|
Name |
Accession |
Description |
Interval |
E-value |
| FKBP_C |
pfam00254 |
FKBP-type peptidyl-prolyl cis-trans isomerase; |
192-285 |
3.31e-28 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase;
Pssm-ID: 459735 Cd Length: 94 Bit Score: 109.21 E-value: 3.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 192 AVETGDSLEVAYTGWLLQnhvlGQVFDSTANKDKPLRLKLGSGKVVKGLEDGLLGMKKGGKRLIITPSACAAGSEGVIGW 271
Cdd:pfam00254 4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79
|
90
....*....|....
gi 568926925 272 TQPTDSILVFEVEV 285
Cdd:pfam00254 80 VIPPNATLVFEVEL 93
|
|
| FkpA |
COG0545 |
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
183-285 |
3.33e-26 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 103.72 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 183 QDLVAAEGPAVETGDSLEVAYTGWLLQnhvlGQVFDSTANKDKPLRLKLGSGKVVKGLEDGLLGMKKGGKRLIITPSACA 262
Cdd:COG0545 4 KVLKEGTGAKPKAGDTVTVHYTGTLLD----GTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
|
90 100
....*....|....*....|....*.
gi 568926925 263 ---AGSEGVIgwtqPTDSILVFEVEV 285
Cdd:COG0545 80 ygeRGAGGVI----PPNSTLVFEVEL 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
561-885 |
8.67e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 8.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 561 IMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNS------LQTATENTQARILHAEQ 634
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerleeLEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 635 EKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRR 714
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 715 QLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERcQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTL 794
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 795 AQAELQSqweakcEQLLASARDEHLQQyrevcAQRDAHQQKLALLQD--------ECLALQAQIAAFTEQKEHMQRLEKT 866
Cdd:COG1196 497 LEAEADY------EGFLEGVKAALLLA-----GLRGLAGAVAVLIGVeaayeaalEAALAAALQNIVVEDDEVAAAAIEY 565
|
330
....*....|....*....
gi 568926925 867 KSQAPAGRAAADPSEKVKK 885
Cdd:COG1196 566 LKAAKAGRATFLPLDKIRA 584
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
601-892 |
1.69e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 601 QRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDL 680
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 681 LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKK---SAQERCQAEA 757
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAElaeAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 758 EMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQsqwEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLA 837
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568926925 838 LLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKKIMNQVFQ 892
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
573-841 |
9.71e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.80 E-value: 9.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 573 ERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLM------MEKRNNSLQTATENTQARILHAEQEKAKVTEELAAA 646
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELrlevseLEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 647 TAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEE 726
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 727 LTDLRAEKTSLEKNLS---ERKKKSAQERCQAEAEMDEIRKS-HQEELDRLRQLLKKArVSTDQAAAEQLTLAQAELqsq 802
Cdd:TIGR02168 395 IASLNNEIERLEARLErleDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEEL-QEELERLEEALEELREEL--- 470
|
250 260 270
....*....|....*....|....*....|....*....
gi 568926925 803 weAKCEQLLASARDEHLQqyrevcaqrdaHQQKLALLQD 841
Cdd:TIGR02168 471 --EEAEQALDAAERELAQ-----------LQARLDSLER 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
531-857 |
1.19e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.42 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 531 LMTKVEELQKHSSgnsMLLPSMSV-TMETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNL 609
Cdd:TIGR02169 693 LQSELRRIENRLD---ELSQELSDaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 610 MMEKRNNsLQTATENTQARILHA-----EQEKAKVTEELAAATAQVSHLQLKMtahqkKETELQLQLTDNLKETdlLRGH 684
Cdd:TIGR02169 770 LEEDLHK-LEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREIEQKL-----NRLTLEKEYLEKEIQE--LQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 685 VTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKsaqeRCQAEAEMDEIRK 764
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK----IEELEAQIEKKRK 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 765 sHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQ-SQWEAKCEQLLASARD------EHLQQYREVCAQRDAHQQKLA 837
Cdd:TIGR02169 918 -RLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSlEDVQAELQRVEEEIRAlepvnmLAIQEYEEVLKRLDELKEKRA 996
|
330 340
....*....|....*....|
gi 568926925 838 LLQDECLALQAQIAAFTEQK 857
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKKK 1016
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
565-821 |
2.00e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 565 IQRIIQENERLKQELLEKSSRIEEQNDKIsDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELA 644
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 645 AATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLE 724
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 725 EELTDLRAEKTSLEKNLSERKKKSAQERcQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWE 804
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLE-EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250
....*....|....*..
gi 568926925 805 AKCEQLLASARDEHLQQ 821
Cdd:COG1196 472 AALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
621-902 |
1.56e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 621 ATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASE 700
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 701 QTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKK--SAQERCQA-EAEMDEIRKSHQEELDRLRQLL 777
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieQLKEELKAlREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 778 KKARVSTDQAAAEQLTLaqAELQSQWEAKCEQL---------LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQA 848
Cdd:TIGR02168 824 ERLESLERRIAATERRL--EDLEEQIEELSEDIeslaaeieeLEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568926925 849 QIAaftEQKEHMQRLEKTKSQAPAGRAAADPS-EKVKKIMNQVFQSLRGEFELEE 902
Cdd:TIGR02168 902 ELR---ELESKRSELRRELEELREKLAQLELRlEGLEVRIDNLQERLSEEYSLTL 953
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
624-831 |
4.97e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 624 NTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQ--LQLTDNLKETDLLRGHVTRLQADLSELREASeq 701
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASS-- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 702 tqTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELD-RLRQLLKKA 780
Cdd:COG4913 685 --DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEeRFAAALGDA 762
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568926925 781 RVstdQAAAEQLTLAQAELQSQwEAKCEQLLASARDEHLQQYREVCAQRDA 831
Cdd:COG4913 763 VE---RELRENLEERIDALRAR-LNRAEEELERAMRAFNREWPAETADLDA 809
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
507-778 |
2.82e-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: 71.63 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 507 MTEARQHNTEIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSvtMETSMIMSNIQRIIQENERLKQELLEKSSRI 586
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR--KDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 587 EEQNDKISDL----------IERNQRYVEQSNLMMEK------------------------RNNSLQTATENTQARILHA 632
Cdd:TIGR02168 764 EELEERLEEAeeelaeaeaeIEELEAQIEQLKEELKAlrealdelraeltllneeaanlreRLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 633 EQEKAKVTEELAAATAQVSHLQLKMTahqkketELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQS 712
