|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
341-607 |
2.53e-21 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 95.48 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 341 VLCLCFSPSEETLVASTSKNQLY---SITMSLTEISKGepahfeylmyplHSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:cd00200 12 VTCVAFSPDGKLLATGSGDGTIKvwdLETGELLRTLKG------------HTGPVRDVAASADGTYLASGSSDKTIRLWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 418 YETN-TLELFKEYQEEAYSISLHPSGHFIVVGFADKlrlmNLLIDDIRSFK-EYSVRGCGE----CSFS-NGGHLFAAVN 490
Cdd:cd00200 80 LETGeCVRTLTGHTSYVSSVAFSPDGRILSSSSRDK----TIKVWDVETGKcLTTLRGHTDwvnsVAFSpDGTFVASSSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 491 GNVIHVYTTTSLENISSLKGHTGKIlreisafdvtyTAIVISHSGRMMFVGTSVGTIRamKYPLPLQKEFNEYQAHAGPI 570
Cdd:cd00200 156 DGTIKLWDLRTGKCVATLTGHTGEV-----------NSVAFSPDGEKLLSSSSDGTIK--LWDLSTGKCLGTLRGHENGV 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 767902636 571 TKMLLTFDDQFLLTAAEDGclfTWKVFDKDGRGIKRE 607
Cdd:cd00200 223 NSVAFSPDGYLLASGSEDG---TIRVWDLRTGECVQT 256
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
632-1150 |
3.31e-21 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 100.09 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 632 ELKTRVEELKMENEYQLRLKD-MNYSEKIKELTDKFI-----------QEMESLKTKNQVLRTEKEKQDVYHHEHIEDLL 699
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVeLNKLEKQKKENKKNIdkflteikkkeKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 700 DKQSrelqDMECCNNQKLLLEY---------EKYQELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFYEAKLQEKTTL 770
Cdd:TIGR04523 184 NIQK----NIDKIKNKLLKLELllsnlkkkiQKNKSLESQISELKKQ-NNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 771 LEEAQEDVRQ---QLREFEETKKQIEEDEDReIQDIKTKYEkKLRDEKESNL--RLKGETGIMRKKFSSLQKE------- 838
Cdd:TIGR04523 259 KDEQNKIKKQlseKQKELEQNNKKIKELEKQ-LNQLKSEIS-DLNNQKEQDWnkELKSELKNQEKKLEEIQNQisqnnki 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 839 IEERTNDIETLKGEQM-------KLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKE 911
Cdd:TIGR04523 337 ISQLNEQISQLKKELTnsesensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 912 LKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL-------WQKLRATDQEMRRERQkerDLEALVKRFKT 984
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntreslETQLKVLSRSINKIKQ---NLEQKQKELKS 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 985 DLHNCVAYIQEPRLLKEKVRGLFEKyvqradmveIAGLNTDlQQEYTRQREHLERNLATLKKKVVK-EGELHRTDYVRIM 1063
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKK---------ISSLKEK-IEKLESEKKEKESKISDLEDELNKdDFELKKENLEKEI 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1064 QENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEpsrdMLSTAPTARLNEQEETGRIIEMQRLEIQRL 1143
Cdd:TIGR04523 564 DEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKE----KKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
....*..
gi 767902636 1144 RDQIQEQ 1150
Cdd:TIGR04523 640 KNKLKQE 646
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
341-596 |
2.38e-19 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 91.90 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 341 VLCLCFSPSEETLvASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWNYET 420
Cdd:COG2319 165 VTSVAFSPDGKLL-ASGSDDG----TVRLWDLATGKLLRT----LTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 421 NT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDDIRSFKEYSVRGCGECSFS-NGGHLFAAVNGNVIHVY 497
Cdd:COG2319 236 GKlLRTLTGHSGSVRSVAFSPDGRLLASGSADGtVRLWDLATGELLRTLTGHSGGVNSVAFSpDGKLLASGSDDGTVRLW 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 498 TTTSLENISSLKGHTGKIlreisafdvtyTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQAHAGPITKMLLTF 577
Cdd:COG2319 316 DLATGKLLRTLTGHTGAV-----------RSVAFSPDGKTLASGSDDGTVRL--WDLATGELLRTLTGHTGAVTSVAFSP 382
|
250
....*....|....*....
gi 767902636 578 DDQFLLTAAEDGCLFTWKV 596
Cdd:COG2319 383 DGRTLASGSADGTVRLWDL 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
749-1095 |
8.19e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.26 E-value: 8.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 749 KSQALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNlRLKGETGIM 828
Cdd:TIGR02168 675 RRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 829 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYK 908
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 909 IKELKKQIEPRENEIRVMKEQIQ--------------EMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERD 974
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIEslaaeieeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 975 LEALVKRFKTDLHNCVAYIQEPRL----LKEKVRglfEKYVQRADMVEIAGLNTDLQQEYTRQRehlernLATLKKKVVK 1050
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVridnLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR------LKRLENKIKE 983
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 767902636 1051 EGELhrtdyvrimqeNVSLIKEINELRRELKFTRSQVYDLEAALK 1095
Cdd:TIGR02168 984 LGPV-----------NLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
772-1131 |
6.19e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.58 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 772 EEAQEDVRQQLREFEETKKQIEEDEdrEIQDIKTKYEKKLRDEKESNLRLKGETGIMRK-KFSSLQKEIEERTNDIETLK 850
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLD--LIIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 851 GEqmklqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGkfkfvlDYKIKELKKQIEPRENEIRVMKEQI 930
Cdd:TIGR02169 244 RQ-------LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 931 QEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEprlLKEKVRGLFEKY 1010
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE---VDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1011 VQRADMVEiaglntdlqqEYTRQREHLERNLATL---KKKVVKEGELHRTDYVRIMQ-------ENVSLIKEINELRREL 1080
Cdd:TIGR02169 388 KDYREKLE----------KLKREINELKRELDRLqeeLQRLSEELADLNAAIAGIEAkineleeEKEDKALEIKKQEWKL 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 767902636 1081 KFTRSQVYDLEAAL-KLTKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGR 1131
Cdd:TIGR02169 458 EQLAADLSKYEQELyDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGG 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
722-976 |
1.14e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.42 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 722 EKYQELQLKSQRMqEEYE--KQLRDNDETKSQALEELTEFyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIE---EDE 796
Cdd:TIGR02169 211 ERYQALLKEKREY-EGYEllKEKEALERQKEAIERQLASL-EEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 797 DREIQ----DIKTKYEKKLRDEKESNLRLKGETGIMRKKFS---SLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQG 869
Cdd:TIGR02169 289 QLRVKekigELEAEIASLERSIAEKERELEDAEERLAKLEAeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 870 LKREIQERDETIQ-------DKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHK 942
Cdd:TIGR02169 369 LRAELEEVDKEFAetrdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
250 260 270
....*....|....*....|....*....|....
gi 767902636 943 QNTQLELNITELWQKLRATDQEMRRERQKERDLE 976
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
403-598 |
1.48e-15 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 80.34 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 403 LIATCSLDRSIRLWNYETNT-LELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDD-IRSFK--EYSVRGcgeC 477
Cdd:COG2319 134 TLASGSADGTVRLWDLATGKlLRTLTGHSGAVTSVAFSPDGKLLASGSDDGtVRLWDLATGKlLRTLTghTGAVRS---V 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 478 SFS-NGGHLFAAVNGNVIHVYTTTSLENISSLKGHTGKIlreisafdvtyTAIVISHSGRMMFVGTSVGTIRAmkYPLPL 556
Cdd:COG2319 211 AFSpDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSV-----------RSVAFSPDGRLLASGSADGTVRL--WDLAT 277
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767902636 557 QKEFNEYQAHAGPITKMLLTFDDQFLLTAAEDGclfTWKVFD 598
Cdd:COG2319 278 GELLRTLTGHSGGVNSVAFSPDGKLLASGSDDG---TVRLWD 316
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
625-948 |
3.32e-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: 80.88 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 625 EKAQVMLELKTRVEELkmenEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQdvyhHEHIEDLLDKQSR 704
Cdd:TIGR02169 208 EKAERYQALLKEKREY----EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR----LEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 705 ELQDM---ECCNNQKLLLEYEKYQElqlKSQRMQEEYEKQLRDNDETKSQALEELTefyeaKLQEKTTLLEEAQEDVRQQ 781
Cdd:TIGR02169 280 KIKDLgeeEQLRVKEKIGELEAEIA---SLERSIAEKERELEDAEERLAKLEAEID-----KLLAEIEELEREIEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 782 LREFEEtkkqieededrEIQDIKTKYEK---KLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQG 858
Cdd:TIGR02169 352 RDKLTE-----------EYAELKEELEDlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 859 VIKSLEKDIQGLKREIQERDETIQDKEKRIydlKKKNQELgkfkfvldykiKELKKQIEPRENEIRVMKEQIQEMEAELE 938
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEI---KKQEWKL-----------EQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
330
....*....|
gi 767902636 939 NFHKQNTQLE 948
Cdd:TIGR02169 487 KLQRELAEAE 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
641-1151 |
1.01e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.34 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 641 KMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKtkNQVLRTEKEKQDVYHH-EHIEDLLDKQSRELQDMEccnnqKLLL 719
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIE--ELIKEKEKELEEVLREiNEISSELPELREELEKLE-----KEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 720 EYEKYQELQLKSQRMQEEYEKQLRdndetksqaleeltefyeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE----- 794
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKR-------------------KLEEKIRELEERIEELKKEIEELEEKVKELKElkeka 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 795 DEDREIQDIKTKYEKKLRDEKESNLRLKGE-TGIMR--KKFSSLQKEIEERTNDIETLKGEQMKLQG------VIKSLEK 865
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEiNGIEEriKELEEKEERLEELKKKLKELEKRLEELEErhelyeEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 866 DIQGLK-----REIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQI-------------------EPREN 921
Cdd:PRK03918 373 ELERLKkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteEHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 922 EIRVMKEQIQEMEAELENFHKQNTQLELNITELwQKLRATDQEMRRERQKERDLEALVKRFKT-DLHNCVAYIQEPRLLK 1000
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1001 EKVRGLFEkyvqradmvEIAGLNTDLQ--QEYTRQREHLERNLATLKKKVvkeGELHRtdyvRIMQENVSLIKEINELRR 1078
Cdd:PRK03918 532 EKLIKLKG---------EIKSLKKELEklEELKKKLAELEKKLDELEEEL---AELLK----ELEELGFESVEELEERLK 595
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902636 1079 ELKFTRSQVYDLEAAlkltkkvrPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQE 1151
Cdd:PRK03918 596 ELEPFYNEYLELKDA--------EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
758-1099 |
4.59e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.40 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 758 EFYEAKLQEKTTLLEEA------QEDVRQQLREFEETKKQIEEDED--REI---------QDIKTKYEKKLRDEKEsNLR 820
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAagiskyKERRKETERKLERTRENLDRLEDilNELerqlkslerQAEKAERYKELKAELR-ELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 821 LkgetGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGK 900
Cdd:TIGR02168 227 L----ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 901 FKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVK 980
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 981 RFKTDLHncvayiqeprLLKEKVrglfekYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEgelHRTDYV 1060
Cdd:TIGR02168 383 TLRSKVA----------QLELQI------ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE---LQAELE 443
|
330 340 350
....*....|....*....|....*....|....*....
gi 767902636 1061 RIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKK 1099
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
386-596 |
1.02e-13 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 74.56 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 386 PLHSAPITGLATCIRKPLIATCSLDRSIRLWNYETN-TLELFKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNL----L 459
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGlLLRTLTGHTGAVRSVAFSPDGKTLASGSADGtVRLWDLatgkL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 460 IDDIRSFKE--YSVrgcgecSFSNGGHLFAAVNG-NVIHVYTTTSLENISSLKGHTGKIlreisafdvtyTAIVISHSGR 536
Cdd:COG2319 155 LRTLTGHSGavTSV------AFSPDGKLLASGSDdGTVRLWDLATGKLLRTLTGHTGAV-----------RSVAFSPDGK 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 537 MMFVGTSVGTIRAmkYPLPLQKEFNEYQAHAGPITKMLLTFDDQFLLTAAEDGCLFTWKV 596
Cdd:COG2319 218 LLASGSADGTVRL--WDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL 275
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
614-984 |
1.19e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.87 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 614 EEVLVTKTDMEEKAQVMLELKTRVEELKmENEYQLRLKDMNYSEKIKELTDKfIQEMESLKTKNQVLRTEKE--KQDVYH 691
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEER-IKELEEKEERLEELKKKLKelEKRLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 692 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQ----------ALEEL----- 756
Cdd:PRK03918 357 LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGElkkeikelkkAIEELkkakg 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 757 ---------TEFYEAKLQEKTTLleeaqedvrqQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKE--SNLRLKGET 825
Cdd:PRK03918 437 kcpvcgrelTEEHRKELLEEYTA----------ELKRIEKELKEIEEKE-RKLRKELRELEKVLKKESEliKLKELAEQL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 826 GIMRKKFSSLQKE-IEERTNDIETLKGEQMKLQGVIKSLEKDI---QGLKREIQERDETIQDKEKRIYDLKKKNQELGkF 901
Cdd:PRK03918 506 KELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELeklEELKKKLAELEKKLDELEEELAELLKELEELG-F 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 902 KFV--LDYKIKEL-------------KKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMR 966
Cdd:PRK03918 585 ESVeeLEERLKELepfyneylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEEL 664
|
410 420
....*....|....*....|
gi 767902636 967 RER--QKERDLEALVKRFKT 984
Cdd:PRK03918 665 REEylELSRELAGLRAELEE 684
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
655-978 |
1.34e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.87 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 655 YSEKIKELTDkfiqEMESLKTKNQVLRTEKEkqdvyhheHIEDLLDKQSRELQDMEccnnqKLLLEYEKYQELQLKSQRM 734
Cdd:TIGR02169 672 EPAELQRLRE----RLEGLKRELSSLQSELR--------RIENRLDELSQELSDAS-----RKIGEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 735 QEEYEKQLRDNDETKSQALEEltefYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDE 814
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIEN----VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 815 KESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK 894
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 895 NQElgkfkfvLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL----WQKLRATDQEMRRERq 970
Cdd:TIGR02169 891 RDE-------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipEEELSLEDVQAELQR- 962
|
....*...
gi 767902636 971 KERDLEAL 978
Cdd:TIGR02169 963 VEEEIRAL 970
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
621-1151 |
1.52e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.54 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 621 TDMEEK-AQVMLELK--TRVEELKMEN-EYQLRLKDMNYSEKIKElTDKFIQEMESLKTKNQVLRTekekqDVYHHEHIE 696
Cdd:pfam15921 320 SDLESTvSQLRSELReaKRMYEDKIEElEKQLVLANSELTEARTE-RDQFSQESGNLDDQLQKLLA-----DLHKREKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 697 DLLDKQSRELQDMECCNN-------QKLLLEYEKYQELQLKSQRMQEEYEKQLrdndETKSQALEELTEFYEaKLQEKTT 769
Cdd:pfam15921 394 SLEKEQNKRLWDRDTGNSitidhlrRELDDRNMEVQRLEALLKAMKSECQGQM----ERQMAAIQGKNESLE-KVSSLTA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 770 LLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKESNlrlkgetgimrKKFSSLQKEIEERTNDIETL 849
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSE-RTVSDLTASLQEKERAIEATN-----------AEITKLRSRVDLKLQELQHL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 850 KGEQMKLQGVikslEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQ 929
Cdd:pfam15921 537 KNEGDHLRNV----QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 930 IQEMEAELENFHKQNTQLELNITELwqkLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEk 1009
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLELEKVKL---VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE- 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1010 yvqradmvEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGElhrtdyvrIMQENVSLIKEINELRRELKFTRSQVYD 1089
Cdd:pfam15921 689 --------EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH--------AMKVAMGMQKQITAKRGQIDALQSKIQF 752
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902636 1090 LEAALKLTKKVRPQEVSETEPSRDMLSTAPTarlnEQEETGRIIEMQRLEIQRLRDQIQEQE 1151
Cdd:pfam15921 753 LEEAMTNANKEKHFLKEEKNKLSQELSTVAT----EKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
599-1099 |
2.38e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 74.76 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 599 KDGRGIKREReVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEyQLRLKdmnYSEKIKELTDkFIQEMESLKTKNQ 678
Cdd:pfam05483 85 KEAEKIKKWK-VSIEAELKQKENKLQENRKIIEAQRKAIQELQFENE-KVSLK---LEEEIQENKD-LIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 679 VLR------TEKEKQDVYHHEHIEDL-------LDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDN 745
Cdd:pfam05483 159 LLKetcarsAEKTKKYEYEREETRQVymdlnnnIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 746 DETKSQALEELTEfYEAKLQEKTTLLEEAQEDVRQ---QLREFEETKKQIEEDED---REIQDIK--------------- 804
Cdd:pfam05483 239 EKQVSLLLIQITE-KENKMKDLTFLLEESRDKANQleeKTKLQDENLKELIEKKDhltKELEDIKmslqrsmstqkalee 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 805 -----TKYEKKLRDEKESNLRlkgETGIMRKKFSSLQKEIEERTNDIETL-KGEQMKLQG---VIKSLEKDIQGLKREIQ 875
Cdd:pfam05483 318 dlqiaTKTICQLTEEKEAQME---ELNKAKAAHSFVVTEFEATTCSLEELlRTEQQRLEKnedQLKIITMELQKKSSELE 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 876 ERDETIQDKEKRIYDLKK----------KNQELGKFKFVLDYKIKELKKQIEPRENEIRVMK--------------EQIQ 931
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKilaedeklldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqltaiktseehylKEVE 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 932 EMEAELENFHKQNTQLELNITELwqklratDQEMRRERQKERDLEALVKRFKTDLHNCVAyiQEPRLLKEkVRGLFEKYV 1011
Cdd:pfam05483 475 DLKTELEKEKLKNIELTAHCDKL-------LLENKELTQEASDMTLELKKHQEDIINCKK--QEERMLKQ-IENLEEKEM 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1012 QRADMVEiaglntDLQQEYTRQREHLERNLatlkKKVVKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLE 1091
Cdd:pfam05483 545 NLRDELE------SVREEFIQKGDEVKCKL----DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH 614
|
....*...
gi 767902636 1092 AALKLTKK 1099
Cdd:pfam05483 615 QENKALKK 622
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
717-977 |
2.63e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 717 LLLEYEKYQElQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDE 796
Cdd:COG1196 230 LLLKLRELEA-ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 797 DReiqdiktkyekkLRDEKESNLRLKGETgimrkkfSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQE 876
Cdd:COG1196 309 ER------------RRELEERLEELEEEL-------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 877 RDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQ 956
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260
....*....|....*....|.
