|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
574-1092 |
5.65e-20 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 95.86 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 574 ELKTRVEELKMENEYQLRLKD-MNYSEKIKELTDKFI-----------QEMESLKTKNQVLRTEKEKQDVYHHEHIEDLL 641
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVeLNKLEKQKKENKKNIdkflteikkkeKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 642 DKQSrelqDMECCNNQKLLLEY---------EKYQELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFYEAKLQEKTTL 712
Cdd:TIGR04523 184 NIQK----NIDKIKNKLLKLELllsnlkkkiQKNKSLESQISELKKQ-NNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 713 LEEAQEDVRQ---QLREFEETKKQIEEDEDReIQDIKTKYEkKLRDEKESNL--RLKGETGIMRKKFSSLQKEIEERTND 787
Cdd:TIGR04523 259 KDEQNKIKKQlseKQKELEQNNKKIKELEKQ-LNQLKSEIS-DLNNQKEQDWnkELKSELKNQEKKLEEIQNQISQNNKI 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 788 IETLK--------------GEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKE 853
Cdd:TIGR04523 337 ISQLNeqisqlkkeltnseSENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 854 LKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL-------WQKLRATDQEMRRERQkerDLEALVKRFKT 926
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntreslETQLKVLSRSINKIKQ---NLEQKQKELKS 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 927 DLHNCVAYIQEPRLLKEKVRGLFEKyvqradmveIAGLNTDlQQEYTRQREHLERNLATLKKKVVK-EGELHRTDYVRIM 1005
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKK---------ISSLKEK-IEKLESEKKEKESKISDLEDELNKdDFELKKENLEKEI 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 1006 QENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEpsrdMLSTAPTARLNEQEETGRIIEMQRLEIQRL 1085
Cdd:TIGR04523 564 DEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKE----KKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
....*..
gi 767902638 1086 RDQIQEQ 1092
Cdd:TIGR04523 640 KNKLKQE 646
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
338-537 |
3.32e-17 |
|
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: 83.54 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 338 KQDVLCLCFSPSEeTLVASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:cd00200 93 TSYVSSVAFSPDG-RILSSSSRDK----TIKVWDVETGKCLTT----LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 418 YETNTL-ELFKEYQEEAYSISLHPSGHFIVVGFADKlrlmNLLIDDIRSFKE-YSVRGCGE----CSFSNGGHLFAAVNG 491
Cdd:cd00200 164 LRTGKCvATLTGHTGEVNSVAFSPDGEKLLSSSSDG----TIKLWDLSTGKClGTLRGHENgvnsVAFSPDGYLLASGSE 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767902638 492 -NVIHVYTTTSLENISSLKGHTGK---MLLTFDDQFLLTAAEDGCLFTWK 537
Cdd:cd00200 240 dGTIRVWDLRTGECVQTLSGHTNSvtsLAWSPDGKRLASGSADGTIRIWD 289
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
691-1037 |
1.90e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.11 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 691 KSQALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNlRLKGETGIM 770
Cdd:TIGR02168 675 RRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 771 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYK 850
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 851 IKELKKQIEPRENEIRVMKEQIQ--------------EMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERD 916
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIEslaaeieeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 917 LEALVKRFKTDLHNCVAYIQEPRL----LKEKVRglfEKYVQRADMVEIAGLNTDLQQEYTRQRehlernLATLKKKVVK 992
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVridnLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR------LKRLENKIKE 983
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 767902638 993 EGELhrtdyvrimqeNVSLIKEINELRRELKFTRSQVYDLEAALK 1037
Cdd:TIGR02168 984 LGPV-----------NLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
341-536 |
6.63e-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: 79.69 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 341 VLCLCFSPSEETLVASTSKNQLY---SITMSLTEISKGepahfeylmyplHSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:cd00200 12 VTCVAFSPDGKLLATGSGDGTIKvwdLETGELLRTLKG------------HTGPVRDVAASADGTYLASGSSDKTIRLWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 418 YETN-TLELFKEYQEEAYSISLHPSGHFIVVGFADKlrlmNLLIDDIRSFK-EYSVRGCGE----CSFS-NGGHLFAAVN 490
Cdd:cd00200 80 LETGeCVRTLTGHTSYVSSVAFSPDGRILSSSSRDK----TIKVWDVETGKcLTTLRGHTDwvnsVAFSpDGTFVASSSQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767902638 491 GNVIHVYTTTSLENISSLKGHTGKML-LTF--DDQFLLTAAEDGCLFTW 536
Cdd:cd00200 156 DGTIKLWDLRTGKCVATLTGHTGEVNsVAFspDGEKLLSSSSDGTIKLW 204
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
714-1073 |
1.40e-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: 82.04 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 714 EEAQEDVRQQLREFEETKKQIEEDEdrEIQDIKTKYEKKLRDEKESNLRLKGETGIMRK-KFSSLQKEIEERTNDIETLK 792
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLD--LIIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 793 GEqmklqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGkfkfvlDYKIKELKKQIEPRENEIRVMKEQI 872
Cdd:TIGR02169 244 RQ-------LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 873 QEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEprlLKEKVRGLFEKY 952
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE---VDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 953 VQRADMVEiaglntdlqqEYTRQREHLERNLATL---KKKVVKEGELHRTDYVRIMQ-------ENVSLIKEINELRREL 1022
Cdd:TIGR02169 388 KDYREKLE----------KLKREINELKRELDRLqeeLQRLSEELADLNAAIAGIEAkineleeEKEDKALEIKKQEWKL 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 767902638 1023 KFTRSQVYDLEAAL-KLTKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGR 1073
Cdd:TIGR02169 458 EQLAADLSKYEQELyDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGG 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
664-918 |
2.15e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.65 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 664 EKYQELQLKSQ-RMQEEYEKQLRDNDETKSQALEELTEFyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIE---EDED 739
Cdd:TIGR02169 211 ERYQALLKEKReYEGYELLKEKEALERQKEAIERQLASL-EEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 740 REIQ----DIKTKYEKKLRDEKESNLRLKGETGIMRKKFS---SLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGL 812
Cdd:TIGR02169 290 LRVKekigELEAEIASLERSIAEKERELEDAEERLAKLEAeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 813 KREIQERDETIQ-------DKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQ 885
Cdd:TIGR02169 370 RAELEEVDKEFAetrdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
250 260 270
....*....|....*....|....*....|...
gi 767902638 886 NTQLELNITELWQKLRATDQEMRRERQKERDLE 918
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
567-890 |
7.87e-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: 79.73 E-value: 7.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 567 EKAQVMLELKTRVEELkmenEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQdvyhHEHIEDLLDKQSR 646
Cdd:TIGR02169 208 EKAERYQALLKEKREY----EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR----LEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 647 ELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTefyeaKLQEKTTLLEEAQEDVRQQLRE 726
Cdd:TIGR02169 280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID-----KLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 727 FEEtkkqieededrEIQDIKTKYEK---KLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIK 803
Cdd:TIGR02169 355 LTE-----------EYAELKEELEDlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 804 SLEKDIQGLKREIQERDETIQDKEKRIydlKKKNQELgkfkfvldykiKELKKQIEPRENEIRVMKEQIQEMEAELENFH 883
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEI---KKQEWKL-----------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
....*..
gi 767902638 884 KQNTQLE 890
Cdd:TIGR02169 490 RELAEAE 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
583-1093 |
5.92e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 5.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 583 KMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKtkNQVLRTEKEKQDVYHH-EHIEDLLDKQSRELQDMEccnnqKLLL 661
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIE--ELIKEKEKELEEVLREiNEISSELPELREELEKLE-----KEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 662 EYEKYQELQLKSQRMQEEYEKQLRdndetksqaleeltefyeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE----- 736
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKR-------------------KLEEKIRELEERIEELKKEIEELEEKVKELKElkeka 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 737 DEDREIQDIKTKYEKKLRDEKESNLRLKGE-TGIMR--KKFSSLQKEIEERTNDIETLKGEQMKLQG------VIKSLEK 807
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEiNGIEEriKELEEKEERLEELKKKLKELEKRLEELEErhelyeEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 808 DIQGLK-----REIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQI-------------------EPREN 863
Cdd:PRK03918 373 ELERLKkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteEHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 864 EIRVMKEQIQEMEAELENFHKQNTQLELNITELwQKLRATDQEMRRERQKERDLEALVKRFKT-DLHNCVAYIQEPRLLK 942
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 943 EKVRGLFEkyvqradmvEIAGLNTDLQ--QEYTRQREHLERNLATLKKKVvkeGELHRtdyvRIMQENVSLIKEINELRR 1020
Cdd:PRK03918 532 EKLIKLKG---------EIKSLKKELEklEELKKKLAELEKKLDELEEEL---AELLK----ELEELGFESVEELEERLK 595
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902638 1021 ELKFTRSQVYDLEAAlkltkkvrPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQE 1093
Cdd:PRK03918 596 ELEPFYNEYLELKDA--------EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
341-549 |
6.71e-14 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 74.95 E-value: 6.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 341 VLCLCFSPSEETLvASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWNYET 420
Cdd:COG2319 165 VTSVAFSPDGKLL-ASGSDDG----TVRLWDLATGKLLRT----LTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 421 NT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDDIRSFKEYSVRGCGECSFS-NGGHLFAAVNGNVIHVY 497
Cdd:COG2319 236 GKlLRTLTGHSGSVRSVAFSPDGRLLASGSADGtVRLWDLATGELLRTLTGHSGGVNSVAFSpDGKLLASGSDDGTVRLW 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767902638 498 TTTSLENISSLKGHTGKML-LTF--DDQFLLTAAEDGclfTWKVFDKDGRGIKRE 549
Cdd:COG2319 316 DLATGKLLRTLTGHTGAVRsVAFspDGKTLASGSDDG---TVRLWDLATGELLRT 367
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
700-1041 |
1.03e-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: 76.25 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 700 EFYEAKLQEKTTLLEEA------QEDVRQQLREFEETKKQIEEDED--REI---------QDIKTKYEKKLRDEKEsNLR 762
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAagiskyKERRKETERKLERTRENLDRLEDilNELerqlkslerQAEKAERYKELKAELR-ELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 763 LkgetGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGK 842
Cdd:TIGR02168 227 L----ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 843 FKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVK 922
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 923 RFKTDLHncvayiqeprLLKEKVrglfekYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEgelHRTDYV 1002
Cdd:TIGR02168 383 TLRSKVA----------QLELQI------ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE---LQAELE 443
|
330 340 350
....*....|....*....|....*....|....*....
gi 767902638 1003 RIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKK 1041
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
341-538 |
1.87e-13 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 73.79 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 341 VLCLCFSPSEETLvASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCirkP---LIATCSLDRSIRLWN 417
Cdd:COG2319 207 VRSVAFSPDGKLL-ASGSADG----TVRLWDLATGKLLRT----LTGHSGSVRSVAFS---PdgrLLASGSADGTVRLWD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 418 YETNT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDD-IRSFKEYSVRGCGeCSFS-NGGHLFAAVNGNV 493
Cdd:COG2319 275 LATGElLRTLTGHSGGVNSVAFSPDGKLLASGSDDGtVRLWDLATGKlLRTLTGHTGAVRS-VAFSpDGKTLASGSDDGT 353
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767902638 494 IHVYTTTSLENISSLKGHTGKML-LTF--DDQFLLTAAEDGCLFTWKV 538
Cdd:COG2319 354 VRLWDLATGELLRTLTGHTGAVTsVAFspDGRTLASGSADGTVRLWDL 401
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
597-920 |
2.66e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.72 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 597 YSEKIKELTDkfiqEMESLKTKNQVLRTEKEkqdvyhheHIEDLLDKQSRELQDMEccnnqKLLLEYEKYQELQLKSQRM 676
Cdd:TIGR02169 672 EPAELQRLRE----RLEGLKRELSSLQSELR--------RIENRLDELSQELSDAS-----RKIGEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 677 QEEYEKQLRDNDETKSQALEEltefYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDE 756
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIEN----VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 757 KESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK 836
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 837 NQElgkfkfvLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL----WQKLRATDQEMRRERq 912
Cdd:TIGR02169 891 RDE-------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipEEELSLEDVQAELQR- 962
|
....*...
gi 767902638 913 KERDLEAL 920
Cdd:TIGR02169 963 VEEEIRAL 970
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
563-1093 |
3.33e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 74.38 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 563 TDMEEK-AQVMLELK--TRVEELKMEN-EYQLRLKDMNYSEKIKElTDKFIQEMESLKTKNQVLRTekekqDVYHHEHIE 638
Cdd:pfam15921 320 SDLESTvSQLRSELReaKRMYEDKIEElEKQLVLANSELTEARTE-RDQFSQESGNLDDQLQKLLA-----DLHKREKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 639 DLLDKQSRELQDMECCNN-------QKLLLEYEKYQELQLKSQRMQEEYEKQLrdndETKSQALEELTEFYEaKLQEKTT 711
Cdd:pfam15921 394 SLEKEQNKRLWDRDTGNSitidhlrRELDDRNMEVQRLEALLKAMKSECQGQM----ERQMAAIQGKNESLE-KVSSLTA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 712 LLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKESNlrlkgetgimrKKFSSLQKEIEERTNDIETL 791
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSE-RTVSDLTASLQEKERAIEATN-----------AEITKLRSRVDLKLQELQHL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 792 KGEQMKLQGVikslEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQ 871
Cdd:pfam15921 537 KNEGDHLRNV----QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 872 IQEMEAELENFHKQNTQLELNITELwqkLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEk 951
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLELEKVKL---VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE- 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 952 yvqradmvEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGElhrtdyvrIMQENVSLIKEINELRRELKFTRSQVYD 1031
Cdd:pfam15921 689 --------EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH--------AMKVAMGMQKQITAKRGQIDALQSKIQF 752
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902638 1032 LEAALKLTKKVRPQEVSETEPSRDMLSTAPTarlnEQEETGRIIEMQRLEIQRLRDQIQEQE 1093
Cdd:pfam15921 753 LEEAMTNANKEKHFLKEEKNKLSQELSTVAT----EKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
659-919 |
4.06e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 659 LLLEYEKYQElQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDE 738
Cdd:COG1196 230 LLLKLRELEA-ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 739 DReiqdiktkyekkLRDEKESNLRLKGETgimrkkfSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQE 818
Cdd:COG1196 309 ER------------RRELEERLEELEEEL-------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 819 RDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQ 898
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260
....*....|....*....|.
gi 767902638 899 KLRATDQEMRRERQKERDLEA 919
Cdd:COG1196 450 EEAELEEEEEALLELLAELLE 470
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
556-926 |
5.96e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 556 EEVLVTKTDMEEKAQVMLELKTRVEELKmENEYQLRLKDMNYSEKIKELTDKfIQEMESLKTKNQVLRTEKE--KQDVYH 633
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEER-IKELEEKEERLEELKKKLKelEKRLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 634 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQ----------ALEEL----- 698
Cdd:PRK03918 357 LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGElkkeikelkkAIEELkkakg 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 699 ---------TEFYEAKLQEKTTLleeaqedvrqQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKE--SNLRLKGET 767
Cdd:PRK03918 437 kcpvcgrelTEEHRKELLEEYTA----------ELKRIEKELKEIEEKE-RKLRKELRELEKVLKKESEliKLKELAEQL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 768 GIMRKKFSSLQKE-IEERTNDIETLKGEQMKLQGVIKSLEKDI---QGLKREIQERDETIQDKEKRIYDLKKKNQELGkF 843
Cdd:PRK03918 506 KELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELeklEELKKKLAELEKKLDELEEELAELLKELEELG-F 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 844 KFV--LDYKIKEL-------------KKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMR 908
Cdd:PRK03918 585 ESVeeLEERLKELepfyneylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEEL 664
|
410 420
....*....|....*....|
gi 767902638 909 RER--QKERDLEALVKRFKT 926
Cdd:PRK03918 665 REEylELSRELAGLRAELEE 684
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
388-536 |
1.19e-12 |
|
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: 69.67 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 388 HSAPITGLATCIRKPLIATCSLDRSIRLWNYETNTLEL-FKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNL----LID 461
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtLKGHTGPVRDVAASADGTYLASGSSDKtIRLWDLetgeCVR 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902638 462 DIRSFKEYsVRGcgeCSFSNGGHLFAAVNG-NVIHVYTTTSLENISSLKGHTGK-MLLTF--DDQFLLTAAEDGCLFTW 536
Cdd:cd00200 88 TLTGHTSY-VSS---VAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDWvNSVAFspDGTFVASSSQDGTIKLW 162
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
561-930 |
1.80e-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: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 561 TKTDMEEKAQVMLELKTRVEELKME-NEYQLRLKDMNySEKIKELTDKFIQEMESLKTKNQVLRTE---KEKQDVYHHEH 636
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQlNQLKSEISDLN-NQKEQDWNKELKSELKNQEKKLEEIQNQisqNNKIISQLNEQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 637 IEDLldkqSRELQDMECCNNQKLLLEYEKYQELQlKSQRMQEEYEKQLRdNDETKSQALEELTEFYEAKLQEKTTLLEEA 716
Cdd:TIGR04523 344 ISQL----KKELTNSESENSEKQRELEEKQNEIE-KLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 717 QEDVRQQLREFEETKKQIEEDED------REIQDIKTKYE--KKLRDEKESNLR-LKGETGIMRKKFSSLQKEIEERTND 787
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSeikdltNQDSVKELIIKnlDNTRESLETQLKvLSRSINKIKQNLEQKQKELKSKEKE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 788 IETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKK---------KNQELGKFKFVLDYKIKELKKQI 858
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQ 577
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902638 859 EPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHN 930
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
541-1041 |
2.17e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 71.68 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 541 KDGRGIKREReVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEyQLRLKdmnYSEKIKELTDkFIQEMESLKTKNQ 620
Cdd:pfam05483 85 KEAEKIKKWK-VSIEAELKQKENKLQENRKIIEAQRKAIQELQFENE-KVSLK---LEEEIQENKD-LIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 621 VLR------TEKEKQDVYHHEHIEDL-------LDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDN 687
Cdd:pfam05483 159 LLKetcarsAEKTKKYEYEREETRQVymdlnnnIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 688 DETKSQALEELTEfYEAKLQEKTTLLEEAQEDVRQ---QLREFEETKKQIEEDED---REIQDIK--------------- 746
Cdd:pfam05483 239 EKQVSLLLIQITE-KENKMKDLTFLLEESRDKANQleeKTKLQDENLKELIEKKDhltKELEDIKmslqrsmstqkalee 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 747 -----TKYEKKLRDEKESNLRlkgETGIMRKKFSSLQKEIEERTNDIETL-KGEQMKLQG---VIKSLEKDIQGLKREIQ 817
Cdd:pfam05483 318 dlqiaTKTICQLTEEKEAQME---ELNKAKAAHSFVVTEFEATTCSLEELlRTEQQRLEKnedQLKIITMELQKKSSELE 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 818 ERDETIQDKEKRIYDLKK----------KNQELGKFKFVLDYKIKELKKQIEPRENEIRVMK--------------EQIQ 873
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKilaedeklldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqltaiktseehylKEVE 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 874 EMEAELENFHKQNTQLELNITELwqklratDQEMRRERQKERDLEALVKRFKTDLHNCVAyiQEPRLLKEkVRGLFEKYV 953
Cdd:pfam05483 475 DLKTELEKEKLKNIELTAHCDKL-------LLENKELTQEASDMTLELKKHQEDIINCKK--QEERMLKQ-IENLEEKEM 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 954 QRADMVEiaglntDLQQEYTRQREHLERNLatlkKKVVKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLE 1033
Cdd:pfam05483 545 NLRDELE------SVREEFIQKGDEVKCKL----DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH 614
|
....*...
