKREIQE-RDETIQDK 955
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKASREE---TFARTALKNARLDLR----RLFDEKQSEKDKKNKaLAERKDSA 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 956 EKRIYDLKKKnqelgkfKFVLDYKIKELKKQIEPRENEIRV-MKEQIQEMEAELENFHKQ-NTQLELNITELWQKLRATD 1033
Cdd:pfam12128 681 NERLNSLEAQ-------LKQLDKKHQAWLEEQKEQKREARTeKQAYWQVVEGALDAQLALlKAAIAARRSGAKAELKALE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1034 QEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLF----EKYVQRADMVEIAGLNT-----DLQQEYTRQ 1104
Cdd:pfam12128 754 TWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFdwyqETWLQRRPRLATQLSNIeraisELQQQLARL 833
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902630 1105 -------REHLERNLATLKKKVVKEGELHRTdyVRIMQENVSLIKE---INELRRELKFTRSQVYDL 1161
Cdd:pfam12128 834 iadtklrRAKLEMERKASEKQQVRLSENLRG--LRCEMSKLATLKEdanSEQAQGSIGERLAQLEDL 898
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
739-1000 |
4.03e-05 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 47.26 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 739 QEMESLKTKNQVLRTEKEKQDVYHHEHIE--DLLDKQSRELQ----DMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQ 812
Cdd:pfam09728 39 KDLKKLKKKQDQLQKEKDQLQSELSKAILakSKLEKLCRELQkqnkKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 813 LRDNDETKSQALEELTEFYE--AKLQEKTTLLEE------AQEDVRQQLRE------FEETKKQIEEDEDREIQDIKTKY 878
Cdd:pfam09728 119 MEEKSEKNNKLREENEELREklKSLIEQYELRELhfekllKTKELEVQLAEaklqqaTEEEEKKAQEKEVAKARELKAQV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 879 EKKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDetiqdkeKR 958
Cdd:pfam09728 199 QTLSETEKE----LREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSN-------KA 267
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767902630 959 IYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQ 1000
Cdd:pfam09728 268 LLEMAEERQKLKE-------ELEKLQKKLEKLENLCRALQAE 302
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
837-1122 |
4.18e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 48.29 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 837 EKTTLLEEAQEDVRQQLREFEETKKQIEE---DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIM-------------- 899
Cdd:PTZ00440 404 KYTNIISLSEHTLKAAEDVLKENSQKIADyalYSNLEIIEIKKKYDEKINELKKSINQLKTLISIMksfydliisekdsm 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 900 ------RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLE---KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELG 970
Cdd:PTZ00440 484 dskekkESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEdyyITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKR 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 971 KFKFVLDYKIKELKKQIEpRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKeRDLEALV 1050
Cdd:PTZ00440 564 SMKNDIKNKIKYIEENVD-HIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYK-GDLQELL 641
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902630 1051 KRFKTDLHNCVAYIQEPRlLKEKVRGLFEKYVQRADmvEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKE 1122
Cdd:PTZ00440 642 DELSHFLDDHKYLYHEAK-SKEDLQTLLNTSKNEYE--KLEFMKSDNIDNIIKNLKKELQNLLSLKENIIKK 710
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
791-1057 |
5.61e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.52 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 791 EYEKYQELQLKSQRmQEEYEKQLRDNDETKSQALEELTE-------------FYEAKLQEKTT--LLEEAQEDVRQQLRE 855
Cdd:PRK04778 49 ELEKVKKLNLTGQS-EEKFEEWRQKWDEIVTNSLPDIEEqlfeaeelndkfrFRKAKHEINEIesLLDLIEEDIEQILEE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 856 FEETKKQiEEDEDREIQDIKTKYEKkLRDEKESNlrlkgetgimRKKFSSLQKEIEERTNDIETL---------KGEQMK 926
Cdd:PRK04778 128 LQELLES-EEKNREEVEQLKDLYRE-LRKSLLAN----------RFSFGPALDELEKQLENLEEEfsqfvelteSGDYVE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 927 LQGVIKSLEKDIQGLKR---EIQERDETIQDK---------------------------EKRIYDLKKKNQE----LGKF 972
Cdd:PRK04778 196 AREILDQLEEELAALEQimeEIPELLKELQTElpdqlqelkagyrelveegyhldhldiEKEIQDLKEQIDEnlalLEEL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 973 KF-VLDYKIKELKKQI----EPRENEI---RVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKER 1044
Cdd:PRK04778 276 DLdEAEEKNEEIQERIdqlyDILEREVkarKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEK 355
|
330
....*....|...
gi 767902630 1045 DLEALVKRFKTDL 1057
Cdd:PRK04778 356 QLESLEKQYDEIT 368
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
764-960 |
5.74e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 764 EHIEDLLDKQS------------REL-QDMECCNNQKLLLE-----YEKYQELQLKS-----QRMQEEYEKQL---RDND 817
Cdd:PHA02562 154 KLVEDLLDISVlsemdklnkdkiRELnQQIQTLDMKIDHIQqqiktYNKNIEEQRKKngeniARKQNKYDELVeeaKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 818 ETKSQALEELTEF------YEAKLQEKTTLLEEAQEDVRQQLRE---FEE-----TKKQIEEDEDREIQDIKTK---YEK 880
Cdd:PHA02562 234 AEIEELTDELLNLvmdiedPSAALNKLNTAAAKIKSKIEQFQKVikmYEKggvcpTCTQQISEGPDRITKIKDKlkeLQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 881 KLRDEKESNLRLKG---ETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKD-------IQGLKREIQERDE 950
Cdd:PHA02562 314 SLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdnaeeLAKLQDELDKIVK 393
|
250
....*....|
gi 767902630 951 TIQDKEKRIY 960
Cdd:PHA02562 394 TKSELVKEKY 403
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
725-952 |
6.27e-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: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 725 NYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDvyHHEHIEDLLDKQSRELQdmeccnnqkllleyekyqELQLKSQR 804
Cdd:cd22656 80 NYAQNAGGTIDSYYAEILELIDDLADATDDEELEE--AKKTIKALLDDLLKEAK------------------KYQDKAAK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 805 MQEEYeKQLRDNDETKSQALEELTEFYEAKLQEKttLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKkLRD 884
Cdd:cd22656 140 VVDKL-TDFENQTEKDQTALETLEKALKDLLTDE--GGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIAD-DEA 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902630 885 EKESNLRLKGETGIMRKKFSSLQKEIEERTNDIEtlkgeqmKLQGVIKSLEKDIQGLKREIQERDETI 952
Cdd:cd22656 216 KLAAALRLIADLTAADTDLDNLLALIGPAIPALE-------KLQGAWQAIATDLDSLKDLLEDDISKI 276
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
695-1152 |
7.27e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.38 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 695 EEKAQVMLELK-----TRVEELKMENEYQLRLKDMNYSEKIKELTDKfiqEMESLKTKNQVLRTEKEKQDVyhHEHIEDL 769
Cdd:COG5022 902 LELESEIIELKkslssDLIENLEFKTELIARLKKLLNNIDLEEGPSI---EYVKLPELNKLHEVESKLKET--SEEYEDL 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 770 LDKQS---RELQDMeccnNQKLLLEYEKYQELQLKSQRMQEEyEKQLRDNDeTKSQALEELTEFY---------EAKLQE 837
Cdd:COG5022 977 LKKSTilvREGNKA----NSELKNFKKELAELSKQYGALQES-TKQLKELP-VEVAELQSASKIIssestelsiLKPLQK 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 838 KTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKK---LRDEKESNLRLKGETGIMR------KKFSSLQK 908
Cdd:COG5022 1051 LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKtinVKDLEVTNRNLVKPANVLQfivaqmIKLNLLQE 1130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 909 EIEERTNDIETLKGEQMKLqgviKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFvldykiKELKKQIE 988
Cdd:COG5022 1131 ISKFLSQLVNTLEPVFQKL----SVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKS------KLSSSEVN 1200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 989 PRENEIRVMKEQIQEmEAELENFHKQNTQLELNITELWQKLRAT-DQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEP 1067
Cdd:COG5022 1201 DLKNELIALFSKIFS-GWPRGDKLKKLISEGWVPTEYSTSLKGFnNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEE 1279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1068 RLLKEKVRGLFEKYVQRADMVEIAGLNT-------------------DLQQEYTRQREHLERNLATLKKKVVKEGELHRT 1128
Cdd:COG5022 1280 EVLPATINSLLQYINVGLFNALRTKASSlrwksatevnynseelddwCREFEISDVDEELEELIQAVKVLQLLKDDLNKL 1359
|
490 500
....*....|....*....|....