gi 767902636 957 KLRATDQEMRRERQKERDLEA 977
Cdd:COG1196 450 EEAELEEEEEALLELLAELLE 470
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
619-988 |
2.97e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 74.29 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 619 TKTDMEEKAQVMLELKTRVEELKME-NEYQLRLKDMNySEKIKELTDKFIQEMESLKTKNQVLRTE---KEKQDVYHHEH 694
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQlNQLKSEISDLN-NQKEQDWNKELKSELKNQEKKLEEIQNQisqNNKIISQLNEQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 695 IEDLldkqSRELQDMECCNNQKLLLEYEKYQELQlKSQRMQEEYEKQLRdNDETKSQALEELTEFYEAKLQEKTTLLEEA 774
Cdd:TIGR04523 344 ISQL----KKELTNSESENSEKQRELEEKQNEIE-KLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 775 QEDVRQQLREFEETKKQIEEDED------REIQDIKTKYE--KKLRDEKESNLR-LKGETGIMRKKFSSLQKEIEERTND 845
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSeikdltNQDSVKELIIKnlDNTRESLETQLKvLSRSINKIKQNLEQKQKELKSKEKE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 846 IETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKK---------KNQELGKFKFVLDYKIKELKKQI 916
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQ 577
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902636 917 EPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHN 988
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
605-995 |
1.81e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.48 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 605 KREREVGFAEEvLVTKTDMEEKAQvmlELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEK 684
Cdd:PTZ00121 1438 KKAEEAKKADE-AKKKAEEAKKAE---EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 685 EKQDVYHHEHIEDLLD-KQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAK 763
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 764 LQEKTTLLEEAQEDVRQQLREFEETKKQIEE-DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEER 842
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 843 TNDIETLKGEQmklqgviKSLEKDIQGLKREIQERDETIQDKeKRIYDLKKKNQELGKFKFVLDYKIKELKKQieprENE 922
Cdd:PTZ00121 1674 KKKAEEAKKAE-------EDEKKAAEALKKEAEEAKKAEELK-KKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEE 1741
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902636 923 IRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEalVKRFKTDLHNCVAYIQE 995
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIE 1812
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
654-982 |
1.82e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 654 NYSEKIKELTDKfIQEMESLKTKNQVLRTEKEKQdvyhHEHIEDLLDKQSRELQDMEccnnQKLLLEYEKYQELQLKSQR 733
Cdd:TIGR02168 674 ERRREIEELEEK-IEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 734 mqeeYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLLEEAqEDVRQQLREfeetkkQIEEDEDR--EIQDIKTKYEKKL 811
Cdd:TIGR02168 745 ----LEERIAQLSKELTELEAEIEE-LEERLEEAEEELAEA-EAEIEELEA------QIEQLKEElkALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 812 RDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDL 891
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 892 KKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQ-NTQLELNITELWQKLRATDQEMRRERQ 970
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARR 972
|
330
....*....|..
gi 767902636 971 KERDLEALVKRF 982
Cdd:TIGR02168 973 RLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
720-983 |
2.11e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.02 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 720 EYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEeltefYEAKLQEKTTLLEEAQEDvRQQLREFEETKKQIEEDEDRE 799
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDE-----LSQELSDASRKIGEIEKE-IEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 800 IQDIktkyEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERtndietlkgEQMKLQGVIKSLEKDIQGLKREIQERDE 879
Cdd:TIGR02169 746 LSSL----EQEIENVKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 880 TIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLR 959
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
250 260
....*....|....*....|....
gi 767902636 960 ATDQEMRRERQKERDLEALVKRFK 983
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKR 916
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
621-939 |
5.65e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.05 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 621 TDMEEKAQVMLELKTRVEELKMENE-YQLRLKDMNYSEKIKELTDKFIQEMESLKTKN-QVLRTEKEKQDvyhhEHIEDL 698
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQsYKQEIKNLESQINDLESKIQNQEKLNQQKDEQiKKLQQEKELLE----KEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 699 LDKQSRELQDMECCNNQKLLLE--------YEKYQELQLKSqrMQEEYEKQLRDNDETKSQALEELTEFyeAKLQEKTTL 770
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKEliiknldnTRESLETQLKV--LSRSINKIKQNLEQKQKELKSKEKEL--KKLNEEKKE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 771 LEEAQEDVRQQLREFEETKKQIEED---EDREIQDIKTKYEKKLRDEKESNLRlkgetgimrKKFSSLQKEIEERTNDIE 847
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEkkeKESKISDLEDELNKDDFELKKENLE---------KEIDEKNKEIEELKQTQK 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 848 TLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMK 927
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
330
....*....|..
gi 767902636 928 EQIQEMEAELEN 939
Cdd:TIGR04523 659 NKWPEIIKKIKE 670
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
620-1151 |
1.19e-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: 69.00 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 620 KTDMEEKAQVMLELKTRVEELKMENEYQlrlkdmnySEKIKELTDKFIQEMESLKTKNQVLRtEKEKQDVYHHEHIEDLL 699
Cdd:pfam05557 40 KRQLDRESDRNQELQKRIRLLEKREAEA--------EEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 700 DKQSRELQDMEccnnqkllleyekYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQE--- 776
Cdd:pfam05557 111 NELSELRRQIQ-------------RAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElef 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 777 DVRQQLREFEETKKQIEE-----DEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEErtndIETLKG 851
Cdd:pfam05557 178 EIQSQEQDSEIVKNSKSElaripELEKELERLR-EHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREE----AATLEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 852 EQMKLQGVIKSLEKDIQGLKREIQerdeTIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQ 931
Cdd:pfam05557 253 EKEKLEQELQSWVKLAQDTGLNLR----SPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 932 EMEAELENFHKQNTQLELnitelwQKLRATdqemrrerqKERD-LEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKY 1010
Cdd:pfam05557 329 DLNKKLKRHKALVRRLQR------RVLLLT---------KERDgYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1011 VQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVvkegELHRTDYVRimQENVSLIKEINELRRELKFTRSQVYDL 1090
Cdd:pfam05557 394 AHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQE----SLADPSYSK--EEVDSLRRKLETLELERQRLREQKNEL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902636 1091 EAALKltkKVRPQEVSETEPSRDM-LSTAPTARLNEQeeTGRIIEMQRLEIQRLRDQIQEQE 1151
Cdd:pfam05557 468 EMELE---RRCLQGDYDPKKTKVLhLSMNPAAEAYQQ--RKNQLEKLQAEIERLKRLLKKLE 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
736-1068 |
4.23e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 736 EEYEKQLRDNDETKSQ---ALEELTEFYEaKLQEKTTLLEEAQEdVRQQLREFEET----KKQIEEDEDREIQDIKTKYE 808
Cdd:TIGR02168 175 KETERKLERTRENLDRledILNELERQLK-SLERQAEKAERYKE-LKAELRELELAllvlRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 809 KKlRDEKESNLRLKGEtgimrkKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI 888
Cdd:TIGR02168 253 EE-LEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 889 YDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRE 968
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 969 RQKERDLEALVKRFKTDLHNCVAYIQEPRlLKEKVRGLFEKyvqRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKV 1048
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEEL---EEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
330 340
....*....|....*....|.
gi 767902636 1049 VKEGELH-RTDYVRIMQENVS 1068
Cdd:TIGR02168 482 RELAQLQaRLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
722-1051 |
4.57e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 722 EKYQELQLKsqrmQEEYEKQLRdndetkSQALEELtefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEdedreiq 801
Cdd:COG1196 213 ERYRELKEE----LKELEAELL------LLKLREL----EAELEELEAELEELEAELEELEAELAELEAELEE------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 802 diktkyekklrdekesnlrlkgetgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETI 881
Cdd:COG1196 272 --------------------------LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 882 QDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL-WQKLRA 960
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELaAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 961 TDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRAdmvEIAGLNTDLQQEYTRQREHLERN 1040
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE---ALLELLAELLEEAALLEAALAEL 482
|
330
....*....|.
gi 767902636 1041 LATLKKKVVKE 1051
Cdd:COG1196 483 LEELAEAAARL 493
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
620-1154 |
5.58e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 67.30 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 620 KTDMEEKAQVMLELKTRVEELK--MENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDV------YH 691
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKklIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLlyldylKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 692 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKyQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLL 771
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEK-LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 772 EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKgetgimrkkfssLQKEIEERTNDIETLKG 851
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL------------QEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 852 EQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVM--KEQ 929
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 930 IQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRR--ERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLF 1007
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSqkESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1008 EKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDYVRImQENVSLIKEINELRRELKFTRSQV 1087
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV-LEIDPILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902636 1088 YDLEAA--LKLTKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQVT 1154
Cdd:pfam02463 621 RAKVVEgiLKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
338-452 |
1.06e-10 |
|
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: 63.89 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 338 KQDVLCLCFSPSEETLVASTSKNqlysiTMSLTEISKGEPAHfeylMYPLHSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:cd00200 177 TGEVNSVAFSPDGEKLLSSSSDG-----TIKLWDLSTGKCLG----TLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
|
90 100 110
....*....|....*....|....*....|....*.
gi 767902636 418 YET-NTLELFKEYQEEAYSISLHPSGHFIVVGFADK 452
Cdd:cd00200 248 LRTgECVQTLSGHTNSVTSLAWSPDGKRLASGSADG 283
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
723-1162 |
1.28e-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: 65.53 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 723 KYQELQLKSQRMQEEYE-KQLRDNDETKSQALEELTEFYEAKLQEKTTlleeaqedvRQQLREFEETKKQIEEDEDREIQ 801
Cdd:pfam05557 8 KARLSQLQNEKKQMELEhKRARIELEKKASALKRQLDRESDRNQELQK---------RIRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 802 DIKTKYEK---KLRDEKESNLRLKGETgimrkkFSSLQKEIEErtndietLKGEQMKLQGVIKSLEKDIQGLKREIQERD 878
Cdd:pfam05557 79 RLKKKYLEalnKKLNEKESQLADAREV------ISCLKNELSE-------LRRQIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 879 ETIQDKEKRIYDLKKKNQELGkfkfVLDYKIKELKKQIEPRENEIRVMK------EQIQEMEAELENFHKQNTQL-ELNI 951
Cdd:pfam05557 146 AKASEAEQLRQNLEKQQSSLA----EAEQRIKELEFEIQSQEQDSEIVKnskselARIPELEKELERLREHNKHLnENIE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 952 TELWQKLRATDQEMRRERQKER-----DLEALVKRFKTDLHNCVAYIQEPRL---LKEKVRGLFEKYVQR--ADMVEIAG 1021
Cdd:pfam05557 222 NKLLLKEEVEDLKRKLEREEKYreeaaTLELEKEKLEQELQSWVKLAQDTGLnlrSPEDLSRRIEQLQQReiVLKEENSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1022 LNTDLQQEYTRQREhLERNLATLKKKVVKEG-ELHRTD-YVRIMQENVSLI-KEINELRRELKFTRSQVYDLEAALKLTK 1098
Cdd:pfam05557 302 LTSSARQLEKARRE-LEQELAQYLKKIEDLNkKLKRHKaLVRRLQRRVLLLtKERDGYRAILESYDKELTMSNYSPQLLE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1099 KVRP-----QEV---------------SETEPSRDMLSTA---------------PTARLNEQEETGRIIEMQRLEIQRL 1143
Cdd:pfam05557 381 RIEEaedmtQKMqahneemeaqlsvaeEELGGYKQQAQTLerelqalrqqesladPSYSKEEVDSLRRKLETLELERQRL 460
|
490
....*....|....*....
gi 767902636 1144 RDQIQEQEQVTGFHTLAGV 1162
Cdd:pfam05557 461 REQKNELEMELERRCLQGD 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
625-950 |
1.93e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 625 EKAQVMLELKTRVEELKMEnEYQLRLKDMNYS-EKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHIEDLLDKQS 703
Cdd:TIGR02168 210 EKAERYKELKAELRELELA-LLVLRLEELREElEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 704 R------ELQDMEccnNQKllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELtefyeAKLQEKTTLLEEAQED 777
Cdd:TIGR02168 289 ElyalanEISRLE---QQK-----QILRERLANLERQLEELEAQLEELESKLDELAEEL-----AELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 778 VRQQLREFEETKKQIEEDEdREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETL--KGEQMK 855
Cdd:TIGR02168 356 LEAELEELEAELEELESRL-EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 856 LQGVIKSLEKDIQGLKrEIQERDETIQDKEKRIYDLKKKNQElgkfkfvldyKIKELKKQieprENEIRVMKEQIQEMEA 935
Cdd:TIGR02168 435 LKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQ----------ALDAAERE----LAQLQARLDSLERLQE 499
|
330
....*....|....*
gi 767902636 936 ELENFHKQNTQLELN 950
Cdd:TIGR02168 500 NLEGFSEGVKALLKN 514
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
723-1046 |
4.46e-10 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 64.43 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 723 KYQELQlKSQRMQEEYEKQLRDNDETKSQALEELTEFYEaKLQEKTTLLEEAQEdvrqqLREFEETKKQieededrEIQD 802
Cdd:pfam01576 10 KEEELQ-KVKERQQKAESELKELEKKHQQLCEEKNALQE-QLQAETELCAEAEE-----MRARLAARKQ-------ELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 803 IKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGL----------KR 872
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLedqnsklskeRK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 873 EIQER-------------------------DETIQDKEKRIYDLKKKNQELGKFKFVLD--------------YKIKELK 913
Cdd:pfam01576 156 LLEERiseftsnlaeeeekakslsklknkhEAMISDLEERLKKEEKGRQELEKAKRKLEgestdlqeqiaelqAQIAELR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 914 KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCV--- 990
Cdd:pfam01576 236 AQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLdtt 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902636 991 AYIQEPRLLKEKVRGLF------EKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKK 1046
Cdd:pfam01576 316 AAQQELRSKREQEVTELkkaleeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
604-1080 |
9.64e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 604 IKREREVGFAEEVLVTKTDMEEKAQVMLELKtRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRTE 683
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 684 KEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQAleeltefYEAK 763
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA-------EEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 764 LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlrlkgetgimRKKFSSLQKEIEERT 843
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE------------KKKIAHLKKEEEKKA 1770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 844 NDIETLKgeqmklQGVIKslekdiQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfvldykikelkkqieprENEI 923
Cdd:PTZ00121 1771 EEIRKEK------EAVIE------EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK-------------------EGNL 1819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 924 RVMKEQIQEMEAELENFHKQNTQLElNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNcvayIQEPRLLKEKV 1003
Cdd:PTZ00121 1820 VINDSKEMEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE----IEEADEIEKID 1894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1004 RGLFEKYVQRADMveiAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELH------RTDYVRIMQENVSLIKEINELR 1077
Cdd:PTZ00121 1895 KDDIEREIPNNNM---AGKNNDIIDDKLDKDEYIKRDAEETREEIIKISKKDmcindfSSKFCDYMKDNISSGNCSDEER 1971
|
...
gi 767902636 1078 REL 1080
Cdd:PTZ00121 1972 KEL 1974
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
628-1155 |
1.32e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.83 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 628 QVMLELKTRVEELKMENE--YQLRLKDMNYSEKIKELTDKFIQEMESLK-----------TKNQVLRT------------ 682
Cdd:pfam15921 110 QSVIDLQTKLQEMQMERDamADIRRRESQSQEDLRNQLQNTVHELEAAKclkedmledsnTQIEQLRKmmlshegvlqei 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 683 --------EKEKQDVYHHEHIEDL--------LDKQSRELQ--------------------DMECCNNQKLLLEYEKYQE 726
Cdd:pfam15921 190 rsilvdfeEASGKKIYEHDSMSTMhfrslgsaISKILRELDteisylkgrifpvedqlealKSESQNKIELLLQQHQDRI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 727 LQLKSQR---------------------------MQEE-------YEKQLRDNDETKSQALEELTE---FYEAKLQ--EK 767
Cdd:pfam15921 270 EQLISEHeveitgltekassarsqansiqsqleiIQEQarnqnsmYMRQLSDLESTVSQLRSELREakrMYEDKIEelEK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 768 TTLLEEAQ-EDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDI 846
Cdd:pfam15921 350 QLVLANSElTEARTERDQFSQESGNLDDQLQKLLADLH-KREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 847 EtlkgeqmKLQGVIKSLEKDIQGlkrEIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKEL---KKQIEPRENEI 923
Cdd:pfam15921 429 Q-------RLEALLKAMKSECQG---QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTV 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 924 RVMKEQIQEMEAELENFHKQNTQLELNITELWQKLratdQEMRRERQKERDLEALVKRFKTDLHNCVAYIQeprLLKEKV 1003
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL----QHLKNEGDHLRNVQTECEALKLQMAEKDKVIE---ILRQQI 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1004 RGLFEKYVQR-----ADMVEIAGLNTDLQ------QEYTRQREHLERNLATLKKKvVKEGELHRTDYVRIMQENVSLIKE 1072
Cdd:pfam15921 572 ENMTQLVGQHgrtagAMQVEKAQLEKEINdrrlelQEFKILKDKKDAKIRELEAR-VSDLELEKVKLVNAGSERLRAVKD 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1073 I----NELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIE-MQRLEIQRLRDQI 1147
Cdd:pfam15921 651 IkqerDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKsMEGSDGHAMKVAM 730
|
....*...
gi 767902636 1148 QEQEQVTG 1155
Cdd:pfam15921 731 GMQKQITA 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
792-1160 |
1.78e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 792 IEEDEDRE--------IQDIKTKYEKKLRDEKESNLRLKG-ETGIMRKkfSSLQKEIEERTNDIETLKGEQMKLQGVIKS 862
Cdd:PRK03918 141 LESDESREkvvrqilgLDDYENAYKNLGEVIKEIKRRIERlEKFIKRT--ENIEELIKEKEKELEEVLREINEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 863 LEKDIQGLKREIQERDETiqdKEKrIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEaELENFHK 942
Cdd:PRK03918 219 LREELEKLEKEVKELEEL---KEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 943 QNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKrfktDLHNCVAYIQEprlLKEKVRGLFEKYvqrADMVEIAGL 1022
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEE---LKKKLKELEKRL---EELEERHEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1023 NTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAAlKLTKKVRP 1102
Cdd:PRK03918 364 YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA-KGKCPVCG 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1103 QEVSETEPSRDMLS-TAPTARL-NEQEETGRIIEMQRLEIQRLRDQIQEQEQVTGFHTLA 1160
Cdd:PRK03918 443 RELTEEHRKELLEEyTAELKRIeKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA 502
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
614-938 |
1.84e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.06 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 614 EEVLVTKTDMEEKAQVMLELKTRVEElkmeneyQLRLKDMNYSE--KIKELTDKFIQEMESLKTKNQVLR---TEKE--K 686
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASLQE-------KERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRnvqTECEalK 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 687 QDVYHHEHIEDLLDKQSRELQDMECCNNQKL-LLEYEKYQ-ELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAkl 764
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTAgAMQVEKAQlEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL-- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 765 qEKTTLLEEAQEDVRQqLREFEETKKQI--EEDEDR-EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 841
Cdd:pfam15921 633 -EKVKLVNAGSERLRA-VKDIKQERDQLlnEVKTSRnELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 842 RTNDIETLKGEQ-------MKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKK 914
Cdd:pfam15921 711 TRNTLKSMEGSDghamkvaMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
330 340
....*....|....*....|....
gi 767902636 915 QIEPRENEIRVMKEQIQEMEAELE 938
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEVALD 814
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
657-995 |
1.98e-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: 61.90 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 657 EKIKELTDKFIQEMESLKTKN-QVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQLKSQRMQ 735
Cdd:COG5185 159 GIIKDIFGKLTQELNQNLKKLeIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGF 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 736 EEYEKQLRDNDETK---SQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLR 812
Cdd:COG5185 239 QDPESELEDLAQTSdklEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 813 DEKESN-----LRLKGETGIMR------KKFSSLQKEIEERTNDIETLKGEQM--KLQGVIKSLEKDIQGLKREIQERDE 879
Cdd:COG5185 319 AAAEAEqeleeSKRETETGIQNltaeieQGQESLTENLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 880 TIQDKEKRIydlkkkNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELE-NFHKQNTQLELNITELWQKL 958
Cdd:COG5185 399 NQRGYAQEI------LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNkVMREADEESQSRLEEAYDEI 472
|
330 340 350
....*....|....*....|....*....|....*...
gi 767902636 959 RATDQEMRRERQKER-DLEALVKRFKTDLHNCVAYIQE 995
Cdd:COG5185 473 NRSVRSKKEDLNEELtQIESRVSTLKATLEKLRAKLER 510
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
736-1149 |
3.15e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 736 EEYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLlEEAQEDVRQQLREFEETKkqieEDEDREIQDIKTKYEKkLRDEK 815
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEE-HEERREELETL-EAEIEDLRETIAETERER----EELAEEVRDLRERLEE-LEEER 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 816 ESnlrLKGETGimrkkFSSLqkeieertnDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKN 895
Cdd:PRK02224 296 DD---LLAEAG-----LDDA---------DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 896 QELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENfhkQNTQLElNITELWQKLRATDQEMrreRQKERDL 975
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD---APVDLG-NAEDFLEELREERDEL---REREAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 976 EAlvkrfktDLHNCVAYIQEPRLLKEK---------------VRGLFEKYVQRADmveiagLNTDLQQEYTrQREHLERN 1040
Cdd:PRK02224 432 EA-------TLRTARERVEEAEALLEAgkcpecgqpvegsphVETIEEDRERVEE------LEAELEDLEE-EVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1041 LATLKKKVVKEGELHRtdyvriMQENVSLIKE--------INELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSR 1112
Cdd:PRK02224 498 LERAEDLVEAEDRIER------LEERREDLEEliaerretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430
....*....|....*....|....*....|....*....