gi 767902638 1034 AALKLTKK 1041
Cdd:pfam05483 615 QENKALKK 622
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
596-924 |
3.47e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 596 NYSEKIKELTDKfIQEMESLKTKNQVLRTEKEKQdvyhHEHIEDLLDKQSRELQDMEccnnQKLLLEYEKYQELQLKSQR 675
Cdd:TIGR02168 674 ERRREIEELEEK-IEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 676 mqeeYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLLEEAqEDVRQQLREfeetkkQIEEDEDR--EIQDIKTKYEKKL 753
Cdd:TIGR02168 745 ----LEERIAQLSKELTELEAEIEE-LEERLEEAEEELAEA-EAEIEELEA------QIEQLKEElkALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 754 RDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDL 833
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 834 KKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQ-NTQLELNITELWQKLRATDQEMRRERQ 912
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARR 972
|
330
....*....|..
gi 767902638 913 KERDLEALVKRF 924
Cdd:TIGR02168 973 RLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
662-925 |
3.48e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.25 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 662 EYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEeltefYEAKLQEKTTLLEEAQEDvRQQLREFEETKKQIEEDEDRE 741
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDE-----LSQELSDASRKIGEIEKE-IEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 742 IQDIktkyEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERtndietlkgEQMKLQGVIKSLEKDIQGLKREIQERDE 821
Cdd:TIGR02169 746 LSSL----EQEIENVKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 822 TIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLR 901
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
250 260
....*....|....*....|....
gi 767902638 902 ATDQEMRRERQKERDLEALVKRFK 925
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKR 916
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
547-937 |
3.76e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 547 KREREVGFAEEvLVTKTDMEEKAQvmlELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEK 626
Cdd:PTZ00121 1438 KKAEEAKKADE-AKKKAEEAKKAE---EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 627 EKQDVYHHEHIEDLLD-KQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAK 705
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 706 LQEKTTLLEEAQEDVRQQLREFEETKKQIEE-DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEER 784
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 785 TNDIETLKGEQmklqgviKSLEKDIQGLKREIQERDETIQDKeKRIYDLKKKNQELGKFKFVLDYKIKELKKQieprENE 864
Cdd:PTZ00121 1674 KKKAEEAKKAE-------EDEKKAAEALKKEAEEAKKAEELK-KKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEE 1741
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902638 865 IRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEalVKRFKTDLHNCVAYIQE 937
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIE 1812
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
563-881 |
2.94e-11 |
|
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: 67.74 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 563 TDMEEKAQVMLELKTRVEELKMENE-YQLRLKDMNYSEKIKELTDKFIQEMESLKTKN-QVLRTEKEKQDvyhhEHIEDL 640
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQsYKQEIKNLESQINDLESKIQNQEKLNQQKDEQiKKLQQEKELLE----KEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 641 LDKQSRELQDMECCNNQKLLLE--------YEKYQELQLKSqrMQEEYEKQLRDNDETKSQALEELTEFyeAKLQEKTTL 712
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKEliiknldnTRESLETQLKV--LSRSINKIKQNLEQKQKELKSKEKEL--KKLNEEKKE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 713 LEEAQEDVRQQLREFEETKKQIEEDE---DREIQDIKTKYEKKLRDEKESNLRlkgetgimrKKFSSLQKEIEERTNDIE 789
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEKkekESKISDLEDELNKDDFELKKENLE---------KEIDEKNKEIEELKQTQK 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 790 TLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMK 869
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
330
....*....|..
gi 767902638 870 EQIQEMEAELEN 881
Cdd:TIGR04523 659 NKWPEIIKKIKE 670
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
562-1093 |
5.45e-11 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 66.69 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 562 KTDMEEKAQVMLELKTRVEELKMENEYQlrlkdmnySEKIKELTDKFIQEMESLKTKNQVLRtEKEKQDVYHHEHIEDLL 641
Cdd:pfam05557 40 KRQLDRESDRNQELQKRIRLLEKREAEA--------EEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 642 DKQSRELQDMEccnnqkllleyekYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQE--- 718
Cdd:pfam05557 111 NELSELRRQIQ-------------RAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElef 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 719 DVRQQLREFEETKKQIEE-----DEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEErtndIETLKG 793
Cdd:pfam05557 178 EIQSQEQDSEIVKNSKSElaripELEKELERLR-EHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREE----AATLEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 794 EQMKLQGVIKSLEKDIQGLKREIQerdeTIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQ 873
Cdd:pfam05557 253 EKEKLEQELQSWVKLAQDTGLNLR----SPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 874 EMEAELENFHKQNTQLELnitelwQKLRATdqemrrerqKERD-LEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKY 952
Cdd:pfam05557 329 DLNKKLKRHKALVRRLQR------RVLLLT---------KERDgYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 953 VQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVvkegELHRTDYVRimQENVSLIKEINELRRELKFTRSQVYDL 1032
Cdd:pfam05557 394 AHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQE----SLADPSYSK--EEVDSLRRKLETLELERQRLREQKNEL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902638 1033 EAALKltkKVRPQEVSETEPSRDM-LSTAPTARLNEQeeTGRIIEMQRLEIQRLRDQIQEQE 1093
Cdd:pfam05557 468 EMELE---RRCLQGDYDPKKTKVLhLSMNPAAEAYQQ--RKNQLEKLQAEIERLKRLLKKLE 524
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
664-993 |
7.75e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 664 EKYQELQLKsqrmQEEYEKQLRdndetkSQALEELtefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEdedreiq 743
Cdd:COG1196 213 ERYRELKEE----LKELEAELL------LLKLREL----EAELEELEAELEELEAELEELEAELAELEAELEE------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 744 diktkyekklrdekesnlrlkgetgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETI 823
Cdd:COG1196 272 --------------------------LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 824 QDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL-WQKLRA 902
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELaAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 903 TDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRAdmvEIAGLNTDLQQEYTRQREHLERN 982
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE---ALLELLAELLEEAALLEAALAEL 482
|
330
....*....|.
gi 767902638 983 LATLKKKVVKE 993
Cdd:COG1196 483 LEELAEAAARL 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
705-1010 |
8.77e-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: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 705 KLQEKTTLLEEAQEDVrqQLREFEETKKQIEEdedreIQDIKTKYEKKlRDEKESNLRLKGEtgimrkKFSSLQKEIEER 784
Cdd:TIGR02168 214 RYKELKAELRELELAL--LVLRLEELREELEE-----LQEELKEAEEE-LEELTAELQELEE------KLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 785 TNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENE 864
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 865 IRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRlLKEK 944
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-LKEL 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902638 945 VRGLFEKyvqRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELH-RTDYVRIMQENVS 1010
Cdd:TIGR02168 439 QAELEEL---EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQaRLDSLERLQENLE 502
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
403-538 |
1.21e-10 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 64.93 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 403 LIATCSLDRSIRLWNYETNT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDD-IRSFK--EYSVRGcgeC 477
Cdd:COG2319 134 TLASGSADGTVRLWDLATGKlLRTLTGHSGAVTSVAFSPDGKLLASGSDDGtVRLWDLATGKlLRTLTghTGAVRS---V 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902638 478 SFS-NGGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKML-LTF--DDQFLLTAAEDGCLFTWKV 538
Cdd:COG2319 211 AFSpDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRsVAFspDGRLLASGSADGTVRLWDL 275
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
562-1096 |
2.34e-10 |
|
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: 64.99 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 562 KTDMEEKAQVMLELKTRVEELK--MENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDV------YH 633
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKklIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLlyldylKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 634 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKyQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLL 713
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEK-LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 714 EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKgetgimrkkfssLQKEIEERTNDIETLKG 793
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL------------QEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 794 EQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVM--KEQ 871
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 872 IQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRR--ERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLF 949
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSqkESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 950 EKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDYVRImQENVSLIKEINELRRELKFTRSQV 1029
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV-LEIDPILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902638 1030 YDLEAA--LKLTKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQVT 1096
Cdd:pfam02463 621 RAKVVEgiLKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
567-892 |
4.24e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 567 EKAQVMLELKTRVEELKMEnEYQLRLKDMNYS-EKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHIEDLLDKQS 645
Cdd:TIGR02168 210 EKAERYKELKAELRELELA-LLVLRLEELREElEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 646 R------ELQDMEccnNQKllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELtefyeAKLQEKTTLLEEAQED 719
Cdd:TIGR02168 289 ElyalanEISRLE---QQK-----QILRERLANLERQLEELEAQLEELESKLDELAEEL-----AELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 720 VRQQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETL--KGEQMK 797
Cdd:TIGR02168 356 LEAELEELEAELEELESRL-EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 798 LQGVIKSLEKDIQGLKrEIQERDETIQDKEKRIYDLKKKNQElgkfkfvldyKIKELKKQieprENEIRVMKEQIQEMEA 877
Cdd:TIGR02168 435 LKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQ----------ALDAAERE----LAQLQARLDSLERLQE 499
|
330
....*....|....*
gi 767902638 878 ELENFHKQNTQLELN 892
Cdd:TIGR02168 500 NLEGFSEGVKALLKN 514
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
665-1104 |
6.81e-10 |
|
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: 63.22 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 665 KYQELQLKSQRMQEEYE-KQLRDNDETKSQALEELTEFYEAKLQEKTTlleeaqedvRQQLREFEETKKQIEEDEDREIQ 743
Cdd:pfam05557 8 KARLSQLQNEKKQMELEhKRARIELEKKASALKRQLDRESDRNQELQK---------RIRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 744 DIKTKYEK---KLRDEKESNLRLKGETgimrkkFSSLQKEIEErtndietLKGEQMKLQGVIKSLEKDIQGLKREIQERD 820
Cdd:pfam05557 79 RLKKKYLEalnKKLNEKESQLADAREV------ISCLKNELSE-------LRRQIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 821 ETIQDKEKRIYDLKKKNQELGkfkfVLDYKIKELKKQIEPRENEIRVMK------EQIQEMEAELENFHKQNTQL-ELNI 893
Cdd:pfam05557 146 AKASEAEQLRQNLEKQQSSLA----EAEQRIKELEFEIQSQEQDSEIVKnskselARIPELEKELERLREHNKHLnENIE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 894 TELWQKLRATDQEMRRERQKER-----DLEALVKRFKTDLHNCVAYIQEPRL---LKEKVRGLFEKYVQR--ADMVEIAG 963
Cdd:pfam05557 222 NKLLLKEEVEDLKRKLEREEKYreeaaTLELEKEKLEQELQSWVKLAQDTGLnlrSPEDLSRRIEQLQQReiVLKEENSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 964 LNTDLQQEYTRQREhLERNLATLKKKVVKEG-ELHRTD-YVRIMQENVSLI-KEINELRRELKFTRSQVYDLEAALKLTK 1040
Cdd:pfam05557 302 LTSSARQLEKARRE-LEQELAQYLKKIEDLNkKLKRHKaLVRRLQRRVLLLtKERDGYRAILESYDKELTMSNYSPQLLE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 1041 KVRP-----QEV---------------SETEPSRDMLSTA---------------PTARLNEQEETGRIIEMQRLEIQRL 1085
Cdd:pfam05557 381 RIEEaedmtQKMqahneemeaqlsvaeEELGGYKQQAQTLerelqalrqqesladPSYSKEEVDSLRRKLETLELERQRL 460
|
490
....*....|....*....
gi 767902638 1086 RDQIQEQEQVTGFHTLAGV 1104
Cdd:pfam05557 461 REQKNELEMELERRCLQGD 479
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
665-988 |
1.54e-09 |
|
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: 62.50 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 665 KYQELQlKSQRMQEEYEKQLRDNDETKSQALEELTEFYEaKLQEKTTLLEEAQEdvrqqLREFEETKKQieededrEIQD 744
Cdd:pfam01576 10 KEEELQ-KVKERQQKAESELKELEKKHQQLCEEKNALQE-QLQAETELCAEAEE-----MRARLAARKQ-------ELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 745 IKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGL----------KR 814
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLedqnsklskeRK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 815 EIQER-------------------------DETIQDKEKRIYDLKKKNQELGKFKFVLD--------------YKIKELK 855
Cdd:pfam01576 156 LLEERiseftsnlaeeeekakslsklknkhEAMISDLEERLKKEEKGRQELEKAKRKLEgestdlqeqiaelqAQIAELR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 856 KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCV--- 932
Cdd:pfam01576 236 AQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLdtt 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902638 933 AYIQEPRLLKEKVRGLF------EKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKK 988
Cdd:pfam01576 316 AAQQELRSKREQEVTELkkaleeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
546-1022 |
1.81e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 546 IKREREVGFAEEVLVTKTDMEEKAQVMLELKtRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTE 625
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 626 KEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQAleeltefYEAK 705
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA-------EEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 706 LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlrlkgetgimRKKFSSLQKEIEERT 785
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE------------KKKIAHLKKEEEKKA 1770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 786 NDIETLKgeqmklQGVIKslekdiQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfvldykikelkkqieprENEI 865
Cdd:PTZ00121 1771 EEIRKEK------EAVIE------EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK-------------------EGNL 1819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 866 RVMKEQIQEMEAELENFHKQNTQLElNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNcvayIQEPRLLKEKV 945
Cdd:PTZ00121 1820 VINDSKEMEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE----IEEADEIEKID 1894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 946 RGLFEKYVQRADMveiAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELH------RTDYVRIMQENVSLIKEINELR 1019
Cdd:PTZ00121 1895 KDDIEREIPNNNM---AGKNNDIIDDKLDKDEYIKRDAEETREEIIKISKKDmcindfSSKFCDYMKDNISSGNCSDEER 1971
|
...
gi 767902638 1020 REL 1022
Cdd:PTZ00121 1972 KEL 1974
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
386-540 |
2.40e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 60.70 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 386 PLHSAPITGLATCIRKPLIATCSLDRSIRLWNYETN-TLELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNL----L 459
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGlLLRTLTGHTGAVRSVAFSPDGKTLASGSADGtVRLWDLatgkL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 460 IDDIRSFKE--YSVrgcgecSFSNGGHLFAAVNG-NVIHVYTTTSLENISSLKGHTGKML-LTF--DDQFLLTAAEDGcl 533
Cdd:COG2319 155 LRTLTGHSGavTSV------AFSPDGKLLASGSDdGTVRLWDLATGKLLRTLTGHTGAVRsVAFspDGKLLASGSADG-- 226
|
....*..
gi 767902638 534 fTWKVFD 540
Cdd:COG2319 227 -TVRLWD 232
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
556-880 |
3.55e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.29 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 556 EEVLVTKTDMEEKAQVMLELKTRVEElkmeneyQLRLKDMNYSE--KIKELTDKFIQEMESLKTKNQVLRT-----EKEK 628
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASLQE-------KERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRNvqtecEALK 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 629 QDVYHHEHIEDLLDKQSRELQDMECCNNQKL-LLEYEKYQ-ELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAkl 706
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTAgAMQVEKAQlEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL-- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 707 qEKTTLLEEAQEDVRQqLREFEETKKQI--EEDEDR-EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 783
Cdd:pfam15921 633 -EKVKLVNAGSERLRA-VKDIKQERDQLlnEVKTSRnELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 784 RTNDIETLKGEQ-------MKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKK 856
Cdd:pfam15921 711 TRNTLKSMEGSDghamkvaMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
330 340
....*....|....*....|....
gi 767902638 857 QIEPRENEIRVMKEQIQEMEAELE 880
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEVALD 814
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
570-1097 |
4.35e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.90 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 570 QVMLELKTRVEELKMENE--YQLRLKDMNYSEKIKELTDKFIQEMESLK-----------TKNQVLRT------------ 624
Cdd:pfam15921 110 QSVIDLQTKLQEMQMERDamADIRRRESQSQEDLRNQLQNTVHELEAAKclkedmledsnTQIEQLRKmmlshegvlqei 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 625 --------EKEKQDVYHHEHIEDL--------LDKQSRELQ--------------------DMECCNNQKLLLEYEKYQE 668
Cdd:pfam15921 190 rsilvdfeEASGKKIYEHDSMSTMhfrslgsaISKILRELDteisylkgrifpvedqlealKSESQNKIELLLQQHQDRI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 669 LQLKSQR---------------------------MQEE-------YEKQLRDNDETKSQALEELTE---FYEAKLQ--EK 709
Cdd:pfam15921 270 EQLISEHeveitgltekassarsqansiqsqleiIQEQarnqnsmYMRQLSDLESTVSQLRSELREakrMYEDKIEelEK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 710 TTLLEEAQ-EDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDI 788
Cdd:pfam15921 350 QLVLANSElTEARTERDQFSQESGNLDDQLQKLLADLH-KREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 789 EtlkgeqmKLQGVIKSLEKDIQGlkrEIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKEL---KKQIEPRENEI 865
Cdd:pfam15921 429 Q-------RLEALLKAMKSECQG---QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTV 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 866 RVMKEQIQEMEAELENFHKQNTQLELNITELWQKLratdQEMRRERQKERDLEALVKRFKTDLHNCVAYIQeprLLKEKV 945
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL----QHLKNEGDHLRNVQTECEALKLQMAEKDKVIE---ILRQQI 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 946 RGLFEKYVQR-----ADMVEIAGLNTDLQ------QEYTRQREHLERNLATLKKKvVKEGELHRTDYVRIMQENVSLIKE 1014
Cdd:pfam15921 572 ENMTQLVGQHgrtagAMQVEKAQLEKEINdrrlelQEFKILKDKKDAKIRELEAR-VSDLELEKVKLVNAGSERLRAVKD 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 1015 I----NELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIE-MQRLEIQRLRDQI 1089
Cdd:pfam15921 651 IkqerDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKsMEGSDGHAMKVAM 730
|
....*...