gi 767902630 1129 DYVRIMQENVSLIkEINELRRELK 1152
Cdd:COG5022 1360 DELLDACYSLNPA-EIQNLKSRYD 1382
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
926-1223 |
8.15e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 926 KLQGVIKSLEKDIQGLKREiqerdetiqdKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEME 1005
Cdd:TIGR02168 190 RLEDILNELERQLKSLERQ----------AEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1006 AELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEalvkrfktdlhncvayiQEPRLLKEKVRGLFEKYVQra 1085
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE-----------------QQKQILRERLANLERQLEE-- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1086 dmveiagLNTDLQQEyTRQREHLERNLATLKKKVVkegelhrtdyvrimqenvSLIKEINELRRELKFTRSQVYDLEAAL 1165
Cdd:TIGR02168 321 -------LEAQLEEL-ESKLDELAEELAELEEKLE------------------ELKEELESLEAELEELEAELEELESRL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767902630 1166 KLTKKVRPQEVSETepsrdmlstaptARLNEQEETgriiemQRLEIQRLRDQIQEQEQ 1223
Cdd:TIGR02168 375 EELEEQLETLRSKV------------AQLELQIAS------LNNEIERLEARLERLED 414
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
683-958 |
1.12e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 683 FAEEVLvTKTDMEEKAQVMLELktrVEELkmeNEYQLRLKDMnySEKIKELTD--KFIQEMESLKTKNQVLRTEKEKQDV 760
Cdd:COG4913 213 VREYML-EEPDTFEAADALVEH---FDDL---ERAHEALEDA--REQIELLEPirELAERYAAARERLAELEYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 761 YHHEHIEDLLDKQSRELQdmeccnnqkllleyEKYQELqlksqrmqeeyEKQLRDNDETKSQALEELTEFYEAKLQEKTT 840
Cdd:COG4913 284 WFAQRRLELLEAELEELR--------------AELARL-----------EAELERLEARLDALREELDELEAQIRGNGGD 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 841 LLEEAQEDVRQQlrefEETKKQIEEDEDReiqdiktkYEKKLRDekesnLRLKGETGimRKKFSSLQKEIEERtndIETL 920
Cdd:COG4913 339 RLEQLEREIERL----ERELEERERRRAR--------LEALLAA-----LGLPLPAS--AEEFAALRAEAAAL---LEAL 396
|
250 260 270
....*....|....*....|....*....|....*...
gi 767902630 921 KGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKR 958
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
749-1208 |
1.21e-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: 46.58 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 749 QVLRTEKEKQDV-----YHHEHIEDLLDKQSRELQdmECCNNQKLLLEYekyqelqLKSQRMQEEYEKQLRdndETKSQA 823
Cdd:TIGR01612 328 KILESEGEQGHIinkliFLEKEFEDTIHKSDIYKD--ECLSNHLFMEDY-------LKDDKISPYYYEFLE---EIKKIA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 824 LEELTEFYEAKLQEKTTLLEEAQEDVrqqLREFEETKKQ--IEEDEDREIQDIKTKYEKKLRDEKESNLRL--KGETGIM 899
Cdd:TIGR01612 396 KQRAIFFYNAKKLKHLEILYKHQEDI---LNNFHKTIERliFEKPDPNNNNIFKDDFDEFNKPIPKSKLKAleKRFFEIF 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 900 RKKFSS--LQKEIEERTNDIETLKG--EQMK-LQGVIKSLEkdiQGLKREIQERDETIQDKEKRIYDLKKKNQELGkfkf 974
Cdd:TIGR01612 473 EEEWGSydIKKDIDENSKQDNTVKLilMRMKdFKDIIDFME---LYKPDEVPSKNIIGFDIDQNIKAKLYKEIEAG---- 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 975 vldykikeLKKQIEPRENeirvMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEmrrerqkerdlealvkrfk 1054
Cdd:TIGR01612 546 --------LKESYELAKN----WKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDE------------------- 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1055 tdlhncVAYIQEPRL-LKEKVRGLFEK--YVQRA-DMVEIAGLNTDLQQEYTRQR-----EHLERN---LATLKKKVVKe 1122
Cdd:TIGR01612 595 ------IIYINKLKLeLKEKIKNISDKneYIKKAiDLKKIIENNNAYIDELAKISpyqvpEHLKNKdkiYSTIKSELSK- 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1123 geLHRTDYVRIMQENVSLIKEINELRRELKftrSQVYDLEAalKLTKKVRPQEVSETEPSRDMLSTAPTarlNEQEETGR 1202
Cdd:TIGR01612 668 --IYEDDIDALYNELSSIVKENAIDNTEDK---AKLDDLKS--KIDKEYDKIQNMETATVELHLSNIEN---KKNELLDI 737
|
....*.
gi 767902630 1203 IIEMQR 1208
Cdd:TIGR01612 738 IVEIKK 743
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
728-1056 |
1.22e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 728 EKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHH--EHIEDLLDKQS--RELQDMEccnnqkllleyEKYQELQLKSQ 803
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASaeREIAELE-----------AELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 804 RMQEeyekqLRDNDETKSQALEELTEFYEAkLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDRE-IQDIKTKYEKKL 882
Cdd:COG4913 686 DLAA-----LEEQLEELEAELEELEEELDE-LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 883 RDEKESNLR--LKGETGIMRKKFSSLQKEIEERTND-IETLKGEQMKLQGVIKSLEkDIQGLKREIQERDetIQDKEKRI 959
Cdd:COG4913 760 GDAVERELRenLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLP-EYLALLDRLEEDG--LPEYEERF 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 960 YDLKKKNQElgkfkfvldYKIKELKKQIeprENEIRVMKEQIQEMEAELEN----------FHKQNTQLElNITELWQKL 1029
Cdd:COG4913 837 KELLNENSI---------EFVADLLSKL---RRAIREIKERIDPLNDSLKRipfgpgrylrLEARPRPDP-EVREFRQEL 903
|
330 340 350
....*....|....*....|....*....|...
gi 767902630 1030 RA------TDQEMRRERQKERdLEALVKRFKTD 1056
Cdd:COG4913 904 RAvtsgasLFDEELSEARFAA-LKRLIERLRSE 935
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
789-1074 |
1.49e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.01 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 789 LLEYEKYQELQlKSQRMQEEYEKQlRDNDETKSQALEELTEfyeaklQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED 868
Cdd:pfam02029 64 FLDRTAKREER-RQKRLQEALERQ-KEFDPTIADEKESVAE------RKENNEEEENSSWEKEEKRDSRLGRYKEEETEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 869 REIQDIKTKYEKKLRDEKEsnlrlKGEtgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQER 948
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEE-----EGE---EEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 949 deTIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPrENEIRVMKEQIQEME-AELENFHKQNTQLELNITELwQ 1027
Cdd:pfam02029 208 --KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEA-EQKLEELRRRRQEKEsEEFEKLRQKQQEAELELEEL-K 283
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767902630 1028 KLRATDQEMRRERQKERDLEALVKRFKTDlhncvayiQEPRLLKEKV 1074
Cdd:pfam02029 284 KKREERRKLLEEEEQRRKQEEAERKLREE--------EEKRRMKEEI 322
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
791-1210 |
1.57e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.22 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 791 EYEKYQELQLKSQRMQEEYEK-QLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE--DE 867
Cdd:COG5022 811 EYRSYLACIIKLQKTIKREKKlRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQElkID 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 868 DREIQDIKTKYEK------KLRDEKESNLRLKGEtgIMRKKFSSLQKEIEERtnDIETLKGEQMKLQGVIKSLEKDIQGL 941
Cdd:COG5022 891 VKSISSLKLVNLEleseiiELKKSLSSDLIENLE--FKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLHEVESKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 942 KREIQERDETIQDKEKRIYDLKKKNQELGKFKfvldYKIKELKKQIEPRENEIRVMKEQIQEMEaelenFHKQNTQLELN 1021
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFK----KELAELSKQYGALQESTKQLKELPVEVA-----ELQSASKIISS 1037
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1022 ITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYiqeprllkekvrgLFEKYVQRADMVEIAGLNTDLQQEY 1101
Cdd:COG5022 1038 ESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLD-------------DKQLYQLESTENLLKTINVKDLEVT 1104
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1102 TRQREHLERNLATLKKKVVKEGELHRTDyvRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEP 1181
Cdd:COG5022 1105 NRNLVKPANVLQFIVAQMIKLNLLQEIS--KFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRL 1182
|
410 420 430
....*....|....*....|....*....|.
gi 767902630 1182 SRD-MLSTAPTARLNEQEE-TGRIIEMQRLE 1210
Cdd:COG5022 1183 YQSaLYDEKSKLSSSEVNDlKNELIALFSKI 1213
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
968-1170 |
1.68e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 968 ELGK---FKFVLDYKIKELKKQIE----PRENEIRVMKEQIQEMEAELENFHKQNTQLElnitELWQKLRATDQEMRRER 1040
Cdd:COG4717 33 EAGKstlLAFIRAMLLERLEKEADelfkPQGRKPELNLKELKELEEELKEAEEKEEEYA----ELQEELEELEEELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1041 QKERDLEALVKRFKtDLHNCVAYIQEPRLLKEKVRGLFEKYVQ-RADMVEIAglntDLQQEYTRQREHLERNLATLKKKV 1119
Cdd:COG4717 109 AELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERLEElEERLEELR----ELEEELEELEAELAELQEELEELL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767902630 1120 VKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKK 1170
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
976-1160 |
2.05e-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: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 976 LDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN--TQLELNITELWQKLRATDQEMRRERQKERDLEALVKRF 1053
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1054 KTDL---HNCVAYIQEPRLLKEKVRGLFEKYVQRADMV---------------EIAGLNTDLQQEYTRQREHLERNLATL 1115
Cdd:COG3206 246 RAQLgsgPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvialraQIAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767902630 1116 KKkvvKEGELHRT--DYVRIMQENVSLIKEINELRRELKFTRsQVYD 1160
Cdd:COG3206 326 QA---REASLQAQlaQLEARLAELPELEAELRRLEREVEVAR-ELYE 368
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
949-1201 |
2.10e-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: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 949 DETIQDKEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQK 1028
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1029 LRATDQEMRRERQKERDLEALVKrfKTDlhncvayiqeprllkekvrglFEKYVQRADMVE-IAGLNTDLQQEYTRQREH 1107
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLG--SES---------------------FSDFLDRLSALSkIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1108 LERNLATLKKKvVKEGELHRTDYVRIMQENVSLIKE----INELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSR 1183
Cdd:COG3883 145 LEAKKAELEAK-LAELEALKAELEAAKAELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250
....*....|....*...