gi 767902636 1113 DMLSTAPTAR--LNEQEETGRIIEMQRLEIQRLRDQIQE 1149
Cdd:PRK02224 572 EEVAELNSKLaeLKERIESLERIRTLLAAIADAEDEIER 610
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
665-1152 |
3.90e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 665 KFIQEM--ESLKTKNQVLRTEKEKQDVYHHEHIEDLlDKQSRELQDmeccnnqklllEYEKYQELQLKSQRMQEEYE--K 740
Cdd:COG4717 41 AFIRAMllERLEKEADELFKPQGRKPELNLKELKEL-EEELKEAEE-----------KEEEYAELQEELEELEEELEelE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 741 QLRDNDETKSQALEELTEFYEA-----KLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDrEIQDIKTKYEKKLRDek 815
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLyqeleALEAELAELPERLEELEERLEELRELEEELEELEA-ELAELQEELEELLEQ-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 816 eSNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKD--IQGLKREIQERDET---------IQDK 884
Cdd:COG4717 186 -LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEleAAALEERLKEARLLlliaaallaLLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 885 EKRIYDLKKKNQELGK--------FKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQ 956
Cdd:COG4717 265 GGSLLSLILTIAGVLFlvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 957 KLRATDQEMR--RERQKERDLEALVKRFKTDLHNCVAyiqeprllkekvrGLFEKYVQRADMVEIaglntdlQQEYTRQR 1034
Cdd:COG4717 345 RIEELQELLReaEELEEELQLEELEQEIAALLAEAGV-------------EDEEELRAALEQAEE-------YQELKEEL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1035 EHLERNLATLKKKVvkEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALkltkkvrpqevsetepsrdm 1114
Cdd:COG4717 405 EELEEQLEELLGEL--EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-------------------- 462
|
490 500 510
....*....|....*....|....*....|....*...
gi 767902636 1115 lstaptarlnEQEETGRIIEMQRLEIQRLRDQIQEQEQ 1152
Cdd:COG4717 463 ----------EQLEEDGELAELLQELEELKAELRELAE 490
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
665-1152 |
4.44e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 665 KFIQEMESLKTKNQVLRTEKEKQDVYHHehIEDLLDKQSRELQDMEccnnqkllleyEKYQELQLKSQRMqeEYEKQLRD 744
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAE--LQEELEELEEELEELE-----------AELEELREELEKL--EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 745 NDETKSQALEELTEFYE--AKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEdedrEIQDIKTKYEKKLRDEKESNLRLK 822
Cdd:COG4717 130 LYQELEALEAELAELPErlEELEERLEELRELEEELEELEAELAELQEELEE----LLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 823 GETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQgVIKSLEK------------DIQGLKREIQERDETIQDKEKRIYD 890
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEarlllliaaallALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 891 LkkknqeLGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMR--RE 968
Cdd:COG4717 285 L------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLReaEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 969 RQKERDLEALVKRFKTDLHNCVAyiqeprllkekvrGLFEKYVQRADMVEIaglntdlQQEYTRQREHLERNLATLKKKV 1048
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGV-------------EDEEELRAALEQAEE-------YQELKEELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1049 vkEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRpqEVSETEPSRDMLStaptARLNEQEE 1128
Cdd:COG4717 419 --EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG--ELAELLQELEELK----AELRELAE 490
|
490 500
....*....|....*....|....
gi 767902636 1129 TGRIIEMQRLEIQRLRDQIQEQEQ 1152
Cdd:COG4717 491 EWAALKLALELLEEAREEYREERL 514
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
613-1092 |
4.82e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 613 AEEVLvtkTDMEEKAQVMLELKTRVEELKMENEYQLRLKDmNYSEKIKELTDkfiqEMESLKTKNQVLRTEKEKQDVyHH 692
Cdd:PRK02224 239 ADEVL---EEHEERREELETLEAEIEDLRETIAETERERE-ELAEEVRDLRE----RLEELEEERDDLLAEAGLDDA-DA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 693 EHIEDLLDKQSRELQDMEccnnqkllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQAlEELTEfyEAKLQEKTtlLE 772
Cdd:PRK02224 310 EAVEARREELEDRDEELR-----------DRLEECRVAAQAHNEEAESLREDADDLEERA-EELRE--EAAELESE--LE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 773 EAQEDVRQQLREFEETKKQIEEDEDReIQDIKTKYEK--KLRDEKESNL-RLKGETGIMRKKFSSLQK------------ 837
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRER-FGDAPVDLGNaeDFLEELREERdELREREAELEATLRTARErveeaealleag 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 838 ----------------EIEERTNDIETLKGEQMKLQGVIKSLEKDIqglkreiqERDETIQDKEKRIYDLKKKNQELGKf 901
Cdd:PRK02224 453 kcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERL--------ERAEDLVEAEDRIERLEERREDLEE- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 902 kfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQemRRERQKERdLEALvKR 981
Cdd:PRK02224 524 ------LIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKER-IESL-ER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 982 FKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADMVE-----IAGLN--------TDLQQEYTRQREHLERNLATLKKKV 1048
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrerKRELEaefdeariEEAREDKERAEEYLEQVEEKLDELR 673
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 767902636 1049 VKEGELHRtdyvRI-MQENVslIKEINELRRELKFTRSQVYDLEA 1092
Cdd:PRK02224 674 EERDDLQA----EIgAVENE--LEELEELRERREALENRVEALEA 712
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
726-977 |
6.31e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.77 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 726 ELQLKSQRMQEEYEkQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEdVRQQLREFEETKKQIEEDEDREIQDIKT 805
Cdd:COG1340 12 ELEEKIEELREEIE-ELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 806 KYEK--KLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIEtlkgEQMKLQGVIKSLEKDIQGLKREIQERDEtIQD 883
Cdd:COG1340 90 LREEldELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPE----EEKELVEKIKELEKELEKAKKALEKNEK-LKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 884 KEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQ 963
Cdd:COG1340 165 LRAELKELRKEAEEIHK-------KIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250
....*....|....
gi 767902636 964 EMRRERQKERDLEA 977
Cdd:COG1340 238 ELRELRKELKKLRK 251
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
742-984 |
9.62e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.65 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 742 LRDNDETKSQA-LEELTEFY-EAKLQEKTTLLEEAQEDVRQQLrefEETKKQIEEDEdREIQDIKTKYekklrdekeSNL 819
Cdd:COG3206 142 YTSPDPELAAAvANALAEAYlEQNLELRREEARKALEFLEEQL---PELRKELEEAE-AALEEFRQKN---------GLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 820 RLKGETGIMRKKFSSLQKEIEErtndietLKGEQMKLQGVIKSLEKDIQGLKREIQE--RDETIQDKEKRIYDLKKKNQE 897
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAE-------ARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 898 LGKfKFVLDY-KIKELKKQIEPRENEIRVMKEQI-QEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDL 975
Cdd:COG3206 282 LSA-RYTPNHpDVIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
....*....
gi 767902636 976 EALVKRFKT 984
Cdd:COG3206 361 EVARELYES 369
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
604-1114 |
1.25e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.68 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 604 IKREREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQ------EMESLKTKN 677
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKElqqlegSSDRILELD 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 678 QVLRTE---------------KEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEyekyQELQLKSQRMQEEyeKQL 742
Cdd:TIGR00606 478 QELRKAerelskaeknsltetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT----QMEMLTKDKMDKD--EQI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 743 RDNDETKSQALEELTEFYEAKLQEKTTL---------LEEAQEDVRQQLREFEETKKQIEEDEDREIQDIkTKYEKKLRD 813
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYFPNKKQLEDWLhskskeinqTRDRLAKLNKELASLEQNKNHINNELESKEEQL-SSYEDKLFD 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 814 -----EKESNL-RLKGETGIMRKKFSSLQKEIEERTNDIETLKGE--------------QMKLQGVIKSLEKDIQGLKRE 873
Cdd:TIGR00606 631 vcgsqDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcqrvfqtEAELQEFISDLQSKLRLAPDK 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 874 IQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITE 953
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTD 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 954 LwqklRATDQEMRRERQKERDLEALVKrfKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADmveiagLNTDLQQEYTRQ 1033
Cdd:TIGR00606 791 V----TIMERFQMELKDVERKIAQQAA--KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIE------LNRKLIQDQQEQ 858
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1034 REHLERNLATLKKKVVKEGE-LHRTDyvRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSR 1112
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTnLQRRQ--QFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN 936
|
..
gi 767902636 1113 DM 1114
Cdd:TIGR00606 937 KK 938
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
829-986 |
1.46e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.86 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 829 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIyDLKKKNQELGkfkfVLDYK 908
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-GNVRNNKEYE----ALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902636 909 IKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQK-ERDLEALVKRFKTDL 986
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEElEAEREELAAKIPPEL 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
829-986 |
1.59e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 829 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfVLDYK 908
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA---ELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 909 IKELKKQI-------------------EPRENEIRVM---------KEQIQEMEAELENFHKQNTQLELNITELWQKLRA 960
Cdd:COG4942 103 KEELAELLralyrlgrqpplalllspeDFLDAVRRLQylkylaparREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180
....*....|....*....|....*.
gi 767902636 961 TDQEMRRERQKERDLEALVKRFKTDL 986
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKEL 208
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
725-922 |
1.63e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 725 QELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIK 804
Cdd:COG4942 27 AELEQLQQEIAEL-EKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAELAELEKEIAELR-AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 805 TKYEKKLR--------------------DEKESNLR-LKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSL 863
Cdd:COG4942 104 EELAELLRalyrlgrqpplalllspedfLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902636 864 EKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENE 922
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
632-1043 |
2.52e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.52 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 632 ELKTRVEELKMENEYQLRLKDMNYSEkikelTDKFIQEMESLKTKNQVLRTE--KEKQDVyhhEHIEDLLDKQSRELQDM 709
Cdd:TIGR00606 713 STESELKKKEKRRDEMLGLAPGRQSI-----IDLKEKEIPELRNKLQKVNRDiqRLKNDI---EEQETLLGTIMPEEESA 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 710 ECCnnqklLLEYEKYQELQLKSQRMQEEYEKQLRDNDETksqaleELTEFYEAKLQEKttllEEAQEDVRQQLREFEETK 789
Cdd:TIGR00606 785 KVC-----LTDVTIMERFQMELKDVERKIAQQAAKLQGS------DLDRTVQQVNQEK----QEKQHELDTVVSKIELNR 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 790 KQIEeDEDREIQDIKTKYeKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQgviKSLEKDIQG 869
Cdd:TIGR00606 850 KLIQ-DQQEQIQHLKSKT-NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLE---TFLEKDQQE 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 870 LKREIQERDETIQDKEKRIYDLKKK-NQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLE 948
Cdd:TIGR00606 925 KEELISSKETSNKKAQDKVNDIKEKvKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMR 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 949 LNITELWQKLR-ATDQEMRRERQKErdlealVKRFKTDLHNCVAYIQEPRLLKEKvrglfEKYVQRADMVEIAGLNTDL- 1026
Cdd:TIGR00606 1005 QDIDTQKIQERwLQDNLTLRKRENE------LKEVEEELKQHLKEMGQMQVLQMK-----QEHQKLEENIDLIKRNHVLa 1073
|
410 420
....*....|....*....|
gi 767902636 1027 ---QQEYTRQREHLERNLAT 1043
Cdd:TIGR00606 1074 lgrQKGYEKEIKHFKKELRE 1093
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
606-938 |
2.75e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.19 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 606 REREVGFAE-EVLVTKTDMEEKAQVMLELKTRVEELKMENeyqlrLKDMNYSEKIKELTDKFIQEmeslkTKNQVLRTEK 684
Cdd:pfam05483 448 REKEIHDLEiQLTAIKTSEEHYLKEVEDLKTELEKEKLKN-----IELTAHCDKLLLENKELTQE-----ASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 685 EKQDVYHHEHIEDLLDKQSRELQdmeccnnqkllleyEKYQELQLKSQRMQEEYeKQLRDNDETKSQALEELTEFYEAKL 764
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLE--------------EKEMNLRDELESVREEF-IQKGDEVKCKLDKSEENARSIEYEV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 765 QEKTTLLEEAQEDVRQQLREFEETKKQIEE--DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSL----QKE 838
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEElhQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIidnyQKE 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 839 IEERTNDIETLKGEQMKLQGVIKS---LEKDIQG------------LKREIQERDETIQDKEKRIYDLKKKNQELGKFKF 903
Cdd:pfam05483 663 IEDKKISEEKLLEEVEKAKAIADEavkLQKEIDKrcqhkiaemvalMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKA 742
|
330 340 350
....*....|....*....|....*....|....*
gi 767902636 904 VLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELE 938
Cdd:pfam05483 743 ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
879-1095 |
4.64e-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: 56.70 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 879 ETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKL 958
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 959 ratdqemrrERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGL-FEKYVQRADMVEIAGLNTDlQQEYTRQREHL 1037
Cdd:COG4942 100 ---------EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqYLKYLAPARREQAEELRAD-LAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902636 1038 ERNLATLkKKVVKEGELHRTDYVRIMQENVSLI----KEINELRRELKFTRSQVYDLEAALK 1095
Cdd:COG4942 170 EAERAEL-EALLAELEEERAALEALKAERQKLLarleKELAELAAELAELQQEAEELEALIA 230
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
624-950 |
5.12e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 624 EEKAQVMLELKTRVEELkMENEYQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLRTEKEKqdvyhhEHIEDLLDKQS 703
Cdd:PRK03918 387 EKLEKELEELEKAKEEI-EEEISKITARIGELKKEIKEL-KKAIEELKKAKGKCPVCGRELTE------EHRKELLEEYT 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 704 RELQDMEccNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQ---ALEELTEFYEAKLQEKTTLLEEAQEDVRQ 780
Cdd:PRK03918 459 AELKRIE--KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkeLEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 781 QLREFEETKKQIEEDEdrEIQDIKTKYEKKLRDEKESNLRLKGEtgIMRKKFSSLqKEIEERTNDIETLKGEQMKLQGV- 859
Cdd:PRK03918 537 LKGEIKSLKKELEKLE--ELKKKLAELEKKLDELEEELAELLKE--LEELGFESV-EELEERLKELEPFYNEYLELKDAe 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 860 --IKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDY------------------------------ 907
Cdd:PRK03918 612 keLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYeelreeylelsrelaglraeleelekrree 691
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 767902636 908 ------KIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELN 950
Cdd:PRK03918 692 ikktleKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
761-1151 |
1.22e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 761 EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReiqdiKTKYEkKLRDEKESNLRLKgetgimrkkfsSLQKEIE 840
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-----REALQ-RLAEYSWDEIDVA-----------SAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 841 ERTNDIETLKGEQmklqgviksleKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELgkfkfvldykikelkkqieprE 920
Cdd:COG4913 672 ELEAELERLDASS-----------DDLAALEEQLEELEAELEELEEELDELKGEIGRL---------------------E 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 921 NEIRVMKEQIQEMEAELENF-HKQNTQLELNITELWQKLRATdqemRRERQKERDLEALVKRFKTDLHNcvayiqeprlL 999
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALGD----AVERELRENLEERIDALRARLNR----------A 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1000 KEKVRGLFEKYVQRADMvEIAGLNTDL------QQEYTR-QREHLERNLATLKKKVVKEGELHRTDYVRIMQENVSLIKE 1072
Cdd:COG4913 786 EEELERAMRAFNREWPA-ETADLDADLeslpeyLALLDRlEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKE 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1073 ----INELRRELKFTRSQVYDLEAalkltKKVRPQEVSETepsRDMLStapTARLNEQEETGRIIEMQRLEIQRLRDQIQ 1148
Cdd:COG4913 865 ridpLNDSLKRIPFGPGRYLRLEA-----RPRPDPEVREF---RQELR---AVTSGASLFDEELSEARFAALKRLIERLR 933
|
...
gi 767902636 1149 EQE 1151
Cdd:COG4913 934 SEE 936
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
745-942 |
1.75e-07 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 54.30 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 745 NDETKSQALEELTEFYEaKLQEKTTLLEEAQEDVRQQLREFEetkKQIEEDEDrEIQDIKTKYEKKLRDEKESnlrlkge 824
Cdd:cd22656 108 DDEELEEAKKTIKALLD-DLLKEAKKYQDKAAKVVDKLTDFE---NQTEKDQT-ALETLEKALKDLLTDEGGA------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 825 tgIMRKKFSSLQKEIEERTNDIetlkgeqmklqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKknqelgkfkfv 904
Cdd:cd22656 176 --IARKEIKDLQKELEKLNEEY-------------AAKLKAKIDELKALIADDEAKLAAALRLIADLTA----------- 229
|
170 180 190
....*....|....*....|....*....|....*...
gi 767902636 905 LDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHK 942
Cdd:cd22656 230 ADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKD 267
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
636-1152 |
1.84e-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: 55.83 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 636 RVEELKMENEYQLRLKDMNysEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHhEHIEDLLDKQSRELQDMECCNNQ 715
Cdd:TIGR02168 325 LEELESKLDELAEELAELE--EKLEELKEELESLEAELEELEAELEELESRLEELE-EQLETLRSKVAQLELQIASLNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 716 KLLLEYEKyQELQLKSQRMQEEYEKQLRDNDETKSQALE---ELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQI 792
Cdd:TIGR02168 402 IERLEARL-ERLEDRRERLQQEIEELLKKLEEAELKELQaelEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 793 EEDEDR------EIQDIKTKYEKKLRDEKE---SNLRLKGETGIMRKKFS---SLQKEIE----ERTNDIETlKGEQMKL 856
Cdd:TIGR02168 481 ERELAQlqarldSLERLQENLEGFSEGVKAllkNQSGLSGILGVLSELISvdeGYEAAIEaalgGRLQAVVV-ENLNAAK 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 857 QGvIKSLEK-----------------DIQGLKREIQERDETIQDKEKRIY---------------------------DLK 892
Cdd:TIGR02168 560 KA-IAFLKQnelgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVkfdpklrkalsyllggvlvvddldnalELA 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 893 KKNQELGKFkFVLD------------------YKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNIT-- 952
Cdd:TIGR02168 639 KKLRPGYRI-VTLDgdlvrpggvitggsaktnSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEql 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 953 -----ELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLFEkyvqrADMVEIAGLNTDLQ 1027
Cdd:TIGR02168 718 rkeleELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----EAEAEIEELEAQIE 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1028 QeYTRQREHLERNLATLKKKVvkegELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKvrpqEVSE 1107
Cdd:TIGR02168 793 Q-LKEELKALREALDELRAEL----TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA----EIEE 863
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 767902636 1108 TEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQ 1152
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
762-888 |
2.43e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 762 AKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKL---RDEKESNlRLKGETGIMRKKFSSLQKE 838
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLgnvRNNKEYE-ALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767902636 839 IEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI 888
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
742-983 |
2.59e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 742 LRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQedvrQQLREFEETKKQIEEDEDREIqdiktkYEKKLRDEKESNLRL 821
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQKNGLVDLSEEAKL------LLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 822 KGETGIMRKKFSSLQKEIEERTNDIETLKGEQmklqgVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKF 901
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 902 KFvldykiKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLelnitelwQKLRATDQEMRRERQKERDL-EALVK 980
Cdd:COG3206 307 LQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL--------PELEAELRRLEREVEVARELyESLLQ 372
|
...