gi 767902638 1090 QEQEQVTG 1097
Cdd:pfam15921 731 GMQKQITA 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
734-1102 |
5.27e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 734 IEEDEDRE--------IQDIKTKYEKKLRDEKESNLRLKG-ETGIMRKkfSSLQKEIEERTNDIETLKGEQMKLQGVIKS 804
Cdd:PRK03918 141 LESDESREkvvrqilgLDDYENAYKNLGEVIKEIKRRIERlEKFIKRT--ENIEELIKEKEKELEEVLREINEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 805 LEKDIQGLKREIQERDETiqdKEKrIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEaELENFHK 884
Cdd:PRK03918 219 LREELEKLEKEVKELEEL---KEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 885 QNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKrfktDLHNCVAYIQEprlLKEKVRGLFEKYvqrADMVEIAGL 964
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEE---LKKKLKELEKRL---EELEERHEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 965 NTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAAlKLTKKVRP 1044
Cdd:PRK03918 364 YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA-KGKCPVCG 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 1045 QEVSETEPSRDMLS-TAPTARL-NEQEETGRIIEMQRLEIQRLRDQIQEQEQVTGFHTLA 1102
Cdd:PRK03918 443 RELTEEHRKELLEEyTAELKRIeKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA 502
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
599-937 |
5.47e-09 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 60.36 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 599 EKIKELTDKFIQEMESLKTKN-QVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQ 677
Cdd:COG5185 159 GIIKDIFGKLTQELNQNLKKLeIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGF 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 678 EEYEKQLRDNDETK---SQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLR 754
Cdd:COG5185 239 QDPESELEDLAQTSdklEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 755 DEKESN-----LRLKGETGIMR------KKFSSLQKEIEERTNDIETLKGEQM--KLQGVIKSLEKDIQGLKREIQERDE 821
Cdd:COG5185 319 AAAEAEqeleeSKRETETGIQNltaeieQGQESLTENLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 822 TIQDKEKRIydlkkkNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELE-NFHKQNTQLELNITELWQKL 900
Cdd:COG5185 399 NQRGYAQEI------LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNkVMREADEESQSRLEEAYDEI 472
|
330 340 350
....*....|....*....|....*....|....*...
gi 767902638 901 RATDQEMRRERQKER-DLEALVKRFKTDLHNCVAYIQE 937
Cdd:COG5185 473 NRSVRSKKEDLNEELtQIESRVSTLKATLEKLRAKLER 510
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
678-1091 |
9.00e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 678 EEYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLlEEAQEDVRQQLREFEETKkqieEDEDREIQDIKTKYEKkLRDEK 757
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEE-HEERREELETL-EAEIEDLRETIAETERER----EELAEEVRDLRERLEE-LEEER 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 758 ESnlrLKGETGimrkkFSSLqkeieertnDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKN 837
Cdd:PRK02224 296 DD---LLAEAG-----LDDA---------DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 838 QELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENfhkQNTQLElNITELWQKLRATDQEMrreRQKERDL 917
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD---APVDLG-NAEDFLEELREERDEL---REREAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 918 EAlvkrfktDLHNCVAYIQEPR-LLKEKVRGLFEKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGEL 996
Cdd:PRK02224 432 EA-------TLRTARERVEEAEaLLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 997 HRT-DYVRIMQENVSLIKE--------INELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTAPTAR--L 1065
Cdd:PRK02224 505 VEAeDRIERLEERREDLEEliaerretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaeL 584
|
410 420
....*....|....*....|....*.
gi 767902638 1066 NEQEETGRIIEMQRLEIQRLRDQIQE 1091
Cdd:PRK02224 585 KERIESLERIRTLLAAIADAEDEIER 610
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
684-926 |
1.07e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.26 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 684 LRDNDETKSQA-LEELTEFY-EAKLQEKTTLLEEAQEDVRQQLrefEETKKQIEEDEdREIQDIKTKYekklrdekeSNL 761
Cdd:COG3206 142 YTSPDPELAAAvANALAEAYlEQNLELRREEARKALEFLEEQL---PELRKELEEAE-AALEEFRQKN---------GLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 762 RLKGETGIMRKKFSSLQKEIEErtndietLKGEQMKLQGVIKSLEKDIQGLKREIQE--RDETIQDKEKRIYDLKKKNQE 839
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAE-------ARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 840 LGKfKFVLDY-KIKELKKQIEPRENEIRVMKEQI-QEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDL 917
Cdd:COG3206 282 LSA-RYTPNHpDVIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
....*....
gi 767902638 918 EALVKRFKT 926
Cdd:COG3206 361 EVARELYES 369
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
607-1094 |
1.48e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 607 KFIQEMESLKTKNQVLRTEKEKQDVYHHehIEDLLDKQSRELQDMEccnnqkllleyEKYQELQLKSQRMqeEYEKQLRD 686
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAE--LQEELEELEEELEELE-----------AELEELREELEKL--EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 687 NDETKSQALEELTEFYE--AKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEdedrEIQDIKTKYEKKLRDEKESNLRLK 764
Cdd:COG4717 130 LYQELEALEAELAELPErlEELEERLEELRELEEELEELEAELAELQEELEE----LLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 765 GETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQgVIKSLEK------------DIQGLKREIQERDETIQDKEKRIYD 832
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEarlllliaaallALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 833 LkkknqeLGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMR--RE 910
Cdd:COG4717 285 L------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLReaEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 911 RQKERDLEALVKRFKTDLHNCVAyiqeprllkekvrGLFEKYVQRADMVEIaglntdlQQEYTRQREHLERNLATLKKKV 990
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGV-------------EDEEELRAALEQAEE-------YQELKEELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 991 vkEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRpqEVSETEPSRDMLStaptARLNEQEE 1070
Cdd:COG4717 419 --EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG--ELAELLQELEELK----AELRELAE 490
|
490 500
....*....|....*....|....
gi 767902638 1071 TGRIIEMQRLEIQRLRDQIQEQEQ 1094
Cdd:COG4717 491 EWAALKLALELLEEAREEYREERL 514
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
607-1094 |
1.52e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 607 KFIQEM--ESLKTKNQVLRTEKEKQDVYHHEHIEDLlDKQSRELQDmeccnnqklllEYEKYQELQLKSQRMQEEYE--K 682
Cdd:COG4717 41 AFIRAMllERLEKEADELFKPQGRKPELNLKELKEL-EEELKEAEE-----------KEEEYAELQEELEELEEELEelE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 683 QLRDNDETKSQALEELTEFYEA-----KLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDrEIQDIKTKYEKKLRDek 757
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLyqeleALEAELAELPERLEELEERLEELRELEEELEELEA-ELAELQEELEELLEQ-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 758 eSNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKD--IQGLKREIQERDET---------IQDK 826
Cdd:COG4717 186 -LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEleAAALEERLKEARLLlliaaallaLLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 827 EKRIYDLKKKNQELGK--------FKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQ 898
Cdd:COG4717 265 GGSLLSLILTIAGVLFlvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 899 KLRATDQEMR--RERQKERDLEALVKRFKTDLHNCVAyiqeprllkekvrGLFEKYVQRADMVEIaglntdlQQEYTRQR 976
Cdd:COG4717 345 RIEELQELLReaEELEEELQLEELEQEIAALLAEAGV-------------EDEEELRAALEQAEE-------YQELKEEL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 977 EHLERNLATLKKKVvkEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALkltkkvrpqevsetepsrdm 1056
Cdd:COG4717 405 EELEEQLEELLGEL--EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-------------------- 462
|
490 500 510
....*....|....*....|....*....|....*...
gi 767902638 1057 lstaptarlnEQEETGRIIEMQRLEIQRLRDQIQEQEQ 1094
Cdd:COG4717 463 ----------EQLEEDGELAELLQELEELKAELRELAE 490
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
555-1034 |
1.82e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 555 AEEVLvtkTDMEEKAQVMLELKTRVEELKMENEYQLRLKDmNYSEKIKELTDkfiqEMESLKTKNQVLRTEKEKQDVyHH 634
Cdd:PRK02224 239 ADEVL---EEHEERREELETLEAEIEDLRETIAETERERE-ELAEEVRDLRE----RLEELEEERDDLLAEAGLDDA-DA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 635 EHIEDLLDKQSRELQDMEccnnqkllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQAlEELTEfyEAKLQEKTtlLE 714
Cdd:PRK02224 310 EAVEARREELEDRDEELR-----------DRLEECRVAAQAHNEEAESLREDADDLEERA-EELRE--EAAELESE--LE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 715 EAQEDVRQQLREFEETKKQIEEDEDReIQDIKTKYEK--KLRDEKESNL-RLKGETGIMRKKFSSLQK------------ 779
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRER-FGDAPVDLGNaeDFLEELREERdELREREAELEATLRTARErveeaealleag 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 780 ----------------EIEERTNDIETLKGEQMKLQGVIKSLEKDIqglkreiqERDETIQDKEKRIYDLKKKNQELGKf 843
Cdd:PRK02224 453 kcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERL--------ERAEDLVEAEDRIERLEERREDLEE- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 844 kfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQemRRERQKERdLEALvKR 923
Cdd:PRK02224 524 ------LIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKER-IESL-ER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 924 FKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADMVE-----IAGLN--------TDLQQEYTRQREHLERNLATLKKKV 990
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrerKRELEaefdeariEEAREDKERAEEYLEQVEEKLDELR 673
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 767902638 991 VKEGELHRtdyvRI-MQENVslIKEINELRRELKFTRSQVYDLEA 1034
Cdd:PRK02224 674 EERDDLQA----EIgAVENE--LEELEELRERREALENRVEALEA 712
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
668-919 |
1.93e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.23 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 668 ELQLKSQRMQEEYEkQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEdVRQQLREFEETKKQIEEDEDREIQDIKT 747
Cdd:COG1340 12 ELEEKIEELREEIE-ELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 748 KYEK--KLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIEtlkgEQMKLQGVIKSLEKDIQGLKREIQERDEtIQD 825
Cdd:COG1340 90 LREEldELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPE----EEKELVEKIKELEKELEKAKKALEKNEK-LKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 826 KEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQ 905
Cdd:COG1340 165 LRAELKELRKEAEEIHK-------KIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250
....*....|....
gi 767902638 906 EMRRERQKERDLEA 919
Cdd:COG1340 238 ELRELRKELKKLRK 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
771-928 |
2.28e-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: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 771 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfVLDYK 850
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA---ELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 851 IKELKKQI-------------------EPRENEIRVM---------KEQIQEMEAELENFHKQNTQLELNITELWQKLRA 902
Cdd:COG4942 103 KEELAELLralyrlgrqpplalllspeDFLDAVRRLQylkylaparREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180
....*....|....*....|....*.
gi 767902638 903 TDQEMRRERQKERDLEALVKRFKTDL 928
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKEL 208
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
667-864 |
2.32e-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: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 667 QELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIK 746
Cdd:COG4942 27 AELEQLQQEIAEL-EKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAELAELEKEIAELR-AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 747 TKYEKKLR--------------------DEKESNLR-LKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSL 805
Cdd:COG4942 104 EELAELLRalyrlgrqpplalllspedfLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902638 806 EKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENE 864
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
771-928 |
2.78e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.70 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 771 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIyDLKKKNQELGkfkfVLDYK 850
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-GNVRNNKEYE----ALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902638 851 IKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQK-ERDLEALVKRFKTDL 928
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEElEAEREELAAKIPPEL 176
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
546-1056 |
3.37e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 546 IKREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTE 625
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELD 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 626 KE---------------------KQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEyekyQELQLKSQRMQEEyeKQL 684
Cdd:TIGR00606 478 QElrkaerelskaeknsltetlkKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT----QMEMLTKDKMDKD--EQI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 685 RDNDETKSQALEELTEFYEAKLQEKTTL---------LEEAQEDVRQQLREFEETKKQIEEDEDREIQDIkTKYEKKLRD 755
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYFPNKKQLEDWLhskskeinqTRDRLAKLNKELASLEQNKNHINNELESKEEQL-SSYEDKLFD 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 756 -----EKESNL-RLKGETGIMRKKFSSLQKEIEERTNDIETLKGE--------------QMKLQGVIKSLEKDIQGLKRE 815
Cdd:TIGR00606 631 vcgsqDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcqrvfqtEAELQEFISDLQSKLRLAPDK 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 816 IQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITE 895
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTD 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 896 LwqklRATDQEMRRERQKERDLEALVKrfKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADmveiagLNTDLQQEYTRQ 975
Cdd:TIGR00606 791 V----TIMERFQMELKDVERKIAQQAA--KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIE------LNRKLIQDQQEQ 858
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 976 REHLERNLATLKKKVVKEGE-LHRTDyvRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSR 1054
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTnLQRRQ--QFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN 936
|
..
gi 767902638 1055 DM 1056
Cdd:TIGR00606 937 KK 938
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
821-1037 |
6.53e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 821 ETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKL 900
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 901 ratdqemrrERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGL-FEKYVQRADMVEIAGLNTDlQQEYTRQREHL 979
Cdd:COG4942 100 ---------EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqYLKYLAPARREQAEELRAD-LAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902638 980 ERNLATLkKKVVKEGELHRTDYVRIMQENVSLI----KEINELRRELKFTRSQVYDLEAALK 1037
Cdd:COG4942 170 EAERAEL-EALLAELEEERAALEALKAERQKLLarleKELAELAAELAELQQEAEELEALIA 230
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
574-985 |
6.74e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.98 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 574 ELKTRVEELKMENEYQLRLKDMNYSEkikelTDKFIQEMESLKTKNQVLRTE--KEKQDVyhhEHIEDLLDKQSRELQDM 651
Cdd:TIGR00606 713 STESELKKKEKRRDEMLGLAPGRQSI-----IDLKEKEIPELRNKLQKVNRDiqRLKNDI---EEQETLLGTIMPEEESA 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 652 ECCnnqklLLEYEKYQELQLKSQRMQEEYEKQLRDNDETksqaleELTEFYEAKLQEKttllEEAQEDVRQQLREFEETK 731
Cdd:TIGR00606 785 KVC-----LTDVTIMERFQMELKDVERKIAQQAAKLQGS------DLDRTVQQVNQEK----QEKQHELDTVVSKIELNR 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 732 KQIEeDEDREIQDIKTKYeKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQgviKSLEKDIQG 811
Cdd:TIGR00606 850 KLIQ-DQQEQIQHLKSKT-NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLE---TFLEKDQQE 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 812 LKREIQERDETIQDKEKRIYDLKKK-NQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLE 890
Cdd:TIGR00606 925 KEELISSKETSNKKAQDKVNDIKEKvKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMR 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 891 LNITELWQKLR-ATDQEMRRERQKErdlealVKRFKTDLHNCVAYIQEPRLLKEKvrglfEKYVQRADMVEIAGLNTDL- 968
Cdd:TIGR00606 1005 QDIDTQKIQERwLQDNLTLRKRENE------LKEVEEELKQHLKEMGQMQVLQMK-----QEHQKLEENIDLIKRNHVLa 1073
|
410 420
....*....|....*....|
gi 767902638 969 ---QQEYTRQREHLERNLAT 985
Cdd:TIGR00606 1074 lgrQKGYEKEIKHFKKELRE 1093
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
548-880 |
8.02e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 56.65 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 548 REREVGFAE-EVLVTKTDMEEKAQVMLELKTRVEELKMENeyqlrLKDMNYSEKIKELTDKFIQEmeslkTKNQVLRTEK 626
Cdd:pfam05483 448 REKEIHDLEiQLTAIKTSEEHYLKEVEDLKTELEKEKLKN-----IELTAHCDKLLLENKELTQE-----ASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 627 EKQDVYHHEHIEDLLDKQSRELQdmeccnnqkllleyEKYQELQLKSQRMQEEYeKQLRDNDETKSQALEELTEFYEAKL 706
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLE--------------EKEMNLRDELESVREEF-IQKGDEVKCKLDKSEENARSIEYEV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 707 QEKTTLLEEAQEDVRQQLREFEETKKQIEE--DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSL----QKE 780
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEElhQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIidnyQKE 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 781 IEERTNDIETLKGEQMKLQGVIKS---LEKDIQG------------LKREIQERDETIQDKEKRIYDLKKKNQELGKFKF 845
Cdd:pfam05483 663 IEDKKISEEKLLEEVEKAKAIADEavkLQKEIDKrcqhkiaemvalMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKA 742
|
330 340 350
....*....|....*....|....*....|....*
gi 767902638 846 VLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELE 880
Cdd:pfam05483 743 ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
566-892 |
1.65e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 566 EEKAQVMLELKTRVEELkMENEYQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLRTEKEKqdvyhhEHIEDLLDKQS 645
Cdd:PRK03918 387 EKLEKELEELEKAKEEI-EEEISKITARIGELKKEIKEL-KKAIEELKKAKGKCPVCGRELTE------EHRKELLEEYT 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 646 RELQDMEccNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQ---ALEELTEFYEAKLQEKTTLLEEAQEDVRQ 722
Cdd:PRK03918 459 AELKRIE--KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkeLEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 723 QLREFEETKKQIEEDEdrEIQDIKTKYEKKLRDEKESNLRLKGEtgIMRKKFSSLqKEIEERTNDIETLKGEQMKLQGV- 801
Cdd:PRK03918 537 LKGEIKSLKKELEKLE--ELKKKLAELEKKLDELEEELAELLKE--LEELGFESV-EELEERLKELEPFYNEYLELKDAe 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 802 --IKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDY------------------------------ 849
Cdd:PRK03918 612 keLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYeelreeylelsrelaglraeleelekrree 691
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 767902638 850 ------KIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELN 892
Cdd:PRK03918 692 ikktleKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
703-1093 |
2.29e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 703 EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReiqdiKTKYEkKLRDEKESNLRLKgetgimrkkfsSLQKEIE 782
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-----REALQ-RLAEYSWDEIDVA-----------SAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 783 ERTNDIETLKGEQmklqgviksleKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELgkfkfvldykikelkkqieprE 862
Cdd:COG4913 672 ELEAELERLDASS-----------DDLAALEEQLEELEAELEELEEELDELKGEIGRL---------------------E 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 863 NEIRVMKEQIQEMEAELENF-HKQNTQLELNITELWQKLRATdqemRRERQKERDLEALVKRFKTDLHNcvayiqeprlL 941
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALGD----AVERELRENLEERIDALRARLNR----------A 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 942 KEKVRGLFEKYVQRADMvEIAGLNTDL------QQEYTR-QREHLERNLATLKKKVVKEGELHRTDYVRIMQENVSLIKE 1014
Cdd:COG4913 786 EEELERAMRAFNREWPA-ETADLDADLeslpeyLALLDRlEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKE 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 1015 ----INELRRELKFTRSQVYDLEAalkltKKVRPQEVSETepsRDMLStapTARLNEQEETGRIIEMQRLEIQRLRDQIQ 1090
Cdd:COG4913 865 ridpLNDSLKRIPFGPGRYLRLEA-----RPRPDPEVREF---RQELR---AVTSGASLFDEELSEARFAALKRLIERLR 933
|
...