gi 767902630 1184 DMLSTAPTARLNEQEETG 1201
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAA 241
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
685-1018 |
2.57e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 685 EEVLVTKTDMEE------KAQVML-----ELKTRVEELKMENEYqlrLKDMNYSEKIKELTDKfIQEMESLKTKNQVLRT 753
Cdd:PRK04778 205 EELAALEQIMEEipellkELQTELpdqlqELKAGYRELVEEGYH---LDHLDIEKEIQDLKEQ-IDENLALLEELDLDEA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 754 EKEKQDVyhHEHIEDLLDKqsrelqdMEccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKsqalEELTEfyea 833
Cdd:PRK04778 281 EEKNEEI--QERIDQLYDI-------LE--------REVKARKYVEKNSDTLPDFLEHAKEQNKELK----EEIDR---- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 834 kLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTkyekklrdekesnlrlkgetgimrkkFSSLQKEIEER 913
Cdd:PRK04778 336 -VKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIA--------------------------YSELQEELEEI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 914 TNDIETLKGEQMKLQGVIKSLEKDiqglkrEIQERdETIQDKEKRIYDLK----KKN-----QELGKFKFVLDYKIKELK 984
Cdd:PRK04778 389 LKQLEEIEKEQEKLSEMLQGLRKD------ELEAR-EKLERYRNKLHEIKryleKSNlpglpEDYLEMFFEVSDEIEALA 461
|
330 340 350
....*....|....*....|....*....|....
gi 767902630 985 KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQL 1018
Cdd:PRK04778 462 EELEEKPINMEAVNRLLEEATEDVETLEEETEEL 495
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
843-1014 |
2.64e-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: 45.40 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 843 EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFsslqKEIEERTNDIEtlkg 922
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESSIK-QVEEELEELKEQNEELEKQYKVKKKTL----DLLPDAEENIA---- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 923 eqmKLQGVIKSLEKDIQGLKREIQERDETIQdKEKRIYDLKKKNQELgKFKFVLDyKIKELKKQIEPRENEIRVMKEQIQ 1002
Cdd:pfam05667 405 ---KLQALVDASAQRLVELAGQWEKHRVPLI-EEYRALKEAKSNKED-ESQRKLE-EIKELREKIKEVAEEAKQKEELYK 478
|
170
....*....|..
gi 767902630 1003 EMEAELENFHKQ 1014
Cdd:pfam05667 479 QLVAEYERLPKD 490
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
784-884 |
2.79e-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: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 784 NNQKLLLEYEKYQELQLKSQRMQEEYEKQLrdndETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQI 863
Cdd:pfam03938 6 DMQKILEESPEGKAAQAQLEKKFKKRQAEL----EAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKA 81
|
90 100
....*....|....*....|.
gi 767902630 864 EEDEDREIQDIKTKYEKKLRD 884
Cdd:pfam03938 82 QQELQKKQQELLQPIQDKINK 102
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
702-1151 |
2.90e-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: 45.43 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 702 LELKTRVEELKMENEYQLRLKDMnysEKIKELTDKFIQEM---------ESLKTKNQVLRTEK-EKQDVYhhehiEDLLD 771
Cdd:TIGR01612 603 LELKEKIKNISDKNEYIKKAIDL---KKIIENNNAYIDELakispyqvpEHLKNKDKIYSTIKsELSKIY-----EDDID 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 772 KQSRELQDMECCNNQKLLLEYEKYQELQLKSqrmqeeyekqlrDNDETKSQALEelTEFYEAKLqektTLLEEAQEDVRQ 851
Cdd:TIGR01612 675 ALYNELSSIVKENAIDNTEDKAKLDDLKSKI------------DKEYDKIQNME--TATVELHL----SNIENKKNELLD 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 852 QLREFEE-TKKQIEEDEDREIQDIKTKyEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNdIETLKGEQMKlQGV 930
Cdd:TIGR01612 737 IIVEIKKhIHGEINKDLNKILEDFKNK-EKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQIN-IDNIKDEDAK-QNY 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 931 IKSlekdiqglkreiQERDETIQDKEKRIydlkkknqelgkFKFVldykikelkkqiepreNEIRVMKEQIQ---EMEAE 1007
Cdd:TIGR01612 814 DKS------------KEYIKTISIKEDEI------------FKII----------------NEMKFMKDDFLnkvDKFIN 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1008 LENFHKQNTQLE-LNITELWQKLRA--TDQEMRRERQKERDLEALV-----------------KRFKTDLHNCVAYIQEP 1067
Cdd:TIGR01612 854 FENNCKEKIDSEhEQFAELTNKIKAeiSDDKLNDYEKKFNDSKSLIneinksieeeyqnintlKKVDEYIKICENTKESI 933
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1068 RLLKEKVRGLFEKYVQRADMVEIAGLntdLQQEYTRQREHLERNLATLKKKVVKEGELhrTDYvriMQENVSLIKEINEL 1147
Cdd:TIGR01612 934 EKFHNKQNILKEILNKNIDTIKESNL---IEKSYKDKFDNTLIDKINELDKAFKDASL--NDY---EAKNNELIKYFNDL 1005
|
....
gi 767902630 1148 RREL 1151
Cdd:TIGR01612 1006 KANL 1009
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
388-417 |
4.21e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.87 E-value: 4.21e-04
10 20 30
....*....|....*....|....*....|
gi 767902630 388 HSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:pfam00400 10 HTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
691-969 |
4.39e-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: 44.46 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 691 KTDMEEKAQVMLELKTRVEELkmeneyqlrlkdMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedll 770
Cdd:pfam09726 408 KAELQASRQTEQELRSQISSL------------TSLERSLKSELGQLRQENDLLQTKLHNAVSAKQK------------- 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 771 DKQSreLQDMEccnnQKLLLEyekyqelqlksQRMQEEYEKQLrdNDETKSQALEELTEFYEAKLQEKTTllEEAQEDVR 850
Cdd:pfam09726 463 DKQT--VQQLE----KRLKAE-----------QEARASAEKQL--AEEKKRKKEEEATAARAVALAAASR--GECTESLK 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 851 QQLREFEETKKQIEED---EDREIQDIKTKyEKKLRDEKESnlrlKGETGIMRKKFSSLQKEIEERTNDI--ETlkgeQM 925
Cdd:pfam09726 522 QRKRELESEIKKLTHDiklKEEQIRELEIK-VQELRKYKES----EKDTEVLMSALSAMQDKNQHLENSLsaET----RI 592
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767902630 926 KLqgvikSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQEL 969
Cdd:pfam09726 593 KL-----DLFSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEV 631
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
703-969 |
5.23e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 703 ELKTRVEELKMENEYQLRLKDMNYsEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHIEdlLDKQSRELQDME- 781
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELN-EKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS--IDKLRKEIERLEw 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 782 CCNNQKLLLEYEKyqELQLKSQRMQEEYEKqLRDNDETKSQALEELTEFYEAKLQekttlleeaQEDVRQQLREFEETKK 861
Cdd:COG1340 124 RQQTEVLSPEEEK--ELVEKIKELEKELEK-AKKALEKNEKLKELRAELKELRKE---------AEEIHKKIKELAEEAQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 862 QIEEdedrEIQDIKTKYEKkLRDEKESnlrlkgetgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGL 941
Cdd:COG1340 192 ELHE----EMIELYKEADE-LRKEADE----------LHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
250 260
....*....|....*....|....*...
gi 767902630 942 KREiqERDETIQDKEKRIYDLKKKNQEL 969
Cdd:COG1340 257 KRE--KEKEELEEKAEEIFEKLKKGEKL 282
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
385-417 |
5.32e-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: 5.32e-04
10 20 30
....*....|....*....|....*....|...