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIE-------ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568926925 713 RRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLK 778
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
627-905 |
3.18e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 627 ARILHAE-QEKAKVTEELAAataqVSHLQLKmtahqKKETELQL--------QLTDNLKEtdlLRGHVTRLQA------- 690
Cdd:TIGR02168 147 SEIIEAKpEERRAIFEEAAG----ISKYKER-----RKETERKLertrenldRLEDILNE---LERQLKSLERqaekaer 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 691 ------------------DLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKK----- 747
Cdd:TIGR02168 215 ykelkaelrelelallvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyala 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 748 SAQERCQAEAEMDEIRKSH----QEELDRLRQLLKKARVsTDQAAAEQLTLAQAELQSQWEAKCEQL--LASARDEHLQQ 821
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANlerqLEELEAQLEELESKLD-ELAEELAELEEKLEELKEELESLEAELeeLEAELEELESR 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 822 YREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQ-RLEKTKSQAPAGRAAADPSEKvKKIMNQVFQSLRGEFEL 900
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdRRERLQQEIEELLKKLEEAEL-KELQAELEELEEELEEL 452
|
....*
gi 568926925 901 EESYD 905
Cdd:TIGR02168 453 QEELE 457
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
566-865 |
5.09e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 566 QRIIQENERLK------QELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKV 639
Cdd:COG4717 139 AELAELPERLEeleerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 640 TEELAAATAQVSHLQLKMTAHQKKETELQLQ--------------LTDNLKETDLLRGHVTRLQA-----DLSELREASE 700
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLgllalLFLLLAREKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 701 QTQTKFKSEKQSRRQLELKVTSLEEELTDLRAeKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEE--LDRLRQLLK 778
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGL-PPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 779 KARVSTD-------------QAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLA 845
Cdd:COG4717 378 EAGVEDEeelraaleqaeeyQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAE 457
|
330 340
....*....|....*....|
gi 568926925 846 LQAQIAAFTEQKEHMQRLEK 865
Cdd:COG4717 458 LEAELEQLEEDGELAELLQE 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
659-885 |
3.57e-11 |
|
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: 66.71 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 659 AHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLE 738
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 739 KNLSERKKK------SAQERCQAEAEMDEIRKSHQEELDRLRQLLKKArVSTDQAAAEQLTLAQAELQSQWEAKCEQL-- 810
Cdd:COG4942 97 AELEAQKEElaellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEELRADLAELAALRAELEAERae 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568926925 811 LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKK 885
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
566-798 |
9.07e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 9.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 566 QRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQtateNTQARILHAEQEKAKVTEELAA 645
Cdd:TIGR02169 272 QLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA----KLEAEIDKLLAEIEELEREIEE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 646 ATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEE 725
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568926925 726 ELTDLRAEKTSLE---KNLSERKKKSAQERCQAEAEMDEIRKSH---QEELDRLRQLLKKARVSTDQAAAEQLTLAQAE 798
Cdd:TIGR02169 428 AIAGIEAKINELEeekEDKALEIKKQEWKLEQLAADLSKYEQELydlKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
561-825 |
1.27e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 561 IMSNIQRIIQENERLK--QELLEKssrIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAK 638
Cdd:COG4913 223 TFEAADALVEHFDDLEraHEALED---AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 639 VTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNlkETDLLrghvTRLQADLSELREASEQTQTKFKSEKQSRRQLEL 718
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGN--GGDRL----EQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 719 KVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQE---ELDRLRQL-------LKKARvstdQAA 788
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREleaEIASLERRksniparLLALR----DAL 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568926925 789 AEQLTLAQAEL------------QSQWEAKCEQLLASAR------DEHLQQYREV 825
Cdd:COG4913 450 AEALGLDEAELpfvgelievrpeEERWRGAIERVLGGFAltllvpPEHYAAALRW 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
515-739 |
3.33e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 515 TEIRMAVNKVADKMDHLMTKVEELQKhssgnsmllpsmsvtmETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKIS 594
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALAN----------------EISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 595 DLIERNQRYVEQSNL--------------------MMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQ 654
Cdd:TIGR02168 334 ELAEELAELEEKLEElkeelesleaeleeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 655 lkmtAHQKKETELQLQLTDNLKETDL--LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRA 732
Cdd:TIGR02168 414 ----DRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
....*..
gi 568926925 733 EKTSLEK 739
Cdd:TIGR02168 490 RLDSLER 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
563-898 |
9.22e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 9.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 563 SNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTA---TENTQARILHAEQEKAKV 639
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgltPEKLEKELEELEKAKEEI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 640 TEELAAATAQVSHL------------QLK------------MTAHQKKE-------------------TELQLQLTDNLK 676
Cdd:PRK03918 404 EEEISKITARIGELkkeikelkkaieELKkakgkcpvcgreLTEEHRKElleeytaelkriekelkeiEEKERKLRKELR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 677 ETDLLRGHVTRLQA------------------DLSELREASEQTQT-------------KFKSEKQSRRQLELKVTSLEE 725
Cdd:PRK03918 484 ELEKVLKKESELIKlkelaeqlkeleeklkkyNLEELEKKAEEYEKlkekliklkgeikSLKKELEKLEELKKKLAELEK 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 726 ELTDLRAEKTSLEKNLSERKKKSAQErcqAEAEMDEIRKSHQE---------ELDRLRQLLKKARVSTDQAAAEqLTLAQ 796
Cdd:PRK03918 564 KLDELEEELAELLKELEELGFESVEE---LEERLKELEPFYNEylelkdaekELEREEKELKKLEEELDKAFEE-LAETE 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 797 AELQSQwEAKCEQLLASARDEhlqQYREVcaqrdahQQKLALLQDECLALQAQIAAFTEQKEHMQR-LEKTKSQAPAGRA 875
Cdd:PRK03918 640 KRLEEL-RKELEELEKKYSEE---EYEEL-------REEYLELSRELAGLRAELEELEKRREEIKKtLEKLKEELEEREK 708
|
410 420
....*....|....*....|...
gi 568926925 876 AADPSEKVKKIMNQVfQSLRGEF 898
Cdd:PRK03918 709 AKKELEKLEKALERV-EELREKV 730
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
563-808 |
1.59e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 563 SNIQRIIQENErlkQELLEKSSRIEEQNDKISDLIERnqryVEqsnlMMEKRNNSLqtatENTQARILHAEQEKAKVTEE 642
Cdd:PRK03918 189 ENIEELIKEKE---KELEEVLREINEISSELPELREE----LE----KLEKEVKEL----EELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 643 LAAATAQVSHLQlKMTAHQKKETElqlQLTDNLKETDLLRGHVTRLQAdLSELREaseqtqtKFKSEKqsrRQLELKVTS 722
Cdd:PRK03918 254 KRKLEEKIRELE-ERIEELKKEIE---ELEEKVKELKELKEKAEEYIK-LSEFYE-------EYLDEL---REIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 723 LEEELTDLRAEKTSLEKnLSERKKKSAQERCQAEAEMDEIRKSHqEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQ 802
Cdd:PRK03918 319 LEEEINGIEERIKELEE-KEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL 396
|
....*.