gi 767902638 1091 EQE 1093
Cdd:COG4913 934 SEE 936
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
687-884 |
2.36e-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: 53.91 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 687 NDETKSQALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEetkKQIEEDEDrEIQDIKTKYEKKLRDEKESnlrlkge 766
Cdd:cd22656 108 DDEELEEAKKTIKALLD-DLLKEAKKYQDKAAKVVDKLTDFE---NQTEKDQT-ALETLEKALKDLLTDEGGA------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 767 tgIMRKKFSSLQKEIEERTNDIetlkgeqmklqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKknqelgkfkfv 846
Cdd:cd22656 176 --IARKEIKDLQKELEKLNEEY-------------AAKLKAKIDELKALIADDEAKLAAALRLIADLTA----------- 229
|
170 180 190
....*....|....*....|....*....|....*...
gi 767902638 847 LDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHK 884
Cdd:cd22656 230 ADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKD 267
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
684-925 |
2.94e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 684 LRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQedvrQQLREFEETKKQIEEDEDREIqdiktkYEKKLRDEKESNLRL 763
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQKNGLVDLSEEAKL------LLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 764 KGETGIMRKKFSSLQKEIEERTNDIETLKGEQmklqgVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKF 843
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 844 KFvldykiKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLelnitelwQKLRATDQEMRRERQKERDL-EALVK 922
Cdd:COG3206 307 LQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL--------PELEAELRRLEREVEVARELyESLLQ 372
|
...
gi 767902638 923 RFK 925
Cdd:COG3206 373 RLE 375
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
704-830 |
4.37e-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: 52.23 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 704 AKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKL---RDEKESNlRLKGETGIMRKKFSSLQKE 780
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLgnvRNNKEYE-ALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767902638 781 IEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI 830
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
692-923 |
5.36e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 692 SQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIktkyEKKLRDekesnlrLKGETGIMR 771
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-RRIAAL----ARRIRA-------LEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 772 KKFSSLQKEIEERTNDIETLKGEqmkLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKI 851
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902638 852 KELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKR 923
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
735-1091 |
5.59e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 735 EEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKR 814
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 815 EIQERDETIQDKEKRIYDLKKKnqelgkfkfvldykIKELKKQIEPRENEIRvmKEQIQEMEAELENFHKQNTQLELNIT 894
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEED--------------LHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 895 ELWQKLRATDQEMRRERQKERDLEALVkrfktdlhncvayiqeprllkekvrglfekyvqradmveiagLNTDLQQEYTR 974
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQR------------------------------------------IDLKEQIKSIE 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 975 QREHLernlatlkkkvvkegelhrtdyvrimqenvsLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQ---EVSETE 1051
Cdd:TIGR02169 854 KEIEN-------------------------------LNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELE 902
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 767902638 1052 PSRDMLSTA---PTARLNEQEETGRIIEMQRLEIQRLRDQIQE 1091
Cdd:TIGR02169 903 RKIEELEAQiekKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
578-1094 |
5.79e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 578 RVEELKMENEYQLRLKDMNysEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHhEHIEDLLDKQSRELQDMECCNNQ 657
Cdd:TIGR02168 325 LEELESKLDELAEELAELE--EKLEELKEELESLEAELEELEAELEELESRLEELE-EQLETLRSKVAQLELQIASLNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 658 KLLLEYEKyQELQLKSQRMQEEYEKQLRDNDETKSQALE---ELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQI 734
Cdd:TIGR02168 402 IERLEARL-ERLEDRRERLQQEIEELLKKLEEAELKELQaelEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 735 EEDEDR------EIQDIKTKYEKKLRDEKE---SNLRLKGETGIMRKKFS---SLQKEIE----ERTNDIETlKGEQMKL 798
Cdd:TIGR02168 481 ERELAQlqarldSLERLQENLEGFSEGVKAllkNQSGLSGILGVLSELISvdeGYEAAIEaalgGRLQAVVV-ENLNAAK 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 799 QGvIKSLEK-----------------DIQGLKREIQERDETIQDKEKRIY---------------------------DLK 834
Cdd:TIGR02168 560 KA-IAFLKQnelgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVkfdpklrkalsyllggvlvvddldnalELA 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 835 KKNQELGKFkFVLD------------------YKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNI--- 893
Cdd:TIGR02168 639 KKLRPGYRI-VTLDgdlvrpggvitggsaktnSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELeql 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 894 ----TELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEkyvqrADMVEIAGLNTDLQ 969
Cdd:TIGR02168 718 rkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----EAEAEIEELEAQIE 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 970 QeYTRQREHLERNLATLKKKVvkegELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKvrpqEVSE 1049
Cdd:TIGR02168 793 Q-LKEELKALREALDELRAEL----TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA----EIEE 863
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 767902638 1050 TEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQ 1094
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
589-1049 |
9.02e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 589 QLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLRTEKEK--QDVYHHEHIEDLLDKQsRELQDMEccnnqkllLEYEKY 666
Cdd:COG4717 82 EAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKleKLLQLLPLYQELEALE-AELAELP--------ERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 667 QELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEdVRQQLREFEETKKQIEEDEDREIQDIK 746
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE-LQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 747 TKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVI-KSLEKDIQGLKREIQERDETIQD 825
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLaLLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 826 KEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEpRENEIRVMKEQIQEMEAELenfhkQNTQLELNITELWQKLRATDQ 905
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLD-RIEELQELLREAEELEEEL-----QLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 906 EMRRERQKE-RDLEALVKRFktdlhncvayiqepRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQQ------EYTRQREH 978
Cdd:COG4717 385 EELRAALEQaEEYQELKEEL--------------EELEEQLEELLGELEELLEALDEEELEEELEEleeeleELEEELEE 450
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767902638 979 LERNLATLKKKVvkEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSE 1049
Cdd:COG4717 451 LREELAELEAEL--EQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLE 519
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
689-925 |
1.89e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 689 ETKSQALEELTEFYeAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED-----REIQDIktkyEKKLRDEKESNLRL 763
Cdd:COG4913 613 AALEAELAELEEEL-AEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAEL----EAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 764 KGetgimrkkfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI-----YDLKKKNQ 838
Cdd:COG4913 688 AA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 839 ELGKFKFVldykiKELKKQIeprENEIRVMKEQIQEMEAELEN-FHKQNTQLELNITELWQKLRATDQ-EMRRERQKERD 916
Cdd:COG4913 757 AALGDAVE-----RELRENL---EERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLESLPEyLALLDRLEEDG 828
|
....*....
gi 767902638 917 LEALVKRFK 925
Cdd:COG4913 829 LPEYEERFK 837
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
637-1095 |
2.10e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.21 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 637 IEDLLDKQSRELQDMEccNNQKLLLEYEKYQELQLKS-QRMQEEYEKQLRDNDETKSQ-----ALEELTEFYEAKLQEKT 710
Cdd:PRK01156 185 IDYLEEKLKSSNLELE--NIKKQIADDEKSHSITLKEiERLSIEYNNAMDDYNNLKSAlnelsSLEDMKNRYESEIKTAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 711 TLLEEAQEDVrQQLREFEETKKQIEEDE---DREIQDIKTKYEKKLRDEKESNLRLKGETG----IMRK---------KF 774
Cdd:PRK01156 263 SDLSMELEKN-NYYKELEERHMKIINDPvykNRNYINDYFKYKNDIENKKQILSNIDAEINkyhaIIKKlsvlqkdynDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 775 SSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKdiqgLKREIQERDETIQDKEKRIYDLKKKN----QELGKFKFVLDYK 850
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIES----LKKKIEEYSKNIERMSAFISEILKIQeidpDAIKKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 851 IKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNT----QLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKT 926
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 927 DLHNCVAyiQEPRLLKEKVRGLFEKYVQRADMVeiAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELH--RTDYVRI 1004
Cdd:PRK01156 498 KIVDLKK--RKEYLESEEINKSINEYNKIESAR--ADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDskRTSWLNA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 1005 MQEnVSLI------KEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTaptaRLNEQEETGRIIEMQ 1078
Cdd:PRK01156 574 LAV-ISLIdietnrSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNN----KYNEIQENKILIEKL 648
|
490
....*....|....*..
gi 767902638 1079 RLEIQRLRDQIQEQEQV 1095
Cdd:PRK01156 649 RGKIDNYKKQIAEIDSI 665
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
713-877 |
3.12e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.40 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 713 LEEAQEDVRQQLREFEETKKQIEEDEDREIQdikTKYEKKLRdekesnlrlkgetgimrkkfsslqkeieertndietlk 792
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEEREL---TEEEEEIR-------------------------------------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 793 geqmKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK-NQELGKFKFV--LDYKIKELKKQIEPRENEIRVMK 869
Cdd:COG2433 417 ----RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEeRREIRKDREIsrLDREIERLERELEEERERIEELK 492
|
....*...
gi 767902638 870 EQIQEMEA 877
Cdd:COG2433 493 RKLERLKE 500
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
660-899 |
3.14e-06 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 50.58 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 660 LLEYEKYQELQLKSQRMQEEYEKQLRD------NDETKSQALEELTEFYEAKLQ----EKTTLLEEAQEdVRQQLREF-- 727
Cdd:pfam15905 58 SLELKKKSQKNLKESKDQKELEKEIRAlvqergEQDKRLQALEEELEKVEAKLNaavrEKTSLSASVAS-LEKQLLELtr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 728 -----------EETKKQIE-------------EDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 783
Cdd:pfam15905 137 vnellkakfseDGTQKKMSslsmelmklrnklEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 784 RTNDIETLKGEQMKLQGVIKSLEKdiqgLKREIQERDETiqdkekriydLKKKNQELGKFKFVLDYKIKELKKQIEPR-- 861
Cdd:pfam15905 217 EKSETEKLLEYITELSCVSEQVEK----YKLDIAQLEEL----------LKEKNDEIESLKQSLEEKEQELSKQIKDLne 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767902638 862 ---------ENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQK 899
Cdd:pfam15905 283 kckllesekEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
557-989 |
3.40e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.33 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 557 EVLVTKTDMEEKAQVMLELKTRVEelKMENEYQLRLKdmnysekiKEltDKFIQEMESLKTKNQVLRTEKEKQDVYHHEH 636
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHE--AMISDLEERLK--------KE--EKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 637 IEDL---LDKQSRELQ------DMECCNNQKLLleyEKYQELQLKSQRMQE--EYEKQLRDNDETKSQALEELTEFYEAK 705
Cdd:pfam01576 231 IAELraqLAKKEEELQaalarlEEETAQKNNAL---KKIRELEAQISELQEdlESERAARNKAEKQRRDLGEELEALKTE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 706 LqEKTTLLEEAQEDVR-QQLREFEETKKQIEED---EDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEI 781
Cdd:pfam01576 308 L-EDTLDTTAAQQELRsKREQEVTELKKALEEEtrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 782 EERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPR 861
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 862 ENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLratDQEMRRERQKERDLEALV-------KRFKTDLHNCVAY 934
Cdd:pfam01576 467 ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQL---EEEEEAKRNVERQLSTLQaqlsdmkKKLEEDAGTLEAL 543
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902638 935 IQEPRLLKEKVRGLFEKYVQRADMVE-IAGLNTDLQQEY---TRQREHLERNLATLKKK 989
Cdd:pfam01576 544 EEGKKRLQRELEALTQQLEEKAAAYDkLEKTKNRLQQELddlLVDLDHQRQLVSNLEKK 602
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
743-964 |
3.48e-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: 50.53 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 743 QDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDET 822
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 823 IQDKEKRIYDLKKKNQELGK---FKFVLD-------YKIKELKKQIEP-RENEIRVMKEQIQEMEAELENFHKQNTQLEL 891
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRqppLALLLSpedfldaVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902638 892 NITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLhncVAYIQEPRLLKEKVRGLFEKYVQRADMVEIAGL 964
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
721-881 |
3.70e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 721 RQQLREFEETKKQIEEDEDREIQDIKtkyEKKLRDEKESNLRLKGEtgimrkkfssLQKEIEERtndietlkgeqmklqg 800
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIK---KEALLEAKEEIHKLRNE----------FEKELRER---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 801 vikslEKDIQGLKREIQERDETIqdkEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEpreneirVMKEQIQEMEAELE 880
Cdd:PRK12704 81 -----RNELQKLEKRLLQKEENL---DRKLELLEKREEELEKKEKELEQKQQELEKKEE-------ELEELIEEQLQELE 145
|
.
gi 767902638 881 N 881
Cdd:PRK12704 146 R 146
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
771-919 |
5.76e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 771 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIqdkEKRIYDLKKKNQELGKFKFVL--- 847
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGSVSYLDVLLgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 848 ---DY-------------------KIKELKKQIEPRENEIRVMKEQIQEMEAELEnfhKQNTQLELNITELWQKLRATDQ 905
Cdd:COG3883 113 sfsDFldrlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELE---AAKAELEAQQAEQEALLAQLSA 189
|
170
....*....|....
gi 767902638 906 EMRRERQKERDLEA 919
Cdd:COG3883 190 EEAAAEAQLAELEA 203
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
762-1036 |
6.19e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 762 RLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELG 841
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 842 KFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFhkQNTQLELNITELWQKLRATDQEMRRERQKERDLEALV 921
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 922 KRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDY 1001
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
250 260 270
....*....|....*....|....*....|....*
gi 767902638 1002 VRIMQENVSLIKEINELRRELKFTRSQVYDLEAAL 1036
Cdd:COG4372 287 ALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
677-1023 |
6.45e-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: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 677 QEEYEKQLRDNDETKSQALEeLTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEdreiqdiktKYEKKLRDE 756
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE---------TLLGTIMPE 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 757 KESNLRLKGETGIMRKkfssLQKEIEERTNDIETLKGeqmKLQGVikSLEKDIQGLKREIQERDET-------------- 822
Cdd:TIGR00606 781 EESAKVCLTDVTIMER----FQMELKDVERKIAQQAA---KLQGS--DLDRTVQQVNQEKQEKQHEldtvvskielnrkl 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 823 IQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRA 902
Cdd:TIGR00606 852 IQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISS 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 903 TDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRllkekvrglfEKYVQRADmVEIAGLNTDLqQEYTRQREHLERN 982
Cdd:TIGR00606 932 KETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK----------DDYLKQKE-TELNTVNAQL-EECEKHQEKINED 999
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 767902638 983 LATLKKKVVKEGELHrtdyvRIMQENVSLIK---EINELRRELK 1023
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQE-----RWLQDNLTLRKrenELKEVEEELK 1038
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
668-946 |
6.91e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.89 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 668 ELQLKSQRMQEEYeKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEaQEDVRQQLREFEEtkkqieededreiqDIKT 747
Cdd:pfam07888 77 ELESRVAELKEEL-RQSREKHEELEEKYKELSASSEELSEEKDALLAQ-RAAHEARIRELEE--------------DIKT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 748 KYEKKLrdEKESNL-RLKGETgimrKKFSSLQKEIEErtnDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDK 826
Cdd:pfam07888 141 LTQRVL--ERETELeRMKERA----KKAGAQRKEEEA---ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 827 EKRIYDLKKKNQELGKFKFVLDYKIKELK----------KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL 896
Cdd:pfam07888 212 QDTITTLTQKLTTAHRKEAENEALLEELRslqerlnaseRKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADA 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 767902638 897 WQKLRATDQEMRRERQK-----ERDLEALVKrFKTDLHNCVAYIQEPRLLKEKVR 946
Cdd:pfam07888 292 SLALREGRARWAQERETlqqsaEADKDRIEK-LSAELQRLEERLQEERMEREKLE 345
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
649-912 |
7.55e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.12 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 649 QDMECCNNQKLLLEYEKYQELQ-LKSQRMQEEYEKQLRDNDetKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREF 727
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEkMEQERLRQEKEEKAREVE--RRRKLEEAEKARQAEMDRQAAIYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 728 EETKkqiEEDEDREIQDIKTK-----------YEKKLRDEKESNLRLKGETGIMRKKF---SSLQKEIEERTNDIETLKG 793
Cdd:pfam17380 351 ERIR---QEERKRELERIRQEeiameisrmreLERLQMERQQKNERVRQELEAARKVKileEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 794 EQ-----MKLQGVIKSLEKDIQGLKREIQERDETI----QDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENE 864
Cdd:pfam17380 428 EQeearqREVRRLEEERAREMERVRLEEQERQQQVerlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767902638 865 IRVMKEQIQEMEAELENfhKQNTQLELNITELWQKLRATDQEMRRERQ 912
Cdd:pfam17380 508 MIEEERKRKLLEKEMEE--RQKAIYEEERRREAEEERRKQQEMEERRR 553
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
62-420 |
9.38e-06 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 49.52 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 62 ALSISPNRRYLAiseTVQEKPAITIYELSSIPCRKrkVLNNFDFQVQkfiSMAFSPDSKYLLAqTSppESNLVYwLWEKQ 141
Cdd:COG2319 125 SVAFSPDGKTLA---SGSADGTVRLWDLATGKLLR--TLTGHSGAVT---SVAFSPDGKLLAS-GS--DDGTVR-LWDLA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 142 KVMAIVRIDTQNNPVYQVSFSPqDNTQVcVTG--NGMFKLLRFAEGTLKQTSfqRGEPQNYLAHTWVADDK-IVVGTDTG 218
Cdd:COG2319 193 TGKLLRTLTGHTGAVRSVAFSP-DGKLL-ASGsaDGTVRLWDLATGKLLRTL--TGHSGSVRSVAFSPDGRlLASGSADG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 219 KLFLfesgdqrWETsimvkeptNGSKSLDVIQESESliefpPVSSplpsyeqmVAASSHSQMsmpqvfaiaayskgFACS 298
Cdd:COG2319 269 TVRL-------WDL--------ATGELLRTLTGHSG-----GVNS--------VAFSPDGKL--------------LASG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 299 AGPGRVLLFEkmeekdfYRESREIRIPVDPQSndpsqsdkqDVLCLCFSPSEETLVASTSKNqlysiTMSLTEISKGEPA 378
Cdd:COG2319 307 SDDGTVRLWD-------LATGKLLRTLTGHTG---------AVRSVAFSPDGKTLASGSDDG-----TVRLWDLATGELL 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 767902638 379 HFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWNYET 420
Cdd:COG2319 366 RT----LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
549-1094 |
1.54e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 549 EREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQlRLKDMNYSEKIKELTDKFIQEM----------ESLKTK 618
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-KAEDARKAEEARKAEDAKRVEIarkaedarkaEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 619 NQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQL-----KSQRMQEEYEKQLRDNDETKSQ 693
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkKAEEAKKDAEEAKKAEEERNNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 694 ALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIE---EDEDREIQDIKTKYEKKlrdEKESNLRLKGETGim 770
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakkAEEKKKADEAKKKAEEA---KKADEAKKKAEEA-- 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 771 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQErdetiqdKEKRIYDLKKKNQELgkfkfvldYK 850
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-------AKKKADAAKKKAEEK--------KK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 851 IKELKKQIEprenEIRVMKEQIQEMEAELENFHKQNTQLElnitelwQKLRAtdQEMRRERQKERDLEALVKRF--KTDL 928
Cdd:PTZ00121 1393 ADEAKKKAE----EDKKKADELKKAAAAKKKADEAKKKAE-------EKKKA--DEAKKKAEEAKKADEAKKKAeeAKKA 1459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 929 HNCVAYIQEPRLLKEKVRGLFEKyvQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKvvkeGELHRTDYVRIMQEN 1008
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEA--KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA----EEAKKADEAKKAEEA 1533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 1009 vsliKEINELRR-ELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDM-LSTAPTARLNEQEETGRIIEMQRLEIQRLR 1086
Cdd:PTZ00121 1534 ----KKADEAKKaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMaLRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
....*...