gi 767902630 385 YPLHSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:smart00320 8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
748-1045 |
5.35e-04 |
|
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: 43.75 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 748 NQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQ----ELQLKSQRMQEEYEKQLRDNDETKSQA 823
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEeqieEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 824 LEELTEFYEAKLQEKTTLLEEAQEDVRQQlREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKF 903
Cdd:pfam13868 111 QEEDQAEAEEKLEKQRQLREEIDEFNEEQ-AEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 904 SSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIydlkkknqelgkfkfvldyKIKEL 983
Cdd:pfam13868 190 RAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI-------------------ELKER 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902630 984 KKQIEPRENE---IRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERD 1045
Cdd:pfam13868 251 RLAEEAEREEeefERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELE 315
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-179 |
5.43e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.75 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 26 DEQIIIFPSGNHCVK-YNVD-QKWQKFIPGSekSQGMLALSISPNRRYLAiseTVQEKPAITIYELSSipcrkRKVLNNF 103
Cdd:COG2319 257 DGRLLASGSADGTVRlWDLAtGELLRTLTGH--SGGVNSVAFSPDGKLLA---SGSDDGTVRLWDLAT-----GKLLRTL 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902630 104 DFQVQKFISMAFSPDSKYLLAQTSppeSNLVYwLWEKQKVMAIVRIDTQNNPVYQVSFSPQDNTQVCVTGNGMFKL 179
Cdd:COG2319 327 TGHTGAVRSVAFSPDGKTLASGSD---DGTVR-LWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
681-889 |
5.44e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 681 VGFAEEVLVTKTDMEEKAQVMLEL-KTRVEELKMENEYQLRLKDMNYSEKIKELTDKFiqEMESLKTKNQVLRTEKEKQD 759
Cdd:PRK12704 16 VGAVIGYFVRKKIAEAKIKEAEEEaKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF--EKELRERRNELQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 760 VyhhehiEDLLDKQSRELQDMEccnnqkllleyekyQELQLKsqrmQEEYEKQLRDndetksqaLEELTEFYEAKLQEKT 839
Cdd:PRK12704 94 K------EENLDRKLELLEKRE--------------EELEKK----EKELEQKQQE--------LEKKEEELEELIEEQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767902630 840 TLLEEA----QEDVRQQLreFEETKKQIEEDEDREIQDIKTKYekKLRDEKESN 889
Cdd:PRK12704 142 QELERIsgltAEEAKEIL--LEKVEEEARHEAAVLIKEIEEEA--KEEADKKAK 191
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
817-1223 |
5.55e-04 |
|
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: 44.23 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 817 DETKSQALEELTEFYEAKLQEKTTLLEEaqedvRQQLREFEETKKqieededreIQDIKTKY-------EKKLRDEKESN 889
Cdd:NF033838 53 NESQKEHAKEVESHLEKILSEIQKSLDK-----RKHTQNVALNKK---------LSDIKTEYlyelnvlKEKSEAELTSK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 890 LR---------LKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVI--KSLEKDIQGLKREIQERD-ETIQDKEK 957
Cdd:NF033838 119 TKkeldaafeqFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNtyKTLELEIAESDVEVKKAElELVKEEAK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 958 RIYDLKKKNQELGKFkfvldykikELKKQIEPRENEIRVMKEQIQE-----MEAELENFHKQNTQLELNITELWQKLRAT 1032
Cdd:NF033838 199 EPRDEEKIKQAKAKV---------ESKKAEATRLEKIKTDREKAEEeakrrADAKLKEAVEKNVATSEQDKPKRRAKRGV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1033 DQEMRRERQKERDLEAlvkrfkTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRAdmveiaglntdlQQEYTRQREHLERNL 1112
Cdd:NF033838 270 LGEPATPDKKENDAKS------SDSSVGEETLPSPSLKPEKKVAEAEKKVEEA------------KKKAKDQKEEDRRNY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1113 ATLKKKVVkEGELHRTDyVRIMQENVSLIKEI-NELRRELKFTRSQvydleaalkltKKVrpqEVSETEPSRdmLSTAPT 1191
Cdd:NF033838 332 PTNTYKTL-ELEIAESD-VKVKEAELELVKEEaKEPRNEEKIKQAK-----------AKV---ESKKAEATR--LEKIKT 393
|
410 420 430
....*....|....*....|....*....|..
gi 767902630 1192 ARLNEQEETGRIIEmqrlEIQRLRDQIQEQEQ 1223
Cdd:NF033838 394 DRKKAEEEAKRKAA----EEDKVKEKPAEQPQ 421
|
|
| PTZ00332 |
PTZ00332 |
paraflagellar rod protein; Provisional |
775-1172 |
5.83e-04 |
|
paraflagellar rod protein; Provisional
Pssm-ID: 240364 [Multi-domain] Cd Length: 589 Bit Score: 44.18 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 775 RELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRD-------------NDETKSQALEELTEFyeakLQEKTTL 841
Cdd:PTZ00332 162 ATLKNIEDIMNVTQIQNALASTDDQIKTQLAQLEKTNEIQNvamhdgemqvaeeQMWTKVQLQERLIEL----VADKFRL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 842 LEEAqEDVRQQLREFEETKKQIEEdEDREIQDIKtkyeKKLRDEKESNLRlkgetgimrkkfsSLQKEIEERtnDIEtlK 921
Cdd:PTZ00332 238 IGKC-EEENKSFSKIHEVQKQANQ-ETSQMKDAK----RRLKQRCETDLK-------------HIHDAIQKA--DLE--D 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 922 GEQMKLQGVIKslEKDiqglKREIQERDETIQDKEKRIYDLKKKNQELGKFKFvldykiKELKKQIEP--RENEIRVMKE 999
Cdd:PTZ00332 295 AEAMKRYATNK--EKS----ERFIRENEDRQEEAWNKIQDLERQLQRLGTERF------EEVKRRIEEndREEKRRVEYQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1000 QIQEMEAElenfHKQ-------NTQLELNITELWQKLRA------------TDQEM---RRERQKERdLEALVKRFKTdl 1057
Cdd:PTZ00332 363 QFLEVAGQ----HKKlleltvyNCDLALRCTGLVEELVSegcaavkarhdkTNQDLaalRLQVHKEH-LEYFRMLYLT-- 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1058 HNCVAYIQEPRLlKEKVRGLFEKYVQRADMVEI----AGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDYVRI 1133
Cdd:PTZ00332 436 LGSLIYKKEKRL-EEIDRNIRTTHIQLEFCVETfdpnAKKHADMKKELYKLRQGVEEELAMLKEKQAQALEMFKESEEAL 514
|
410 420 430
....*....|....*....|....*....|....*....
gi 767902630 1134 MQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVR 1172
Cdd:PTZ00332 515 DAAGIEFVHPVDENNEEVLTRRSKMVEYRSHLAKQEEVK 553
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
825-963 |
6.87e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 41.84 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 825 EELTEFYeAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYE---KKLRDEKESNLRLKGEtgimrk 901
Cdd:pfam08614 3 LELIDAY-NRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllAQLREELAELYRSRGE------ 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902630 902 kfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 963
Cdd:pfam08614 76 ----LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQ 133
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
810-1224 |
6.90e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 810 EKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQlREFEETKKQIEEDEDREIQDIKTKYEKklrdEKESN 889
Cdd:pfam10174 44 ERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQ-RDLNQLLQQDFTTSPVDGEDKFSTPEL----TEENF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 890 LRLKGETGIMRKKFSSLQKEIEERTNDIETLKG-------------EQMKLQGVIKSLEKDIQGLKREIQERDETIQDKE 956
Cdd:pfam10174 119 RRLQSEHERQAKELFLLRKTLEEMELRIETQKQtlgardesikkllEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 957 KRiydLKKKNQELGKFKFVLDY---------KIKELKKQIEPRENEIRVMKEQIQEMEAELEN------FHKQNTQLELN 1021
Cdd:pfam10174 199 VL---LDQKEKENIHLREELHRrnqlqpdpaKTKALQTVIEMKDTKISSLERNIRDLEDEVQMlktnglLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1022 ITELWQ--------KLRATDQEMRRerqKERDLEALVKRFKTdLHN----CVAYIQeprLLKEKvrgLFEKYvQRADMve 1089
Cdd:pfam10174 276 QMEVYKshskfmknKIDQLKQELSK---KESELLALQTKLET-LTNqnsdCKQHIE---VLKES---LTAKE-QRAAI-- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1090 iaglntdLQQEYTRQREHLERNLATLKKKvvkegelhrTDYVRIMQENVSL-------------IKE--INELRRELKFT 1154
Cdd:pfam10174 343 -------LQTEVDALRLRLEEKESFLNKK---------TKQLQDLTEEKSTlageirdlkdmldVKErkINVLQKKIENL 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1155 RSQVYDLEAALKlTKKVRPQEVSETEPSRDMLSTAPTARLNEQEetgRIIEmqRLEIQRLRDQIQEQEQV 1224
Cdd:pfam10174 407 QEQLRDKDKQLA-GLKERVKSLQTDSSNTDTALTTLEEALSEKE---RIIE--RLKEQREREDRERLEEL 470
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
676-954 |
8.13e-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: 43.89 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 676 KREREVGFAEEVLVTKTDMEEKAQVMLE----LKTRVEELKME-----NEYQLRLKDMNYSEKIKELTDKFIQEMESLKT 746
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEelkaLREALDELRAEltllnEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 747 KNQVLRTEKEKQdvyhHEHIEDLLDKQSRELQdmeccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEE 826
Cdd:TIGR02168 849 ELSEDIESLAAE----IEELEELIEELESELE-----------ALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 827 ltefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGetgiMRKKFSSL 906
Cdd:TIGR02168 914 -----RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR----LENKIKEL 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902630 907 Q----------KEIEERtndIETLKGEQMKLQGVIKSLEKDIQGLKREIQER-DETIQD 954
Cdd:TIGR02168 985 GpvnlaaieeyEELKER---YDFLTAQKEDLTEAKETLEEAIEEIDREARERfKDTFDQ 1040
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-190 |
8.82e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.36 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 26 DEQIIIFPSGNHCVK-YNVD-QKWQKFIPGSekSQGMLALSISPNRRYLAiseTVQEKPAITIYELSSipcrkRKVLNNF 103
Cdd:COG2319 215 DGKLLASGSADGTVRlWDLAtGKLLRTLTGH--SGSVRSVAFSPDGRLLA---SGSADGTVRLWDLAT-----GELLRTL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 104 DFQVQKFISMAFSPDSKYLLAQTsppESNLVyWLWEKQKVMAIVRIDTQNNPVYQVSFSPQDNTQVCVTGNGMFKLLRFA 183
Cdd:COG2319 285 TGHSGGVNSVAFSPDGKLLASGS---DDGTV-RLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA 360
|
....*..