gi 767902636 981 RFK 983
Cdd:COG3206 373 RLE 375
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
793-1149 |
2.92e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 793 EEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKR 872
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 873 EIQERDETIQDKEKRIYDLKKKnqelgkfkfvldykIKELKKQIEPRENEIRvmKEQIQEMEAELENFHKQNTQLELNIT 952
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEED--------------LHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 953 ELWQKLRATDQEMRRERQKERDLEALVkrfktdlhncvayiqeprllkekvrglfekyvqradmveiagLNTDLQQEYTR 1032
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQR------------------------------------------IDLKEQIKSIE 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1033 QREHLernlatlkkkvvkegelhrtdyvrimqenvsLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQ---EVSETE 1109
Cdd:TIGR02169 854 KEIEN-------------------------------LNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELE 902
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 767902636 1110 PSRDMLSTA---PTARLNEQEETGRIIEMQRLEIQRLRDQIQE 1149
Cdd:TIGR02169 903 RKIEELEAQiekKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
647-1107 |
3.30e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 647 QLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLRTEKEK--QDVYHHEHIEDLLDKQsRELQDMEccnnqkllLEYEKY 724
Cdd:COG4717 82 EAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKleKLLQLLPLYQELEALE-AELAELP--------ERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 725 QELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEdVRQQLREFEETKKQIEEDEDREIQDIK 804
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE-LQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 805 TKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVI-KSLEKDIQGLKREIQERDETIQD 883
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLaLLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 884 KEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEpRENEIRVMKEQIQEMEAELenfhkQNTQLELNITELWQKLRATDQ 963
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLD-RIEELQELLREAEELEEEL-----QLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 964 EMRRERQKE-RDLEALVKRFktdlhncvayiqepRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQQ------EYTRQREH 1036
Cdd:COG4717 385 EELRAALEQaEEYQELKEEL--------------EELEEQLEELLGELEELLEALDEEELEEELEEleeeleELEEELEE 450
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767902636 1037 LERNLATLKKKVvkEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSE 1107
Cdd:COG4717 451 LREELAELEAEL--EQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLE 519
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
750-981 |
3.97e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 750 SQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIktkyEKKLRDekesnlrLKGETGIMR 829
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-RRIAAL----ARRIRA-------LEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 830 KKFSSLQKEIEERTNDIETLKGEqmkLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKI 909
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902636 910 KELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKR 981
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
340-468 |
4.23e-07 |
|
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: 53.11 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 340 DVLCLCFSPSEeTLVASTSKNQlysiTMSLTEISKGEPAHFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWNYE 419
Cdd:cd00200 137 WVNSVAFSPDG-TFVASSSQDG----TIKLWDLRTGKCVAT----LTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767902636 420 T-NTLELFKEYQEEAYSISLHPSGHFIVVGFADKlrlmNLLIDDIRSFKE 468
Cdd:cd00200 208 TgKCLGTLRGHENGVNSVAFSPDGYLLASGSEDG----TIRVWDLRTGEC 253
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
695-1153 |
8.77e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.37 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 695 IEDLLDKQSRELQDMEccNNQKLLLEYEKYQELQLKS-QRMQEEYEKQLRDNDETKSQ-----ALEELTEFYEAKLQEKT 768
Cdd:PRK01156 185 IDYLEEKLKSSNLELE--NIKKQIADDEKSHSITLKEiERLSIEYNNAMDDYNNLKSAlnelsSLEDMKNRYESEIKTAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 769 TLLEEAQEDVrQQLREFEETKKQIEEDE---DREIQDIKTKYEKKLRDEKESNLRLKGETG----IMRK---------KF 832
Cdd:PRK01156 263 SDLSMELEKN-NYYKELEERHMKIINDPvykNRNYINDYFKYKNDIENKKQILSNIDAEINkyhaIIKKlsvlqkdynDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 833 SSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKdiqgLKREIQERDETIQDKEKRIYDLKKKN----QELGKFKFVLDYK 908
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIES----LKKKIEEYSKNIERMSAFISEILKIQeidpDAIKKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 909 IKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNT----QLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKT 984
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 985 DLHNCVAyiQEPRLLKEKVRGLFEKYVQRADMVeiAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELH--RTDYVRI 1062
Cdd:PRK01156 498 KIVDLKK--RKEYLESEEINKSINEYNKIESAR--ADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDskRTSWLNA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1063 MQEnVSLI------KEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTaptaRLNEQEETGRIIEMQ 1136
Cdd:PRK01156 574 LAV-ISLIdietnrSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNN----KYNEIQENKILIEKL 648
|
490
....*....|....*..
gi 767902636 1137 RLEIQRLRDQIQEQEQV 1153
Cdd:PRK01156 649 RGKIDNYKKQIAEIDSI 665
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
615-1047 |
9.09e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 53.26 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 615 EVLVTKTDMEEKAQVMLELKTRVEelKMENEYQLRLKdmnysekiKEltDKFIQEMESLKTKNQVLRTEKEKQDVYHHEH 694
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHE--AMISDLEERLK--------KE--EKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 695 IEDL---LDKQSRELQ------DMECCNNQKLLleyEKYQELQLKSQRMQE--EYEKQLRDNDETKSQALEELTEFYEAK 763
Cdd:pfam01576 231 IAELraqLAKKEEELQaalarlEEETAQKNNAL---KKIRELEAQISELQEdlESERAARNKAEKQRRDLGEELEALKTE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 764 LqEKTTLLEEAQEDVR-QQLREFEETKKQIEED---EDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEI 839
Cdd:pfam01576 308 L-EDTLDTTAAQQELRsKREQEVTELKKALEEEtrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 840 EERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPR 919
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 920 ENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLratDQEMRRERQKERDLEALV-------KRFKTDLHNCVAY 992
Cdd:pfam01576 467 ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQL---EEEEEAKRNVERQLSTLQaqlsdmkKKLEEDAGTLEAL 543
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902636 993 IQEPRLLKEKVRGLFEKYVQRADMVE-IAGLNTDLQQEY---TRQREHLERNLATLKKK 1047
Cdd:pfam01576 544 EEGKKRLQRELEALTQQLEEKAAAYDkLEKTKNRLQQELddlLVDLDHQRQLVSNLEKK 602
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
718-957 |
9.76e-07 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 52.12 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 718 LLEYEKYQELQLKSQRMQEEYEKQLRD------NDETKSQALEELTEFYEAKLQ----EKTTLLEEAQEdVRQQLREF-- 785
Cdd:pfam15905 58 SLELKKKSQKNLKESKDQKELEKEIRAlvqergEQDKRLQALEEELEKVEAKLNaavrEKTSLSASVAS-LEKQLLELtr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 786 -----------EETKKQIE-------------EDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 841
Cdd:pfam15905 137 vnellkakfseDGTQKKMSslsmelmklrnklEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 842 RTNDIETLKGEQMKLQGVIKSLEKdiqgLKREIQERDETiqdkekriydLKKKNQELGKFKFVLDYKIKELKKQIEPR-- 919
Cdd:pfam15905 217 EKSETEKLLEYITELSCVSEQVEK----YKLDIAQLEEL----------LKEKNDEIESLKQSLEEKEQELSKQIKDLne 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767902636 920 ---------ENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQK 957
Cdd:pfam15905 283 kckllesekEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
747-983 |
1.34e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 747 ETKSQALEELTEFYeAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED-----REIQDIktkyEKKLRDEKESNLRL 821
Cdd:COG4913 613 AALEAELAELEEEL-AEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAEL----EAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 822 KGetgimrkkfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRI-----YDLKKKNQ 896
Cdd:COG4913 688 AA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 897 ELGKFKFVldykiKELKKQIeprENEIRVMKEQIQEMEAELEN-FHKQNTQLELNITELWQKLRATDQ-EMRRERQKERD 974
Cdd:COG4913 757 AALGDAVE-----RELRENL---EERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLESLPEyLALLDRLEEDG 828
|
....*....
gi 767902636 975 LEALVKRFK 983
Cdd:COG4913 829 LPEYEERFK 837
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
820-1094 |
2.19e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 820 RLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELG 899
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 900 KFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFhkQNTQLELNITELWQKLRATDQEMRRERQKERDLEALV 979
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 980 KRFKTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDY 1059
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
250 260 270
....*....|....*....|....*....|....*
gi 767902636 1060 VRIMQENVSLIKEINELRRELKFTRSQVYDLEAAL 1094
Cdd:COG4372 287 ALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
726-1004 |
2.34e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 726 ELQLKSQRMQEEYeKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEaQEDVRQQLREFEEtkkqieededreiqDIKT 805
Cdd:pfam07888 77 ELESRVAELKEEL-RQSREKHEELEEKYKELSASSEELSEEKDALLAQ-RAAHEARIRELEE--------------DIKT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 806 KYEKKLrdEKESNL-RLKGETgimrKKFSSLQKEIEErtnDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDK 884
Cdd:pfam07888 141 LTQRVL--ERETELeRMKERA----KKAGAQRKEEEA---ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 885 EKRIYDLKKKNQELGKFKFVLDYKIKELK----------KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITEL 954
Cdd:pfam07888 212 QDTITTLTQKLTTAHRKEAENEALLEELRslqerlnaseRKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADA 291
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 955 ----------WQKLRATdqeMRRERQKERDleaLVKRFKTDLHNCVAYIQEPRLLKEKVR 1004
Cdd:pfam07888 292 slalregrarWAQERET---LQQSAEADKD---RIEKLSAELQRLEERLQEERMEREKLE 345
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
641-1081 |
2.44e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.97 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 641 KMENEYQLRLK-----DMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQ 715
Cdd:TIGR00606 605 QNKNHINNELEskeeqLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQ 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 716 KLLLEYEKYQELQLKSQRM-------QEEYEKQLRDNDETKSQALEeLTEFYEAKLQEKTTLLEEAQEDVRQQLREFEET 788
Cdd:TIGR00606 685 RVFQTEAELQEFISDLQSKlrlapdkLKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 789 KKQIEEDEdreiqdiktKYEKKLRDEKESNLRLKGETGIMRKkfssLQKEIEERTNDIETLKGeqmKLQGVikSLEKDIQ 868
Cdd:TIGR00606 764 KNDIEEQE---------TLLGTIMPEEESAKVCLTDVTIMER----FQMELKDVERKIAQQAA---KLQGS--DLDRTVQ 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 869 GLKREIQERDET--------------IQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEME 934
Cdd:TIGR00606 826 QVNQEKQEKQHEldtvvskielnrklIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK 905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 935 AELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRllkekvrglfEKYVQRA 1014
Cdd:TIGR00606 906 DAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK----------DDYLKQK 975
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1015 DmVEIAGLNTDLqQEYTRQREHLERNLATLKKKVVKEGELHrtdyvRIMQENVSLIK---EINELRRELK 1081
Cdd:TIGR00606 976 E-TELNTVNAQL-EECEKHQEKINEDMRLMRQDIDTQKIQE-----RWLQDNLTLRKrenELKEVEEELK 1038
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
426-594 |
2.51e-06 |
|
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: 50.80 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 426 FKEYQEEAYSISLHPSGHFIVVGFADK-LRLMNLLIDD-IRSFKEYSVrGCGECSFSNGGHLFAAV-NGNVIHVYTTTSL 502
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGtIKVWDLETGElLRTLKGHTG-PVRDVAASADGTYLASGsSDKTIRLWDLETG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 503 ENISSLKGHTGKIlreisafdvtyTAIVISHSGRMMFVGTSVGTIRAmkYPLPLQKEFNEYQAHAGPITKMLLTFDDQFL 582
Cdd:cd00200 84 ECVRTLTGHTSYV-----------SSVAFSPDGRILSSSSRDKTIKV--WDVETGKCLTTLRGHTDWVNSVAFSPDGTFV 150
|
170
....*....|..
gi 767902636 583 LTAAEDGCLFTW 594
Cdd:cd00200 151 ASSSQDGTIKLW 162
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
801-1022 |
2.58e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 801 QDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDET 880
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 881 IQDKEKRIYDLKKKNQELGK---FKFVLD-------YKIKELKKQIEP-RENEIRVMKEQIQEMEAELENFHKQNTQLEL 949
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRqppLALLLSpedfldaVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902636 950 NITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLhncVAYIQEPRLLKEKVRGLFEKYVQRADMVEIAGL 1022
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
771-935 |
2.75e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.78 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 771 LEEAQEDVRQQLREFEETKKQIEEDEDREIQdikTKYEKKLRdekesnlrlkgetgimrkkfsslqkeieertndietlk 850
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEEREL---TEEEEEIR-------------------------------------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 851 geqmKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK-NQELGKFKFV--LDYKIKELKKQIEPRENEIRVMK 927
Cdd:COG2433 417 ----RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEeRREIRKDREIsrLDREIERLERELEEERERIEELK 492
|
....*...
gi 767902636 928 EQIQEMEA 935
Cdd:COG2433 493 RKLERLKE 500
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
779-939 |
2.96e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 779 RQQLREFEETKKQIEEDEDREIQDIKtkyEKKLRDEKESNLRLKGEtgimrkkfssLQKEIEERtndietlkgeqmklqg 858
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIK---KEALLEAKEEIHKLRNE----------FEKELRER---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 859 vikslEKDIQGLKREIQERDETIqdkEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEpreneirVMKEQIQEMEAELE 938
Cdd:PRK12704 81 -----RNELQKLEKRLLQKEENL---DRKLELLEKREEELEKKEKELEQKQQELEKKEE-------ELEELIEEQLQELE 145
|
.
gi 767902636 939 N 939
Cdd:PRK12704 146 R 146
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
707-970 |
4.13e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.28 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 707 QDMECCNNQKLLLEYEKYQELQ-LKSQRMQEEYEKQLRDNDetKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREF 785
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEkMEQERLRQEKEEKAREVE--RRRKLEEAEKARQAEMDRQAAIYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 786 EETKkqiEEDEDREIQDIKTK-----------YEKKLRDEKESNLRLKGETGIMRKKF---SSLQKEIEERTNDIETLKG 851
Cdd:pfam17380 351 ERIR---QEERKRELERIRQEeiameisrmreLERLQMERQQKNERVRQELEAARKVKileEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 852 EQ-----MKLQGVIKSLEKDIQGLKREIQERDETI----QDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENE 922
Cdd:pfam17380 428 EQeearqREVRRLEEERAREMERVRLEEQERQQQVerlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767902636 923 IRVMKEQIQEMEAELENfhKQNTQLELNITELWQKLRATDQEMRRERQ 970
Cdd:pfam17380 508 MIEEERKRKLLEKEMEE--RQKAIYEEERRREAEEERRKQQEMEERRR 553
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
829-977 |
4.35e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 829 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIqdkEKRIYDLKKKNQELGKFKFVL--- 905
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGSVSYLDVLLgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 906 ---DY-------------------KIKELKKQIEPRENEIRVMKEQIQEMEAELEnfhKQNTQLELNITELWQKLRATDQ 963
Cdd:COG3883 113 sfsDFldrlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELE---AAKAELEAQQAEQEALLAQLSA 189
|
170
....*....|....
gi 767902636 964 EMRRERQKERDLEA 977
Cdd:COG3883 190 EEAAAEAQLAELEA 203
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
761-1004 |
5.39e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 761 EAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEK--KLRDEKESNLRLKGEtgiMRKKFSSLQKE 838
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEaqELREKRDELNEKVKE---LKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 839 IEERTNDIETLKGEQMKLQGV---IKSLEKDIQGLKREIQERDETIqDKEKRIYD-LKKKNQELGKFKFVLDY--KIKEL 912
Cdd:COG1340 87 LNELREELDELRKELAELNKAggsIDKLRKEIERLEWRQQTEVLSP-EEEKELVEkIKELEKELEKAKKALEKneKLKEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 913 KKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNcvaY 992
Cdd:COG1340 166 RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE---L 242
|
250
....*....|..
gi 767902636 993 IQEPRLLKEKVR 1004
Cdd:COG1340 243 RKELKKLRKKQR 254
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
607-1152 |
7.51e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 607 EREVGFAEEVLVTKTDMEEKAQVMLELKTRVEELKMENEYQlRLKDMNYSEKIKELTDKFIQEM----------ESLKTK 676
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-KAEDARKAEEARKAEDAKRVEIarkaedarkaEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 677 NQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQL-----KSQRMQEEYEKQLRDNDETKSQ 751
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkKAEEAKKDAEEAKKAEEERNNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 752 ALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIE---EDEDREIQDIKTKYEKKlrdEKESNLRLKGETGim 828
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakkAEEKKKADEAKKKAEEA---KKADEAKKKAEEA-- 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 829 RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQErdetiqdKEKRIYDLKKKNQELgkfkfvldYK 908
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-------AKKKADAAKKKAEEK--------KK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 909 IKELKKQIEprenEIRVMKEQIQEMEAELENFHKQNTQLElnitelwQKLRAtdQEMRRERQKERDLEALVKRF--KTDL 986
Cdd:PTZ00121 1393 ADEAKKKAE----EDKKKADELKKAAAAKKKADEAKKKAE-------EKKKA--DEAKKKAEEAKKADEAKKKAeeAKKA 1459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 987 HNCVAYIQEPRLLKEKVRGLFEKyvQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKvvkeGELHRTDYVRIMQEN 1066
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEA--KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA----EEAKKADEAKKAEEA 1533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1067 vsliKEINELRR-ELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDM-LSTAPTARLNEQEETGRIIEMQRLEIQRLR 1144
Cdd:PTZ00121 1534 ----KKADEAKKaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMaLRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
....*...
gi 767902636 1145 DQIQEQEQ 1152
Cdd:PTZ00121 1610 EEAKKAEE 1617
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
62-420 |
9.96e-06 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 49.52 E-value: 9.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 62 ALSISPNRRYLAiseTVQEKPAITIYELSSIPCRKrkVLNNFDFQVQkfiSMAFSPDSKYLLAqTSppESNLVYwLWEKQ 141
Cdd:COG2319 125 SVAFSPDGKTLA---SGSADGTVRLWDLATGKLLR--TLTGHSGAVT---SVAFSPDGKLLAS-GS--DDGTVR-LWDLA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 142 KVMAIVRIDTQNNPVYQVSFSPqDNTQVcVTG--NGMFKLLRFAEGTLKQTSfqRGEPQNYLAHTWVADDK-IVVGTDTG 218
Cdd:COG2319 193 TGKLLRTLTGHTGAVRSVAFSP-DGKLL-ASGsaDGTVRLWDLATGKLLRTL--TGHSGSVRSVAFSPDGRlLASGSADG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 219 KLFLfesgdqrWETsimvkeptNGSKSLDVIQESESliefpPVSSplpsyeqmVAASSHSQMsmpqvfaiaayskgFACS 298
Cdd:COG2319 269 TVRL-------WDL--------ATGELLRTLTGHSG-----GVNS--------VAFSPDGKL--------------LASG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 299 AGPGRVLLFEkmeekdfYRESREIRIPVDPQSndpsqsdkqDVLCLCFSPSEETLVASTSKNqlysiTMSLTEISKGEPA 378
Cdd:COG2319 307 SDDGTVRLWD-------LATGKLLRTLTGHTG---------AVRSVAFSPDGKTLASGSDDG-----TVRLWDLATGELL 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 767902636 379 HFeylmYPLHSAPITGLATCIRKPLIATCSLDRSIRLWNYET 420
Cdd:COG2319 366 RT----LTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
811-951 |
1.22e-05 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 48.82 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 811 LRDEKESNLRLKGEtgIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGV------IKSLEKDIQGLKREIQERDETIQDK 884
Cdd:pfam17060 96 IPASFISALELKED--VKSSPRSEADSLGTPIKVDLLRNLKPQESPETPrrinrkYKSLELRVESMKDELEFKDETIMEK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 885 E-------KRIYDLKKKNQELGK-FKFVLDYK-----------------IKELKKQIEPRENEIRVMKEQIQEMEAELEN 939
Cdd:pfam17060 174 DrelteltSTISKLKDKYDFLSReFEFYKQHHehggnnsiktatkhefiISELKRKLQEQNRLIRILQEQIQFDPGALHD 253
|
170
....*....|..