gi 767902638 1087 DQIQEQEQ 1094
Cdd:PTZ00121 1610 EEAKKAEE 1617
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
703-946 |
1.60e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 703 EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEK--KLRDEKESNLRLKGEtgiMRKKFSSLQKE 780
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEaqELREKRDELNEKVKE---LKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 781 IEERTNDIETLKGEQMKLQGV---IKSLEKDIQGLKREIQERDETIqDKEKRIYD-LKKKNQELGKFKFVLDY--KIKEL 854
Cdd:COG1340 87 LNELREELDELRKELAELNKAggsIDKLRKEIERLEWRQQTEVLSP-EEEKELVEkIKELEKELEKAKKALEKneKLKEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 855 KKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNcvaY 934
Cdd:COG1340 166 RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE---L 242
|
250
....*....|..
gi 767902638 935 IQEPRLLKEKVR 946
Cdd:COG1340 243 RKELKKLRKKQR 254
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
753-893 |
1.73e-05 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 48.43 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 753 LRDEKESNLRLKGEtgIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGV------IKSLEKDIQGLKREIQERDETIQDK 826
Cdd:pfam17060 96 IPASFISALELKED--VKSSPRSEADSLGTPIKVDLLRNLKPQESPETPrrinrkYKSLELRVESMKDELEFKDETIMEK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 827 E-------KRIYDLKKKNQELGK-FKFVLDYK-----------------IKELKKQIEPRENEIRVMKEQIQEMEAELEN 881
Cdd:pfam17060 174 DrelteltSTISKLKDKYDFLSReFEFYKQHHehggnnsiktatkhefiISELKRKLQEQNRLIRILQEQIQFDPGALHD 253
|
170
....*....|..
gi 767902638 882 FHKQNTQLELNI 893
Cdd:pfam17060 254 NGPKNLVLNGAI 265
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
771-926 |
3.02e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 771 RKKFSSLQKEIEERTnDIETLKGEQMK---LQGVIKSLEKDIQGLK-----REIQERDETIQDKEKRIYDLKKKNQELGK 842
Cdd:COG2433 349 KNKFERVEKKVPPDV-DRDEVKARVIRglsIEEALEELIEKELPEEepeaeREKEHEERELTEEEEEIRRLEEQVERLEA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 843 FKFVLDYKIKELKKQIEPRENEIRVMKEQIQE---MEAELENFHKQNTQLElnitelwqklratdQEMRRERQKERDLEA 919
Cdd:COG2433 428 EVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDREIERLE--------------RELEEERERIEELKR 493
|
....*..
gi 767902638 920 LVKRFKT 926
Cdd:COG2433 494 KLERLKE 500
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
635-923 |
3.31e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 635 EHIEDLLDKQSRElQDMECCNNQKLLLeyekyqelqlKSQRMQEEYEKQLRDNDETKSQALEELtefyeAKLQEKTTLLE 714
Cdd:TIGR00618 594 VRLQDLTEKLSEA-EDMLACEQHALLR----------KLQPEQDLQDVRLHLQQCSQELALKLT-----ALHALQLTLTQ 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 715 EAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKY----------EKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEER 784
Cdd:TIGR00618 658 ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkemlaqcQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 785 TNDIETLKGEQMKLQG-VIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPREN 863
Cdd:TIGR00618 738 EDALNQSLKELMHQARtVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 864 EIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKR 923
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
580-820 |
3.59e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 580 EELKMENEYQLRLKDMNySEKIKELTDKF---IQEMESLKT-----KNQVLRTEKEKQDVyhHEHIEDLLDKQSRELQDM 651
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKN-GENIARKQNKYdelVEEAKTIKAeieelTDELLNLVMDIEDP--SAALNKLNTAAAKIKSKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 652 ECCnnQKLLLEYEKYQELQLKSQrmqeeyekQLRDNDETKSQALEELTEfyeakLQEKTTLLEEAQEDVRQQLREFEETK 731
Cdd:PHA02562 272 EQF--QKVIKMYEKGGVCPTCTQ--------QISEGPDRITKIKDKLKE-----LQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 732 KqieededrEIQDIKTKYEKKLRDekesnlrLKGEtgimRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQG 811
Cdd:PHA02562 337 K--------KLLELKNKISTNKQS-------LITL----VDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
....*....
gi 767902638 812 LKREIQERD 820
Cdd:PHA02562 398 LVKEKYHRG 406
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
677-903 |
5.03e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 677 QEEYEKQLRDNDETKSQALEELtefyeAKLQEKttlLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYEKKlRDE 756
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAEL-----DALQAE---LEELNEEYNELQAELEALQAEIDKLQ-AEIAEAEAEIEER-REE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 757 KESNLRLKGETGIMRKKFSSL--QKEIEERTNDIETLKgeqmKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 834
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLlgSESFSDFLDRLSALS----KIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902638 835 KKNQElgkfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRAT 903
Cdd:COG3883 164 AELEA----------AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
544-844 |
5.88e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 544 RGIKREREVGFAEEVlvTKTDMEEKAQVMLELktrvEELKMENEYQLrlkdmnysEKIKEltdkfiqemESLKTKNQVLR 623
Cdd:pfam17380 310 REVERRRKLEEAEKA--RQAEMDRQAAIYAEQ----ERMAMEREREL--------ERIRQ---------EERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 624 TEKEKQDVYHHEHIEDLL----DKQSRELQDMECCNNQKLLLEyekyqELQLKSQRMQEEYEKQLRDNDETKSQALEELT 699
Cdd:pfam17380 367 QEEIAMEISRMRELERLQmerqQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQIRAEQEEARQREVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 700 EFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQ--IEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKkfsSL 777
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKklELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK---LL 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902638 778 QKEIEERTNDIetLKGEQMKLQGVIKSLEKDIQGlKREIQERDETIQDKEKRIYDLKKKNQELGKFK 844
Cdd:pfam17380 519 EKEMEERQKAI--YEEERRREAEEERRKQQEMEE-RRRIQEQMRKATEERSRLEAMEREREMMRQIV 582
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
562-983 |
6.50e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.12 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 562 KTDMEEKAQVMLELKTRVEELKMENEyqlrlkdmNYSEKIKELTdkfiqemESLKTKNQ---VLRTEKEKQDVYHHEHiE 638
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQNS--------DCKQHIEVLK-------ESLTAKEQraaILQTEVDALRLRLEEK-E 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 639 DLLDKQSRELQDMeccNNQKLLLEYE-------------KYQELQLKSQRMQEeyekQLRDNDetksQALEELTEFYEAk 705
Cdd:pfam10174 359 SFLNKKTKQLQDL---TEEKSTLAGEirdlkdmldvkerKINVLQKKIENLQE----QLRDKD----KQLAGLKERVKS- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 706 LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREiqdiktkyEKKLRDEKESnlrLKGETGIMRKKFSSLQKEIEERT 785
Cdd:pfam10174 427 LQTDSSNTDTALTTLEEALSEKERIIERLKEQRERE--------DRERLEELES---LKKENKDLKEKVSALQPELTEKE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 786 NDIETLKGEQ-------MKLQGVIKSLEKDIQgLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQI 858
Cdd:pfam10174 496 SSLIDLKEHAsslassgLKKDSKLKSLEIAVE-QKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEES 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 859 EPRENEIRVMKEQIQEMEAELENFHKQNTQLELNI-------TELWQKLRATDQEMRRERQKERDleaLVKRFKTDLHNC 931
Cdd:pfam10174 575 GKAQAEVERLLGILREVENEKNDKDKKIAELESLTlrqmkeqNKKVANIKHGQQEMKKKGAQLLE---EARRREDNLADN 651
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902638 932 VAYIQEPRLLK--EKVRGLFEKYVQRADMVEIA-----GLNTDLQQEytrQREHLERNL 983
Cdd:pfam10174 652 SQQLQLEELMGalEKTRQELDATKARLSSTQQSlaekdGHLTNLRAE---RRKQLEEIL 707
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
857-1094 |
6.95e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 857 QIEPRENEIRVmkEQIQEMEAELENFhkqNTQLEL-----NITELWQKLRATDQEMRRERQKERDLEALVKRFK------ 925
Cdd:COG3206 60 LVEPQSSDVLL--SGLSSLSASDSPL---ETQIEIlksrpVLERVVDKLNLDEDPLGEEASREAAIERLRKNLTvepvkg 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 926 TDLHNcVAYI-QEPRLLKEKVRGLFEKYVQRadmveiaglNTDLQQEYTRQ-REHLERNLATLKKKVVK-EGELH----R 998
Cdd:COG3206 135 SNVIE-ISYTsPDPELAAAVANALAEAYLEQ---------NLELRREEARKaLEFLEEQLPELRKELEEaEAALEefrqK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 999 TDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALK-LTKKVRPQEVSETEPSRDMLSTAPTARLNEQEetGRIIEM 1077
Cdd:COG3206 205 NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAaLRAQLGSGPDALPELLQSPVIQQLRAQLAELE--AELAEL 282
|
250 260
....*....|....*....|...
gi 767902638 1078 QRL------EIQRLRDQIQEQEQ 1094
Cdd:COG3206 283 SARytpnhpDVIALRAQIAALRA 305
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
748-1032 |
1.05e-04 |
|
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: 46.76 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 748 KYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIeerTNDIETLKGEQMKLQgvikSLEKDIQGLKREIQE-RDETIQDK 826
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKASREE---TFARTALKNARLDLR----RLFDEKQSEKDKKNKaLAERKDSA 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 827 EKRIYDLKKKnqelgkfKFVLDYKIKELKKQIEPRENEIRV-MKEQIQEMEAELENFHKQ-NTQLELNITELWQKLRATD 904
Cdd:pfam12128 681 NERLNSLEAQ-------LKQLDKKHQAWLEEQKEQKREARTeKQAYWQVVEGALDAQLALlKAAIAARRSGAKAELKALE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 905 QEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLF----EKYVQRADMVEIAGLNT-----DLQQEYTRQ 975
Cdd:pfam12128 754 TWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFdwyqETWLQRRPRLATQLSNIeraisELQQQLARL 833
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902638 976 -------REHLERNLATLKKKVVKEGELHRTdyVRIMQENVSLIKE---INELRRELKFTRSQVYDL 1032
Cdd:pfam12128 834 iadtklrRAKLEMERKASEKQQVRLSENLRG--LRCEMSKLATLKEdanSEQAQGSIGERLAQLEDL 898
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
596-823 |
1.06e-04 |
|
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: 45.82 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 596 NYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDvyHHEHIEDLLDKQSRELQdmeccnnqkllleyekyqELQLKSQR 675
Cdd:cd22656 80 NYAQNAGGTIDSYYAEILELIDDLADATDDEELEE--AKKTIKALLDDLLKEAK------------------KYQDKAAK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 676 MQEEYeKQLRDNDETKSQALEELTEFYEAKLQEKttLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKkLRD 755
Cdd:cd22656 140 VVDKL-TDFENQTEKDQTALETLEKALKDLLTDE--GGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIAD-DEA 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902638 756 EKESNLRLKGETGIMRKKFSSLQKEIEERTNDIEtlkgeqmKLQGVIKSLEKDIQGLKREIQERDETI 823
Cdd:cd22656 216 KLAAALRLIADLTAADTDLDNLLALIGPAIPALE-------KLQGAWQAIATDLDSLKDLLEDDISKI 276
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
635-831 |
1.06e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 635 EHIEDLLDKQS------------REL-QDMECCNNQKLLLE-----YEKYQELQLKS-----QRMQEEYEKQL---RDND 688
Cdd:PHA02562 154 KLVEDLLDISVlsemdklnkdkiRELnQQIQTLDMKIDHIQqqiktYNKNIEEQRKKngeniARKQNKYDELVeeaKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 689 ETKSQALEELTEF------YEAKLQEKTTLLEEAQEDVRQQLRE---FEE-----TKKQIEEDEDREIQDIKTK---YEK 751
Cdd:PHA02562 234 AEIEELTDELLNLvmdiedPSAALNKLNTAAAKIKSKIEQFQKVikmYEKggvcpTCTQQISEGPDRITKIKDKlkeLQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 752 KLRDEKESNLRLKG---ETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKD-------IQGLKREIQERDE 821
Cdd:PHA02562 314 SLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdnaeeLAKLQDELDKIVK 393
|
250
....*....|
gi 767902638 822 TIQDKEKRIY 831
Cdd:PHA02562 394 TKSELVKEKY 403
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
599-970 |
1.07e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 599 EKIKELTDKFIQEMESLKTKNQVLRTEkekqdvyhhehIEDLLDKQsRELQdmeccnnQKLLLEYEKYQELqlksqrmQE 678
Cdd:PRK04778 115 DLIEEDIEQILEELQELLESEEKNREE-----------VEQLKDLY-RELR-------KSLLANRFSFGPA-------LD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 679 EYEKQLrDNDETKSQALEELTE---FYEA-----KLQEKTTLLEEAQEDVRQQLREFEETKKQieededrEIQDIKTKYe 750
Cdd:PRK04778 169 ELEKQL-ENLEEEFSQFVELTEsgdYVEAreildQLEEELAALEQIMEEIPELLKELQTELPD-------QLQELKAGY- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 751 kklRDEKESNLRLKgETGIMrKKFSSLQKEIEERTNDIETLKGEQMKLQgvIKSLEKDIQGL----------KREIQERD 820
Cdd:PRK04778 240 ---RELVEEGYHLD-HLDIE-KEIQDLKEQIDENLALLEELDLDEAEEK--NEEIQERIDQLydilerevkaRKYVEKNS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 821 ETIQDKEKRiydLKKKNQELG------KFKFVLDYKIKELKKQIEPRENEIRVMKEQIQ-----------EMEAELENFH 883
Cdd:PRK04778 313 DTLPDFLEH---AKEQNKELKeeidrvKQSYTLNESELESVRQLEKQLESLEKQYDEITeriaeqeiaysELQEELEEIL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 884 KQNTQLELNITELWQKLRATdqemrreRQKERDLEALVKRFKTDLHNCVAYIQeprllKEKVRGLFEKYVQRADMV--EI 961
Cdd:PRK04778 390 KQLEEIEKEQEKLSEMLQGL-------RKDELEAREKLERYRNKLHEIKRYLE-----KSNLPGLPEDYLEMFFEVsdEI 457
|
....*....
gi 767902638 962 AGLNTDLQQ 970
Cdd:PRK04778 458 EALAEELEE 466
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
708-993 |
1.14e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.75 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 708 EKTTLLEEAQEDVRQQLREFEETKKQIEE---DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIM-------------- 770
Cdd:PTZ00440 404 KYTNIISLSEHTLKAAEDVLKENSQKIADyalYSNLEIIEIKKKYDEKINELKKSINQLKTLISIMksfydliisekdsm 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 771 ------RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLE---KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELG 841
Cdd:PTZ00440 484 dskekkESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEdyyITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKR 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 842 KFKFVLDYKIKELKKQIEpRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKeRDLEALV 921
Cdd:PTZ00440 564 SMKNDIKNKIKYIEENVD-HIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYK-GDLQELL 641
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902638 922 KRFKTDLHNCVAYIQEPRlLKEKVRGLFEKYVQRADmvEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKE 993
Cdd:PTZ00440 642 DELSHFLDDHKYLYHEAK-SKEDLQTLLNTSKNEYE--KLEFMKSDNIDNIIKNLKKELQNLLSLKENIIKK 710
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
634-1091 |
1.18e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 634 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQ------LKSQRMQEEYEKQLRDNDETKSQA--LEELTEFYEAK 705
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEkelkhlREALQQTQQSHAYLTQKREAQEEQlkKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 706 LQEKTTL---LEEAQEDV---RQQLREFEETKK--QIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSL 777
Cdd:TIGR00618 269 IEELRAQeavLEETQERInraRKAAPLAAHIKAvtQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 778 QKEIEERTNDIETlkgEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQelgkfkfvldykikELKKQ 857
Cdd:TIGR00618 349 TLHSQEIHIRDAH---EVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ--------------REQAT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 858 IEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKT----------- 926
Cdd:TIGR00618 412 IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlqetrkkav 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 927 DLHNCVAYIQEPRLLKEKVRglfeKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGElHRTDY----V 1002
Cdd:TIGR00618 492 VLARLLELQEEPCPLCGSCI----HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK-QRASLkeqmQ 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 1003 RIMQENVSLIKEINELRRELKFTRSQVYDL----EAALKLTKKVRPQ---EVSETEPSRDMLSTAPTARLNEQEETGRII 1075
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRLqdltEKLSEAEDMLACEqhaLLRKLQPEQDLQDVRLHLQQCSQELALKLT 646
|
490
....*....|....*.