gi 767902630 184 EGTLKQT 190
Cdd:COG2319 361 TGELLRT 367
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
930-1223 |
8.99e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 930 VIKSLEKDIQGLKR--EIQERDETIQDKEKRiydlkKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAE 1007
Cdd:COG1196 194 ILGELERQLEPLERqaEKAERYRELKEELKE-----LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1008 LENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLhncvayiqeprllkekvrglfekyvqradm 1087
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1088 veiaglntdlqQEYTRQREHLERNLATLKkkvvkegelhrtdyvrimQENVSLIKEINELRRELKFTRSQVYDLEAALKL 1167
Cdd:COG1196 319 -----------EELEEELAELEEELEELE------------------EELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 767902630 1168 TKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQ 1223
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
676-1048 |
9.12e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 676 KREREVGFAEEVLVTKTDMEEkAQvMLELKTR----VEELKMENEyQLRLKDMNYsEKIKELTDKFIQEM-ESLKTKNQV 750
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHE-AQ-LQEMRQKhtqaLEELTEQLE-QAKRNKANL-EKAKQALESENAELqAELRTLQQA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 751 lrtekeKQDVyhhEHIEDLLDKQSRELQdmeccnnQKLLLEYEKYQELQLKSQRMQEEYE--------------KQLRDN 816
Cdd:pfam01576 400 ------KQDS---EHKRKKLEGQLQELQ-------ARLSESERQRAELAEKLSKLQSELEsvssllneaegkniKLSKDV 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 817 DETKSQ---ALEELTEFYEAKLQEKTTL--LEEAQEDVRQQLREFEETKKQIEED---EDREIQDIKTKYE--------- 879
Cdd:pfam01576 464 SSLESQlqdTQELLQEETRQKLNLSTRLrqLEDERNSLQEQLEEEEEAKRNVERQlstLQAQLSDMKKKLEedagtleal 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 880 ----KKLRDEKES-NLRLKGETGI---MRKKFSSLQKEIEERTND-------IETLKGEQMKLQGVI------------- 931
Cdd:pfam01576 544 eegkKRLQRELEAlTQQLEEKAAAydkLEKTKNRLQQELDDLLVDldhqrqlVSNLEKKQKKFDQMLaeekaisaryaee 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 932 ------KSLEKDIQGLK--REIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQE 1003
Cdd:pfam01576 624 rdraeaEAREKETRALSlaRALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEE 703
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 767902630 1004 MEAELENFHKQNTQLELNItelwQKLRAtdqemrrerQKERDLEA 1048
Cdd:pfam01576 704 LEDELQATEDAKLRLEVNM----QALKA---------QFERDLQA 735
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
796-876 |
1.03e-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: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 796 QELQLKSQRMQEEYEKQLRdndETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLrefEETKKQIEEDEDREIQDIK 875
Cdd:cd06503 43 EKAKEEAEELLAEYEEKLA---EARAEAQEIIEEARKEAEKIKEEILAEAKEEAERIL---EQAKAEIEQEKEKALAELR 116
|
.
gi 767902630 876 T 876
Cdd:cd06503 117 K 117
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
849-1045 |
1.36e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 849 VRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQ 928
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKT----IKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 929 GVIKSLEKDI-------------QGLKREiQERDETIQDK----EKRIYDLKKKNQELGKFKFVLD---YKIKELKKQIE 988
Cdd:PHA02562 269 SKIEQFQKVIkmyekggvcptctQQISEG-PDRITKIKDKlkelQHSLEKLDTAIDELEEIMDEFNeqsKKLLELKNKIS 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767902630 989 PRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEmRRERQKERD 1045
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT-KSELVKEKY 403
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
827-1058 |
1.45e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 827 LTEFYEAKLQEKTTLLEEAqEDVRQQLREFEETKKQIEEDEDR-----EIQDIKTKYEKKLRDEKESN-LRLKGETGIMR 900
Cdd:COG4913 209 LDDFVREYMLEEPDTFEAA-DALVEHFDDLERAHEALEDAREQiellePIRELAERYAAARERLAELEyLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 901 KKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDetiqdkekriydlkkknqelGKfkfvldyki 980
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG--------------------GD--------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 981 kelkkQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLEL-----------NITELWQKLRATDQEMRRERQKERDLEAL 1049
Cdd:COG4913 339 -----RLEQLEREIERLERELEERERRRARLEALLAALGLplpasaeefaaLRAEAAALLEALEEELEALEEALAEAEAA 413
|
....*....
gi 767902630 1050 VKRFKTDLH 1058
Cdd:COG4913 414 LRDLRRELR 422
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
952-1110 |
1.47e-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: 42.05 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 952 IQDKEKRIYDLKK-KNQELGKFKFVLDYKIKELKK-------QIEPRENEIRVMKEQIQEMEA----ELENFHKQNTQLE 1019
Cdd:pfam09787 20 LQSKEKLIASLKEgSGVEGLDSSTALTLELEELRQerdllreEIQKLRGQIQQLRTELQELEAqqqeEAESSREQLQELE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1020 LNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCV----AYIQEPRL--------------LKEKVRGLFEKY 1081
Cdd:pfam09787 100 EQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIkdreAEIEKLRNqltsksqssssqseLENRLHQLTETL 179
|
170 180
....*....|....*....|....*....
gi 767902630 1082 VQRADMVEiaglntDLQQEYTRQREHLER 1110
Cdd:pfam09787 180 IQKQTMLE------ALSTEKNSLVLQLER 202
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
842-1189 |
1.51e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 842 LEEAQEDVRQQLREFEETKKQIEEDEDR--EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKfsslQKEIEERTNDIET 919
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKacEIRDQITSKEAQLESSREIVKSYENELDPLKNR----LKEIEHNLSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 920 LKGEQMKLQGVIKSLEKDIQGLK----------------------REIQERDETIQDKEKRIYDLKKKNQELGKFKFVLD 977
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELElkmekvfqgtdeqlndlyhnhqRTVREKERELVDCQRELEKLNKERRLLNQEKTELL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 978 YKIKELKKQIEPRENEIRVMKEQIQEMEaelenfhkqnTQLELNITElwqklRATDQEMRRERQKERDLEALVKRFKTDL 1057
Cdd:TIGR00606 347 VEQGRLQLQADRHQEHIRARDSLIQSLA----------TRLELDGFE-----RGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1058 HNCVAYIQEPRLLKEKVRGLfekyvqradMVEIAGLNTDLQQEytrqREHLERNLATLKKKvVKEGELHRTDYVRIMQEN 1137
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEI---------RDEKKGLGRTIELK----KEILEKKQEELKFV-IKELQQLEGSSDRILELD 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902630 1138 VSLIKEINEL------------RRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTA 1189
Cdd:TIGR00606 478 QELRKAERELskaeknsltetlKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT 541
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
701-1177 |
1.86e-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: 42.85 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 701 MLELKTRVEELKM-----ENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQ-------VLRTEKEKQDVYHHEHIED 768
Cdd:pfam01576 224 IAELQAQIAELRAqlakkEEELQAALARLEEETAQKNNALKKIRELEAQISELQedleserAARNKAEKQRRDLGEELEA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 769 LldkqSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEE---YEKQLRDNDETKSQALEELTEFYEAKLQEKTTL---- 841
Cdd:pfam01576 304 L----KTELEDTLDTTAAQQELRSKREQEVTELKKALEEEtrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLekak 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 842 --LEEAQEDVRQQLREFEETKKQIEEDEDR---EIQDIKTKYEKKLRDEKESNLRL-KGETGI---------MRKKFSSL 906
Cdd:pfam01576 380 qaLESENAELQAELRTLQQAKQDSEHKRKKlegQLQELQARLSESERQRAELAEKLsKLQSELesvssllneAEGKNIKL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 907 QKE---IEERTNDIETLKGEQ----MKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI-------YDLKKKNQELGKF 972
Cdd:pfam01576 460 SKDvssLESQLQDTQELLQEEtrqkLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLstlqaqlSDMKKKLEEDAGT 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 973 KFVLDYKIKELKKQIEpreneirVMKEQIQEMEAELENFHKQNTQL--EL------------NITELWQKLRATDQEMRR 1038
Cdd:pfam01576 540 LEALEEGKKRLQRELE-------ALTQQLEEKAAAYDKLEKTKNRLqqELddllvdldhqrqLVSNLEKKQKKFDQMLAE 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1039 ER------QKERD-LEALVKRFKTDLHNCVAYIQEPRLLKEKvrglFEKY--VQRADMVEIAGLNTDLQQ---EYTRQRE 1106
Cdd:pfam01576 613 EKaisaryAEERDrAEAEAREKETRALSLARALEEALEAKEE----LERTnkQLRAEMEDLVSSKDDVGKnvhELERSKR 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1107 HLERNLATLKKKVVK-EGELHRTDYVRIMQE-NVSLIK-----------EINELRRelKFTRSQVYDLEAALKLTKKVRP 1173
Cdd:pfam01576 689 ALEQQVEEMKTQLEElEDELQATEDAKLRLEvNMQALKaqferdlqardEQGEEKR--RQLVKQVRELEAELEDERKQRA 766
|
....
gi 767902630 1174 QEVS 1177
Cdd:pfam01576 767 QAVA 770
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
836-1025 |
1.86e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 836 QEKTTLLEEAQEdvrQQLREFEETKKQIEEDEDREIQDIKTKYEK---KLRDEKESNLRLKGETGIMRKK---------- 902
Cdd:PRK05771 16 SYKDEVLEALHE---LGVVHIEDLKEELSNERLRKLRSLLTKLSEaldKLRSYLPKLNPLREEKKKVSVKsleelikdve 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 903 --FSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEK------DIQ-------------GLKREIQERDETI--------- 952
Cdd:PRK05771 93 eeLEKIEKEIKELEEEISELENEIKELEQEIERLEPwgnfdlDLSlllgfkyvsvfvgTVPEDKLEELKLEsdvenveyi 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 953 -QDKEKRIY-------DLKKKNQELGKF---KFVLDYK--IKELKKQIEPRENEIrvmKEQIQEMEAELENFHKQNTQLE 1019
Cdd:PRK05771 173 sTDKGYVYVvvvvlkeLSDEVEEELKKLgfeRLELEEEgtPSELIREIKEELEEI---EKERESLLEELKELAKKYLEEL 249
|
....*.