gi 767902636 940 FHKQNTQLELNI 951
Cdd:pfam17060 254 NGPKNLVLNGAI 265
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
693-981 |
1.65e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 693 EHIEDLLDKQSRElQDMECCNNQKLLLeyekyqelqlKSQRMQEEYEKQLRDNDETKSQALEELtefyeAKLQEKTTLLE 772
Cdd:TIGR00618 594 VRLQDLTEKLSEA-EDMLACEQHALLR----------KLQPEQDLQDVRLHLQQCSQELALKLT-----ALHALQLTLTQ 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 773 EAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKY----------EKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEER 842
Cdd:TIGR00618 658 ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkemlaqcQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 843 TNDIETLKGEQMKLQG-VIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPREN 921
Cdd:TIGR00618 738 EDALNQSLKELMHQARtVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 922 EIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKR 981
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
620-1041 |
1.70e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.05 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 620 KTDMEEKAQVMLELKTRVEELKMENEyqlrlkdmNYSEKIKELTdkfiqemESLKTKNQ---VLRTEKEKQDVYHHEHiE 696
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQNS--------DCKQHIEVLK-------ESLTAKEQraaILQTEVDALRLRLEEK-E 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 697 DLLDKQSRELQDMeccNNQKLLLEYE-------------KYQELQLKSQRMQEeyekQLRDNDetksQALEELTEFYEAk 763
Cdd:pfam10174 359 SFLNKKTKQLQDL---TEEKSTLAGEirdlkdmldvkerKINVLQKKIENLQE----QLRDKD----KQLAGLKERVKS- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 764 LQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREiqdiktkyEKKLRDEKESnlrLKGETGIMRKKFSSLQKEIEERT 843
Cdd:pfam10174 427 LQTDSSNTDTALTTLEEALSEKERIIERLKEQRERE--------DRERLEELES---LKKENKDLKEKVSALQPELTEKE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 844 NDIETLKGEQ-------MKLQGVIKSLEKDIQgLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQI 916
Cdd:pfam10174 496 SSLIDLKEHAsslassgLKKDSKLKSLEIAVE-QKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEES 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 917 EPRENEIRVMKEQIQEMEAELENFHKQNTQLELNI-------TELWQKLRATDQEMRRERQKERDleaLVKRFKTDLHNC 989
Cdd:pfam10174 575 GKAQAEVERLLGILREVENEKNDKDKKIAELESLTlrqmkeqNKKVANIKHGQQEMKKKGAQLLE---EARRREDNLADN 651
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902636 990 VAYIQEPRLLK--EKVRGLFEKYVQRADMVEIA-----GLNTDLQQEytrQREHLERNL 1041
Cdd:pfam10174 652 SQQLQLEELMGalEKTRQELDATKARLSSTQQSlaekdGHLTNLRAE---RRKQLEEIL 707
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
638-878 |
2.64e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 638 EELKMENEYQLRLKDMNySEKIKELTDKF---IQEMESLKT-----KNQVLRTEKEKQDVyhHEHIEDLLDKQSRELQDM 709
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKN-GENIARKQNKYdelVEEAKTIKAeieelTDELLNLVMDIEDP--SAALNKLNTAAAKIKSKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 710 ECCnnQKLLLEYEKYQELQLKSQrmqeeyekQLRDNDETKSQALEELTEfyeakLQEKTTLLEEAQEDVRQQLREFEETK 789
Cdd:PHA02562 272 EQF--QKVIKMYEKGGVCPTCTQ--------QISEGPDRITKIKDKLKE-----LQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 790 KqieededrEIQDIKTKYEKKLRDekesnlrLKGEtgimRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQG 869
Cdd:PHA02562 337 K--------KLLELKNKISTNKQS-------LITL----VDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
....*....
gi 767902636 870 LKREIQERD 878
Cdd:PHA02562 398 LVKEKYHRG 406
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
829-984 |
2.87e-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: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 829 RKKFSSLQKEIEERTnDIETLKGEQMK---LQGVIKSLEKDIQGLK-----REIQERDETIQDKEKRIYDLKKKNQELGK 900
Cdd:COG2433 349 KNKFERVEKKVPPDV-DRDEVKARVIRglsIEEALEELIEKELPEEepeaeREKEHEERELTEEEEEIRRLEEQVERLEA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 901 FKFVLDYKIKELKKQIEPRENEIRVMKEQIQE---MEAELENFHKQNTQLElnitelwqklratdQEMRRERQKERDLEA 977
Cdd:COG2433 428 EVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDREIERLE--------------RELEEERERIEELKR 493
|
....*..
gi 767902636 978 LVKRFKT 984
Cdd:COG2433 494 KLERLKE 500
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
602-902 |
3.10e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 602 RGIKREREVGFAEEVlvTKTDMEEKAQVMLELktrvEELKMENEYQLrlkdmnysEKIKEltdkfiqemESLKTKNQVLR 681
Cdd:pfam17380 310 REVERRRKLEEAEKA--RQAEMDRQAAIYAEQ----ERMAMEREREL--------ERIRQ---------EERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 682 TEKEKQDVYHHEHIEDLL----DKQSRELQDMECCNNQKLLLEyekyqELQLKSQRMQEEYEKQLRDNDETKSQALEELT 757
Cdd:pfam17380 367 QEEIAMEISRMRELERLQmerqQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQIRAEQEEARQREVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 758 EFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQ--IEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKkfsSL 835
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKklELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK---LL 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902636 836 QKEIEERTNDIetLKGEQMKLQGVIKSLEKDIQGlKREIQERDETIQDKEKRIYDLKKKNQELGKFK 902
Cdd:pfam17380 519 EKEMEERQKAI--YEEERRREAEEERRKQQEMEE-RRRIQEQMRKATEERSRLEAMEREREMMRQIV 582
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
632-1155 |
3.66e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 632 ELKTRVEELKmeneyQLRLKDMNYSEKIKELtDKFIQEMESLKTKNQVLR------TEKEKQDVYHHEHIE--DLLDKQS 703
Cdd:TIGR00606 249 PLKNRLKEIE-----HNLSKIMKLDNEIKAL-KSRKKQMEKDNSELELKMekvfqgTDEQLNDLYHNHQRTvrEKERELV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 704 RELQDMECCNNQKLLLEYEKYQ------ELQLKSQRMQEEYEKqlRDNDETKSQALEELTEFyeaklqekttlleEAQED 777
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTEllveqgRLQLQADRHQEHIRA--RDSLIQSLATRLELDGF-------------ERGPF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 778 VRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKES----NLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQ 853
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQadeiRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 854 MKLQGVIKsLEKDIQGLKREIQERDE--TIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQ 931
Cdd:TIGR00606 468 GSSDRILE-LDQELRKAERELSKAEKnsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 932 EMEAELENFHKQNTQLE------LNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNcvaYIQEPRLLKEKVRG 1005
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTsllgyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNH---INNELESKEEQLSS 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1006 LFEKyvqradMVEIAGlNTDLQQEYTRQREHLER---NLATLKKKV------VKEGELHRTDYVRIMQENVSLIKEINEL 1076
Cdd:TIGR00606 624 YEDK------LFDVCG-SQDEESDLERLKEEIEKsskQRAMLAGATavysqfITQLTDENQSCCPVCQRVFQTEAELQEF 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1077 RRELK-FTRSQVYDLEAALKLTKKV--RPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMqrlEIQRLRDQIQEQEQV 1153
Cdd:TIGR00606 697 ISDLQsKLRLAPDKLKSTESELKKKekRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNR---DIQRLKNDIEEQETL 773
|
..
gi 767902636 1154 TG 1155
Cdd:TIGR00606 774 LG 775
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
692-1149 |
3.67e-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: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 692 HEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQELQ------LKSQRMQEEYEKQLRDNDETKSQA--LEELTEFYEAK 763
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEkelkhlREALQQTQQSHAYLTQKREAQEEQlkKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 764 LQEKTTL---LEEAQEDV---RQQLREFEETKK--QIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSL 835
Cdd:TIGR00618 269 IEELRAQeavLEETQERInraRKAAPLAAHIKAvtQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 836 QKEIEERTNDIETlkgEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQelgkfkfvldykikELKKQ 915
Cdd:TIGR00618 349 TLHSQEIHIRDAH---EVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ--------------REQAT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 916 IEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKT----------- 984
Cdd:TIGR00618 412 IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlqetrkkav 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 985 DLHNCVAYIQEPRLLKEKVRglfeKYVQRADMVEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKEGElHRTDY----V 1060
Cdd:TIGR00618 492 VLARLLELQEEPCPLCGSCI----HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK-QRASLkeqmQ 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1061 RIMQENVSLIKEINELRRELKFTRSQVYDL----EAALKLTKKVRPQ---EVSETEPSRDMLSTAPTARLNEQEETGRII 1133
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRLqdltEKLSEAEDMLACEqhaLLRKLQPEQDLQDVRLHLQQCSQELALKLT 646
|
490
....*....|....*.
gi 767902636 1134 EMQRLEIQRLRDQIQE 1149
Cdd:TIGR00618 647 ALHALQLTLTQERVRE 662
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
735-961 |
3.94e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 735 QEEYEKQLRDNDETKSQALEELtefyeAKLQEKttlLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYEKKlRDE 814
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAEL-----DALQAE---LEELNEEYNELQAELEALQAEIDKLQ-AEIAEAEAEIEER-REE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 815 KESNLRLKGETGIMRKKFSSL--QKEIEERTNDIETLKgeqmKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 892
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLlgSESFSDFLDRLSALS----KIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902636 893 KKNQElgkfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRAT 961
Cdd:COG3883 164 AELEA----------AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
657-1028 |
4.12e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.52 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 657 EKIKELTDKFIQEMESLKTKNQVLRTEkekqdvyhhehIEDLLDKQsRELQdmeccnnQKLLLEYEKYQELqlksqrmQE 736
Cdd:PRK04778 115 DLIEEDIEQILEELQELLESEEKNREE-----------VEQLKDLY-RELR-------KSLLANRFSFGPA-------LD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 737 EYEKQLrDNDETKSQALEELTE---FYEA-----KLQEKTTLLEEAQEDVRQQLREFEETKKQieededrEIQDIKTKYe 808
Cdd:PRK04778 169 ELEKQL-ENLEEEFSQFVELTEsgdYVEAreildQLEEELAALEQIMEEIPELLKELQTELPD-------QLQELKAGY- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 809 kklRDEKESNLRLKgETGIMrKKFSSLQKEIEERTNDIETLKGEQMKLQgvIKSLEKDIQGL----------KREIQERD 878
Cdd:PRK04778 240 ---RELVEEGYHLD-HLDIE-KEIQDLKEQIDENLALLEELDLDEAEEK--NEEIQERIDQLydilerevkaRKYVEKNS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 879 ETIQDKEKRiydLKKKNQELG------KFKFVLDYKIKELKKQIEPRENEIRVMKEQIQ-----------EMEAELENFH 941
Cdd:PRK04778 313 DTLPDFLEH---AKEQNKELKeeidrvKQSYTLNESELESVRQLEKQLESLEKQYDEITeriaeqeiaysELQEELEEIL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 942 KQNTQLELNITELWQKLRATdqemrreRQKERDLEALVKRFKTDLHNCVAYIQeprllKEKVRGLFEKYVQRADMV--EI 1019
Cdd:PRK04778 390 KQLEEIEKEQEKLSEMLQGL-------RKDELEAREKLERYRNKLHEIKRYLE-----KSNLPGLPEDYLEMFFEVsdEI 457
|
....*....
gi 767902636 1020 AGLNTDLQQ 1028
Cdd:PRK04778 458 EALAEELEE 466
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
787-960 |
5.31e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 787 ETKKQIEEDEDREIQ-DIKTKyEKKLRD-EKESNLRlkgetgimRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLE 864
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKnELKNK-EKELKNlDKNLNKD--------EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 865 KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN 944
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170
....*....|....*.
gi 767902636 945 TQLELNITELWQKLRA 960
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLK 198
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
915-1152 |
5.71e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 915 QIEPRENEIRVmkEQIQEMEAELENFhkqNTQLEL-----NITELWQKLRATDQEMRRERQKERDLEALVKRFK------ 983
Cdd:COG3206 60 LVEPQSSDVLL--SGLSSLSASDSPL---ETQIEIlksrpVLERVVDKLNLDEDPLGEEASREAAIERLRKNLTvepvkg 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 984 TDLHNcVAYI-QEPRLLKEKVRGLFEKYVQRadmveiaglNTDLQQEYTRQ-REHLERNLATLKKKVVK-EGELH----R 1056
Cdd:COG3206 135 SNVIE-ISYTsPDPELAAAVANALAEAYLEQ---------NLELRREEARKaLEFLEEQLPELRKELEEaEAALEefrqK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1057 TDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALK-LTKKVRPQEVSETEPSRDMLSTAPTARLNEQEetGRIIEM 1135
Cdd:COG3206 205 NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAaLRAQLGSGPDALPELLQSPVIQQLRAQLAELE--AELAEL 282
|
250 260
....*....|....*....|...
gi 767902636 1136 QRL------EIQRLRDQIQEQEQ 1152
Cdd:COG3206 283 SARytpnhpDVIALRAQIAALRA 305
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
806-1090 |
5.78e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.53 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 806 KYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIeerTNDIETLKGEQMKLQgvikSLEKDIQGLKREIQE-RDETIQDK 884
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKASREE---TFARTALKNARLDLR----RLFDEKQSEKDKKNKaLAERKDSA 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 885 EKRIYDLKKKnqelgkfKFVLDYKIKELKKQIEPRENEIRV-MKEQIQEMEAELENFHKQ-NTQLELNITELWQKLRATD 962
Cdd:pfam12128 681 NERLNSLEAQ-------LKQLDKKHQAWLEEQKEQKREARTeKQAYWQVVEGALDAQLALlKAAIAARRSGAKAELKALE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 963 QEMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLF----EKYVQRADMVEIAGLNT-----DLQQEYTRQ 1033
Cdd:pfam12128 754 TWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFdwyqETWLQRRPRLATQLSNIeraisELQQQLARL 833
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902636 1034 -------REHLERNLATLKKKVVKEGELHRTdyVRIMQENVSLIKE---INELRRELKFTRSQVYDL 1090
Cdd:pfam12128 834 iadtklrRAKLEMERKASEKQQVRLSENLRG--LRCEMSKLATLKEdanSEQAQGSIGERLAQLEDL 898
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
630-1056 |
6.15e-05 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 47.25 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 630 MLELKTR----VEELKMENEyqlrlKDMNYSEKIkeltDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedlLDKQSRE 705
Cdd:pfam15818 2 LLDFKTSlleaLEELRMRRE-----AETQYEEQI----GKIIVETQELKWQKETLQNQKET------------LAKQHKE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 706 LqdMECCNNQkllleyekyqeLQLKSQRMQEEYEK-QLRDndETKSQALEELTEFYEAKLQEKTTL---LEEAQEDVRQQ 781
Cdd:pfam15818 61 A--MAVFKKQ-----------LQMKMCALEEEKGKyQLAT--EIKEKEIEGLKETLKALQVSKYSLqkkVSEMEQKLQLH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 782 LREFEETKKQIEEDEdreiqdiktKYEKKLrdekesnlrlKGETGIMRKKFSSLQKEIEERtndIETLKgeqmKLQGVIK 861
Cdd:pfam15818 126 LLAKEDHHKQLNEIE---------KYYATI----------TGQFGLVKENHGKLEQNVQEA---IQLNK----RLSALNK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 862 SLEKDIQGLKREiqerdetiqdkekriydLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQeMEAEL---- 937
Cdd:pfam15818 180 KQESEICSLKKE-----------------LKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLN-MELELnkki 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 938 --ENFHKQNTQLELNITelwqkLRATDQEMRRERQKERDLEALVKRFKtdlHNCVAYIQEPRLLKEKVRGLFEKYVQRAD 1015
Cdd:pfam15818 242 neEITHIQEEKQDIIIS-----FQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQREKVKENEEKFLNLQN 313
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 767902636 1016 MVEIAglntdlQQEYTRQREHLERNLATLKKKVVKEGELHR 1056
Cdd:pfam15818 314 EHEKA------LGTWKKHVEELNGEINEIKNELSSLKETHI 348
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
762-988 |
6.41e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.16 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 762 AKLQEKTTLLEEAQEDVRQQLREFEETKKQiEEDEDREIQDIKTKYEKkLRDEKESNlrlkgetgimRKKFSSLQKEIEE 841
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLES-EEKNREEVEELKDKYRE-LRKTLLAN----------RFSYGPAIDELEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 842 RTNDIE---------TLKGEQMKLQGVIKSLEKDIQGLKR---EIQERDETIQDK-EKRIYDLKKKNQELGKFKFVLDY- 907
Cdd:pfam06160 154 QLAEIEeefsqfeelTESGDYLEAREVLEKLEEETDALEElmeDIPPLYEELKTElPDQLEELKEGYREMEEEGYALEHl 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 908 ----KIKELKKQIEPR------------ENEIRVMKEQIQE----MEAELENFH-----------------KQNTQLELN 950
Cdd:pfam06160 234 nvdkEIQQLEEQLEENlallenleldeaEEALEEIEERIDQlydlLEKEVDAKKyveknlpeiedylehaeEQNKELKEE 313
|
250 260 270
....*....|....*....|....*....|....*...
gi 767902636 951 ITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHN 988
Cdd:pfam06160 314 LERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVER 351
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
766-1051 |
6.46e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.52 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 766 EKTTLLEEAQEDVRQQLREFEETKKQIEE---DEDREIQDIKTKYEKKLRDEKESNLRLKGETGIM-------------- 828
Cdd:PTZ00440 404 KYTNIISLSEHTLKAAEDVLKENSQKIADyalYSNLEIIEIKKKYDEKINELKKSINQLKTLISIMksfydliisekdsm 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 829 ------RKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLE---KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELG 899
Cdd:PTZ00440 484 dskekkESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEdyyITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKR 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 900 KFKFVLDYKIKELKKQIEpRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKeRDLEALV 979
Cdd:PTZ00440 564 SMKNDIKNKIKYIEENVD-HIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYK-GDLQELL 641
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902636 980 KRFKTDLHNCVAYIQEPRlLKEKVRGLFEKYVQRADmvEIAGLNTDLQQEYTRQREHLERNLATLKKKVVKE 1051
Cdd:PTZ00440 642 DELSHFLDDHKYLYHEAK-SKEDLQTLLNTSKNEYE--KLEFMKSDNIDNIIKNLKKELQNLLSLKENIIKK 710
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
778-1154 |
6.62e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 778 VRQQLREFEETKKQIEEDEDrEIQDIKTKYEKKLRDEKESNLRLKgetgIMRKKFSSLQKEIEERTNDIETLKGEQMKLQ 857
Cdd:TIGR04523 35 EKQLEKKLKTIKNELKNKEK-ELKNLDKNLNKDEEKINNSNNKIK----ILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 858 GVIKS-------LEKDIQGLKREIQERDETIQD-------KEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEI 923
Cdd:TIGR04523 110 SEIKNdkeqknkLEVELNKLEKQKKENKKNIDKflteikkKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 924 RVMKEQI-----------------QEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDL 986
Cdd:TIGR04523 190 DKIKNKLlklelllsnlkkkiqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 987 HNCVAYI-QEPRLLKEKvrglfEKYVQRADMvEIAGLNTDLQQEYTRQrehLERNLATLKKKVvkegELHRTDYVRIMQE 1065
Cdd:TIGR04523 270 SEKQKELeQNNKKIKEL-----EKQLNQLKS-EISDLNNQKEQDWNKE---LKSELKNQEKKL----EEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1066 NVSLIKEINELRRELKFTRSQvyDLEAALKLTKKVRPQEVSEtepsrdmlstaptarlNEQEETGRIIEMQRLEIQRLRD 1145
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESE--NSEKQRELEEKQNEIEKLK----------------KENQSYKQEIKNLESQINDLES 398
|
....*....