gi 767902638 1076 EMQRLEIQRLRDQIQE 1091
Cdd:TIGR00618 647 ALHALQLTLTQERVRE 662
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
574-1097 |
1.20e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 574 ELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHIE--DLLDKQSRELQDM 651
Cdd:TIGR00606 249 PLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTvrEKERELVDCQREL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 652 ECCNNQKLLLEYEKYQ------ELQLKSQRMQEEYEKqlRDNDETKSQALEELTEFyeaklqekttlleEAQEDVRQQLR 725
Cdd:TIGR00606 329 EKLNKERRLLNQEKTEllveqgRLQLQADRHQEHIRA--RDSLIQSLATRLELDGF-------------ERGPFSERQIK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 726 EFEETKKQIEEDEDREIQDIKTKYEKKLRDEKES----NLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGV 801
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQadeiRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 802 IKsLEKDIQGLKREIQERDE--TIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAEL 879
Cdd:TIGR00606 474 LE-LDQELRKAERELSKAEKnsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 880 ENFHKQNTQLE------LNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNcvaYIQEPRLLKEKVRGLFEKyv 953
Cdd:TIGR00606 553 KIKSRHSDELTsllgyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNH---INNELESKEEQLSSYEDK-- 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 954 qradMVEIAGlNTDLQQEYTRQREHLER---NLATLKKKV------VKEGELHRTDYVRIMQENVSLIKEINELRRELK- 1023
Cdd:TIGR00606 628 ----LFDVCG-SQDEESDLERLKEEIEKsskQRAMLAGATavysqfITQLTDENQSCCPVCQRVFQTEAELQEFISDLQs 702
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902638 1024 FTRSQVYDLEAALKLTKKV--RPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMqrlEIQRLRDQIQEQEQVTG 1097
Cdd:TIGR00606 703 KLRLAPDKLKSTESELKKKekRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNR---DIQRLKNDIEEQETLLG 775
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
704-930 |
1.25e-04 |
|
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: 46.00 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 704 AKLQEKTTLLEEAQEDVRQQLREFEETKKQiEEDEDREIQDIKTKYEKkLRDEKESNlrlkgetgimRKKFSSLQKEIEE 783
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLES-EEKNREEVEELKDKYRE-LRKTLLAN----------RFSYGPAIDELEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 784 RTNDIE---------TLKGEQMKLQGVIKSLEKDIQGLKR---EIQERDETIQDK-EKRIYDLKKKNQELGKFKFVLDY- 849
Cdd:pfam06160 154 QLAEIEeefsqfeelTESGDYLEAREVLEKLEEETDALEElmeDIPPLYEELKTElPDQLEELKEGYREMEEEGYALEHl 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 850 ----KIKELKKQIEPR------------ENEIRVMKEQIQE----MEAELENFH-----------------KQNTQLELN 892
Cdd:pfam06160 234 nvdkEIQQLEEQLEENlallenleldeaEEALEEIEERIDQlydlLEKEVDAKKyveknlpeiedylehaeEQNKELKEE 313
|
250 260 270
....*....|....*....|....*....|....*...
gi 767902638 893 ITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHN 930
Cdd:pfam06160 314 LERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVER 351
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
729-902 |
1.30e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 729 ETKKQIEEDEDREIQ-DIKTKyEKKLRD-EKESNLRlkgetgimRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLE 806
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKnELKNK-EKELKNlDKNLNKD--------EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 807 KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN 886
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170
....*....|....*.
gi 767902638 887 TQLELNITELWQKLRA 902
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLK 198
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
566-1023 |
1.81e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 566 EEKAQVMLELK-----TRVEELKMENEYQLRLKDMNYSEKIKELTDKfiqEMESLKTKNQVLRTEKEKQDVyhHEHIEDL 640
Cdd:COG5022 902 LELESEIIELKkslssDLIENLEFKTELIARLKKLLNNIDLEEGPSI---EYVKLPELNKLHEVESKLKET--SEEYEDL 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 641 LDKQS---RELQDMeccnNQKLLLEYEKYQELQLKSQRMQEEyEKQLRDNDeTKSQALEELTEFY---------EAKLQE 708
Cdd:COG5022 977 LKKSTilvREGNKA----NSELKNFKKELAELSKQYGALQES-TKQLKELP-VEVAELQSASKIIssestelsiLKPLQK 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 709 KTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKK---LRDEKESNLRLKGETGIMR------KKFSSLQK 779
Cdd:COG5022 1051 LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKtinVKDLEVTNRNLVKPANVLQfivaqmIKLNLLQE 1130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 780 EIEERTNDIETLKGEQMKLqgviKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFvldykiKELKKQIE 859
Cdd:COG5022 1131 ISKFLSQLVNTLEPVFQKL----SVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKS------KLSSSEVN 1200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 860 PRENEIRVMKEQIQEmEAELENFHKQNTQLELNITELWQKLRAT-DQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEP 938
Cdd:COG5022 1201 DLKNELIALFSKIFS-GWPRGDKLKKLISEGWVPTEYSTSLKGFnNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEE 1279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 939 RLLKEKVRGLFEKYVQRADMVEIAGLNT-------------------DLQQEYTRQREHLERNLATLKKKVVKEGELHRT 999
Cdd:COG5022 1280 EVLPATINSLLQYINVGLFNALRTKASSlrwksatevnynseelddwCREFEISDVDEELEELIQAVKVLQLLKDDLNKL 1359
|
490 500
....*....|....*....|....
gi 767902638 1000 DYVRIMQENVSLIkEINELRRELK 1023
Cdd:COG5022 1360 DELLDACYSLNPA-EIQNLKSRYD 1382
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
599-1059 |
1.85e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 599 EKIKELTDKFIQEMESLKTKNQVLRTEKEKQdvyhhEHIEDLLdkQSRELQdMECcnnqkllleyekyqelqlkSQRMQE 678
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKA-----CEIRDQI--TSKEAQ-LES-------------------SREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 679 EYEKQLRDNDETKSQALEELTEFYeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE 758
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIM--KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKER 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 759 SNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQ----ERDETIQDKEKRIYDLK 834
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfERGPFSERQIKNFHTLV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 835 KKNQElGKFKFV----LDYKIKELKKQIEPRENEIRvMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRE 910
Cdd:TIGR00606 400 IERQE-DEAKTAaqlcADLQSKERLKQEQADEIRDE-KKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELD 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 911 ---RQKERDLEALVKRFKTD-LHNCVAYIQEPRL-LKEKVRGLFEKYVQRadmveiaglntDLQQEYTRQREHLERNLAT 985
Cdd:TIGR00606 478 qelRKAERELSKAEKNSLTEtLKKEVKSLQNEKAdLDRKLRKLDQEMEQL-----------NHHTTTRTQMEMLTKDKMD 546
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902638 986 LKKKVVKEGELHRTDYVRIMQE---NVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLST 1059
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS 623
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
572-998 |
2.13e-04 |
|
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: 45.71 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 572 MLELKTR----VEELKMENEyqlrlKDMNYSEKIkeltDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedlLDKQSRE 647
Cdd:pfam15818 2 LLDFKTSlleaLEELRMRRE-----AETQYEEQI----GKIIVETQELKWQKETLQNQKET------------LAKQHKE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 648 LqdMECCNNQkllleyekyqeLQLKSQRMQEEYEK-QLRDndETKSQALEELTEFYEAKLQEKTTL---LEEAQEDVRQQ 723
Cdd:pfam15818 61 A--MAVFKKQ-----------LQMKMCALEEEKGKyQLAT--EIKEKEIEGLKETLKALQVSKYSLqkkVSEMEQKLQLH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 724 LREFEETKKQIEEDEdreiqdiktKYEKKLrdekesnlrlKGETGIMRKKFSSLQKEIEERtndIETLKgeqmKLQGVIK 803
Cdd:pfam15818 126 LLAKEDHHKQLNEIE---------KYYATI----------TGQFGLVKENHGKLEQNVQEA---IQLNK----RLSALNK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 804 SLEKDIQGLKREiqerdetiqdkekriydLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQeMEAEL---- 879
Cdd:pfam15818 180 KQESEICSLKKE-----------------LKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLN-MELELnkki 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 880 --ENFHKQNTQLELNITelwqkLRATDQEMRRERQKERDLEALVKRFKtdlHNCVAYIQEPRLLKEKVRGLFEKYVQRAD 957
Cdd:pfam15818 242 neEITHIQEEKQDIIIS-----FQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQREKVKENEEKFLNLQN 313
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 767902638 958 MVEIAglntdlQQEYTRQREHLERNLATLKKKVVKEGELHR 998
Cdd:pfam15818 314 EHEKA------LGTWKKHVEELNGEINEIKNELSSLKETHI 348
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
662-1081 |
2.73e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 662 EYEKYQELQLKSQRMQEEYEK-QLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE--DE 738
Cdd:COG5022 811 EYRSYLACIIKLQKTIKREKKlRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQElkID 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 739 DREIQDIKTKYEK------KLRDEKESNLRLKGEtgIMRKKFSSLQKEIEERtnDIETLKGEQMKLQGVIKSLEKDIQGL 812
Cdd:COG5022 891 VKSISSLKLVNLEleseiiELKKSLSSDLIENLE--FKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLHEVESKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 813 KREIQERDETIQDKEKRIYDLKKKNQELGKFKfvldYKIKELKKQIEPRENEIRVMKEQIQEMEaelenFHKQNTQLELN 892
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFK----KELAELSKQYGALQESTKQLKELPVEVA-----ELQSASKIISS 1037
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 893 ITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYiqeprllkekvrgLFEKYVQRADMVEIAGLNTDLQQEY 972
Cdd:COG5022 1038 ESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLD-------------DKQLYQLESTENLLKTINVKDLEVT 1104
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 973 TRQREHLERNLATLKKKVVKEGELHRTDyvRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEP 1052
Cdd:COG5022 1105 NRNLVKPANVLQFIVAQMIKLNLLQEIS--KFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRL 1182
|
410 420 430
....*....|....*....|....*....|.
gi 767902638 1053 SRD-MLSTAPTARLNEQEE-TGRIIEMQRLE 1081
Cdd:COG5022 1183 YQSaLYDEKSKLSSSEVNDlKNELIALFSKI 1213
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
701-928 |
2.97e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 701 FYEAKLQEKTT--LLEEAQEDVRQQLREFEETKKQiEEDEDREIQDIKTKYEKkLRDEKESNlrlkgetgimRKKFSSLQ 778
Cdd:PRK04778 100 FRKAKHEINEIesLLDLIEEDIEQILEELQELLES-EEKNREEVEQLKDLYRE-LRKSLLAN----------RFSFGPAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 779 KEIEERTNDIETL---------KGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEK----RIYDLKKKNQELGKFKF 845
Cdd:PRK04778 168 DELEKQLENLEEEfsqfvelteSGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTelpdQLQELKAGYRELVEEGY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 846 VLDYK-----IKELKKQI------------EPRENEIRVMKEQIQEM----EAE-----------------LENFHKQNT 887
Cdd:PRK04778 248 HLDHLdiekeIQDLKEQIdenlalleeldlDEAEEKNEEIQERIDQLydilEREvkarkyveknsdtlpdfLEHAKEQNK 327
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767902638 888 QLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDL 928
Cdd:PRK04778 328 ELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEIT 368
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
554-829 |
3.02e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 554 FAEEVLvTKTDMEEKAQVMLELktrVEELkmeNEYQLRLKDMnySEKIKELTD--KFIQEMESLKTKNQVLRTEKEKQDV 631
Cdd:COG4913 213 VREYML-EEPDTFEAADALVEH---FDDL---ERAHEALEDA--REQIELLEPirELAERYAAARERLAELEYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 632 YHHEHIEDLLDKQSRELQdmeccnnqkllleyEKYQELqlksqrmqeeyEKQLRDNDETKSQALEELTEFYEAKLQEKTT 711
Cdd:COG4913 284 WFAQRRLELLEAELEELR--------------AELARL-----------EAELERLEARLDALREELDELEAQIRGNGGD 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 712 LLEEAQEDVRQQlrefEETKKQIEEDEDReiqdiktkYEKKLRDekesnLRLKGETGimRKKFSSLQKEIEERtndIETL 791
Cdd:COG4913 339 RLEQLEREIERL----ERELEERERRRAR--------LEALLAA-----LGLPLPAS--AEEFAALRAEAAAL---LEAL 396
|
250 260 270
....*....|....*....|....*....|....*...
gi 767902638 792 KGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKR 829
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
797-1094 |
3.15e-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: 45.05 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 797 KLQGVIKSLEKDIQGLKREiqerdetiqdKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEME 876
Cdd:TIGR02168 190 RLEDILNELERQLKSLERQ----------AEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 877 AELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEalvkrfktdlhncvayiQEPRLLKEKVRGLFEKYVQra 956
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE-----------------QQKQILRERLANLERQLEE-- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 957 dmveiagLNTDLQQEyTRQREHLERNLATLKKKVVkegelhrtdyvrimqenvSLIKEINELRRELKFTRSQVYDLEAAL 1036
Cdd:TIGR02168 321 -------LEAQLEEL-ESKLDELAEELAELEEKLE------------------ELKEELESLEAELEELEAELEELESRL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767902638 1037 KLTKKVRPQEVSETepsrdmlstaptARLNEQEETgriiemQRLEIQRLRDQIQEQEQ 1094
Cdd:TIGR02168 375 EELEEQLETLRSKV------------AQLELQIAS------LNNEIERLEARLERLED 414
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
847-1031 |
3.39e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 847 LDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN--TQLELNITELWQKLRATDQEMRRERQKERDLEALVKRF 924
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 925 KTDL---HNCVAYIQEPRLLKEKVRGLFEKYVQRADMV---------------EIAGLNTDLQQEYTRQREHLERNLATL 986
Cdd:COG3206 246 RAQLgsgPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvialraQIAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767902638 987 KKkvvKEGELHRT--DYVRIMQENVSLIKEINELRRELKFTRsQVYD 1031
Cdd:COG3206 326 QA---REASLQAQlaQLEARLAELPELEAELRRLEREVEVAR-ELYE 368
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
426-540 |
3.48e-04 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 43.86 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 426 FKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDD-IRSFKEYSVrGCGECSFSNGGHLFAAV-NGNVIHVYTTTSL 502
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGtIKVWDLETGElLRTLKGHTG-PVRDVAASADGTYLASGsSDKTIRLWDLETG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767902638 503 ENISSLKGHTGKML-LTF--DDQFLLTAAEDGclfTWKVFD 540
Cdd:cd00200 84 ECVRTLTGHTSYVSsVAFspDGRILSSSSRDK---TIKVWD 121
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
698-1096 |
3.57e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 698 LTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReIQDIKTKYEKKLRDEKESNLRLKGEtgimRKKFSSL 777
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEK-INNSNNKIKILEQQIKDLNDKLKKN----KDKINKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 778 QKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQ 857
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 858 IEPRENEIRVMKEQI-----------------QEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEAL 920
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLlklelllsnlkkkiqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 921 VKRFKTDLHNCVAYI-QEPRLLKEKvrglfEKYVQRADMvEIAGLNTDLQQEYTRQrehLERNLATLKKKVvkegELHRT 999
Cdd:TIGR04523 262 QNKIKKQLSEKQKELeQNNKKIKEL-----EKQLNQLKS-EISDLNNQKEQDWNKE---LKSELKNQEKKL----EEIQN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 1000 DYVRIMQENVSLIKEINELRRELKFTRSQvyDLEAALKLTKKVRPQEVSEtepsrdmlstaptarlNEQEETGRIIEMQR 1079
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESE--NSEKQRELEEKQNEIEKLK----------------KENQSYKQEIKNLE 390
|
410
....*....|....*..
gi 767902638 1080 LEIQRLRDQIQEQEQVT 1096
Cdd:TIGR04523 391 SQINDLESKIQNQEKLN 407
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
820-1072 |
3.65e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 820 DETIQDKEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQK 899
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 900 LRATDQEMRRERQKERDLEALVKrfKTDlhncvayiqeprllkekvrglFEKYVQRADMVE-IAGLNTDLQQEYTRQREH 978
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLG--SES---------------------FSDFLDRLSALSkIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 979 LERNLATLKKKvVKEGELHRTDYVRIMQENVSLIKE----INELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSR 1054
Cdd:COG3883 145 LEAKKAELEAK-LAELEALKAELEAAKAELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250
....*....|....*...
gi 767902638 1055 DMLSTAPTARLNEQEETG 1072
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAA 241
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
388-417 |
3.78e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.87 E-value: 3.78e-04
10 20 30
....*....|....*....|....*....|
gi 767902638 388 HSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:pfam00400 10 HTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
599-927 |
3.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 599 EKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHH--EHIEDLLDKQS--RELQDMEccnnqkllleyEKYQELQLKSQ 674
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASaeREIAELE-----------AELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 675 RMQEeyekqLRDNDETKSQALEELTEFYEAkLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDRE-IQDIKTKYEKKL 753
Cdd:COG4913 686 DLAA-----LEEQLEELEAELEELEEELDE-LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 754 RDEKESNLR--LKGETGIMRKKFSSLQKEIEERTND-IETLKGEQMKLQGVIKSLEkDIQGLKREIQERDetIQDKEKRI 830
Cdd:COG4913 760 GDAVERELRenLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLP-EYLALLDRLEEDG--LPEYEERF 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 831 YDLKKKNQElgkfkfvldYKIKELKKQIeprENEIRVMKEQIQEMEAELEN----------FHKQNTQLElNITELWQKL 900
Cdd:COG4913 837 KELLNENSI---------EFVADLLSKL---RRAIREIKERIDPLNDSLKRipfgpgrylrLEARPRPDP-EVREFRQEL 903
|
330 340 350
....*....|....*....|....*....|...
gi 767902638 901 RA------TDQEMRRERQKERdLEALVKRFKTD 927
Cdd:COG4913 904 RAvtsgasLFDEELSEARFAA-LKRLIERLRSE 935
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
610-871 |
4.12e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 43.79 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 610 QEMESLKTKNQVLRTEKEKQDVYHHEHIE--DLLDKQSRELQ----DMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQ 683
Cdd:pfam09728 39 KDLKKLKKKQDQLQKEKDQLQSELSKAILakSKLEKLCRELQkqnkKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 684 LRDNDETKSQALEELTEFYE--AKLQEKTTLLEE------AQEDVRQQLRE------FEETKKQIEEDEDREIQDIKTKY 749
Cdd:pfam09728 119 MEEKSEKNNKLREENEELREklKSLIEQYELRELhfekllKTKELEVQLAEaklqqaTEEEEKKAQEKEVAKARELKAQV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 750 EKKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDetiqdkeKR 829
Cdd:pfam09728 199 QTLSETEKE----LREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSN-------KA 267
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767902638 830 IYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQ 871
Cdd:pfam09728 268 LLEMAEERQKLKE-------ELEKLQKKLEKLENLCRALQAE 302
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
385-417 |
4.77e-04 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 38.83 E-value: 4.77e-04
10 20 30
....*....|....*....|....*....|...
gi 767902638 385 YPLHSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:smart00320 8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-179 |
4.79e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.75 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 26 DEQIIIFPSGNHCVK-YNVD-QKWQKFIPGSekSQGMLALSISPNRRYLAiseTVQEKPAITIYELSSipcrkRKVLNNF 103
Cdd:COG2319 257 DGRLLASGSADGTVRlWDLAtGELLRTLTGH--SGGVNSVAFSPDGKLLA---SGSDDGTVRLWDLAT-----GKLLRTL 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902638 104 DFQVQKFISMAFSPDSKYLLAQTSppeSNLVYwLWEKQKVMAIVRIDTQNNPVYQVSFSPQDNTQVCVTGNGMFKL 179
Cdd:COG2319 327 TGHTGAVRSVAFSPDGKTLASGSD---DGTVR-LWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
714-885 |
4.88e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 44.25 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 714 EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFsslqKEIEERTNDIEtlkg 793
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESSIK-QVEEELEELKEQNEELEKQYKVKKKTL----DLLPDAEENIA---- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 794 eqmKLQGVIKSLEKDIQGLKREIQERDETIQdKEKRIYDLKKKNQELgKFKFVLDyKIKELKKQIEPRENEIRVMKEQIQ 873
Cdd:pfam05667 405 ---KLQALVDASAQRLVELAGQWEKHRVPLI-EEYRALKEAKSNKED-ESQRKLE-EIKELREKIKEVAEEAKQKEELYK 478
|
170
....*....|..