gi 767902630 1020 LNITEL 1025
Cdd:PRK05771 250 LALYEY 255
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
800-974 |
1.87e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 800 LKSQRMQEEYEKQLRDNDEtksqalEELTEFYEAKLQEKTTLLEEAQE--DVRQQLRE-FEETKKQIEEdedreiqdikt 876
Cdd:smart00787 128 LEAKKMWYEWRMKLLEGLK------EGLDENLEGLKEDYKLLMKELELlnSIKPKLRDrKDALEEELRQ----------- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 877 kyEKKLRDEKESNLrlKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIqdKE 956
Cdd:smart00787 191 --LKQLEDELEDCD--PTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL--EQ 264
|
170
....*....|....*...
gi 767902630 957 KRIYDLKKKNQELGKFKF 974
Cdd:smart00787 265 CRGFTFKEIEKLKEQLKL 282
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
793-1021 |
2.18e-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: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 793 EKYQELQLKSQRMQEEYEKQlrdndetKSQALEELTEfyeakLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReiq 872
Cdd:pfam13166 279 DEFTEFQNRLQKLIEKVESA-------ISSLLAQLPA-----VSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRA--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 873 diktKYEKKLRDEKESNL-RLKGETGIMRKKFSSLQKEIE---ERTNDIETLKGEQMKL--QGVIKSLEKDIQGLKREIQ 946
Cdd:pfam13166 344 ----LEAKRKDPFKSIELdSVDAKIESINDLVASINELIAkhnEITDNFEEEKNKAKKKlrLHLVEEFKSEIDEYKDKYA 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902630 947 ERDETIQDKEKRIYDLKKKNQELGKfkfvldyKIKELkkqieprENEIRVMKEQIQEMEAELENFHKQNTQLELN 1021
Cdd:pfam13166 420 GLEKAINSLEKEIKNLEAEIKKLRE-------EIKEL-------EAQLRDHKPGADEINKLLKAFGFGELELSFN 480
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
695-874 |
2.21e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 695 EEKAQVMLELKTRVEELKMENEYQLRLKDmnysEKIKELTDKFIQEMESLKTKnqvlrtekekqdvyhhehiEDLLDKQS 774
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERR----NELQKLEKRLLQKEENLDRK-------------------LELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 775 RELQDMECCNNQKLlleyekyQELQLKSQRMQEEYEKQLrdndetksQALEE---LTEFyEAKLQEKTTLLEEAQEDVRQ 851
Cdd:PRK12704 110 EELEKKEKELEQKQ-------QELEKKEEELEELIEEQL--------QELERisgLTAE-EAKEILLEKVEEEARHEAAV 173
|
170 180
....*....|....*....|...
gi 767902630 852 QLREFEEtkkQIEEDEDREIQDI 874
Cdd:PRK12704 174 LIKEIEE---EAKEEADKKAKEI 193
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
909-1174 |
2.23e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 909 EIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIY----DLKKKNQELGKFKFVLDYKIKELK 984
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRtlddQWKEKRDELNGELSAADAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 985 KQIEPRENEIRV-MKEQIQEMEAELENFHKQNTQLEL---NITELWQKLRATDQEMRRERQKeRDLEalVKRFKTDLHNC 1060
Cdd:pfam12128 322 SELEALEDQHGAfLDADIETAAADQEQLPSWQSELENleeRLKALTGKHQDVTAKYNRRRSK-IKEQ--NNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1061 VAYIQEprllkEKVRGLfekyvqradmveiAGLNTDLQQEYTRQREHLERNLATLK--KKVVKE--GELH-RTDYVRIMQ 1135
Cdd:pfam12128 399 LAKIRE-----ARDRQL-------------AVAEDDLQALESELREQLEAGKLEFNeeEYRLKSrlGELKlRLNQATATP 460
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 767902630 1136 ENVSLIK----EINELRRELKFTRSQVYDLEAALKLTKKVRPQ 1174
Cdd:pfam12128 461 ELLLQLEnfdeRIERAREEQEAANAEVERLQSELRQARKRRDQ 503
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
702-887 |
2.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 702 LELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRT-EKEKQDVYHHEHIEDLLDK-QSRELQD 779
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAALLAEaGVEDEEE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 780 MEccnnqKLLLEYEKYQELQLKsqrmQEEYEKQLRDNDETKSQALEELT-EFYEAKLQEKTTLLEEAQEDVRQQLREFEE 858
Cdd:COG4717 387 LR-----AALEQAEEYQELKEE----LEELEEQLEELLGELEELLEALDeEELEEELEELEEELEELEEELEELREELAE 457
|
170 180 190
....*....|....*....|....*....|
gi 767902630 859 TKKQIEE-DEDREIQDIKTKYEKKLRDEKE 887
Cdd:COG4717 458 LEAELEQlEEDGELAELLQELEELKAELRE 487
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
706-897 |
2.29e-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: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 706 TRVEELKMENEYQLRLkdmnySEKIKELTDKfiqEMESLKTKNQVLRTEKEKQDVYHHEhIEDLLDKQSRELQDMeccnn 785
Cdd:smart00787 126 ARLEAKKMWYEWRMKL-----LEGLKEGLDE---NLEGLKEDYKLLMKELELLNSIKPK-LRDRKDALEEELRQL----- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 786 QKLLLEYEKYQELQLKSQRmqEEYEKQLRDNDEtKSQALEELTEfyeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE 865
Cdd:smart00787 192 KQLEDELEDCDPTELDRAK--EKLKKLLQEIMI-KVKKLEELEE----ELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
170 180 190
....*....|....*....|....*....|..
gi 767902630 866 DEDREIQDIKTKYEKKLRDEKESNLRLKGETG 897
Cdd:smart00787 265 CRGFTFKEIEKLKEQLKLLQSLTGWKITKLSG 296
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
902-1056 |
2.34e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 902 KFSSLQKEIEERTNDIETL----KGEQMKLQGVIKSLEKDIQGLKREIQERDETI----QDKEKRIYDLKKKNQELGKFK 973
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQrkknGENIARKQNKYDELVEEAKTIKAEIEELTDELlnlvMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 974 FVLDYKIKELK------------KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLEL----------NITELWQKLRA 1031
Cdd:PHA02562 269 SKIEQFQKVIKmyekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdefneqskKLLELKNKIST 348
|
170 180
....*....|....*....|....*
gi 767902630 1032 TDQEMRRERQKERDLEALVKRFKTD 1056
Cdd:PHA02562 349 NKQSLITLVDKAKKVKAAIEELQAE 373
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
868-1152 |
2.60e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 868 DREIQDIKTKYEKKLRD-EKESNLRLKGETGIMR---KKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQ---- 939
Cdd:PLN02939 105 DEAIAAIDNEQQTNSKDgEQLSDFQLEDLVGMIQnaeKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSetda 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 940 --GLKREIQERDETIQDK-EKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQ---IQEMEAELENFHK 1013
Cdd:PLN02939 185 riKLAAQEKIHVEILEEQlEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAElieVAETEERVFKLEK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1014 QNTQLELNITELWQKLRATDQEMRRER--------QKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLfEKYVQRA 1085
Cdd:PLN02939 265 ERSLLDASLRELESKFIVAQEDVSKLSplqydcwwEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKL-EASLKEA 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902630 1086 DMVEIAGLNTDL-QQEYTRQREHLERNlatlkkkvvkEGELHrtDYVRIMQEnvsLIKEINELRRELK 1152
Cdd:PLN02939 344 NVSKFSSYKVELlQQKLKLLEERLQAS----------DHEIH--SYIQLYQE---SIKEFQDTLSKLK 396
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
801-1074 |
3.05e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 801 KSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQL---REFEETKKQIEEDEDR--EIQDIK 875
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSIneyNKIESARADLEDIKIKinELKDKH 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 876 TKYEKKlrDEKESNLRLkgetGIMRKKFSSLQKEIEERTN-DIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQD 954
Cdd:PRK01156 546 DKYEEI--KNRYKSLKL----EDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 955 KEKRIYDlkKKNQELGKFKfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLeLNITELWQKLRATDQ 1034
Cdd:PRK01156 620 SIREIEN--EANNLNNKYN-----EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRI-NDIEDNLKKSRKALD 691
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767902630 1035 EMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKV 1074
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDINETLESMKKI 731
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
685-895 |
3.31e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 685 EEVLVTKTDMEEKaqvMLELKTRVEELKMENEYQLrlkdmnySEKIKELtDKFIQEMESLKTKNQVLRTEKEKQDVYHHE 764
Cdd:PRK03918 559 AELEKKLDELEEE---LAELLKELEELGFESVEEL-------EERLKEL-EPFYNEYLELKDAEKELEREEKELKKLEEE 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 765 hIEDLLDKQSRELQDMECCNNQ--KLLLEY--EKYQELQLKSQRMQEEYE------KQLRDNDETKSQALEELTEFYEA- 833
Cdd:PRK03918 628 -LDKAFEELAETEKRLEELRKEleELEKKYseEEYEELREEYLELSRELAglraelEELEKRREEIKKTLEKLKEELEEr 706
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902630 834 -KLQEKTTLLEEAQEDVrQQLRE-FEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGE 895
Cdd:PRK03918 707 eKAKKELEKLEKALERV-EELREkVKKYKALLKERALSKVGEIASEIFEELTEGKYSGVRVKAE 769
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
728-945 |
3.42e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 728 EKIKELTD--KFIQE----MESLKTKNQVLRTEKE-----KQDVYHHEHIEDLLDKQSRELQDMeccNNQKLLLEYEKYQ 796
Cdd:PRK04863 901 EQLDEAEEakRFVQQhgnaLAQLEPIVSVLQSDPEqfeqlKQDYQQAQQTQRDAKQQAFALTEV---VQRRAHFSYEDAA 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 797 ELQLKSQRMQEEYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLLEEAQE--DV-RQQLREFEetkkqieededREIQD 873
Cdd:PRK04863 978 EMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQ-AQAQLAQYNQVLASLKSsyDAkRQMLQELK-----------QELQD 1045
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902630 874 IKTKY----EKKLRDEKEsnlRLKGETGIMRKKFSSLQKEIEERTNDIETLkgeqmklQGVIKSLEKDIQGLKREI 945
Cdd:PRK04863 1046 LGVPAdsgaEERARARRD---ELHARLSANRSRRNQLEKQLTFCEAEMDNL-------TKKLRKLERDYHEMREQV 1111
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
708-1035 |
3.75e-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: 41.96 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 708 VEELKMENEYQLRLKDMNYS-EKIKELTDKFIQEMESLKT--KNQvlrTEKEKQDVYHHEHIEDLLDKQSRELQDMECCN 784
Cdd:TIGR01612 1401 LEECKSKIESTLDDKDIDECiKKIKELKNHILSEESNIDTyfKNA---DENNENVLLLFKNIEMADNKSQHILKIKKDNA 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 785 NQKLLLEYEKYQELQLKSQRMQEEYEK---QLRDNDETKSQALEELTE----FYEAKLQEKttlLEEAQEDVRQQLREFE 857
Cdd:TIGR01612 1478 TNDHDFNINELKEHIDKSKGCKDEADKnakAIEKNKELFEQYKKDVTEllnkYSALAIKNK---FAKTKKDSEIIIKEIK 1554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 858 ETKKQIEEDEDREIQDIKTKYEKKLRDEKE---SNLRLKGETGI------MRKKFSSLQkEIEERTNDIETlkgEQMKLQ 928
Cdd:TIGR01612 1555 DAHKKFILEAEKSEQKIKEIKKEKFRIEDDaakNDKSNKAAIDIqlslenFENKFLKIS-DIKKKINDCLK---ETESIE 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 929 GVIKSLEKDIQGLK--------REIQERDETIQDKEKRIYDLKKKNQElgkfkfvLDYKIKELKKQIEPREN--EIRVMk 998
Cdd:TIGR01612 1631 KKISSFSIDSQDTElkengdnlNSLQEFLESLKDQKKNIEDKKKELDE-------LDSEIEKIEIDVDQHKKnyEIGII- 1702
|
330 340 350
....*....|....*....|....*....|....*...