gi 568926925 803 WEAKCE 808
Cdd:PRK03918 397 EKAKEE 402
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
670-877 |
1.66e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 670 QLTDNLKETDLLRGHVTRLQADLSELREASEQtqtkfksekqsrrqlelkvtsLEEELTDLRAEKTSLEKNLseRKKKSA 749
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEE---------------------LEAELEELREELEKLEKLL--QLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 750 QERCQAEAEMDEIrkshQEELDRLRQllKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDE---HLQQYREVC 826
Cdd:COG4717 132 QELEALEAELAEL----PERLEELEE--RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdLAEELEELQ 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568926925 827 AQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAA 877
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
566-829 |
1.67e-09 |
|
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: 62.06 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 566 QRIIQENERLKQELlEKSSRIEEQNDKISDLIERNQR-YVEQSNLMMEkRNNSLQTATENTQARilhaEQEKAKvTEELA 644
Cdd:pfam17380 299 ERLRQEKEEKAREV-ERRRKLEEAEKARQAEMDRQAAiYAEQERMAME-RERELERIRQEERKR----ELERIR-QEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 645 AATAQVSHLQ-LKMTAHQKK----------------ETELQLQLTDNLKETDLLRGHVTRL-QADLSELREASEQTQTKF 706
Cdd:pfam17380 372 MEISRMRELErLQMERQQKNervrqeleaarkvkilEEERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMERV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 707 KSEKQSRRQlelKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEElDRLRQLLKKARVSTDQ 786
Cdd:pfam17380 452 RLEEQERQQ---QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEE-ERKRKLLEKEMEERQK 527
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568926925 787 AAAEQLTLAQAELQSQWEAKCEQllasaRDEHLQQYREVCAQR 829
Cdd:pfam17380 528 AIYEEERRREAEEERRKQQEMEE-----RRRIQEQMRKATEER 565
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
567-905 |
2.11e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 62.11 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 567 RIIQENERLKQELLEKSSRIEEQNDK--------------ISDLIERNQRYvEQSNLMMEK-------RNNSLQTATENT 625
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKakslsklknkheamISDLEERLKKE-EKGRQELEKakrklegESTDLQEQIAEL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 626 QARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTD---NLKETDLLRGHVTRLQADLSE----LREA 698
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISElqeDLESERAARNKAEKQRRDLGEeleaLKTE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 699 SEQTQ--TKFKSEKQSRRQLEL---------------------------KVTSLEEELTDLRAEKTSLEKN--------- 740
Cdd:pfam01576 308 LEDTLdtTAAQQELRSKREQEVtelkkaleeetrsheaqlqemrqkhtqALEELTEQLEQAKRNKANLEKAkqalesena 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 741 --------LSERKKKSAQERCQAEAEMDEIRKSHQEElDRLRQLLkkarvstdqaaAEQLTLAQAELQS------QWEAK 806
Cdd:pfam01576 388 elqaelrtLQQAKQDSEHKRKKLEGQLQELQARLSES-ERQRAEL-----------AEKLSKLQSELESvssllnEAEGK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 807 CEQLL--ASARDEHLQQYREVCAQRDahQQKLAL------LQDECLALQAQIAAFTEQKEHMQR--------LEKTKSQA 870
Cdd:pfam01576 456 NIKLSkdVSSLESQLQDTQELLQEET--RQKLNLstrlrqLEDERNSLQEQLEEEEEAKRNVERqlstlqaqLSDMKKKL 533
|
410 420 430
....*....|....*....|....*....|....*.
gi 568926925 871 PAGRAAADPSEKVKKIMNQVFQSLRGEF-ELEESYD 905
Cdd:pfam01576 534 EEDAGTLEALEEGKKRLQRELEALTQQLeEKAAAYD 569
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
569-864 |
2.35e-09 |
|
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: 60.70 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 569 IQENERLKQELLEKSSRIEEqndkisdliernqryveqsnlMMEKRNnslqtatENTQARILHAEQEKAKVTEELAAAta 648
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDE---------------------MMEEER-------ERALEEEEEKEEERKEERKRYRQE-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 649 qvshLQLKMTAHQKKETELQLQLtdnLKETDLLRGHVTRLQA-DLSELRE-ASEQTQT-----KFKSEKQSRRQLELKvt 721
Cdd:pfam13868 78 ----LEEQIEEREQKRQEEYEEK---LQEREQMDEIVERIQEeDQAEAEEkLEKQRQLreeidEFNEEQAEWKELEKE-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 722 slEEELTDLRAEKTSLEKNLSERKKksaqercqaEAEMDEIRKSHQEELDRLRQLLKKARVstDQAAAEQL--TLAQAEL 799
Cdd:pfam13868 149 --EEREEDERILEYLKEKAEREEER---------EAEREEIEEEKEREIARLRAQQEKAQD--EKAERDELraKLYQEEQ 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568926925 800 QSQWEAK----------CEQLLASARDEHL---QQYREVCAQRDAHQQKLALLQdecLALQAQIAAFTEQKEHMQRLE 864
Cdd:pfam13868 216 ERKERQKereeaekkarQRQELQQAREEQIelkERRLAEEAEREEEEFERMLRK---QAEDEEIEQEEAEKRRMKRLE 290
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
562-803 |
2.71e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 562 MSNIQRIIQENERLKQELLEKssrIEEQNDKISDLIERNQRYVEQSNLmMEKRNNSLQTATENTQARIlhaEQEKAKVTE 641
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAEL---EAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 642 ELAAATAQVSHLQLKMTAHQKketelqlQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKfksekqsRRQLELKVT 721
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPE-------DFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-------RAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 722 SLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEElDRLRQLLKKARVSTDQAAAEQLTLAQAELQS 801
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
..
gi 568926925 802 QW 803
Cdd:COG4942 254 KL 255
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
571-884 |
3.43e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 571 ENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKvTEELAAATAQV 650
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK-ADAAKKKAEEK 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 651 shlqlKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEqtqTKFKSEkQSRRQLELKVTSlEEELTDL 730
Cdd:PTZ00121 1391 -----KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE---AKKKAE-EAKKADEAKKKA-EEAKKAE 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 731 RAEKTSLEKNLSERKKKSAQERCQAE--AEMDEIRKSHQEELDRLRQLLKKA---RVSTDQAAAEQLTLAQAELQSQWEA 805
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADeaKKKAEEAKKKADEAKKAAEAKKKAdeaKKAEEAKKADEAKKAEEAKKADEAK 1540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 806 KCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQK--EHMQRLEKTKSQAPAGRAAADPSEKV 883
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
.