gi 767902638 874 EMEAELENFHKQ 885
Cdd:pfam05667 479 QLVAEYERLPKD 490
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
839-1041 |
6.85e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 839 ELGK---FKFVLDYKIKELKKQIE----PRENEIRVMKEQIQEMEAELENFHKQNTQLElnitELWQKLRATDQEMRRER 911
Cdd:COG4717 33 EAGKstlLAFIRAMLLERLEKEADelfkPQGRKPELNLKELKELEEELKEAEEKEEEYA----ELQEELEELEEELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 912 QKERDLEALVKRFKtDLHNCVAYIQEPRLLKEKVRGLFEKYVQ-RADMVEIAglntDLQQEYTRQREHLERNLATLKKKV 990
Cdd:COG4717 109 AELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERLEElEERLEELR----ELEEELEELEAELAELQEELEELL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767902638 991 VKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKK 1041
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
620-1079 |
6.89e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 620 QVLRTEKEKQDV-----YHHEHIEDLLDKQSRELQdmECCNNQKLLLEYekyqelqLKSQRMQEEYEKQLRdndETKSQA 694
Cdd:TIGR01612 328 KILESEGEQGHIinkliFLEKEFEDTIHKSDIYKD--ECLSNHLFMEDY-------LKDDKISPYYYEFLE---EIKKIA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 695 LEELTEFYEAKLQEKTTLLEEAQEDVrqqLREFEETKKQ--IEEDEDREIQDIKTKYEKKLRDEKESNLRL--KGETGIM 770
Cdd:TIGR01612 396 KQRAIFFYNAKKLKHLEILYKHQEDI---LNNFHKTIERliFEKPDPNNNNIFKDDFDEFNKPIPKSKLKAleKRFFEIF 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 771 RKKFSS--LQKEIEERTNDIETLKG--EQMK-LQGVIKSLEkdiQGLKREIQERDETIQDKEKRIYDLKKKNQELGkfkf 845
Cdd:TIGR01612 473 EEEWGSydIKKDIDENSKQDNTVKLilMRMKdFKDIIDFME---LYKPDEVPSKNIIGFDIDQNIKAKLYKEIEAG---- 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 846 vldykikeLKKQIEPRENeirvMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEmrrerqkerdlealvkrfk 925
Cdd:TIGR01612 546 --------LKESYELAKN----WKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDE------------------- 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 926 tdlhncVAYIQEPRL-LKEKVRGLFEK--YVQRA-DMVEIAGLNTDLQQEYTRQR-----EHLERN---LATLKKKVVKe 993
Cdd:TIGR01612 595 ------IIYINKLKLeLKEKIKNISDKneYIKKAiDLKKIIENNNAYIDELAKISpyqvpEHLKNKdkiYSTIKSELSK- 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 994 geLHRTDYVRIMQENVSLIKEINELRRELKftrSQVYDLEAalKLTKKVRPQEVSETEPSRDMLSTAPTarlNEQEETGR 1073
Cdd:TIGR01612 668 --IYEDDIDALYNELSSIVKENAIDNTEDK---AKLDDLKS--KIDKEYDKIQNMETATVELHLSNIEN---KKNELLDI 737
|
....*.
gi 767902638 1074 IIEMQR 1079
Cdd:TIGR01612 738 IVEIKK 743
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
655-755 |
6.91e-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: 41.02 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 655 NNQKLLLEYEKYQELQLKSQRMQEEYEKQLrdndETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQI 734
Cdd:pfam03938 6 DMQKILEESPEGKAAQAQLEKKFKKRQAEL----EAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKA 81
|
90 100
....*....|....*....|.
gi 767902638 735 EEDEDREIQDIKTKYEKKLRD 755
Cdd:pfam03938 82 QQELQKKQQELLQPIQDKINK 102
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-190 |
7.78e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.36 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 26 DEQIIIFPSGNHCVK-YNVD-QKWQKFIPGSekSQGMLALSISPNRRYLAiseTVQEKPAITIYELSSipcrkRKVLNNF 103
Cdd:COG2319 215 DGKLLASGSADGTVRlWDLAtGKLLRTLTGH--SGSVRSVAFSPDGRLLA---SGSADGTVRLWDLAT-----GELLRTL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 104 DFQVQKFISMAFSPDSKYLLAQTsppESNLVyWLWEKQKVMAIVRIDTQNNPVYQVSFSPQDNTQVCVTGNGMFKLLRFA 183
Cdd:COG2319 285 TGHSGGVNSVAFSPDGKLLASGS---DDGTV-RLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA 360
|
....*..
gi 767902638 184 EGTLKQT 190
Cdd:COG2319 361 TGELLRT 367
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
562-840 |
8.25e-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: 43.30 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 562 KTDMEEKAQVMLELKTRVEELkmeneyqlrlkdMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedll 641
Cdd:pfam09726 408 KAELQASRQTEQELRSQISSL------------TSLERSLKSELGQLRQENDLLQTKLHNAVSAKQK------------- 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 642 DKQSreLQDMEccnnQKLLLEyekyqelqlksQRMQEEYEKQLrdNDETKSQALEELTEFYEAKLQEKTTllEEAQEDVR 721
Cdd:pfam09726 463 DKQT--VQQLE----KRLKAE-----------QEARASAEKQL--AEEKKRKKEEEATAARAVALAAASR--GECTESLK 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 722 QQLREFEETKKQIEED---EDREIQDIKTKyEKKLRDEKESnlrlKGETGIMRKKFSSLQKEIEERTNDI--ETlkgeQM 796
Cdd:pfam09726 522 QRKRELESEIKKLTHDiklKEEQIRELEIK-VQELRKYKES----EKDTEVLMSALSAMQDKNQHLENSLsaET----RI 592
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767902638 797 KLqgvikSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQEL 840
Cdd:pfam09726 593 KL-----DLFSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEV 631
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
552-760 |
8.30e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 552 VGFAEEVLVTKTDMEEKAQVMLEL-KTRVEELKMENEYQLRLKDMNYSEKIKELTDKFiqEMESLKTKNQVLRTEKEKQD 630
Cdd:PRK12704 16 VGAVIGYFVRKKIAEAKIKEAEEEaKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF--EKELRERRNELQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 631 VyhhehiEDLLDKQSRELQDMEccnnqkllleyekyQELQLKsqrmQEEYEKQLRDndetksqaLEELTEFYEAKLQEKT 710
Cdd:PRK12704 94 K------EENLDRKLELLEKRE--------------EELEKK----EKELEQKQQE--------LEKKEEELEELIEEQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767902638 711 TLLEEA----QEDVRQQLreFEETKKQIEEDEDREIQDIKTKYekKLRDEKESN 760
Cdd:PRK12704 142 QELERIsgltAEEAKEIL--LEKVEEEARHEAAVLIKEIEEEA--KEEADKKAK 191
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
674-945 |
8.58e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 674 QRMQEEYEKQlRDNDETKSQALEELTEfyeaklQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKL 753
Cdd:pfam02029 77 KRLQEALERQ-KEFDPTIADEKESVAE------RKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 754 RDEKEsnlrlKGEtgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERdeTIQDKEKRIYDL 833
Cdd:pfam02029 150 RQAEE-----EGE---EEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV--KSQNGEEEVTKL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 834 KKKNQELGKFKFVLDYKIKELKKQIEPrENEIRVMKEQIQEME-AELENFHKQNTQLELNITELwQKLRATDQEMRRERQ 912
Cdd:pfam02029 220 KVTTKRRQGGLSQSQEREEEAEVFLEA-EQKLEELRRRRQEKEsEEFEKLRQKQQEAELELEEL-KKKREERRKLLEEEE 297
|
250 260 270
....*....|....*....|....*....|...
gi 767902638 913 KERDLEALVKRFKTDlhncvayiQEPRLLKEKV 945
Cdd:pfam02029 298 QRRKQEEAERKLREE--------EEKRRMKEEI 322
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
556-889 |
1.48e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 556 EEVLVTKTDMEE------KAQVML-----ELKTRVEELKMENEYqlrLKDMNYSEKIKELTDKfIQEMESLKTKNQVLRT 624
Cdd:PRK04778 205 EELAALEQIMEEipellkELQTELpdqlqELKAGYRELVEEGYH---LDHLDIEKEIQDLKEQ-IDENLALLEELDLDEA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 625 EKEKQDVyhHEHIEDLLDKqsrelqdMEccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKsqalEELTEfyea 704
Cdd:PRK04778 281 EEKNEEI--QERIDQLYDI-------LE--------REVKARKYVEKNSDTLPDFLEHAKEQNKELK----EEIDR---- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 705 kLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTkyekklrdekesnlrlkgetgimrkkFSSLQKEIEER 784
Cdd:PRK04778 336 -VKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIA--------------------------YSELQEELEEI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 785 TNDIETLKGEQMKLQGVIKSLEKDiqglkrEIQERdETIQDKEKRIYDLK----KKN-----QELGKFKFVLDYKIKELK 855
Cdd:PRK04778 389 LKQLEEIEKEQEKLSEMLQGLRKD------ELEAR-EKLERYRNKLHEIKryleKSNlpglpEDYLEMFFEVSDEIEALA 461
|
330 340 350
....*....|....*....|....*....|....
gi 767902638 856 KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQL 889
Cdd:PRK04778 462 EELEEKPINMEAVNRLLEEATEDVETLEEETEEL 495
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
688-1094 |
1.56e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.69 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 688 DETKSQALEELTEFYEAKLQEKTTLLEEaqedvRQQLREFEETKKqieededreIQDIKTKY-------EKKLRDEKESN 760
Cdd:NF033838 53 NESQKEHAKEVESHLEKILSEIQKSLDK-----RKHTQNVALNKK---------LSDIKTEYlyelnvlKEKSEAELTSK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 761 LR---------LKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVI--KSLEKDIQGLKREIQERD-ETIQDKEK 828
Cdd:NF033838 119 TKkeldaafeqFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNtyKTLELEIAESDVEVKKAElELVKEEAK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 829 RIYDLKKKNQELGKFkfvldykikELKKQIEPRENEIRVMKEQIQE-----MEAELENFHKQNTQLELNITELWQKLRAT 903
Cdd:NF033838 199 EPRDEEKIKQAKAKV---------ESKKAEATRLEKIKTDREKAEEeakrrADAKLKEAVEKNVATSEQDKPKRRAKRGV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 904 DQEMRRERQKERDLEAlvkrfkTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRAdmveiaglntdlQQEYTRQREHLERNL 983
Cdd:NF033838 270 LGEPATPDKKENDAKS------SDSSVGEETLPSPSLKPEKKVAEAEKKVEEA------------KKKAKDQKEEDRRNY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 984 ATLKKKVVkEGELHRTDyVRIMQENVSLIKEI-NELRRELKFTRSQvydleaalkltKKVrpqEVSETEPSRdmLSTAPT 1062
Cdd:NF033838 332 PTNTYKTL-ELEIAESD-VKVKEAELELVKEEaKEPRNEEKIKQAK-----------AKV---ESKKAEATR--LEKIKT 393
|
410 420 430
....*....|....*....|....*....|..
gi 767902638 1063 ARLNEQEETGRIIEmqrlEIQRLRDQIQEQEQ 1094
Cdd:NF033838 394 DRKKAEEEAKRKAA----EEDKVKEKPAEQPQ 421
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
573-1022 |
1.56e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 573 LELKTRVEELKMENEYQLRLKDMnysEKIKELTDKFIQEM---------ESLKTKNQVLRTEK-EKQDVYhhehiEDLLD 642
Cdd:TIGR01612 603 LELKEKIKNISDKNEYIKKAIDL---KKIIENNNAYIDELakispyqvpEHLKNKDKIYSTIKsELSKIY-----EDDID 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 643 KQSRELQDMECCNNQKLLLEYEKYQELQLKSqrmqeeyekqlrDNDETKSQALEelTEFYEAKLqektTLLEEAQEDVRQ 722
Cdd:TIGR01612 675 ALYNELSSIVKENAIDNTEDKAKLDDLKSKI------------DKEYDKIQNME--TATVELHL----SNIENKKNELLD 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 723 QLREFEE-TKKQIEEDEDREIQDIKTKyEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNdIETLKGEQMKlQGV 801
Cdd:TIGR01612 737 IIVEIKKhIHGEINKDLNKILEDFKNK-EKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQIN-IDNIKDEDAK-QNY 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 802 IKSlekdiqglkreiQERDETIQDKEKRIydlkkknqelgkFKFVldykikelkkqiepreNEIRVMKEQIQ---EMEAE 878
Cdd:TIGR01612 814 DKS------------KEYIKTISIKEDEI------------FKII----------------NEMKFMKDDFLnkvDKFIN 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 879 LENFHKQNTQLE-LNITELWQKLRA--TDQEMRRERQKERDLEALV-----------------KRFKTDLHNCVAYIQEP 938
Cdd:TIGR01612 854 FENNCKEKIDSEhEQFAELTNKIKAeiSDDKLNDYEKKFNDSKSLIneinksieeeyqnintlKKVDEYIKICENTKESI 933
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 939 RLLKEKVRGLFEKYVQRADMVEIAGLntdLQQEYTRQREHLERNLATLKKKVVKEGELhrTDYvriMQENVSLIKEINEL 1018
Cdd:TIGR01612 934 EKFHNKQNILKEILNKNIDTIKESNL---IEKSYKDKFDNTLIDKINELDKAFKDASL--NDY---EAKNNELIKYFNDL 1005
|
....
gi 767902638 1019 RREL 1022
Cdd:TIGR01612 1006 KANL 1009
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
707-896 |
1.73e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 707 QEKTTLLEEAQEdvrQQLREFEETKKQIEEDEDREIQDIKTKYEK---KLRDEKESNLRLKGETGIMRKK---------- 773
Cdd:PRK05771 16 SYKDEVLEALHE---LGVVHIEDLKEELSNERLRKLRSLLTKLSEaldKLRSYLPKLNPLREEKKKVSVKsleelikdve 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 774 --FSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEK------DIQ-------------GLKREIQERDETI--------- 823
Cdd:PRK05771 93 eeLEKIEKEIKELEEEISELENEIKELEQEIERLEPwgnfdlDLSlllgfkyvsvfvgTVPEDKLEELKLEsdvenveyi 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 824 -QDKEKRIY-------DLKKKNQELGKF---KFVLDYK--IKELKKQIEPRENEIrvmKEQIQEMEAELENFHKQNTQLE 890
Cdd:PRK05771 173 sTDKGYVYVvvvvlkeLSDEVEEELKKLgfeRLELEEEgtPSELIREIKEELEEI---EKERESLLEELKELAKKYLEEL 249
|
....*.
gi 767902638 891 LNITEL 896
Cdd:PRK05771 250 LALYEY 255
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
667-747 |
1.78e-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: 39.73 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 667 QELQLKSQRMQEEYEKQLRdndETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLrefEETKKQIEEDEDREIQDIK 746
Cdd:cd06503 43 EKAKEEAEELLAEYEEKLA---EARAEAQEIIEEARKEAEKIKEEILAEAKEEAERIL---EQAKAEIEQEKEKALAELR 116
|
.
gi 767902638 747 T 747
Cdd:cd06503 117 K 117
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
696-834 |
1.96e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 40.30 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 696 EELTEFYeAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYE---KKLRDEKESNLRLKGEtgimrk 772
Cdd:pfam08614 3 LELIDAY-NRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllAQLREELAELYRSRGE------ 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902638 773 kfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 834
Cdd:pfam08614 76 ----LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQ 133
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
720-916 |
1.98e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 720 VRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQ 799
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKT----IKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 800 GVIKSLEKDI-------------QGLKREiQERDETIQDK----EKRIYDLKKKNQELGKFKFVLD---YKIKELKKQIE 859
Cdd:PHA02562 269 SKIEQFQKVIkmyekggvcptctQQISEG-PDRITKIKDKlkelQHSLEKLDTAIDELEEIMDEFNeqsKKLLELKNKIS 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767902638 860 PRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEmRRERQKERD 916
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT-KSELVKEKY 403
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
801-1094 |
2.23e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 801 VIKSLEKDIQGLKR--EIQERDETIQDKEKRiydlkKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAE 878
Cdd:COG1196 194 ILGELERQLEPLERqaEKAERYRELKEELKE-----LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 879 LENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLhncvayiqeprllkekvrglfekyvqradm 958
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 959 veiaglntdlqQEYTRQREHLERNLATLKkkvvkegelhrtdyvrimQENVSLIKEINELRRELKFTRSQVYDLEAALKL 1038
Cdd:COG1196 319 -----------EELEEELAELEEELEELE------------------EELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 767902638 1039 TKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQ 1094
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
547-825 |
2.87e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 547 KREREVGFAEEVLVTKTDMEEKAQVMLE----LKTRVEELKME-----NEYQLRLKDMNYSEKIKELTDKFIQEMESLKT 617
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEelkaLREALDELRAEltllnEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 618 KNQVLRTEKEKQdvyhHEHIEDLLDKQSRELQdmeccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEE 697
Cdd:TIGR02168 849 ELSEDIESLAAE----IEELEELIEELESELE-----------ALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 698 ltefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGetgiMRKKFSSL 777
Cdd:TIGR02168 914 -----RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR----LENKIKEL 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902638 778 Q----------KEIEERtndIETLKGEQMKLQGVIKSLEKDIQGLKREIQER-DETIQD 825
Cdd:TIGR02168 985 GpvnlaaieeyEELKER---YDFLTAQKEDLTEAKETLEEAIEEIDREARERfKDTFDQ 1040
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
698-929 |
3.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 698 LTEFYEAKLQEKTTLLEEAqEDVRQQLREFEETKKQIEEDEDR-----EIQDIKTKYEKKLRDEKESN-LRLKGETGIMR 771
Cdd:COG4913 209 LDDFVREYMLEEPDTFEAA-DALVEHFDDLERAHEALEDAREQiellePIRELAERYAAARERLAELEyLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 772 KKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDetiqdkekriydlkkknqelGKfkfvldyki 851
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG--------------------GD--------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 852 kelkkQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLEL-----------NITELWQKLRATDQEMRRERQKERDLEAL 920
Cdd:COG4913 339 -----RLEQLEREIERLERELEERERRRARLEALLAALGLplpasaeefaaLRAEAAALLEALEEELEALEEALAEAEAA 413
|
....*....
gi 767902638 921 VKRFKTDLH 929
Cdd:COG4913 414 LRDLRRELR 422
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
566-745 |
3.05e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 566 EEKAQVMLELKTRVEELKMENEYQLRLKDmnysEKIKELTDKFIQEMESLKTKnqvlrtekekqdvyhhehiEDLLDKQS 645
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERR----NELQKLEKRLLQKEENLDRK-------------------LELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 646 RELQDMECCNNQKLlleyekyQELQLKSQRMQEEYEKQLrdndetksQALEE---LTEFyEAKLQEKTTLLEEAQEDVRQ 722
Cdd:PRK12704 110 EELEKKEKELEQKQ-------QELEKKEEELEELIEEQL--------QELERisgLTAE-EAKEILLEKVEEEARHEAAV 173
|
170 180
....*....|....*....|...