gi 767902630 999 EQIQEM-EAELENFHKQNTQLELNITELWQKLRATDQE 1035
Cdd:TIGR01612 1703 EKIKEIaIANKEEIESIKELIEPTIENLISSFNTNDLE 1740
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
758-998 |
4.10e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 758 QDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQElQLKSQRMQ----EEYEKQLRDNDETKSQALEELTEFYEA 833
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYN-KIESARADlediKIKINELKDKHDKYEEIKNRYKSLKLE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 834 KLQEKTTLLEEAQE-----DVRQQLREFEETKKQIEEDEDR------EIQDIKTKYEKKLR--DEKESNLRLKgetgimR 900
Cdd:PRK01156 562 DLDSKRTSWLNALAvisliDIETNRSRSNEIKKQLNDLESRlqeieiGFPDDKSYIDKSIReiENEANNLNNK------Y 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 901 KKFSSLQKEIEERTNDIETLKGEQMKlqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKI 980
Cdd:PRK01156 636 NEIQENKILIEKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
250
....*....|....*...
gi 767902630 981 KELKKQIEPRENEIRVMK 998
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
907-1219 |
4.10e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 907 QKEIEERTNDIETLKGEQMKLQGVIKSLE---KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfvldyKIKEL 983
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRaeiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLK-------EIERL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 984 KKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQlelnitelwqkLRATDQEMRRERQKERDLEALVKRFKtDLHNCVAY 1063
Cdd:PRK01156 224 SIEYNNAMDDYNNLKSALNELSSLEDMKNRYESE-----------IKTAESDLSMELEKNNYYKELEERHM-KIINDPVY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1064 IQeprllKEKVRGLFEKYVQRADMVEI-AGLNTDLQqeytrQREHLERNLATLKKkvvkegelHRTDYVRIMQENVSLIK 1142
Cdd:PRK01156 292 KN-----RNYINDYFKYKNDIENKKQIlSNIDAEIN-----KYHAIIKKLSVLQK--------DYNDYIKKKSRYDDLNN 353
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902630 1143 EINELRRELKFTRSQVYDLEaalKLTKKVRpqevsETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQ 1219
Cdd:PRK01156 354 QILELEGYEMDYNSYLKSIE---SLKKKIE-----EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
792-909 |
4.39e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.
Pssm-ID: 214016 [Multi-domain] Cd Length: 152 Bit Score: 39.13 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 792 YEKYQELQLKS---QRMQEEYEKqLRDNDETKSQALE---ELTEFYEAKLQEKTTLLEEAQEDVRQQLRE-FEETKKQIE 864
Cdd:cd12923 11 KEINKEYLDKSreyDELYEKYNK-LSQEIQLKRQALEafeEAVKMFEEQLRTQEKFQKEAQPHEKQRLMEnNELLKSRLK 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767902630 865 ededrEIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKE 909
Cdd:cd12923 90 -----ELEESKEQLEEDLRKQVAYNRELEREMNSLKPELMQLRKQ 129
|
|
| WDR74 |
cd22857 |
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ... |
343-420 |
4.96e-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: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 343 CLCFSPSEETLVASTSKNQLYSI---TMSLTEISKGepahfeylmypLHSAPITGLATCIRKPLIATCSLDRSIRLWNYE 419
Cdd:cd22857 228 AVAEDPDGHTVYVGDTSGDLASIdlrTGKLLGCFKG-----------KCGGSIRSIARHPELPLIASCGLDRYLRIWDTE 296
|
.
gi 767902630 420 T 420
Cdd:cd22857 297 T 297
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
676-1151 |
5.06e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 676 KREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEyQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEK 755
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 756 EKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKS----QRMQEEYEKQLRDNDETKSQALEELTEFY 831
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAllerLERLEEELEELEEALAELEEEEEEEEEAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 832 EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKK--------- 902
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLlaglrglag 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 903 -FSSLQKEIEERTNDIETLKGEQMKLQGV--IKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGK-------- 971
Cdd:COG1196 525 aVAVLIGVEAAYEAALEAALAAALQNIVVedDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAigaavdlv 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 972 ---------FKFVLDYKIKELKKQIEPRENEIRVMK-------EQIQEMEAELENFHKQNTQLELNITELWQKLRATDQE 1035
Cdd:COG1196 605 asdlreadaRYYVLGDTLLGRTLVAARLEAALRRAVtlagrlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1036 MRRERQKERDLEALVKRFKTDLHNcvayIQEPRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQQEYTRQ----------- 1104
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERE----LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEeealeelpepp 760
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902630 1105 -REHLERNLATLKKKV----------------VKE--GELH--RTDYVRIMQENVSLIKEINELRREL 1151
Cdd:COG1196 761 dLEELERELERLEREIealgpvnllaieeyeeLEEryDFLSeqREDLEEARETLEEAIEEIDRETRER 828
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
933-1164 |
5.87e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.86 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 933 SLEKDIQGLKREIQERDETIQDKEKRIydlkkkNQELGKFKFVLDYKIKELKKQ---IEPRENEIRVMKEQIQEMEAELE 1009
Cdd:pfam03528 5 DLQQRVAELEKENAEFYRLKQQLEAEF------NQKRAKFKELYLAKEEDLKRQnavLQEAQVELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1010 NFHKQNTQLELNitelwqKLRATDQEMRRERQKERDLEALVKRFKTDlhncvaYIQEPRLLKEKVRGLFEKYVQRADMvE 1089
Cdd:pfam03528 79 NIKAVATVSENT------KQEAIDEVKSQWQEEVASLQAIMKETVRE------YEVQFHRRLEQERAQWNQYRESAER-E 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902630 1090 IAglntDLQQEYTRQREhlERNLATLKKKVVKEGELHRTdYVRIMQenvsliKEINELRRELKFTRSQVYDLEAA 1164
Cdd:pfam03528 146 IA----DLRRRLSEGQE--EENLEDEMKKAQEDAEKLRS-VVMPME------KEIAALKAKLTEAEDKIKELEAS 207
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
841-991 |
6.07e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 39.54 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 841 LLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE-------SNLRLKgetgiMRKKFSSLQKEIEER 913
Cdd:COG1390 11 ILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAErekrriiSSAELE-----ARKELLEAKEELIEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 914 TNDietlkgeqmKLQGVIKSLEKDI---QGLKREIQERDETIQDKEKRIYdLKKKNQELGKfKFVLDYKIKELKKQIEPR 990
Cdd:COG1390 86 VFE---------EALEKLKNLPKDPeykELLKKLLKEAAEELGSGDLVVY-VNEKDKELLE-ELLKELKKKGLEVSEEDI 154
|
.