gi 568926925 884 K 884
Cdd:PTZ00121 1621 K 1621
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
518-869 |
7.53e-09 |
|
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: 60.37 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 518 RMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMETSM--IMSNIQRIIQENERLKQELLEKSSRIEEQNDKisd 595
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKqvLEKELKHLREALQQTQQSHAYLTQKREAQEEQ--- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 596 liERNQRYVEQSNLMMEKRNNsLQTATENTQARIlhaeqEKAKVTEELAAATAQVSHLQLKMtahQKKETELQLQLTDNL 675
Cdd:TIGR00618 256 --LKKQQLLKQLRARIEELRA-QEAVLEETQERI-----NRARKAAPLAAHIKAVTQIEQQA---QRIHTELQSKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 676 KEtdllRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQlelkvtslEEELTDLRAEKtSLEKNLSERKKKSAQERCQA 755
Cdd:TIGR00618 325 KL----LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA--------HEVATSIREIS-CQQHTLTQHIHTLQQQKTTL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 756 EaemdEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYRevcaQRDAHQQK 835
Cdd:TIGR00618 392 T----QKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEK----LEKIHLQE 463
|
330 340 350
....*....|....*....|....*....|....*....
gi 568926925 836 LALLQDECLALQAQIAAFTEQ-----KEHMQRLEKTKSQ 869
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQetrkkAVVLARLLELQEE 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
561-869 |
1.60e-08 |
|
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: 58.88 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 561 IMSNIQRIIQENERLKQELLEkssrIEEQNDKISD-LIERNQRYVEQSNLMMEKRNNSLQTATENT------QARILHAE 633
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISE----LKKQNNQLKDnIEKKQQEINEKTTEISNTQTQLNQLKDEQNkikkqlSEKQKELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 634 QEKAKVTE-------------ELAAATAQVSHLQLK--MTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREA 698
Cdd:TIGR04523 278 QNNKKIKElekqlnqlkseisDLNNQKEQDWNKELKseLKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 699 SEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAeaemdEIRKSHQEELDRLRQLLK 778
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI-----KKLQQEKELLEKEIERLK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 779 KARVS--------TDQAAAEQLTLAQAE-LQSQWEAKCEQLLASARDEHlQQYREVCAQRDAHQQKLALLQDECLALQAQ 849
Cdd:TIGR04523 433 ETIIKnnseikdlTNQDSVKELIIKNLDnTRESLETQLKVLSRSINKIK-QNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
330 340
....*....|....*....|....
gi 568926925 850 IAAFTEQ----KEHMQRLEKTKSQ 869
Cdd:TIGR04523 512 VKDLTKKisslKEKIEKLESEKKE 535
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
516-781 |
2.05e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 516 EIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLlpsmsvTMETSMIMSNIQRI---IQENERLKQELLEKSSRIEEQNDK 592
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKEEIEEL------EKELESLEGSKRKLeekIRELEERIEELKKEIEELEEKVKE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 593 ISDLIERNQRYVEQSNLM---------MEKRNNSLQTATENTQARILHAEQEKAKVtEELaaataqvshlqlkmtahQKK 663
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYeeyldelreIEKRLSRLEEEINGIEERIKELEEKEERL-EEL-----------------KKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 664 ETELQLQLtDNLKETDLLRGHVTRLQADLSELR-EASEQTQTKFKSEKQSrrqLELKVTSLEEELTDLRAEKTSLEKNLS 742
Cdd:PRK03918 347 LKELEKRL-EELEERHELYEEAKAKKEELERLKkRLTGLTPEKLEKELEE---LEKAKEEIEEEISKITARIGELKKEIK 422
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568926925 743 ERKK-----KSAQERC-----------------QAEAEMDEIRKSHQEELDRLRQLLKKAR 781
Cdd:PRK03918 423 ELKKaieelKKAKGKCpvcgrelteehrkelleEYTAELKRIEKELKEIEEKERKLRKELR 483
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
623-805 |
2.43e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 623 ENTQARILHAEQEKAKVTEELAAATAQVSHLQlkmtaHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREaseqt 702
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELR-----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEE----- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 703 qtkfksEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARV 782
Cdd:COG4717 154 ------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180
....*....|....*....|...
gi 568926925 783 STDQAAAEQLTLAQAELQSQWEA 805
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARL 250
|
|
| SlpA |
COG1047 |
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ... |
193-258 |
2.70e-08 |
|
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440668 [Multi-domain] Cd Length: 138 Bit Score: 53.95 E-value: 2.70e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568926925 193 VETGDSLEVAYTGWLLQnhvlGQVFDSTANkDKPLRLKLGSGKVVKGLEDGLLGMKKGGKR-LIITP 258
Cdd:COG1047 1 IEKGDVVTLHYTLKLED----GEVFDSTFE-GEPLEFLHGAGQLIPGLEEALEGMEVGDKKtVTLPP 62
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
567-800 |
2.81e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.60 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 567 RIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQsnlmMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAA 646
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDK----LQEELEQLREELEQAREELEQLEEELEQARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 647 TAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEE 726
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568926925 727 LTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQ 800
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| PRK10902 |
PRK10902 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
190-308 |
3.03e-08 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 56.31 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 190 GPAVETGDSLEVAYTGWLLQnhvlGQVFDSTANKDKPLRLKLGSgkVVKGLEDGLLGMKKGGKRLIITPSACAAGSEGVI 269
Cdd:PRK10902 158 GEAPKDSDTVVVNYKGTLID----GKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
|
90 100 110
....*....|....*....|....*....|....*....