gi 767902636 1146 QIQEQEQVT 1154
Cdd:TIGR04523 399 KIQNQEKLN 407
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
654-881 |
7.38e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 46.21 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 654 NYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDvyHHEHIEDLLDKQSRELQdmeccnnqkllleyekyqELQLKSQR 733
Cdd:cd22656 80 NYAQNAGGTIDSYYAEILELIDDLADATDDEELEE--AKKTIKALLDDLLKEAK------------------KYQDKAAK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 734 MQEEYeKQLRDNDETKSQALEELTEFYEAKLQEKttLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKkLRD 813
Cdd:cd22656 140 VVDKL-TDFENQTEKDQTALETLEKALKDLLTDE--GGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIAD-DEA 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902636 814 EKESNLRLKGETGIMRKKFSSLQKEIEERTNDIEtlkgeqmKLQGVIKSLEKDIQGLKREIQERDETI 881
Cdd:cd22656 216 KLAAALRLIADLTAADTDLDNLLALIGPAIPALE-------KLQGAWQAIATDLDSLKDLLEDDISKI 276
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
657-1117 |
7.51e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 657 EKIKELTDKFIQEMESLKTKNQVLRTEKEKQdvyhhEHIEDLLdkQSRELQdMECcnnqkllleyekyqelqlkSQRMQE 736
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKA-----CEIRDQI--TSKEAQ-LES-------------------SREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 737 EYEKQLRDNDETKSQALEELTEFYeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE 816
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIM--KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKER 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 817 SNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQ----ERDETIQDKEKRIYDLK 892
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfERGPFSERQIKNFHTLV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 893 KKNQElGKFKFV----LDYKIKELKKQIEPRENEIRvMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRE 968
Cdd:TIGR00606 400 IERQE-DEAKTAaqlcADLQSKERLKQEQADEIRDE-KKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELD 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 969 ---RQKERDLEALVKRFKTD-LHNCVAYIQEPRL-LKEKVRGLFEKYVQRadmveiaglntDLQQEYTRQREHLERNLAT 1043
Cdd:TIGR00606 478 qelRKAERELSKAEKNSLTEtLKKEVKSLQNEKAdLDRKLRKLDQEMEQL-----------NHHTTTRTQMEMLTKDKMD 546
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902636 1044 LKKKVVKEGELHRTDYVRIMQE---NVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLST 1117
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS 623
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
693-889 |
8.08e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 693 EHIEDLLDKQS------------REL-QDMECCNNQKLLLE-----YEKYQELQLKS-----QRMQEEYEKQL---RDND 746
Cdd:PHA02562 154 KLVEDLLDISVlsemdklnkdkiRELnQQIQTLDMKIDHIQqqiktYNKNIEEQRKKngeniARKQNKYDELVeeaKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 747 ETKSQALEELTEF------YEAKLQEKTTLLEEAQEDVRQQLRE---FEE-----TKKQIEEDEDREIQDIKTK---YEK 809
Cdd:PHA02562 234 AEIEELTDELLNLvmdiedPSAALNKLNTAAAKIKSKIEQFQKVikmYEKggvcpTCTQQISEGPDRITKIKDKlkeLQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 810 KLRDEKESNLRLKG---ETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKD-------IQGLKREIQERDE 879
Cdd:PHA02562 314 SLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdnaeeLAKLQDELDKIVK 393
|
250
....*....|
gi 767902636 880 TIQDKEKRIY 889
Cdd:PHA02562 394 TKSELVKEKY 403
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
624-1081 |
1.07e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 624 EEKAQVMLELK-----TRVEELKMENEYQLRLKDMNYSEKIKELTDKfiqEMESLKTKNQVLRTEKEKQDVyhHEHIEDL 698
Cdd:COG5022 902 LELESEIIELKkslssDLIENLEFKTELIARLKKLLNNIDLEEGPSI---EYVKLPELNKLHEVESKLKET--SEEYEDL 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 699 LDKQS---RELQDMeccnNQKLLLEYEKYQELQLKSQRMQEEyEKQLRDNDeTKSQALEELTEFY---------EAKLQE 766
Cdd:COG5022 977 LKKSTilvREGNKA----NSELKNFKKELAELSKQYGALQES-TKQLKELP-VEVAELQSASKIIssestelsiLKPLQK 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 767 KTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKK---LRDEKESNLRLKGETGIMR------KKFSSLQK 837
Cdd:COG5022 1051 LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKtinVKDLEVTNRNLVKPANVLQfivaqmIKLNLLQE 1130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 838 EIEERTNDIETLKGEQMKLqgviKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFvldykiKELKKQIE 917
Cdd:COG5022 1131 ISKFLSQLVNTLEPVFQKL----SVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKS------KLSSSEVN 1200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 918 PRENEIRVMKEQIQEmEAELENFHKQNTQLELNITELWQKLRAT-DQEMRRERQKERDLEALVKRFKTDLHNCVAYIQEP 996
Cdd:COG5022 1201 DLKNELIALFSKIFS-GWPRGDKLKKLISEGWVPTEYSTSLKGFnNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEE 1279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 997 RLLKEKVRGLFEKYVQRADMVEIAGLNT-------------------DLQQEYTRQREHLERNLATLKKKVVKEGELHRT 1057
Cdd:COG5022 1280 EVLPATINSLLQYINVGLFNALRTKASSlrwksatevnynseelddwCREFEISDVDEELEELIQAVKVLQLLKDDLNKL 1359
|
490 500
....*....|....*....|....
gi 767902636 1058 DYVRIMQENVSLIkEINELRRELK 1081
Cdd:COG5022 1360 DELLDACYSLNPA-EIQNLKSRYD 1382
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
668-929 |
1.36e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 45.33 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 668 QEMESLKTKNQVLRTEKEKQDVYHHEHIE--DLLDKQSRELQ----DMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQ 741
Cdd:pfam09728 39 KDLKKLKKKQDQLQKEKDQLQSELSKAILakSKLEKLCRELQkqnkKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 742 LRDNDETKSQALEELTEFYE--AKLQEKTTLLEE------AQEDVRQQLRE------FEETKKQIEEDEDREIQDIKTKY 807
Cdd:pfam09728 119 MEEKSEKNNKLREENEELREklKSLIEQYELRELhfekllKTKELEVQLAEaklqqaTEEEEKKAQEKEVAKARELKAQV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 808 EKKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDetiqdkeKR 887
Cdd:pfam09728 199 QTLSETEKE----LREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSN-------KA 267
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767902636 888 IYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQ 929
Cdd:pfam09728 268 LLEMAEERQKLKE-------ELEKLQKKLEKLENLCRALQAE 302
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
720-986 |
1.54e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 720 EYEKYQELQLKSQRmQEEYEKQLRDNDETKSQALEELTE-------------FYEAKLQEKTT--LLEEAQEDVRQQLRE 784
Cdd:PRK04778 49 ELEKVKKLNLTGQS-EEKFEEWRQKWDEIVTNSLPDIEEqlfeaeelndkfrFRKAKHEINEIesLLDLIEEDIEQILEE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 785 FEETKKQiEEDEDREIQDIKTKYEKkLRDEKESNlrlkgetgimRKKFSSLQKEIEERTNDIETL---------KGEQMK 855
Cdd:PRK04778 128 LQELLES-EEKNREEVEQLKDLYRE-LRKSLLAN----------RFSFGPALDELEKQLENLEEEfsqfvelteSGDYVE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 856 LQGVIKSLEKDIQGLKREIQERDETIQDKEK----RIYDLKKKNQELGKFKFVLDYK-----IKELKKQI---------- 916
Cdd:PRK04778 196 AREILDQLEEELAALEQIMEEIPELLKELQTelpdQLQELKAGYRELVEEGYHLDHLdiekeIQDLKEQIdenlalleel 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 917 --EPRENEIRVMKEQIQEM----EAE-----------------LENFHKQNTQLELNITELWQKLRATDQEMRRERQKER 973
Cdd:PRK04778 276 dlDEAEEKNEEIQERIDQLydilEREvkarkyveknsdtlpdfLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEK 355
|
330
....*....|...
gi 767902636 974 DLEALVKRFKTDL 986
Cdd:PRK04778 356 QLESLEKQYDEIT 368
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
855-1152 |
1.73e-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: 45.82 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 855 KLQGVIKSLEKDIQGLKREiqerdetiqdKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEME 934
Cdd:TIGR02168 190 RLEDILNELERQLKSLERQ----------AEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 935 AELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEalvkrfktdlhncvayiQEPRLLKEKVRGLFEKYVQra 1014
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE-----------------QQKQILRERLANLERQLEE-- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1015 dmveiagLNTDLQQEyTRQREHLERNLATLKKKVVkegelhrtdyvrimqenvSLIKEINELRRELKFTRSQVYDLEAAL 1094
Cdd:TIGR02168 321 -------LEAQLEEL-ESKLDELAEELAELEEKLE------------------ELKEELESLEAELEELEAELEELESRL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767902636 1095 KLTKKVRPQEVSETepsrdmlstaptARLNEQEETgriiemQRLEIQRLRDQIQEQEQ 1152
Cdd:TIGR02168 375 EELEEQLETLRSKV------------AQLELQIAS------LNNEIERLEARLERLED 414
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
720-1139 |
1.95e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 720 EYEKYQELQLKSQRMQEEYEK-QLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEE--DE 796
Cdd:COG5022 811 EYRSYLACIIKLQKTIKREKKlRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQElkID 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 797 DREIQDIKTKYEK------KLRDEKESNLRLKGEtgIMRKKFSSLQKEIEERtnDIETLKGEQMKLQGVIKSLEKDIQGL 870
Cdd:COG5022 891 VKSISSLKLVNLEleseiiELKKSLSSDLIENLE--FKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLHEVESKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 871 KREIQERDETIQDKEKRIYDLKKKNQELGKFKfvldYKIKELKKQIEPRENEIRVMKEQIQEMEaelenFHKQNTQLELN 950
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFK----KELAELSKQYGALQESTKQLKELPVEVA-----ELQSASKIISS 1037
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 951 ITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCVAYiqeprllkekvrgLFEKYVQRADMVEIAGLNTDLQQEY 1030
Cdd:COG5022 1038 ESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLD-------------DKQLYQLESTENLLKTINVKDLEVT 1104
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1031 TRQREHLERNLATLKKKVVKEGELHRTDyvRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEP 1110
Cdd:COG5022 1105 NRNLVKPANVLQFIVAQMIKLNLLQEIS--KFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRL 1182
|
410 420 430
....*....|....*....|....*....|.
gi 767902636 1111 SRD-MLSTAPTARLNEQEE-TGRIIEMQRLE 1139
Cdd:COG5022 1183 YQSaLYDEKSKLSSSEVNDlKNELIALFSKI 1213
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
612-887 |
2.05e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 612 FAEEVLvTKTDMEEKAQVMLELktrVEELkmeNEYQLRLKDMnySEKIKELTD--KFIQEMESLKTKNQVLRTEKEKQDV 689
Cdd:COG4913 213 VREYML-EEPDTFEAADALVEH---FDDL---ERAHEALEDA--REQIELLEPirELAERYAAARERLAELEYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 690 YHHEHIEDLLDKQSRELQdmeccnnqkllleyEKYQELqlksqrmqeeyEKQLRDNDETKSQALEELTEFYEAKLQEKTT 769
Cdd:COG4913 284 WFAQRRLELLEAELEELR--------------AELARL-----------EAELERLEARLDALREELDELEAQIRGNGGD 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 770 LLEEAQEDVRQQlrefEETKKQIEEDEDReiqdiktkYEKKLRDekesnLRLKGETGimRKKFSSLQKEIEERtndIETL 849
Cdd:COG4913 339 RLEQLEREIERL----ERELEERERRRAR--------LEALLAA-----LGLPLPAS--AEEFAALRAEAAAL---LEAL 396
|
250 260 270
....*....|....*....|....*....|....*...
gi 767902636 850 KGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKR 887
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
678-1137 |
2.29e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.81 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 678 QVLRTEKEKQDV-----YHHEHIEDLLDKQSRELQdmECCNNQKLLLEYekyqelqLKSQRMQEEYEKQLRdndETKSQA 752
Cdd:TIGR01612 328 KILESEGEQGHIinkliFLEKEFEDTIHKSDIYKD--ECLSNHLFMEDY-------LKDDKISPYYYEFLE---EIKKIA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 753 LEELTEFYEAKLQEKTTLLEEAQEDVrqqLREFEETKKQ--IEEDEDREIQDIKTKYEKKLRDEKESNLRL--KGETGIM 828
Cdd:TIGR01612 396 KQRAIFFYNAKKLKHLEILYKHQEDI---LNNFHKTIERliFEKPDPNNNNIFKDDFDEFNKPIPKSKLKAleKRFFEIF 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 829 RKKFSS--LQKEIEERTNDIETLKG--EQMK-LQGVIKSLEkdiQGLKREIQERDETIQDKEKRIYDLKKKNQELGkfkf 903
Cdd:TIGR01612 473 EEEWGSydIKKDIDENSKQDNTVKLilMRMKdFKDIIDFME---LYKPDEVPSKNIIGFDIDQNIKAKLYKEIEAG---- 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 904 vldykikeLKKQIEPRENeirvMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEmrrerqkerdlealvkrfk 983
Cdd:TIGR01612 546 --------LKESYELAKN----WKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDE------------------- 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 984 tdlhncVAYIQEPRL-LKEKVRGLFEK--YVQRA-DMVEIAGLNTDLQQEYTRQR-----EHLERN---LATLKKKVVKe 1051
Cdd:TIGR01612 595 ------IIYINKLKLeLKEKIKNISDKneYIKKAiDLKKIIENNNAYIDELAKISpyqvpEHLKNKdkiYSTIKSELSK- 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1052 geLHRTDYVRIMQENVSLIKEINELRRELKftrSQVYDLEAalKLTKKVRPQEVSETEPSRDMLSTAPTarlNEQEETGR 1131
Cdd:TIGR01612 668 --IYEDDIDALYNELSSIVKENAIDNTEDK---AKLDDLKS--KIDKEYDKIQNMETATVELHLSNIEN---KKNELLDI 737
|
....*.
gi 767902636 1132 IIEMQR 1137
Cdd:TIGR01612 738 IVEIKK 743
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
657-985 |
2.42e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 657 EKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHH--EHIEDLLDKQS--RELQDMEccnnqkllleyEKYQELQLKSQ 732
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASaeREIAELE-----------AELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 733 RMQEeyekqLRDNDETKSQALEELTEFYEAkLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDRE-IQDIKTKYEKKL 811
Cdd:COG4913 686 DLAA-----LEEQLEELEAELEELEEELDE-LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 812 RDEKESNLR--LKGETGIMRKKFSSLQKEIEERTND-IETLKGEQMKLQGVIKSLEkDIQGLKREIQERDetIQDKEKRI 888
Cdd:COG4913 760 GDAVERELRenLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLP-EYLALLDRLEEDG--LPEYEERF 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 889 YDLKKKNQElgkfkfvldYKIKELKKQIeprENEIRVMKEQIQEMEAELEN----------FHKQNTQLElNITELWQKL 958
Cdd:COG4913 837 KELLNENSI---------EFVADLLSKL---RRAIREIKERIDPLNDSLKRipfgpgrylrLEARPRPDP-EVREFRQEL 903
|
330 340 350
....*....|....*....|....*....|...
gi 767902636 959 RA------TDQEMRRERQKERdLEALVKRFKTD 985
Cdd:COG4913 904 RAvtsgasLFDEELSEARFAA-LKRLIERLRSE 935
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
878-1130 |
3.03e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 878 DETIQDKEKRIYDLKKKNQELGKfkfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQK 957
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 958 LRATDQEMRRERQKERDLEALVKrfKTDlhncvayiqeprllkekvrglFEKYVQRADMVE-IAGLNTDLQQEYTRQREH 1036
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLG--SES---------------------FSDFLDRLSALSkIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1037 LERNLATLKKKvVKEGELHRTDYVRIMQENVSLIKE----INELRRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSR 1112
Cdd:COG3883 145 LEAKKAELEAK-LAELEALKAELEAAKAELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250
....*....|....*...
gi 767902636 1113 DMLSTAPTARLNEQEETG 1130
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAA 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
905-1089 |
3.03e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 905 LDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN--TQLELNITELWQKLRATDQEMRRERQKERDLEALVKRF 982
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 983 KTDL---HNCVAYIQEPRLLKEKVRGLFEKYVQRADMV---------------EIAGLNTDLQQEYTRQREHLERNLATL 1044
Cdd:COG3206 246 RAQLgsgPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvialraQIAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767902636 1045 KKkvvKEGELHRT--DYVRIMQENVSLIKEINELRRELKFTRsQVYD 1089
Cdd:COG3206 326 QA---REASLQAQlaQLEARLAELPELEAELRRLEREVEVAR-ELYE 368
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
718-1003 |
3.54e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.47 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 718 LLEYEKYQELQlKSQRMQEEYEKQlRDNDETKSQALEELTEfyeaklQEKTTLLEEAQEDVRQQLREFEETKKQIEEDED 797
Cdd:pfam02029 64 FLDRTAKREER-RQKRLQEALERQ-KEFDPTIADEKESVAE------RKENNEEEENSSWEKEEKRDSRLGRYKEEETEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 798 REIQDIKTKYEKKLRDEKEsnlrlKGEtgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQER 877
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEE-----EGE---EEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 878 deTIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPrENEIRVMKEQIQEME-AELENFHKQNTQLELNITELwQ 956
Cdd:pfam02029 208 --KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEA-EQKLEELRRRRQEKEsEEFEKLRQKQQEAELELEEL-K 283
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767902636 957 KLRATDQEMRRERQKERDLEALVKRFKTDlhncvayiQEPRLLKEKV 1003
Cdd:pfam02029 284 KKREERRKLLEEEEQRRKQEEAERKLREE--------EEKRRMKEEI 322
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
772-943 |
3.65e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 44.63 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 772 EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKtKYEKKLRDEKESNLRLKGETGIMRKKFsslqKEIEERTNDIEtlkg 851
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESSIK-QVEEELEELKEQNEELEKQYKVKKKTL----DLLPDAEENIA---- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 852 eqmKLQGVIKSLEKDIQGLKREIQERDETIQdKEKRIYDLKKKNQELgKFKFVLDyKIKELKKQIEPRENEIRVMKEQIQ 931
Cdd:pfam05667 405 ---KLQALVDASAQRLVELAGQWEKHRVPLI-EEYRALKEAKSNKED-ESQRKLE-EIKELREKIKEVAEEAKQKEELYK 478
|
170
....*....|..
gi 767902636 932 EMEAELENFHKQ 943
Cdd:pfam05667 479 QLVAEYERLPKD 490
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
897-1099 |
3.83e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 897 ELGK---FKFVLDYKIKELKKQIE----PRENEIRVMKEQIQEMEAELENFHKQNTQLElnitELWQKLRATDQEMRRER 969
Cdd:COG4717 33 EAGKstlLAFIRAMLLERLEKEADelfkPQGRKPELNLKELKELEEELKEAEEKEEEYA----ELQEELEELEEELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 970 QKERDLEALVKRFKtDLHNCVAYIQEPRLLKEKVRGLFEKYVQ-RADMVEIAglntDLQQEYTRQREHLERNLATLKKKV 1048
Cdd:COG4717 109 AELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERLEElEERLEELR----ELEEELEELEAELAELQEELEELL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767902636 1049 VKEGELHRTDYVRIMQENVSLIKEINELRRELKFTRSQVYDLEAALKLTKK 1099
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
388-417 |
3.98e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.87 E-value: 3.98e-04
10 20 30
....*....|....*....|....*....|
gi 767902636 388 HSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:pfam00400 10 HTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
713-813 |
4.93e-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: 41.41 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 713 NNQKLLLEYEKYQELQLKSQRMQEEYEKQLrdndETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLREFEETKKQI 792
Cdd:pfam03938 6 DMQKILEESPEGKAAQAQLEKKFKKRQAEL----EAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKA 81
|
90 100
....*....|....*....|.
gi 767902636 793 EEDEDREIQDIKTKYEKKLRD 813
Cdd:pfam03938 82 QQELQKKQQELLQPIQDKINK 102
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
385-417 |
5.02e-04 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 38.83 E-value: 5.02e-04
10 20 30
....*....|....*....|....*....|...