gi 767902630 991 E 991
Cdd:COG1390 155 D 155
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
822-932 |
6.54e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 822 QALEELtefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE---------SNLRL 892
Cdd:PRK00409 523 ASLEEL----ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikelRQLQK 598
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767902630 893 KGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIK 932
Cdd:PRK00409 599 GGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
808-1164 |
6.63e-03 |
|
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: 40.71 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 808 EYEKQLRDNDETKsQALEELTEFYEAKLQEKTTLLEEAQEDvrQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE 887
Cdd:COG5185 101 EYVNSLIKLPNYE-WSADILISLLYLYKSEIVALKDELIKV--EKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 888 SNLRLKGETGIMrkkfsslQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDET---IQDKEKRIYDLK- 963
Cdd:COG5185 178 KLEIFGLTLGLL-------KGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEAlkgFQDPESELEDLAq 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 964 ---------KKNQELGKFKFV--------LDYKIKELKKQIEPRENEIRVMKEQIqEMEAELENFHKQNTQLELNiTELW 1026
Cdd:COG5185 251 tsdkleklvEQNTDLRLEKLGenaesskrLNENANNLIKQFENTKEKIAEYTKSI-DIKKATESLEEQLAAAEAE-QELE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1027 QKLRATDQEMRRE----RQKERDLEALVKRFKTDLHNCVAyIQEPRLLKEKVRGLfekyvqradMVEIAGLNTDLQQEYT 1102
Cdd:COG5185 329 ESKRETETGIQNLtaeiEQGQESLTENLEAIKEEIENIVG-EVELSKSSEELDSF---------KDTIESTKESLDEIPQ 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902630 1103 RQREHLERNLATL---KKKVVKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAA 1164
Cdd:COG5185 399 NQRGYAQEILATLedtLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS 463
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
676-994 |
6.67e-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: 40.80 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 676 KREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMEneyQLRL-KDMNYSEKIKELTDKFIQEMESLKT-----KNQ 749
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE---KLQIgTNLQRRQQFEEQLVELSTEVQSLIReikdaKEQ 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 750 VLRTE-------KEKQDVYHHEHIEDllDKQSRELQDMEccnnQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQ 822
Cdd:TIGR00606 911 DSPLEtflekdqQEKEELISSKETSN--KKAQDKVNDIK----EKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNA 984
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 823 ALEEltefyEAKLQEKTtlleeaQEDVRQQLREFEETKKQieedeDREIQDIKT--KYEKKLRDEKESNLRLKGETGIMR 900
Cdd:TIGR00606 985 QLEE-----CEKHQEKI------NEDMRLMRQDIDTQKIQ-----ERWLQDNLTlrKRENELKEVEEELKQHLKEMGQMQ 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 901 kkFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDetIQDKEKRIYDL-------KKKNQELGKFK 973
Cdd:TIGR00606 1049 --VLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ--FRDAEEKYREMmivmrttELVNKDLDIYY 1124
|
330 340
....*....|....*....|.
gi 767902630 974 FVLDYKIKELKKQIEPRENEI 994
Cdd:TIGR00606 1125 KTLDQAIMKFHSMKMEEINKI 1145
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
821-1107 |
7.05e-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: 40.06 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 821 SQALEEL------TEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKkLRDEKESNLRLKG 894
Cdd:pfam04108 20 RSLLEELvvllakIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDK-LRNTPVEPALPPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 895 ETG-------IMRKKFSSLQKEIEErtnDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDEtIQDKEKRIYDLKKKNQ 967
Cdd:pfam04108 99 EEKqktlldfIDEDSVEILRDALKE---LIDELQAAQESLDSDLKRFDDDLRDLQKELESLSS-PSESISLIPTLLKELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 968 EL-----GKF-KFVLDY-KIKELKKQIEPRENE---------------IRVMKEQIQEMEAELENFHKQNTQLELNITEL 1025
Cdd:pfam04108 175 SLeeemaSLLeSLTNHYdQCVTAVKLTEGGRAEmlevlendarelddvVPELQDRLDEMENNYERLQKLLEQKNSLIDEL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1026 ---WQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYV-----QRADMVEIAGLNTDL 1097
Cdd:pfam04108 255 lsaLQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREFYEGFPSAYGSLLleverRREWAEKMKKILRKL 334
|
330
....*....|
gi 767902630 1098 QQEYTRQREH 1107
Cdd:pfam04108 335 AEELDRLQEE 344
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
941-1223 |
7.10e-03 |
|
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: 40.65 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 941 LKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEA---ELENFHKQNTQ 1017
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEkykELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1018 ----LELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQradmvEIAGL 1093
Cdd:pfam07888 116 ekdaLLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE-----ELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1094 NTDLQQEYTRQREHlERNLATLKKKVVKEGELHRTDYVRIMqENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRP 1173
Cdd:pfam07888 191 SKEFQELRNSLAQR-DTQVLQLQDTITTLTQKLTTAHRKEA-ENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRD 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902630 1174 QEVSETEPSRdMLSTAPTARLNE-------------QEETG--RIIEMQRLEIQRLRDQIQEQEQ 1223
Cdd:pfam07888 269 RTQAELHQAR-LQAAQLTLQLADaslalregrarwaQERETlqQSAEADKDRIEKLSAELQRLEE 332
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
731-879 |
8.17e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.71 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 731 KELTDKFIQEMeslktKNQVLRTEKEKQDVYHH-EHIE-DLLDKQSRE---------LQDMECCNNQKllleyEKYQELQ 799
Cdd:COG4026 72 RELAEKFFEEL-----KGMVGHVERMKLPLGHDvEYVDvELVRKEIKNaiiraglksLQNIPEYNELR-----EELLELK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 800 LKSQRMQEEYEKQLRDNDETKSQaLEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYE 879
Cdd:COG4026 142 EKIDEIAKEKEKLTKENEELESE-LEELREEYK-KLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEVFSLEELWK 219
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
815-963 |
8.54e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 38.89 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 815 DNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREiqdiKTKYEKKLRDEKESNLRLKG 894
Cdd:pfam05010 7 DAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQ----KELEHAEIQKVLEEKDQALA 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902630 895 ETGIMRKKFSSLQKEIEertndietlkgeqmKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 963
Cdd:pfam05010 83 DLNSVEKSFSDLFKRYE--------------KQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALK 137
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
703-1221 |
9.01e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 703 ELKTRVEELKMENEYQLRLKDMNYSEKIKELtdkfiqemeslktkNQVLRTEKEkqDVYHHEHIEDLLDKQSRelqdmec 782
Cdd:pfam12128 276 SRQEERQETSAELNQLLRTLDDQWKEKRDEL--------------NGELSAADA--AVAKDRSELEALEDQHG------- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 783 cnnqkllleyeKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQ 862
Cdd:pfam12128 333 -----------AFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 863 IEEDEDREIQDIKTKYEKklrdeKESNLRLKGETGIMRkkFSSLQKEIEERtndIETLKGeqmKLQGVIKSLEKDIQglK 942
Cdd:pfam12128 402 IREARDRQLAVAEDDLQA-----LESELREQLEAGKLE--FNEEEYRLKSR---LGELKL---RLNQATATPELLLQ--L 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 943 REIQERDETIQDK-EKRIYDLKKKNQELGKFKFVLDYKIKELkKQIEPRENEIRVMKEQIQEMeaeleNFHKQNTQLELn 1021
Cdd:pfam12128 467 ENFDERIERAREEqEAANAEVERLQSELRQARKRRDQASEAL-RQASRRLEERQSALDELELQ-----LFPQAGTLLHF- 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1022 itelwqkLRATDQEMRRERQKERDLEALVkrfKTDLHncvayiqePRLLKEKVRGLFEKYvqradmveiaGLNTDLQQ-- 1099
Cdd:pfam12128 540 -------LRKEAPDWEQSIGKVISPELLH---RTDLD--------PEVWDGSVGGELNLY----------GVKLDLKRid 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 1100 --EYTRQREHLERNLATLKKKVVKEGELHRtdyvRIMQENVSLIKEINELRRELKFTRsqvydleAALKLTKKVRPQEVS 1177
Cdd:pfam12128 592 vpEWAASEEELRERLDKAEEALQSAREKQA----AAEEQLVQANGELEKASREETFAR-------TALKNARLDLRRLFD 660
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 767902630 1178 ETEPSRDMLSTAPTARLNEQEETGRIIEMQR----LEIQRLRDQIQEQ 1221
Cdd:pfam12128 661 EKQSEKDKKNKALAERKDSANERLNSLEAQLkqldKKHQAWLEEQKEQ 708
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
703-969 |
9.15e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 703 ELKTRVEELKMENEyQLRLKDMNYSEKIKELTDkfIQEMESlktknQVLRTEKEKQDVyhhehiEDLLDKQSRELQDMEc 782
Cdd:PRK02224 472 EDRERVEELEAELE-DLEEEVEEVEERLERAED--LVEAED-----RIERLEERREDL------EELIAERRETIEEKR- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 783 cnnqkllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQA---LEELTEFyEAKLQEKTTLLE---------EAQEDVR 850
Cdd:PRK02224 537 ----------ERAEELRERAAELEAEAEEKREAAAEAEEEAeeaREEVAEL-NSKLAELKERIEslerirtllAAIADAE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 851 QQLREFEETKKQIEEDEDREIQDIKTKYEKK--LRDEKESNlRLKGetgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQ 928
Cdd:PRK02224 606 DEIERLREKREALAELNDERRERLAEKRERKreLEAEFDEA-RIEE----AREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767902630 929 GVIKSLEKDIQGLkREIQERDETIQDKEKRIYDLKKKNQEL 969
Cdd:PRK02224 681 AEIGAVENELEEL-EELRERREALENRVEALEALYDEAEEL 720
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
906-1052 |
9.39e-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: 39.62 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902630 906 LQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQElgkfkfvldyKIKELKK 985
Cdd:smart00787 149 LDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKE----------KLKKLLQ 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902630 986 QIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELwQKLRATDQEMrrERQKERDLEALVKR 1052
Cdd:smart00787 219 EIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEA-EKKLEQCRGF--TFKEIEKLKEQLKL 282
|
|
| |