gi 568926925 270 GWtqPTDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAA 308
Cdd:PRK10902 232 GI--PANSTLVFDVELLDVKPAPKADAKPEADAKAADSA 268
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
569-882 |
3.97e-08 |
|
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: 57.66 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 569 IQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVE----QSNLMMEKRN---NSLQTATENTQARILHAEQE--KAKV 639
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNenaNNLIKQFENTKEKIAEYTKSidIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 640 TEE----LAAATAQVSHLQLKMtahqKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQT--KFKSEKQsr 713
Cdd:COG5185 311 TESleeqLAAAEAEQELEESKR----ETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSseELDSFKD-- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 714 rQLELKVTSLEEELTDLRAEKTSLEKNLSERKkksaqercqaeaemdeirKSHQEELDRLRQLLKKArVSTDQAAAEQLT 793
Cdd:COG5185 385 -TIESTKESLDEIPQNQRGYAQEILATLEDTL------------------KAADRQIEELQRQIEQA-TSSNEEVSKLLN 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 794 LAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAaftEQKEHMQR-LEKTKSQAPA 872
Cdd:COG5185 445 ELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLE---KLRAKLERqLEGVRSKLDQ 521
|
330
....*....|
gi 568926925 873 GRAAADPSEK 882
Cdd:COG5185 522 VAESLKDFMR 531
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
573-798 |
4.65e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 573 ERLKQELLEKSSRIEEQNDKisdliernqRYVEQSNLMMEKRNNSLQTATENTQArilhaeqEKAKVTEELaaataQVSH 652
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKA-------EEARIEEVM-----KLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 653 LQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSE-------LREASEQT-----QTKFKSEKQSRRQLELKV 720
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkkaeeLKKAEEENkikaaEEAKKAEEDKKKAEEAKK 1682
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568926925 721 TSLEEELTDLRAEKTSLEKNLSER-KKKSAQERCQAEaemdEIRKSHQEELDRLRQLLKKARvsTDQAAAEQLTLAQAE 798
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEElKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAE--EDKKKAEEAKKDEEE 1755
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
493-758 |
5.48e-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: 57.42 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 493 APHFQGSGDMMSFLMT--EARQHNTEIRMAVNKVADKmdHLMTKVEELQKH------------SSGNSMLLPSMSVTMET 558
Cdd:pfam05483 431 AEELKGKEQELIFLLQarEKEIHDLEIQLTAIKTSEE--HYLKEVEDLKTElekeklknieltAHCDKLLLENKELTQEA 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 559 S---MIMSNIQRIIQENERLKQELLEKSSRIEE------------------QNDKIS---DLIERNQRYVEQSNLMMEKR 614
Cdd:pfam05483 509 SdmtLELKKHQEDIINCKKQEERMLKQIENLEEkemnlrdelesvreefiqKGDEVKcklDKSEENARSIEYEVLKKEKQ 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 615 N-------NSLQTATENTQARILHAEQE----KAKVTEE---LAAATAQVSHLQLKMTAHQKKETEL----QLQLTDN-L 675
Cdd:pfam05483 589 MkilenkcNNLKKQIENKNKNIEELHQEnkalKKKGSAEnkqLNAYEIKVNKLELELASAKQKFEEIidnyQKEIEDKkI 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 676 KETDLL----RGHVT-----RLQ-----------ADLSELREASEQTQTKFKSEKQS---------RRQLELKVtSLEEE 726
Cdd:pfam05483 669 SEEKLLeeveKAKAIadeavKLQkeidkrcqhkiAEMVALMEKHKHQYDKIIEERDSelglyknkeQEQSSAKA-ALEIE 747
|
330 340 350
....*....|....*....|....*....|...
gi 568926925 727 LTDLRAEKTSLEKNLS-ERKKKsaqERCQAEAE 758
Cdd:pfam05483 748 LSNIKAELLSLKKQLEiEKEEK---EKLKMEAK 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
633-869 |
6.21e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 633 EQEKAKVTEELAAATAQVSHLQLKmtahqkkETELQLQLtDNLKETdllRGHVTRLQADLSELR--EASEQTQTKFKSEK 710
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLI-------IDEKRQQL-ERLRRE---REKAERYQALLKEKReyEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 711 QsRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRL----RQLLKKARVSTDQ 786
Cdd:TIGR02169 238 Q-KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELeaeiASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 787 A--AAEQLTLAQAELQSQwEAKCEQLlasarDEHLQQYRevcAQRDAHQQKLALLQDECLALQAQI--------AAFTEQ 856
Cdd:TIGR02169 317 LedAEERLAKLEAEIDKL-LAEIEEL-----EREIEEER---KRRDKLTEEYAELKEELEDLRAELeevdkefaETRDEL 387
|
250
....*....|...
gi 568926925 857 KEHMQRLEKTKSQ 869
Cdd:TIGR02169 388 KDYREKLEKLKRE 400
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
559-817 |
6.43e-08 |
|
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: 56.95 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 559 SMIMSNIQRIIQENER---LKQEL-------LEKSSRIEEQNDKISDLIERNQRYVEQS-NLMMEKR--NNSLQTATENT 625
Cdd:TIGR04523 328 NQISQNNKIISQLNEQisqLKKELtnsesenSEKQRELEEKQNEIEKLKKENQSYKQEIkNLESQINdlESKIQNQEKLN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 626 Q---ARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQT 702
Cdd:TIGR04523 408 QqkdEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 703 QTKFKSE-------KQSRRQLELKV-------TSLEEELTDLRAEKTSLEKNLSERKKK-----SAQERCQAEAEMDEIr 763
Cdd:TIGR04523 488 QKELKSKekelkklNEEKKELEEKVkdltkkiSSLKEKIEKLESEKKEKESKISDLEDElnkddFELKKENLEKEIDEK- 566
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568926925 764 kshQEELDRLRQLLKKARVSTDQAA--AEQLTLAQAELQSQWEAKcEQLLASARDE 817
Cdd:TIGR04523 567 ---NKEIEELKQTQKSLKKKQEEKQelIDQKEKEKKDLIKEIEEK-EKKISSLEKE 618
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
627-779 |
9.01e-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: 54.55 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 627 ARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQT--QT 704
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568926925 705 KFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKK 779
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
658-830 |
9.35e-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: 54.55 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 658 TAHQKKETELQLQLTDNlkETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSL 737
Cdd:COG1579 1 AMPEDLRALLDLQELDS--ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 738 EKNLSE----------RKKKSAQERCQAEAE------MDEI------RKSHQEELDRLRQLLKKARVSTDQAAAEqltlA 795
Cdd:COG1579 79 EEQLGNvrnnkeyealQKEIESLKRRISDLEdeilelMERIeeleeeLAELEAELAELEAELEEKKAELDEELAE----L 154
|
170 180 190
....*....|....*....|....*....|....*
gi 568926925 796 QAELQSQwEAKCEQLLASARDEHLQQYREVCAQRD 830
Cdd:COG1579 155 EAELEEL-EAEREELAAKIPPELLALYERIRKRKN 188
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
574-870 |
9.52e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 574 RLKQELLEKSSRIEEQNDKIsdliERNQRYVEQSNLMM----EKRN--NSLQTATENTQARILHAEQEKAKVTEELAAAT 647
Cdd:PRK02224 210 GLESELAELDEEIERYEEQR----EQARETRDEADEVLeeheERREelETLEAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 648 AQVSHLQ---------------------LKMTAHQKKETELQ-------LQLTDNLKETDLLRGHVTRLQADLSELREAS 699
Cdd:PRK02224 286 ERLEELEeerddllaeaglddadaeaveARREELEDRDEELRdrleecrVAAQAHNEEAESLREDADDLEERAEELREEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 700 EQTQTKFKSEKQSRRQLELKVTSLEEELTDLRaektsleknlsERKKKSAQERCQAEAEMDEIRkshqEELDRLRQLLKK 779
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELR-----------ERFGDAPVDLGNAEDFLEELR----EERDELREREAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 780 ARVSTdQAAAEQLTLAQAELQSQWEAKCEQLLA-SARDEHLQQYREvcaQRDAHQQKLALLQDECLALQAQIAAFTEQKE 858
Cdd:PRK02224 431 LEATL-RTARERVEEAEALLEAGKCPECGQPVEgSPHVETIEEDRE---RVEELEAELEDLEEEVEEVEERLERAEDLVE 506
|
330
....*....|..