gi 767902636 385 YPLHSAPITGLATCIRKPLIATCSLDRSIRLWN 417
Cdd:smart00320 8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-179 |
5.08e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.75 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 26 DEQIIIFPSGNHCVK-YNVD-QKWQKFIPGSekSQGMLALSISPNRRYLAiseTVQEKPAITIYELSSipcrkRKVLNNF 103
Cdd:COG2319 257 DGRLLASGSADGTVRlWDLAtGELLRTLTGH--SGGVNSVAFSPDGKLLA---SGSDDGTVRLWDLAT-----GKLLRTL 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902636 104 DFQVQKFISMAFSPDSKYLLAQTSppeSNLVYwLWEKQKVMAIVRIDTQNNPVYQVSFSPQDNTQVCVTGNGMFKL 179
Cdd:COG2319 327 TGHTGAVRSVAFSPDGKTLASGSD---DGTVR-LWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
631-1080 |
5.22e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.66 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 631 LELKTRVEELKMENEYQLRLKDMnysEKIKELTDKFIQEM---------ESLKTKNQVLRTEK-EKQDVYhhehiEDLLD 700
Cdd:TIGR01612 603 LELKEKIKNISDKNEYIKKAIDL---KKIIENNNAYIDELakispyqvpEHLKNKDKIYSTIKsELSKIY-----EDDID 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 701 KQSRELQDMECCNNQKLLLEYEKYQELQLKSqrmqeeyekqlrDNDETKSQALEelTEFYEAKLqektTLLEEAQEDVRQ 780
Cdd:TIGR01612 675 ALYNELSSIVKENAIDNTEDKAKLDDLKSKI------------DKEYDKIQNME--TATVELHL----SNIENKKNELLD 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 781 QLREFEE-TKKQIEEDEDREIQDIKTKyEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNdIETLKGEQMKlQGV 859
Cdd:TIGR01612 737 IIVEIKKhIHGEINKDLNKILEDFKNK-EKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQIN-IDNIKDEDAK-QNY 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 860 IKSlekdiqglkreiQERDETIQDKEKRIydlkkknqelgkFKFVldykikelkkqiepreNEIRVMKEQIQ---EMEAE 936
Cdd:TIGR01612 814 DKS------------KEYIKTISIKEDEI------------FKII----------------NEMKFMKDDFLnkvDKFIN 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 937 LENFHKQNTQLE-LNITELWQKLRA--TDQEMRRERQKERDLEALV-----------------KRFKTDLHNCVAYIQEP 996
Cdd:TIGR01612 854 FENNCKEKIDSEhEQFAELTNKIKAeiSDDKLNDYEKKFNDSKSLIneinksieeeyqnintlKKVDEYIKICENTKESI 933
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 997 RLLKEKVRGLFEKYVQRADMVEIAGLntdLQQEYTRQREHLERNLATLKKKVVKEGELhrTDYvriMQENVSLIKEINEL 1076
Cdd:TIGR01612 934 EKFHNKQNILKEILNKNIDTIKESNL---IEKSYKDKFDNTLIDKINELDKAFKDASL--NDY---EAKNNELIKYFNDL 1005
|
....
gi 767902636 1077 RREL 1080
Cdd:TIGR01612 1006 KANL 1009
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
620-898 |
6.44e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 44.07 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 620 KTDMEEKAQVMLELKTRVEELkmeneyqlrlkdMNYSEKIKELTDKFIQEMESLKTKNQVLRTEKEKqdvyhhehiedll 699
Cdd:pfam09726 408 KAELQASRQTEQELRSQISSL------------TSLERSLKSELGQLRQENDLLQTKLHNAVSAKQK------------- 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 700 DKQSreLQDMEccnnQKLLLEyekyqelqlksQRMQEEYEKQLrdNDETKSQALEELTEFYEAKLQEKTTllEEAQEDVR 779
Cdd:pfam09726 463 DKQT--VQQLE----KRLKAE-----------QEARASAEKQL--AEEKKRKKEEEATAARAVALAAASR--GECTESLK 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 780 QQLREFEETKKQIEED---EDREIQDIKTKyEKKLRDEKESnlrlKGETGIMRKKFSSLQKEIEERTNDI--ETlkgeQM 854
Cdd:pfam09726 522 QRKRELESEIKKLTHDiklKEEQIRELEIK-VQELRKYKES----EKDTEVLMSALSAMQDKNQHLENSLsaET----RI 592
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767902636 855 KLqgvikSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQEL 898
Cdd:pfam09726 593 KL-----DLFSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEV 631
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
614-947 |
6.75e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 614 EEVLVTKTDMEE------KAQVML-----ELKTRVEELKMENEYqlrLKDMNYSEKIKELTDKfIQEMESLKTKNQVLRT 682
Cdd:PRK04778 205 EELAALEQIMEEipellkELQTELpdqlqELKAGYRELVEEGYH---LDHLDIEKEIQDLKEQ-IDENLALLEELDLDEA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 683 EKEKQDVyhHEHIEDLLDKqsrelqdMEccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKsqalEELTEfyea 762
Cdd:PRK04778 281 EEKNEEI--QERIDQLYDI-------LE--------REVKARKYVEKNSDTLPDFLEHAKEQNKELK----EEIDR---- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 763 kLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTkyekklrdekesnlrlkgetgimrkkFSSLQKEIEER 842
Cdd:PRK04778 336 -VKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIA--------------------------YSELQEELEEI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 843 TNDIETLKGEQMKLQGVIKSLEKDiqglkrEIQERdETIQDKEKRIYDLK----KKN-----QELGKFKFVLDYKIKELK 913
Cdd:PRK04778 389 LKQLEEIEKEQEKLSEMLQGLRKD------ELEAR-EKLERYRNKLHEIKryleKSNlpglpEDYLEMFFEVSDEIEALA 461
|
330 340 350
....*....|....*....|....*....|....
gi 767902636 914 KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQL 947
Cdd:PRK04778 462 EELEEKPINMEAVNRLLEEATEDVETLEEETEEL 495
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
610-818 |
7.41e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 610 VGFAEEVLVTKTDMEEKAQVMLEL-KTRVEELKMENEYQLRLKDMNYSEKIKELTDKFiqEMESLKTKNQVLRTEKEKQD 688
Cdd:PRK12704 16 VGAVIGYFVRKKIAEAKIKEAEEEaKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF--EKELRERRNELQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 689 VyhhehiEDLLDKQSRELQDMEccnnqkllleyekyQELQLKsqrmQEEYEKQLRDndetksqaLEELTEFYEAKLQEKT 768
Cdd:PRK12704 94 K------EENLDRKLELLEKRE--------------EELEKK----EKELEQKQQE--------LEKKEEELEELIEEQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767902636 769 TLLEEA----QEDVRQQLreFEETKKQIEEDEDREIQDIKTKYekKLRDEKESN 818
Cdd:PRK12704 142 QELERIsgltAEEAKEIL--LEKVEEEARHEAAVLIKEIEEEA--KEEADKKAK 191
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
26-190 |
8.25e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.36 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 26 DEQIIIFPSGNHCVK-YNVD-QKWQKFIPGSekSQGMLALSISPNRRYLAiseTVQEKPAITIYELSSipcrkRKVLNNF 103
Cdd:COG2319 215 DGKLLASGSADGTVRlWDLAtGKLLRTLTGH--SGSVRSVAFSPDGRLLA---SGSADGTVRLWDLAT-----GELLRTL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 104 DFQVQKFISMAFSPDSKYLLAQTsppESNLVyWLWEKQKVMAIVRIDTQNNPVYQVSFSPQDNTQVCVTGNGMFKLLRFA 183
Cdd:COG2319 285 TGHSGGVNSVAFSPDGKLLASGS---DDGTV-RLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA 360
|
....*..
gi 767902636 184 EGTLKQT 190
Cdd:COG2319 361 TGELLRT 367
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
746-1152 |
8.29e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.46 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 746 DETKSQALEELTEFYEAKLQEKTTLLEEaqedvRQQLREFEETKKqieededreIQDIKTKY-------EKKLRDEKESN 818
Cdd:NF033838 53 NESQKEHAKEVESHLEKILSEIQKSLDK-----RKHTQNVALNKK---------LSDIKTEYlyelnvlKEKSEAELTSK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 819 LR---------LKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVI--KSLEKDIQGLKREIQERD-ETIQDKEK 886
Cdd:NF033838 119 TKkeldaafeqFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNtyKTLELEIAESDVEVKKAElELVKEEAK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 887 RIYDLKKKNQELGKFkfvldykikELKKQIEPRENEIRVMKEQIQE-----MEAELENFHKQNTQLELNITELWQKLRAT 961
Cdd:NF033838 199 EPRDEEKIKQAKAKV---------ESKKAEATRLEKIKTDREKAEEeakrrADAKLKEAVEKNVATSEQDKPKRRAKRGV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 962 DQEMRRERQKERDLEAlvkrfkTDLHNCVAYIQEPRLLKEKVRGLFEKYVQRAdmveiaglntdlQQEYTRQREHLERNL 1041
Cdd:NF033838 270 LGEPATPDKKENDAKS------SDSSVGEETLPSPSLKPEKKVAEAEKKVEEA------------KKKAKDQKEEDRRNY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1042 ATLKKKVVkEGELHRTDyVRIMQENVSLIKEI-NELRRELKFTRSQvydleaalkltKKVrpqEVSETEPSRdmLSTAPT 1120
Cdd:NF033838 332 PTNTYKTL-ELEIAESD-VKVKEAELELVKEEaKEPRNEEKIKQAK-----------AKV---ESKKAEATR--LEKIKT 393
|
410 420 430
....*....|....*....|....*....|..
gi 767902636 1121 ARLNEQEETGRIIEmqrlEIQRLRDQIQEQEQ 1152
Cdd:NF033838 394 DRKKAEEEAKRKAA----EEDKVKEKPAEQPQ 421
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
754-892 |
1.26e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 41.07 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 754 EELTEFYeAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYE---KKLRDEKESNLRLKGEtgimrk 830
Cdd:pfam08614 3 LELIDAY-NRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllAQLREELAELYRSRGE------ 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902636 831 kfssLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIYDLK 892
Cdd:pfam08614 76 ----LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQ 133
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
859-1152 |
1.49e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 859 VIKSLEKDIQGLKR--EIQERDETIQDKEKRiydlkKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAE 936
Cdd:COG1196 194 ILGELERQLEPLERqaEKAERYRELKEELKE-----LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 937 LENFHKQNTQLELNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLhncvayiqeprllkekvrglfekyvqradm 1016
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1017 veiaglntdlqQEYTRQREHLERNLATLKkkvvkegelhrtdyvrimQENVSLIKEINELRRELKFTRSQVYDLEAALKL 1096
Cdd:COG1196 319 -----------EELEEELAELEEELEELE------------------EELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 767902636 1097 TKKVRPQEVSETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQEQEQ 1152
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
725-805 |
1.51e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.11 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 725 QELQLKSQRMQEEYEKQLRdndETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQLrefEETKKQIEEDEDREIQDIK 804
Cdd:cd06503 43 EKAKEEAEELLAEYEEKLA---EARAEAQEIIEEARKEAEKIKEEILAEAKEEAERIL---EQAKAEIEQEKEKALAELR 116
|
.
gi 767902636 805 T 805
Cdd:cd06503 117 K 117
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
605-883 |
1.57e-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: 42.74 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 605 KREREVGFAEEVLVTKTDMEEKAQVMLE----LKTRVEELKME-----NEYQLRLKDMNYSEKIKELTDKFIQEMESLKT 675
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEelkaLREALDELRAEltllnEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 676 KNQVLRTEKEKQdvyhHEHIEDLLDKQSRELQdmeccnnqkllLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEE 755
Cdd:TIGR02168 849 ELSEDIESLAAE----IEELEELIEELESELE-----------ALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 756 ltefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGetgiMRKKFSSL 835
Cdd:TIGR02168 914 -----RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR----LENKIKEL 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902636 836 Q----------KEIEERtndIETLKGEQMKLQGVIKSLEKDIQGLKREIQER-DETIQD 883
Cdd:TIGR02168 985 GpvnlaaieeyEELKER---YDFLTAQKEDLTEAKETLEEAIEEIDREARERfKDTFDQ 1040
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
778-974 |
1.60e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 778 VRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQ 857
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKT----IKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 858 GVIKSLEKDI-------------QGLKREiQERDETIQDK----EKRIYDLKKKNQELGKFKFVLD---YKIKELKKQIE 917
Cdd:PHA02562 269 SKIEQFQKVIkmyekggvcptctQQISEG-PDRITKIKDKlkelQHSLEKLDTAIDELEEIMDEFNeqsKKLLELKNKIS 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767902636 918 PRENEIRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEmRRERQKERD 974
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT-KSELVKEKY 403
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
632-898 |
2.03e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 632 ELKTRVEELKMENEYQLRLKDMNYsEKIKELTDKFIQEMESLKTKNQVLRTEKEKQDVYHHEHIEdlLDKQSRELQDME- 710
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELN-EKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS--IDKLRKEIERLEw 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 711 CCNNQKLLLEYEKyqELQLKSQRMQEEYEKqLRDNDETKSQALEELTEFYEAKLQekttlleeaQEDVRQQLREFEETKK 790
Cdd:COG1340 124 RQQTEVLSPEEEK--ELVEKIKELEKELEK-AKKALEKNEKLKELRAELKELRKE---------AEEIHKKIKELAEEAQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 791 QIEEdedrEIQDIKTKYEKkLRDEKESnlrlkgetgiMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGL 870
Cdd:COG1340 192 ELHE----EMIELYKEADE-LRKEADE----------LHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
250 260
....*....|....*....|....*...
gi 767902636 871 KREiqERDETIQDKEKRIYDLKKKNQEL 898
Cdd:COG1340 257 KRE--KEKEELEEKAEEIFEKLKKGEKL 282
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
765-954 |
2.03e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 765 QEKTTLLEEAQEdvrQQLREFEETKKQIEEDEDREIQDIKTKYEK---KLRDEKESNLRLKGETGIMRKK---------- 831
Cdd:PRK05771 16 SYKDEVLEALHE---LGVVHIEDLKEELSNERLRKLRSLLTKLSEaldKLRSYLPKLNPLREEKKKVSVKsleelikdve 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 832 --FSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEK------DIQ-------------GLKREIQERDETI--------- 881
Cdd:PRK05771 93 eeLEKIEKEIKELEEEISELENEIKELEQEIERLEPwgnfdlDLSlllgfkyvsvfvgTVPEDKLEELKLEsdvenveyi 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 882 -QDKEKRIY-------DLKKKNQELGKF---KFVLDYK--IKELKKQIEPRENEIrvmKEQIQEMEAELENFHKQNTQLE 948
Cdd:PRK05771 173 sTDKGYVYVvvvvlkeLSDEVEEELKKLgfeRLELEEEgtPSELIREIKEELEEI---EKERESLLEELKELAKKYLEEL 249
|
....*.
gi 767902636 949 LNITEL 954
Cdd:PRK05771 250 LALYEY 255
|
|
| PTZ00332 |
PTZ00332 |
paraflagellar rod protein; Provisional |
704-1101 |
2.08e-03 |
|
paraflagellar rod protein; Provisional
Pssm-ID: 240364 [Multi-domain] Cd Length: 589 Bit Score: 42.26 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 704 RELQDMECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRD-------------NDETKSQALEELTEFyeakLQEKTTL 770
Cdd:PTZ00332 162 ATLKNIEDIMNVTQIQNALASTDDQIKTQLAQLEKTNEIQNvamhdgemqvaeeQMWTKVQLQERLIEL----VADKFRL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 771 LEEAqEDVRQQLREFEETKKQIEEdEDREIQDIKtkyeKKLRDEKESNLRlkgetgimrkkfsSLQKEIEERtnDIEtlK 850
Cdd:PTZ00332 238 IGKC-EEENKSFSKIHEVQKQANQ-ETSQMKDAK----RRLKQRCETDLK-------------HIHDAIQKA--DLE--D 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 851 GEQMKLQGVIKslEKDiqglKREIQERDETIQDKEKRIYDLKKKNQELGKFKFvldykiKELKKQIEP--RENEIRVMKE 928
Cdd:PTZ00332 295 AEAMKRYATNK--EKS----ERFIRENEDRQEEAWNKIQDLERQLQRLGTERF------EEVKRRIEEndREEKRRVEYQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 929 QIQEMEAE---LENFHKQNTQLELNITELWQKLRA------------TDQEM---RRERQKERdLEALVKRFKTdlHNCV 990
Cdd:PTZ00332 363 QFLEVAGQhkkLLELTVYNCDLALRCTGLVEELVSegcaavkarhdkTNQDLaalRLQVHKEH-LEYFRMLYLT--LGSL 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 991 AYIQEPRLlKEKVRGLFEKYVQRADMVEI----AGLNTDLQQEYTRQREHLERNLATLKKKVVKEGELHRTDYVRIMQEN 1066
Cdd:PTZ00332 440 IYKKEKRL-EEIDRNIRTTHIQLEFCVETfdpnAKKHADMKKELYKLRQGVEEELAMLKEKQAQALEMFKESEEALDAAG 518
|
410 420 430
....*....|....*....|....*....|....*
gi 767902636 1067 VSLIKEINELRRELKFTRSQVYDLEAALKLTKKVR 1101
Cdd:PTZ00332 519 IEFVHPVDENNEEVLTRRSKMVEYRSHLAKQEEVK 553
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
756-987 |
2.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 756 LTEFYEAKLQEKTTLLEEAqEDVRQQLREFEETKKQIEEDEDR-----EIQDIKTKYEKKLRDEKESN-LRLKGETGIMR 829
Cdd:COG4913 209 LDDFVREYMLEEPDTFEAA-DALVEHFDDLERAHEALEDAREQiellePIRELAERYAAARERLAELEyLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 830 KKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDetiqdkekriydlkkknqelGKfkfvldyki 909
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG--------------------GD--------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 910 kelkkQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLEL-----------NITELWQKLRATDQEMRRERQKERDLEAL 978
Cdd:COG4913 339 -----RLEQLEREIERLERELEERERRRARLEALLAALGLplpasaeefaaLRAEAAALLEALEEELEALEEALAEAEAA 413
|
....*....
gi 767902636 979 VKRFKTDLH 987
Cdd:COG4913 414 LRDLRRELR 422
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
722-950 |
2.68e-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: 41.97 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 722 EKYQELQLKSQRMQEEYEKQlrdndetKSQALEELTEfyeakLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDReiq 801
Cdd:pfam13166 279 DEFTEFQNRLQKLIEKVESA-------ISSLLAQLPA-----VSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRA--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 802 diktKYEKKLRDEKESNL-RLKGETGIMRKKFSSLQKEIE---ERTNDIETLKGEQMKL--QGVIKSLEKDIQGLKREIQ 875
Cdd:pfam13166 344 ----LEAKRKDPFKSIELdSVDAKIESINDLVASINELIAkhnEITDNFEEEKNKAKKKlrLHLVEEFKSEIDEYKDKYA 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902636 876 ERDETIQDKEKRIYDLKKKNQELGKfkfvldyKIKELkkqieprENEIRVMKEQIQEMEAELENFHKQNTQLELN 950
Cdd:pfam13166 420 GLEKAINSLEKEIKNLEAEIKKLRE-------EIKEL-------EAQLRDHKPGADEINKLLKAFGFGELELSFN 480
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
831-985 |
2.83e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 831 KFSSLQKEIEERTNDIETL----KGEQMKLQGVIKSLEKDIQGLKREIQERDETI----QDKEKRIYDLKKKNQELGKFK 902
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQrkknGENIARKQNKYDELVEEAKTIKAEIEELTDELlnlvMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 903 FVLDYKIKELK------------KQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLEL----------NITELWQKLRA 960
Cdd:PHA02562 269 SKIEQFQKVIKmyekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdefneqskKLLELKNKIST 348
|
170 180
....*....|....*....|....*
gi 767902636 961 TDQEMRRERQKERDLEALVKRFKTD 985
Cdd:PHA02562 349 NKQSLITLVDKAKKVKAAIEELQAE 373
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
718-977 |
2.83e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 718 LLEYEKYQELQLKSQRMQEEYEK-----QLRDNDETKSQALEELTEF------YEAKLQEKTTLLEEAQEDVRQQLREFE 786
Cdd:pfam01576 476 LLQEETRQKLNLSTRLRQLEDERnslqeQLEEEEEAKRNVERQLSTLqaqlsdMKKKLEEDAGTLEALEEGKKRLQRELE 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 787 ETKKQIEEDEDR--EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLE 864
Cdd:pfam01576 556 ALTQQLEEKAAAydKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKE 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 865 KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQN 944
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAK 715
|
250 260 270
....*....|....*....|....*....|...