gi 767902638 723 QLREFEEtkkQIEEDEDREIQDI 745
Cdd:PRK12704 174 LIKEIEE---EAKEEADKKAKEI 193
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
773-927 |
3.20e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 773 KFSSLQKEIEERTNDIETL----KGEQMKLQGVIKSLEKDIQGLKREIQERDETI----QDKEKRIYDLKKKNQELGKFK 844
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQrkknGENIARKQNKYDELVEEAKTIKAEIEELTDELlnlvMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 845 FVLDYKIKELK------------KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLEL----------NITELWQKLRA 902
Cdd:PHA02562 269 SKIEQFQKVIKmyekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdefneqskKLLELKNKIST 348
|
170 180
....*....|....*....|....*
gi 767902638 903 TDQEMRRERQKERDLEALVKRFKTD 927
Cdd:PHA02562 349 NKQSLITLVDKAKKVKAAIEELQAE 373
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
664-892 |
3.46e-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: 41.58 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 664 EKYQELQLKSQRMQEEYEKQlrdndetKSQALEELTEfyeakLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReiq 743
Cdd:pfam13166 279 DEFTEFQNRLQKLIEKVESA-------ISSLLAQLPA-----VSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRA--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 744 diktKYEKKLRDEKESNL-RLKGETGIMRKKFSSLQKEIE---ERTNDIETLKGEQMKL--QGVIKSLEKDIQGLKREIQ 817
Cdd:pfam13166 344 ----LEAKRKDPFKSIELdSVDAKIESINDLVASINELIAkhnEITDNFEEEKNKAKKKlrLHLVEEFKSEIDEYKDKYA 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902638 818 ERDETIQDKEKRIYDLKKKNQELGKfkfvldyKIKELkkqieprENEIRVMKEQIQEMEAELENFHKQNTQLELN 892
Cdd:pfam13166 420 GLEKAINSLEKEIKNLEAEIKKLRE-------EIKEL-------EAQLRDHKPGADEINKLLKAFGFGELELSFN 480
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
739-1023 |
3.84e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 739 DREIQDIKTKYEKKLRD-EKESNLRLKGETGIMR---KKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQ---- 810
Cdd:PLN02939 105 DEAIAAIDNEQQTNSKDgEQLSDFQLEDLVGMIQnaeKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSetda 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 811 --GLKREIQERDETIQDK-EKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQ---IQEMEAELENFHK 884
Cdd:PLN02939 185 riKLAAQEKIHVEILEEQlEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAElieVAETEERVFKLEK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 885 QNTQLELNITELWQKLRATDQEMRRER--------QKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLfEKYVQRA 956
Cdd:PLN02939 265 ERSLLDASLRELESKFIVAQEDVSKLSplqydcwwEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKL-EASLKEA 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902638 957 DMVEIAGLNTDL-QQEYTRQREHLERNlatlkkkvvkEGELHrtDYVRIMQEnvsLIKEINELRRELK 1023
Cdd:PLN02939 344 NVSKFSSYKVELlQQKLKLLEERLQAS----------DHEIH--SYIQLYQE---SIKEFQDTLSKLK 396
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
823-981 |
4.07e-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: 40.51 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 823 IQDKEKRIYDLKK-KNQELGKFKFVLDYKIKELKK-------QIEPRENEIRVMKEQIQEMEA----ELENFHKQNTQLE 890
Cdd:pfam09787 20 LQSKEKLIASLKEgSGVEGLDSSTALTLELEELRQerdllreEIQKLRGQIQQLRTELQELEAqqqeEAESSREQLQELE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 891 LNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCV----AYIQEPRL--------------LKEKVRGLFEKY 952
Cdd:pfam09787 100 EQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIkdreAEIEKLRNqltsksqssssqseLENRLHQLTETL 179
|
170 180
....*....|....*....|....*....
gi 767902638 953 VQRADMVEiaglntDLQQEYTRQREHLER 981
Cdd:pfam09787 180 IQKQTMLE------ALSTEKNSLVLQLER 202
|
|
| WDR74 |
cd22857 |
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ... |
343-420 |
4.38e-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: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 343 CLCFSPSEETLVASTSKNQLYSI---TMSLTEISKGepahfeylmypLHSAPITGLATCIRKPLIATCSLDRSIRLWNYE 419
Cdd:cd22857 228 AVAEDPDGHTVYVGDTSGDLASIdlrTGKLLGCFKG-----------KCGGSIRSIARHPELPLIASCGLDRYLRIWDTE 296
|
.
gi 767902638 420 T 420
Cdd:cd22857 297 T 297
|
|
| PTZ00332 |
PTZ00332 |
paraflagellar rod protein; Provisional |
646-1043 |
4.46e-03 |
|
paraflagellar rod protein; Provisional
Pssm-ID: 240364 [Multi-domain] Cd Length: 589 Bit Score: 41.10 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 646 RELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRD-------------NDETKSQALEELTEFyeakLQEKTTL 712
Cdd:PTZ00332 162 ATLKNIEDIMNVTQIQNALASTDDQIKTQLAQLEKTNEIQNvamhdgemqvaeeQMWTKVQLQERLIEL----VADKFRL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 713 LEEAqEDVRQQLREFEETKKQIEEdEDREIQDIKtkyeKKLRDEKESNLRlkgetgimrkkfsSLQKEIEERtnDIEtlK 792
Cdd:PTZ00332 238 IGKC-EEENKSFSKIHEVQKQANQ-ETSQMKDAK----RRLKQRCETDLK-------------HIHDAIQKA--DLE--D 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 793 GEQMKLQGVIKslEKDiqglKREIQERDETIQDKEKRIYDLKKKNQELGKFKFvldykiKELKKQIEP--RENEIRVMKE 870
Cdd:PTZ00332 295 AEAMKRYATNK--EKS----ERFIRENEDRQEEAWNKIQDLERQLQRLGTERF------EEVKRRIEEndREEKRRVEYQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 871 QIQEMEAE---LENFHKQNTQLELNITELWQKLRA------------TDQEM---RRERQKERdLEALVKRFKTdlHNCV 932
Cdd:PTZ00332 363 QFLEVAGQhkkLLELTVYNCDLALRCTGLVEELVSegcaavkarhdkTNQDLaalRLQVHKEH-LEYFRMLYLT--LGSL 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 933 AYIQEPRLlKEKVRGLFEKYVQRADMVEI----AGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDYVRIMQEN 1008
Cdd:PTZ00332 440 IYKKEKRL-EEIDRNIRTTHIQLEFCVETfdpnAKKHADMKKELYKLRQGVEEELAMLKEKQAQALEMFKESEEALDAAG 518
|
410 420 430
....*....|....*....|....*....|....*
gi 767902638 1009 VSLIKEINELRRELKFTRSQVYDLEAALKLTKKVR 1043
Cdd:PTZ00332 519 IEFVHPVDENNEEVLTRRSKMVEYRSHLAKQEEVK 553
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
671-845 |
4.95e-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: 40.39 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 671 LKSQRMQEEYEKQLRDNDEtksqalEELTEFYEAKLQEKTTLLEEAQE--DVRQQLRE-FEETKKQIEEdedreiqdikt 747
Cdd:smart00787 128 LEAKKMWYEWRMKLLEGLK------EGLDENLEGLKEDYKLLMKELELlnSIKPKLRDrKDALEEELRQ----------- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 748 kyEKKLRDEKESNLrlKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIqdKE 827
Cdd:smart00787 191 --LKQLEDELEDCD--PTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL--EQ 264
|
170
....*....|....*...
gi 767902638 828 KRIYDLKKKNQELGKFKF 845
Cdd:smart00787 265 CRGFTFKEIEKLKEQLKL 282
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
660-919 |
5.59e-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: 40.93 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 660 LLEYEKYQELQLKSQRMQEEYEK-----QLRDNDETKSQALEELTEF------YEAKLQEKTTLLEEAQEDVRQQLREFE 728
Cdd:pfam01576 476 LLQEETRQKLNLSTRLRQLEDERnslqeQLEEEEEAKRNVERQLSTLqaqlsdMKKKLEEDAGTLEALEEGKKRLQRELE 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 729 ETKKQIEEDEDR--EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLE 806
Cdd:pfam01576 556 ALTQQLEEKAAAydKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKE 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 807 KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN 886
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAK 715
|
250 260 270
....*....|....*....|....*....|...
gi 767902638 887 TQLELNItelwQKLRAtdqemrrerQKERDLEA 919
Cdd:pfam01576 716 LRLEVNM----QALKA---------QFERDLQA 735
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
672-945 |
6.12e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 672 KSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQL---REFEETKKQIEEDEDR--EIQDIK 746
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSIneyNKIESARADLEDIKIKinELKDKH 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 747 TKYEKKlrDEKESNLRLkgetGIMRKKFSSLQKEIEERTN-DIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQD 825
Cdd:PRK01156 546 DKYEEI--KNRYKSLKL----EDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 826 KEKRIYDlkKKNQELGKFKfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLeLNITELWQKLRATDQ 905
Cdd:PRK01156 620 SIREIEN--EANNLNNKYN-----EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRI-NDIEDNLKKSRKALD 691
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767902638 906 EMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKV 945
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDINETLESMKKI 731
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
595-768 |
6.44e-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: 40.00 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 595 MNYSEKIKELTDKfiqEMESLKTKNQVLRTEKEKQDVYHHEhIEDLLDKQSRELQDMeccnnQKLLLEYEKYQELQLKSQ 674
Cdd:smart00787 139 MKLLEGLKEGLDE---NLEGLKEDYKLLMKELELLNSIKPK-LRDRKDALEEELRQL-----KQLEDELEDCDPTELDRA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 675 RmqEEYEKQLRDNDEtKSQALEELTEfyeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLR 754
Cdd:smart00787 210 K--EKLKKLLQEIMI-KVKKLEELEE----ELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKL 282
|
170
....*....|....
gi 767902638 755 DEKESNLRLKGETG 768
Cdd:smart00787 283 LQSLTGWKITKLSG 296
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
574-840 |
6.86e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 574 ELKTRVEELKMENEYQLRLKDMNYsEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHIEdlLDKQSRELQDME- 652
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELN-EKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS--IDKLRKEIERLEw 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 653 CCNNQKLLLEYEKyqELQLKSQRMQEEYEKqLRDNDETKSQALEELTEFYEAKLQekttlleeaQEDVRQQLREFEETKK 732
Cdd:COG1340 124 RQQTEVLSPEEEK--ELVEKIKELEKELEK-AKKALEKNEKLKELRAELKELRKE---------AEEIHKKIKELAEEAQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 733 QIEEdedrEIQDIKTKYEKkLRDEKESnlrlkgetgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGL 812
Cdd:COG1340 192 ELHE----EMIELYKEADE-LRKEADE----------LHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
250 260
....*....|....*....|....*...
gi 767902638 813 KREiqERDETIQDKEKRIYDLKKKNQEL 840
Cdd:COG1340 257 KRE--KEKEELEEKAEEIFEKLKKGEKL 282
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
780-1045 |
6.89e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 780 EIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIY----DLKKKNQELGKFKFVLDYKIKELK 855
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRtlddQWKEKRDELNGELSAADAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 856 KQIEPRENEIRV-MKEQIQEMEAELENFHKQNTQLEL---NITELWQKLRATDQEMRRERQKeRDLEalVKRFKTDLHNC 931
Cdd:pfam12128 322 SELEALEDQHGAfLDADIETAAADQEQLPSWQSELENleeRLKALTGKHQDVTAKYNRRRSK-IKEQ--NNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 932 VAYIQEprllkEKVRGLfekyvqradmveiAGLNTDLQQEYTRQREHLERNLATLK--KKVVKE--GELH-RTDYVRIMQ 1006
Cdd:pfam12128 399 LAKIRE-----ARDRQL-------------AVAEDDLQALESELREQLEAGKLEFNeeEYRLKSrlGELKlRLNQATATP 460
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 767902638 1007 ENVSLIK----EINELRRELKFTRSQVYDLEAALKLTKKVRPQ 1045
Cdd:pfam12128 461 ELLLQLEnfdeRIERAREEQEAANAEVERLQSELRQARKRRDQ 503
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
573-758 |
7.51e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 573 LELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKE--KQDVYHHEHIEDLLDKQSRELQD 650
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEAGVEDEEE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 651 MEccnnqKLLLEYEKYQELQLKsqrmQEEYEKQLRDNDETKSQALEELT-EFYEAKLQEKTTLLEEAQEDVRQQLREFEE 729
Cdd:COG4717 387 LR-----AALEQAEEYQELKEE----LEELEEQLEELLGELEELLEALDeEELEEELEELEEELEELEEELEELREELAE 457
|
170 180 190
....*....|....*....|....*....|
gi 767902638 730 TKKQIEE-DEDREIQDIKTKYEKKLRDEKE 758
Cdd:COG4717 458 LEAELEQlEEDGELAELLQELEELKAELRE 487
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
713-1060 |
7.53e-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: 40.42 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 713 LEEAQEDVRQQLREFEETKKQIEEDEDR--EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKfsslQKEIEERTNDIET 790
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKacEIRDQITSKEAQLESSREIVKSYENELDPLKNR----LKEIEHNLSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 791 LKGEQMKLQGVIKSLEKDIQGLK----------------------REIQERDETIQDKEKRIYDLKKKNQELGKFKFVLD 848
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELElkmekvfqgtdeqlndlyhnhqRTVREKERELVDCQRELEKLNKERRLLNQEKTELL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 849 YKIKELKKQIEPRENEIRVMKEQIQEMEaelenfhkqnTQLELNITElwqklRATDQEMRRERQKERDLEALVKRFKTDL 928
Cdd:TIGR00606 347 VEQGRLQLQADRHQEHIRARDSLIQSLA----------TRLELDGFE-----RGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 929 HNCVAYIQEPRLLKEKVRGLfekyvqradMVEIAGLNTDLQQEytrqREHLERNLATLKKKvVKEGELHRTDYVRIMQEN 1008
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEI---------RDEKKGLGRTIELK----KEILEKKQEELKFV-IKELQQLEGSSDRILELD 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902638 1009 VSLIKEINEL------------RRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTA 1060
Cdd:TIGR00606 478 QELRKAERELskaeknsltetlKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT 541
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
693-803 |
8.10e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 693 QALEELtefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE---------SNLRL 763
Cdd:PRK00409 523 ASLEEL----ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikelRQLQK 598
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767902638 764 KGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIK 803
Cdd:PRK00409 599 GGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
599-816 |
8.17e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 599 EKIKELTD--KFIQE----MESLKTKNQVLRTEKE-----KQDVYHHEHIEDLLDKQSRELQDMeccNNQKLLLEYEKYQ 667
Cdd:PRK04863 901 EQLDEAEEakRFVQQhgnaLAQLEPIVSVLQSDPEqfeqlKQDYQQAQQTQRDAKQQAFALTEV---VQRRAHFSYEDAA 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 668 ELQLKSQRMQEEYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLLEEAQE--DV-RQQLREFEetkkqieededREIQD 744
Cdd:PRK04863 978 EMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQ-AQAQLAQYNQVLASLKSsyDAkRQMLQELK-----------QELQD 1045
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902638 745 IKTKY----EKKLRDEKEsnlRLKGETGIMRKKFSSLQKEIEERTNDIETLkgeqmklQGVIKSLEKDIQGLKREI 816
Cdd:PRK04863 1046 LGVPAdsgaEERARARRD---ELHARLSANRSRRNQLEKQLTFCEAEMDNL-------TKKLRKLERDYHEMREQV 1111
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
629-869 |
8.52e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 629 QDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQElQLKSQRMQ----EEYEKQLRDNDETKSQALEELTEFYEA 704
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYN-KIESARADlediKIKINELKDKHDKYEEIKNRYKSLKLE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 705 KLQEKTTLLEEAQE-----DVRQQLREFEETKKQIEEDEDR------EIQDIKTKYEKKLR--DEKESNLRLKgetgimR 771
Cdd:PRK01156 562 DLDSKRTSWLNALAvisliDIETNRSRSNEIKKQLNDLESRlqeieiGFPDDKSYIDKSIReiENEANNLNNK------Y 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 772 KKFSSLQKEIEERTNDIETLKGEQMKlqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKI 851
Cdd:PRK01156 636 NEIQENKILIEKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
250
....*....|....*...
gi 767902638 852 KELKKQIEPRENEIRVMK 869
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
579-880 |
9.64e-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: 40.42 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 579 VEELKMENEYQLRLKDMNYS-EKIKELTDKFIQEMESLKT--KNQvlrTEKEKQDVYHHEHIEDLLDKQSRELQDMECCN 655
Cdd:TIGR01612 1401 LEECKSKIESTLDDKDIDECiKKIKELKNHILSEESNIDTyfKNA---DENNENVLLLFKNIEMADNKSQHILKIKKDNA 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 656 NQKLLLEYEKYQELQLKSQRMQEEYEK---QLRDNDETKSQALEELTE----FYEAKLQEKttlLEEAQEDVRQQLREFE 728
Cdd:TIGR01612 1478 TNDHDFNINELKEHIDKSKGCKDEADKnakAIEKNKELFEQYKKDVTEllnkYSALAIKNK---FAKTKKDSEIIIKEIK 1554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 729 ETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKE--------IEERTNDIETlkgEQMKLQG 800
Cdd:TIGR01612 1555 DAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFEnkflkisdIKKKINDCLK---ETESIEK 1631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 801 VIKSLEKDIQGLK--------REIQERDETIQDKEKRIYDLKKK----NQELGKFKFVLDYKIKELKKQIEPRENEIRVM 868
Cdd:TIGR01612 1632 KISSFSIDSQDTElkengdnlNSLQEFLESLKDQKKNIEDKKKEldelDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIA 1711
|
330
....*....|...
gi 767902638 869 -KEQIQEMEAELE 880
Cdd:TIGR01612 1712 nKEEIESIKELIE 1724
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
619-916 |
9.82e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.52 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 619 NQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQ----ELQLKSQRMQEEYEKQLRDNDETKSQA 694
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEeqieEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 695 LEELTEFYEAKLQEKTTLLEEAQEDVRQQlREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKF 774
Cdd:pfam13868 111 QEEDQAEAEEKLEKQRQLREEIDEFNEEQ-AEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902638 775 SSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIydlkkknqelgkfkfvldyKIKEL 854
Cdd:pfam13868 190 RAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI-------------------ELKER 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902638 855 KKQIEPRENE---IRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERD 916
Cdd:pfam13868 251 RLAEEAEREEeefERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELE 315
|
|
| |