gi 568926925 859 HMQRLEKTKSQA 870
Cdd:PRK02224 507 AEDRIERLEERR 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
641-849 |
1.04e-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: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 641 EELAAATAQVSHLQLKMTAHQK-KETELQLQLTDNLKEtdllRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELK 719
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERyAAARERLAELEYLRA----ALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 720 VTSLEEELTDLRAEktsLEKNLSERKKKSAQERCQAEAEMDEIrkshQEELDRLRQLLKKARVSTDQAAAEQltlaqAEL 799
Cdd:COG4913 318 LDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEER----ERRRARLEALLAALGLPLPASAEEF-----AAL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568926925 800 QSQWEAKCEQLlASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQ 849
Cdd:COG4913 386 RAEAAALLEAL-EEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
619-872 |
1.21e-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: 55.54 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 619 QTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREA 698
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 699 SEQTQTK--------FKSEKQSRRQLELKVTSLEEELTDLRAektsLEKNLSERKKksaqercqaeaEMDEIRKShQEEL 770
Cdd:COG4942 99 LEAQKEElaellralYRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARRE-----------QAEELRAD-LAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 771 DRLRQLLKKARvstdqaaaEQLTLAQAELQSQweakcEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQI 850
Cdd:COG4942 163 AALRAELEAER--------AELEALLAELEEE-----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250 260
....*....|....*....|..
gi 568926925 851 AAFteQKEHMQRLEKTKSQAPA 872
Cdd:COG4942 230 ARL--EAEAAAAAERTPAAGFA 249
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
562-841 |
2.08e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 562 MSNIQRIIQENERLKQELLEKSSRIEEQNDKISDL---IERNQRYVEQSNLMMEKrnnsLQTATENTQARILHAEQEKAK 638
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQA----AQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 639 VTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELRE-----ASEQTQTKFKSEKQSR 713
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelqalSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 714 RQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKK-ARVSTDQAAAEQL 792
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKeIEELELAILVEKD 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568926925 793 TLAQAELQSQWEAKCE--QLLASARDEHLQQYREVCAQRDAHQQKLALLQD 841
Cdd:COG4372 273 TEEEELEIAALELEALeeAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
528-870 |
2.40e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.51 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 528 MDHLMTKVEELQKHSSGNSMLLPSMSVTMETSM--IMSNIQRiiqenerlKQELLEKSSRIEEQNDKISDLIERNQRYVE 605
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMerQMAAIQG--------KNESLEKVSSLTAQLESTKEMLRKVVEELT 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 606 QSNLMMEKRNNSLQTATENTQARILHAEQEKAKVT----------EELAAATAQVSHLQlkmtaHQKKETE-LQLQLTDN 674
Cdd:pfam15921 486 AKKMTLESSERTVSDLTASLQEKERAIEATNAEITklrsrvdlklQELQHLKNEGDHLR-----NVQTECEaLKLQMAEK 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 675 LKETDLLRGHVTRLQADLSEL-REASEQTQTKFKSEKQ-SRRQLEL------------KVTSLEEELTDLRAEKTSLEKN 740
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVGQHgRTAGAMQVEKAQLEKEiNDRRLELqefkilkdkkdaKIRELEARVSDLELEKVKLVNA 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 741 LSER---KKKSAQERCQAeaeMDEIRKSHQE--ELDRLRQLLKKarvsTDQAAAEQLTLAQAELQSQweakceqlLASAR 815
Cdd:pfam15921 641 GSERlraVKDIKQERDQL---LNEVKTSRNElnSLSEDYEVLKR----NFRNKSEEMETTTNKLKMQ--------LKSAQ 705
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 568926925 816 DEhLQQYREVCAQ---RDAHQQKLAL-LQDECLALQAQIAAFTEQkehMQRLEKTKSQA 870
Cdd:pfam15921 706 SE-LEQTRNTLKSmegSDGHAMKVAMgMQKQITAKRGQIDALQSK---IQFLEEAMTNA 760
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
662-946 |
2.52e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 662 KKETELQLQLT-DNLKE-TDLLRGhvtrLQADLSELREASEQTQtKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEK 739
Cdd:COG1196 174 KEEAERKLEATeENLERlEDILGE----LERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 740 NLSERKKKSAQ-ERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEH 818
Cdd:COG1196 249 EELEAELEELEaELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 819 LQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQkehmqRLEKTKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEF 898
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-----LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568926925 899 ELEESydggtiLRTIMHTIKMVTLQLLNHQEEEEEEEEEEEEEKKPLR 946
Cdd:COG1196 404 ELEEA------EEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
506-904 |
2.69e-07 |
|
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: 55.11 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 506 LMTEARQHNTEIRMAVNKVADKMDHLMTKVE-ELQKHSSGNSMLLPSMSvtmETSMIMSNIQRIIQENeRLKQELLEKSS 584
Cdd:pfam05483 202 LRVQAENARLEMHFKLKEDHEKIQHLEEEYKkEINDKEKQVSLLLIQIT---EKENKMKDLTFLLEES-RDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 585 RIEEQNDKisDLIERNQ---RYVEQSNLMMEKRNNSLQTATENTQArilhAEQEKAKVTEElaaATAQVSHLQLKMTAHQ 661
Cdd:pfam05483 278 KLQDENLK--ELIEKKDhltKELEDIKMSLQRSMSTQKALEEDLQI----ATKTICQLTEE---KEAQMEELNKAKAAHS 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 662 KKETELQlQLTDNLKEtdLLRGHVTRLQADLSEL--------REASE-QTQTKFKSEKQSRRQlELKVTSLEEEltDLRA 732
Cdd:pfam05483 349 FVVTEFE-ATTCSLEE--LLRTEQQRLEKNEDQLkiitmelqKKSSElEEMTKFKNNKEVELE-ELKKILAEDE--KLLD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 733 EKTSLEKnLSERKKKSAQERC---QA--------EAEMDEIRKSHQ---EELDRLRQLLKKARVSTDQ--AAAEQLTLAQ 796
Cdd:pfam05483 423 EKKQFEK-IAEELKGKEQELIfllQArekeihdlEIQLTAIKTSEEhylKEVEDLKTELEKEKLKNIEltAHCDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 797 AELQSQWEAKCEQLLASARD--EHLQQYREVCAQRDAHQQKLALLQDEclaLQAQIAAFTEQKEHMQ-RLEKTKSQAPAG 873
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDiiNCKKQEERMLKQIENLEEKEMNLRDE---LESVREEFIQKGDEVKcKLDKSEENARSI 578
|
410 420 430
....*....|....*....|....*....|.
gi 568926925 874 RAAADPSEKVKKIMNQVFQSLRGEFELEESY 904
Cdd:pfam05483 579 EYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
561-744 |
3.70e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.62 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 561 IMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERnqryVEQsnlmMEKRNNSLQTATENTQARILHAE--QEKAK 638
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE----LED----LEKEIKRLELEIEEVEARIKKYEeqLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 639 VTEELAAATAQVSHLQLKMTAHQKKETELQLQLtdnlketdllrghvTRLQADLSELREASEQTQTKFKSEKQsrrQLEL 718
Cdd:COG1579 87 NNKEYEALQKEIESLKRRISDLEDEILELMERI--------------EELEEELAELEAELAELEAELEEKKA---ELDE 149
|
170 180
....*....|....*....|....*.