gi 767902636 945 TQLELNItelwQKLRAtdqemrrerQKERDLEA 977
Cdd:pfam01576 716 LRLEVNM----QALKA---------QFERDLQA 735
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
677-974 |
2.87e-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: 41.44 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 677 NQVLRTEKEKQDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQ----ELQLKSQRMQEEYEKQLRDNDETKSQA 752
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEeqieEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 753 LEELTEFYEAKLQEKTTLLEEAQEDVRQQlREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKF 832
Cdd:pfam13868 111 QEEDQAEAEEKLEKQRQLREEIDEFNEEQ-AEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 833 SSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIydlkkknqelgkfkfvldyKIKEL 912
Cdd:pfam13868 190 RAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI-------------------ELKER 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902636 913 KKQIEPRENE---IRVMKEQIQEMEAELENFHKQNTQLELNITELWQKLRATDQEMRRERQKERD 974
Cdd:pfam13868 251 RLAEEAEREEeefERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELE 315
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
624-803 |
2.87e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 624 EEKAQVMLELKTRVEELKMENEYQLRLKDmnysEKIKELTDKFIQEMESLKTKnqvlrtekekqdvyhhehiEDLLDKQS 703
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERR----NELQKLEKRLLQKEENLDRK-------------------LELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 704 RELQDMECCNNQKLlleyekyQELQLKSQRMQEEYEKQLrdndetksQALEE---LTEFyEAKLQEKTTLLEEAQEDVRQ 780
Cdd:PRK12704 110 EELEKKEKELEQKQ-------QELEKKEEELEELIEEQL--------QELERisgLTAE-EAKEILLEKVEEEARHEAAV 173
|
170 180
....*....|....*....|...
gi 767902636 781 QLREFEEtkkQIEEDEDREIQDI 803
Cdd:PRK12704 174 LIKEIEE---EAKEEADKKAKEI 193
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
729-903 |
2.89e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 729 LKSQRMQEEYEKQLRDNDEtksqalEELTEFYEAKLQEKTTLLEEAQE--DVRQQLRE-FEETKKQIEEdedreiqdikt 805
Cdd:smart00787 128 LEAKKMWYEWRMKLLEGLK------EGLDENLEGLKEDYKLLMKELELlnSIKPKLRDrKDALEEELRQ----------- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 806 kyEKKLRDEKESNLrlKGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIqdKE 885
Cdd:smart00787 191 --LKQLEDELEDCD--PTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL--EQ 264
|
170
....*....|....*...
gi 767902636 886 KRIYDLKKKNQELGKFKF 903
Cdd:smart00787 265 CRGFTFKEIEKLKEQLKL 282
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
881-1039 |
2.93e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 881 IQDKEKRIYDLKK-KNQELGKFKFVLDYKIKELKK-------QIEPRENEIRVMKEQIQEMEA----ELENFHKQNTQLE 948
Cdd:pfam09787 20 LQSKEKLIASLKEgSGVEGLDSSTALTLELEELRQerdllreEIQKLRGQIQQLRTELQELEAqqqeEAESSREQLQELE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 949 LNITELWQKLRATDQEMRRERQKERDLEALVKRFKTDLHNCV----AYIQEPRL--------------LKEKVRGLFEKY 1010
Cdd:pfam09787 100 EQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIkdreAEIEKLRNqltsksqssssqseLENRLHQLTETL 179
|
170 180
....*....|....*....|....*....
gi 767902636 1011 VQRADMVEiaglntDLQQEYTRQREHLER 1039
Cdd:pfam09787 180 IQKQTMLE------ALSTEKNSLVLQLER 202
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
797-1081 |
3.02e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 797 DREIQDIKTKYEKKLRD-EKESNLRLKGETGIMR---KKFSSLQKEIEERTNDIETLKGEQMKLQGVIKSLEKDIQ---- 868
Cdd:PLN02939 105 DEAIAAIDNEQQTNSKDgEQLSDFQLEDLVGMIQnaeKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSetda 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 869 --GLKREIQERDETIQDK-EKRIYDLKKKNQELGKFKFVLDYKIKELKKQIEPRENEIRVMKEQ---IQEMEAELENFHK 942
Cdd:PLN02939 185 riKLAAQEKIHVEILEEQlEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAElieVAETEERVFKLEK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 943 QNTQLELNITELWQKLRATDQEMRRER--------QKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKVRGLfEKYVQRA 1014
Cdd:PLN02939 265 ERSLLDASLRELESKFIVAQEDVSKLSplqydcwwEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKL-EASLKEA 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902636 1015 DMVEIAGLNTDL-QQEYTRQREHLERNlatlkkkvvkEGELHrtDYVRIMQEnvsLIKEINELRRELK 1081
Cdd:PLN02939 344 NVSKFSSYKVELlQQKLKLLEERLQAS----------DHEIH--SYIQLYQE---SIKEFQDTLSKLK 396
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
739-1153 |
3.44e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 739 EKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQlREFEETKKQIEEDEDREIQDIKTKYEKklrdEKESN 818
Cdd:pfam10174 44 ERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQ-RDLNQLLQQDFTTSPVDGEDKFSTPEL----TEENF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 819 LRLKGETGIMRKKFSSLQKEIEERTNDIETLKG-------------EQMKLQGVIKSLEKDIQGLKREIQERDETIQDKE 885
Cdd:pfam10174 119 RRLQSEHERQAKELFLLRKTLEEMELRIETQKQtlgardesikkllEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 886 KRiydLKKKNQELGKFKFVLDY---------KIKELKKQIEPRENEIRVMKEQIQEMEAELEN------FHKQNTQLELN 950
Cdd:pfam10174 199 VL---LDQKEKENIHLREELHRrnqlqpdpaKTKALQTVIEMKDTKISSLERNIRDLEDEVQMlktnglLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 951 ITELWQ--------KLRATDQEMRRerqKERDLEALVKRFKTdLHN----CVAYIQeprLLKEKvrgLFEKYvQRADMve 1018
Cdd:pfam10174 276 QMEVYKshskfmknKIDQLKQELSK---KESELLALQTKLET-LTNqnsdCKQHIE---VLKES---LTAKE-QRAAI-- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1019 iaglntdLQQEYTRQREHLERNLATLKKKvvkegelhrTDYVRIMQENVSL-------------IKE--INELRRELKFT 1083
Cdd:pfam10174 343 -------LQTEVDALRLRLEEKESFLNKK---------TKQLQDLTEEKSTlageirdlkdmldVKErkINVLQKKIENL 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 1084 RSQVYDLEAALKlTKKVRPQEVSETEPSRDMLSTAPTARLNEQEetgRIIEmqRLEIQRLRDQIQEQEQV 1153
Cdd:pfam10174 407 QEQLRDKDKQLA-GLKERVKSLQTDSSNTDTALTTLEEALSEKE---RIIE--RLKEQREREDRERLEEL 470
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
771-1118 |
3.73e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 771 LEEAQEDVRQQLREFEETKKQIEEDEDR--EIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKfsslQKEIEERTNDIET 848
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKacEIRDQITSKEAQLESSREIVKSYENELDPLKNR----LKEIEHNLSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 849 LKGEQMKLQGVIKSLEKDIQGLK----------------------REIQERDETIQDKEKRIYDLKKKNQELGKFKFVLD 906
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELElkmekvfqgtdeqlndlyhnhqRTVREKERELVDCQRELEKLNKERRLLNQEKTELL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 907 YKIKELKKQIEPRENEIRVMKEQIQEMEaelenfhkqnTQLELNITElwqklRATDQEMRRERQKERDLEALVKRFKTDL 986
Cdd:TIGR00606 347 VEQGRLQLQADRHQEHIRARDSLIQSLA----------TRLELDGFE-----RGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 987 HNCVAYIQEPRLLKEKVRGLfekyvqradMVEIAGLNTDLQQEytrqREHLERNLATLKKKvVKEGELHRTDYVRIMQEN 1066
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEI---------RDEKKGLGRTIELK----KEILEKKQEELKFV-IKELQQLEGSSDRILELD 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902636 1067 VSLIKEINEL------------RRELKFTRSQVYDLEAALKLTKKVRPQEVSETEPSRDMLSTA 1118
Cdd:TIGR00606 478 QELRKAERELskaeknsltetlKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT 541
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
653-826 |
3.83e-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: 40.77 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 653 MNYSEKIKELTDKfiqEMESLKTKNQVLRTEKEKQDVYHHEhIEDLLDKQSRELQDMeccnnQKLLLEYEKYQELQLKSQ 732
Cdd:smart00787 139 MKLLEGLKEGLDE---NLEGLKEDYKLLMKELELLNSIKPK-LRDRKDALEEELRQL-----KQLEDELEDCDPTELDRA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 733 RmqEEYEKQLRDNDEtKSQALEELTEfyeaKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLR 812
Cdd:smart00787 210 K--EKLKKLLQEIMI-KVKKLEELEE----ELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKL 282
|
170
....*....|....
gi 767902636 813 DEKESNLRLKGETG 826
Cdd:smart00787 283 LQSLTGWKITKLSG 296
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
730-1003 |
3.83e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 730 KSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTTLLEEAQEDVRQQL---REFEETKKQIEEDEDR--EIQDIK 804
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSIneyNKIESARADLEDIKIKinELKDKH 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 805 TKYEKKlrDEKESNLRLkgetGIMRKKFSSLQKEIEERTN-DIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQD 883
Cdd:PRK01156 546 DKYEEI--KNRYKSLKL----EDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 884 KEKRIYDlkKKNQELGKFKfvldyKIKELKKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQLeLNITELWQKLRATDQ 963
Cdd:PRK01156 620 SIREIEN--EANNLNNKYN-----EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRI-NDIEDNLKKSRKALD 691
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767902636 964 EMRRERQKERDLEALVKRFKTDLHNCVAYIQEPRLLKEKV 1003
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDINETLESMKKI 731
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
838-1103 |
3.91e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 838 EIEERTNDIETLKGEQMKLQGVIKSLEKDIQGLKREIQERDETIQDKEKRIY----DLKKKNQELGKFKFVLDYKIKELK 913
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRtlddQWKEKRDELNGELSAADAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 914 KQIEPRENEIRV-MKEQIQEMEAELENFHKQNTQLEL---NITELWQKLRATDQEMRRERQKeRDLEalVKRFKTDLHNC 989
Cdd:pfam12128 322 SELEALEDQHGAfLDADIETAAADQEQLPSWQSELENleeRLKALTGKHQDVTAKYNRRRSK-IKEQ--NNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 990 VAYIQEprllkEKVRGLfekyvqradmveiAGLNTDLQQEYTRQREHLERNLATLK--KKVVKE--GELH-RTDYVRIMQ 1064
Cdd:pfam12128 399 LAKIRE-----ARDRQL-------------AVAEDDLQALESELREQLEAGKLEFNeeEYRLKSrlGELKlRLNQATATP 460
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 767902636 1065 ENVSLIK----EINELRRELKFTRSQVYDLEAALKLTKKVRPQ 1103
Cdd:pfam12128 461 ELLLQLEnfdeRIERAREEQEAANAEVERLQSELRQARKRRDQ 503
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
631-816 |
4.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 631 LELKTRVEELKMENEYQLRLKDMNYSEKIKELTDKFIQEMESLKTKNQVLRT-EKEKQDVYHHEHIEDLLDK-QSRELQD 708
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAALLAEaGVEDEEE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 709 MEccnnqKLLLEYEKYQELQLKsqrmQEEYEKQLRDNDETKSQALEELT-EFYEAKLQEKTTLLEEAQEDVRQQLREFEE 787
Cdd:COG4717 387 LR-----AALEQAEEYQELKEE----LEELEEQLEELLGELEELLEALDeEELEEELEELEEELEELEEELEELREELAE 457
|
170 180 190
....*....|....*....|....*....|
gi 767902636 788 TKKQIEE-DEDREIQDIKTKYEKKLRDEKE 816
Cdd:COG4717 458 LEAELEQlEEDGELAELLQELEELKAELRE 487
|
|
| WDR74 |
cd22857 |
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ... |
343-420 |
4.64e-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: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 343 CLCFSPSEETLVASTSKNQLYSI---TMSLTEISKGepahfeylmypLHSAPITGLATCIRKPLIATCSLDRSIRLWNYE 419
Cdd:cd22857 228 AVAEDPDGHTVYVGDTSGDLASIdlrTGKLLGCFKG-----------KCGGSIRSIARHPELPLIASCGLDRYLRIWDTE 296
|
.
gi 767902636 420 T 420
Cdd:cd22857 297 T 297
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
687-927 |
5.34e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 687 QDVYHHEHIEDLLDKQSRELQDMECCNNQKLLLEYEKYQElQLKSQRMQ----EEYEKQLRDNDETKSQALEELTEFYEA 762
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYN-KIESARADlediKIKINELKDKHDKYEEIKNRYKSLKLE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 763 KLQEKTTLLEEAQE-----DVRQQLREFEETKKQIEEDEDR------EIQDIKTKYEKKLR--DEKESNLRLKgetgimR 829
Cdd:PRK01156 562 DLDSKRTSWLNALAvisliDIETNRSRSNEIKKQLNDLESRlqeieiGFPDDKSYIDKSIReiENEANNLNNK------Y 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 830 KKFSSLQKEIEERTNDIETLKGEQMKlqgvIKSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKFKFVLDYKI 909
Cdd:PRK01156 636 NEIQENKILIEKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
250
....*....|....*...
gi 767902636 910 KELKKQIEPRENEIRVMK 927
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
657-874 |
5.58e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 657 EKIKELTD--KFIQE----MESLKTKNQVLRTEKE-----KQDVYHHEHIEDLLDKQSRELQDMeccNNQKLLLEYEKYQ 725
Cdd:PRK04863 901 EQLDEAEEakRFVQQhgnaLAQLEPIVSVLQSDPEqfeqlKQDYQQAQQTQRDAKQQAFALTEV---VQRRAHFSYEDAA 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 726 ELQLKSQRMQEEYEKQLRDNDETKSQALEELTEfYEAKLQEKTTLLEEAQE--DV-RQQLREFEetkkqieededREIQD 802
Cdd:PRK04863 978 EMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQ-AQAQLAQYNQVLASLKSsyDAkRQMLQELK-----------QELQD 1045
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902636 803 IKTKY----EKKLRDEKEsnlRLKGETGIMRKKFSSLQKEIEERTNDIETLkgeqmklQGVIKSLEKDIQGLKREI 874
Cdd:PRK04863 1046 LGVPAdsgaEERARARRD---ELHARLSANRSRRNQLEKQLTFCEAEMDNL-------TKKLRKLERDYHEMREQV 1111
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
637-964 |
5.62e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 637 VEELKMENEYQLRLKDMNYS-EKIKELTDKFIQEMESLKT--KNQvlrTEKEKQDVYHHEHIEDLLDKQSRELQDMECCN 713
Cdd:TIGR01612 1401 LEECKSKIESTLDDKDIDECiKKIKELKNHILSEESNIDTyfKNA---DENNENVLLLFKNIEMADNKSQHILKIKKDNA 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 714 NQKLLLEYEKYQELQLKSQRMQEEYEK---QLRDNDETKSQALEELTE----FYEAKLQEKttlLEEAQEDVRQQLREFE 786
Cdd:TIGR01612 1478 TNDHDFNINELKEHIDKSKGCKDEADKnakAIEKNKELFEQYKKDVTEllnkYSALAIKNK---FAKTKKDSEIIIKEIK 1554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 787 ETKKQIEEDEDREIQDIKTKYEKKLRDEKE---SNLRLKGETGI------MRKKFSSLQkEIEERTNDIETlkgEQMKLQ 857
Cdd:TIGR01612 1555 DAHKKFILEAEKSEQKIKEIKKEKFRIEDDaakNDKSNKAAIDIqlslenFENKFLKIS-DIKKKINDCLK---ETESIE 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 858 GVIKSLEKDIQGLK--------REIQERDETIQDKEKRIYDLKKKNQElgkfkfvLDYKIKELKKQIEPREN--EIRVMk 927
Cdd:TIGR01612 1631 KKISSFSIDSQDTElkengdnlNSLQEFLESLKDQKKNIEDKKKELDE-------LDSEIEKIEIDVDQHKKnyEIGII- 1702
|
330 340 350
....*....|....*....|....*....|....*...
gi 767902636 928 EQIQEM-EAELENFHKQNTQLELNITELWQKLRATDQE 964
Cdd:TIGR01612 1703 EKIKEIaIANKEEIESIKELIEPTIENLISSFNTNDLE 1740
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
836-1148 |
6.43e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 836 QKEIEERTNDIETLKGEQMKLQGVIKSLE---KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELGKfkfvldyKIKEL 912
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRaeiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLK-------EIERL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 913 KKQIEPRENEIRVMKEQIQEMEAELENFHKQNTQlelnitelwqkLRATDQEMRRERQKERDLEALVKRFKtDLHNCVAY 992
Cdd:PRK01156 224 SIEYNNAMDDYNNLKSALNELSSLEDMKNRYESE-----------IKTAESDLSMELEKNNYYKELEERHM-KIINDPVY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 993 IQeprllKEKVRGLFEKYVQRADMVEI-AGLNTDLQqeytrQREHLERNLATLKKkvvkegelHRTDYVRIMQENVSLIK 1071
Cdd:PRK01156 292 KN-----RNYINDYFKYKNDIENKKQIlSNIDAEIN-----KYHAIIKKLSVLQK--------DYNDYIKKKSRYDDLNN 353
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902636 1072 EINELRRELKFTRSQVYDLEaalKLTKKVRpqevsETEPSRDMLSTAPTARLNEQEETGRIIEMQRLEIQRLRDQIQ 1148
Cdd:PRK01156 354 QILELEGYEMDYNSYLKSIE---SLKKKIE-----EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
614-824 |
7.54e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 614 EEVLVTKTDMEEKaqvMLELKTRVEELKMENEYQLrlkdmnySEKIKELtDKFIQEMESLKTKNQVLRTEKEKQDVYHHE 693
Cdd:PRK03918 559 AELEKKLDELEEE---LAELLKELEELGFESVEEL-------EERLKEL-EPFYNEYLELKDAEKELEREEKELKKLEEE 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 694 hIEDLLDKQSRELQDMECCNNQ--KLLLEY--EKYQELQLKSQRMQEEYE------KQLRDNDETKSQALEELTEFYEA- 762
Cdd:PRK03918 628 -LDKAFEELAETEKRLEELRKEleELEKKYseEEYEELREEYLELSRELAglraelEELEKRREEIKKTLEKLKEELEEr 706
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902636 763 -KLQEKTTLLEEAQEDVrQQLRE-FEETKKQIEEDEDREIQDIKTKYEKKLRDEKESNLRLKGE 824
Cdd:PRK03918 707 eKAKKELEKLEKALERV-EELREkVKKYKALLKERALSKVGEIASEIFEELTEGKYSGVRVKAE 769
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
751-861 |
7.62e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 751 QALEELtefyEAKLQEKTTLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYEKKLRDEKE---------SNLRL 821
Cdd:PRK00409 523 ASLEEL----ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikelRQLQK 598
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767902636 822 KGETGIMRKKFSSLQKEIEERTNDIETLKGEQMKLQGVIK 861
Cdd:PRK00409 599 GGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
721-838 |
8.54e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.
Pssm-ID: 214016 [Multi-domain] Cd Length: 152 Bit Score: 38.36 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902636 721 YEKYQELQLKS---QRMQEEYEKqLRDNDETKSQALE---ELTEFYEAKLQEKTTLLEEAQEDVRQQLRE-FEETKKQIE 793
Cdd:cd12923 11 KEINKEYLDKSreyDELYEKYNK-LSQEIQLKRQALEafeEAVKMFEEQLRTQEKFQKEAQPHEKQRLMEnNELLKSRLK 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767902636 794 ededrEIQDIKTKYEKKLRDEKESNLRLKGETGIMRKKFSSLQKE 838
Cdd:cd12923 90 -----ELEESKEQLEEDLRKQVAYNRELEREMNSLKPELMQLRKQ 129
|
|
| |