gi 568926925 719 KVTSLEEELTDLRAEKTSLEKNLSER 744
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKIPPE 175
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
574-847 |
3.89e-07 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 53.66 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 574 RLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAataqvshl 653
Cdd:pfam15905 55 KVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVAS-------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 654 qlkmtahqkketeLQLQLTDNLKETDLLR------GHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEEL 727
Cdd:pfam15905 127 -------------LEKQLLELTRVNELLKakfsedGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 728 TDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQ--EELDRLRQLLKKARVSTDQAAAEQLTLAQA------EL 799
Cdd:pfam15905 194 EHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCvsEQVEKYKLDIAQLEELLKEKNDEIESLKQSleekeqEL 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568926925 800 QSQWE---AKCeQLLASARDEHLQQYREVCAQRDAH----QQKLALLQDECLALQ 847
Cdd:pfam15905 274 SKQIKdlnEKC-KLLESEKEELLREYEEKEQTLNAEleelKEKLTLEEQEHQKLQ 327
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
528-862 |
4.46e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.13 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 528 MDHLMTKVEELQKHSSGNSMLLPSMSVTMetsmimsnIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQS 607
Cdd:pfam07888 3 LDELVTLEEESHGEEGGTDMLLVVPRAEL--------LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 608 NLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQlQLTDNLKETDLLRghvtr 687
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE-EDIKTLTQRVLER----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 688 lQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQ 767
Cdd:pfam07888 149 -ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 768 EELDrLRQLLKKARVSTDQAAAEQLTLA----------------QAEL-QSQWEAKCEQLLASARDEHLQQYREVCAQ-R 829
Cdd:pfam07888 228 KEAE-NEALLEELRSLQERLNASERKVEglgeelssmaaqrdrtQAELhQARLQAAQLTLQLADASLALREGRARWAQeR 306
|
330 340 350
....*....|....*....|....*....|....*
gi 568926925 830 DAHQQKLALLQDECLALQAQIAAFTE--QKEHMQR 862
Cdd:pfam07888 307 ETLQQSAEADKDRIEKLSAELQRLEErlQEERMER 341
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
632-879 |
5.49e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.15 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 632 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETE-LQLQLTDNLKETdllrghvTRLQADLSELReASEQTQTKFKSEK 710
Cdd:PRK11281 49 NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEqLKQQLAQAPAKL-------RQAQAELEALK-DDNDEETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 711 QSRRQLELKVTSLEEELTDLRAEKTSLEKNLSerKKKSAQERCQAEaeMDEirksHQEELDRLRQLLKKARVSTDQAAAE 790
Cdd:PRK11281 121 LSLRQLESRLAQTLDQLQNAQNDLAEYNSQLV--SLQTQPERAQAA--LYA----NSQRLQQIRNLLKGGKVGGKALRPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 791 QLTLAQAELQSqWEAKCE---QLLASArdEHLQQYREvcAQRDAHQQKLALLQDECLALQAQIAA--FTEQKEHMQRLEk 865
Cdd:PRK11281 193 QRVLLQAEQAL-LNAQNDlqrKSLEGN--TQLQDLLQ--KQRDYLTARIQRLEHQLQLLQEAINSkrLTLSEKTVQEAQ- 266
|
250
....*....|....
gi 568926925 866 tkSQAPAGRAAADP 879
Cdd:PRK11281 267 --SQDEAARIQANP 278
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
661-951 |
7.41e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 661 QKKETELQLQLTDNLKETDLLRGHVTRLQadlSELREASEQTqtkfkSEKQSRRQ-LELKVTSLEEELTDL--------- 730
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELS---QELSDASRKI-----GEIEKEIEqLEQEEEKLKERLEELeedlssleq 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 731 -----RAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEqltlAQAELQSqwEA 805
Cdd:TIGR02169 752 eienvKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE----IEQKLNR--LT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 806 KCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAaftEQKEHMQRLEKTKSqapagraaaDPSEKVKK 885
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE---ELEAALRDLESRLG---------DLKKERDE 893
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568926925 886 IMNQVFQSLRGEFELEESYDggtILRTIMHTIKmVTLQLLNHQEEEEEEEEEEEEEKKPLRPSLEQ 951
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIE---KKRKRLSELK-AKLEALEEELSEIEDPKGEDEEIPEEELSLED 955
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
632-852 |
9.38e-07 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 51.53 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 632 AEQEKAKVTEELAAATAQV--SHLQL--KMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSElreaseqtQTKFK 707
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDlqQALSLldKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEA--------APKEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 708 SEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQercqAEAEMDEIRKshqeELDRLRQLLKKARVSTDQA 787
Cdd:pfam12795 75 LASLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPER----AQQQLSEARQ----RLQQIRNRLNGPAPPGEPL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568926925 788 AAEQLTLAQAELQSQW----EAKCEQLLASARDEHLQqyrevcAQRDAHQQKLALLQDECLALQAQIAA 852
Cdd:pfam12795 147 SEAQRWALQAELAALKaqidMLEQELLSNNNRQDLLK------ARRDLLTLRIQRLEQQLQALQELLNE 209
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
570-885 |
1.14e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 570 QENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRN--NSLQTATENTQARILHAEQEKAKVTEELA--A 645
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaeEAKKKAEEAKKADEAKKKAEEAKKADEAKkkA 1492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 646 ATAQVSHLQLKMTAHQKKETElQLQLTDNLKETDLLRGHVTRLQAD----------------LSELREASEQTQTKFKSE 709
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAKKADeakkaeekkkadelkkAEELKKAEEKKKAEEAKK 1571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 710 KQSRRQLELK---------------VTSLEEELTDLRAEKT-----------SLEKNLSERKKKSAQERCQAEA--EMDE 761
Cdd:PTZ00121 1572 AEEDKNMALRkaeeakkaeearieeVMKLYEEEKKMKAEEAkkaeeakikaeELKKAEEEKKKVEQLKKKEAEEkkKAEE 1651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 762 IRKSHQEELDRLRQLLKKARvsTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYREVcAQRDAHQQKLAllqD 841
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAE--EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE-EKKKAEELKKA---E 1725
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568926925 842 ECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKK 885
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
574-904 |
1.25e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.05 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 574 RLKQELLEKSsriEEQNDKISDLIERNQryVEQSNLMMEKRNNSLQTATEntqarilhAEQEKAKVTEELAAATAQVSHl 653
Cdd:TIGR00618 153 EFAQFLKAKS---KEKKELLMNLFPLDQ--YTQLALMEFAKKKSLHGKAE--------LLTLRSQLLTLCTPCMPDTYH- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 654 qlkmTAHQKKETELQlQLTDNLKETDllrghvtRLQADLSELREASEQTQTKFKSEKQSRRQLElKVTSLEEELtdlraE 733
Cdd:TIGR00618 219 ----ERKQVLEKELK-HLREALQQTQ-------QSHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRAQEAVL-----E 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 734 KTSLEKNLSERKKKSAQErcqaEAEMDEIRKSHQEELDRLRQ---LLKKARVSTDQAAAEQLTL-AQAELQSQWEAKCEQ 809
Cdd:TIGR00618 281 ETQERINRARKAAPLAAH----IKAVTQIEQQAQRIHTELQSkmrSRAKLLMKRAAHVKQQSSIeEQRRLLQTLHSQEIH 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 810 LlasaRDEHLQQyrevCAQRDAHQQKLALLQdECLALQAQIAAFTEQkehMQRLEKTKSQAPAGRAAADPSEKVKKIMNQ 889
Cdd:TIGR00618 357 I----RDAHEVA----TSIREISCQQHTLTQ-HIHTLQQQKTTLTQK---LQSLCKELDILQREQATIDTRTSAFRDLQG 424
|
330
....*....|....*
gi 568926925 890 VFQSLRGEFELEESY 904
Cdd:TIGR00618 425 QLAHAKKQQELQQRY 439
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
569-859 |
1.51e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 569 IQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEqsnlmMEKRNNSLQTATEN--TQARILHAEQEKAKVTEELAAA 646
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-----LEAELEELREELEKleKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 647 TAQVSHLQLKMTAHQKKETELQlQLTDNLKEtdlLRGHVTRLQADLS-ELREASEQTQTKFKSEKQSRRQLELKVTSLEE 725
Cdd:COG4717 145 PERLEELEERLEELRELEEELE-ELEAELAE---LQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 726 ELTDLRAEKTSLEKNL--------------------------------------------------------SERKKKSA 749
Cdd:COG4717 221 ELEELEEELEQLENELeaaaleerlkearlllliaaallallglggsllsliltiagvlflvlgllallfllLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 750 QERCQAEAEMDEIRKSHQEELDRLRQLL-------------KKARVSTDQAAAEQLTLAQAELQ-SQWEAKCEQLLASAR 815
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALglppdlspeelleLLDRIEELQELLREAEELEEELQlEELEQEIAALLAEAG 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568926925 816 DEHLQQYREVCAQRDAHQQKLALLQDeclaLQAQIAAFTEQKEH 859
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEE----LEEQLEELLGELEE 420
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
570-869 |
2.14e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 570 QENERLKQELLEKSSRIEEQNDKISDLIERnqryVEQSNLMMEKRNNSLQTATENTQarilhaeqekakvtEELAAATAQ 649
Cdd:pfam01576 422 SESERQRAELAEKLSKLQSELESVSSLLNE----AEGKNIKLSKDVSSLESQLQDTQ--------------ELLQEETRQ 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 650 VSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELR----------EASEQTQTKFKSEKQSRRQ---- 715
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKkkleedagtlEALEEGKKRLQRELEALTQqlee 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 716 -------LELKVTSLEEELTDL-------RAEKTSLEKN-------LSERKKKSAQ---ERCQAEAEMDEIR-------- 763
Cdd:pfam01576 564 kaaaydkLEKTKNRLQQELDDLlvdldhqRQLVSNLEKKqkkfdqmLAEEKAISARyaeERDRAEAEAREKEtralslar 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 764 -----KSHQEELDRLRQLLK---------------------KARVSTDQAAAE---QLTLAQAELQSQWEAKCE-----Q 809
Cdd:pfam01576 644 aleeaLEAKEELERTNKQLRaemedlvsskddvgknvheleRSKRALEQQVEEmktQLEELEDELQATEDAKLRlevnmQ 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 810 LLA-------SARDEH--------LQQYREVCAQRDAH--QQKLAL-----LQDECLALQAQI-AAFTEQKEHMQRLEKT 866
Cdd:pfam01576 724 ALKaqferdlQARDEQgeekrrqlVKQVRELEAELEDErkQRAQAVaakkkLELDLKELEAQIdAANKGREEAVKQLKKL 803
|
...
gi 568926925 867 KSQ 869
Cdd:pfam01576 804 QAQ 806
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
580-871 |
2.26e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 580 LEKSSRIEEQNDKISDLIER--------NQRYVEQ--------SNLMMEK------RNNSLQTATENTQARILHAEQEKA 637
Cdd:PRK03918 100 LDGSEVLEEGDSSVREWVERlipyhvflNAIYIRQgeidaileSDESREKvvrqilGLDDYENAYKNLGEVIKEIKRRIE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 638 KVtEELAAATAQVSHLqLKmtaHQKKETELQLQ----LTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSR 713
Cdd:PRK03918 180 RL-EKFIKRTENIEEL-IK---EKEKELEEVLReineISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 714 RQLELKVTSLEEELTDLRAEKTSLEKNLSERK--KKSAQERCQAEAEMDEIRKSHQE---ELDRLRQLLKK-----ARVS 783
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREiekRLSRLEEEINGieeriKELE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 784 TDQAAAEQLTLAQAELQSQWEA--KCEQLLASARD--EHLQQYR---------EVCAQRDAHQQKLALLQDECLALQAQI 850
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEEleERHELYEEAKAkkEELERLKkrltgltpeKLEKELEELEKAKEEIEEEISKITARI 414
|
330 340
....*....|....*....|....*
gi 568926925 851 AAF----TEQKEHMQRLEKTKSQAP 871
Cdd:PRK03918 415 GELkkeiKELKKAIEELKKAKGKCP 439
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
570-861 |
2.58e-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: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 570 QENERLKQELLEKSSRIEEQ----NDKISDLiERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAA 645
Cdd:pfam07888 69 EQWERQRRELESRVAELKEElrqsREKHEEL-EEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 646 ATAQVSHL---QLKMTAHQKKETELQLQLTDNLKETDllrGHVTRLQADLSELREASEQTQTkfksekqSRRQLELKVTS 722
Cdd:pfam07888 148 RETELERMkerAKKAGAQRKEEEAERKQLQAKLQQTE---EELRSLSKEFQELRNSLAQRDT-------QVLQLQDTITT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 723 LEEELTDlrAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEEL----DRLRQLLKKARVstdQAAAEQLTLAQAE 798
Cdd:pfam07888 218 LTQKLTT--AHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMaaqrDRTQAELHQARL---QAAQLTLQLADAS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 799 L-----QSQWEAKCEQLLASARDEH----------------LQQYR--------EVCAQRDAHQQKLALLQDECLALQAQ 849
Cdd:pfam07888 293 LalregRARWAQERETLQQSAEADKdrieklsaelqrleerLQEERmereklevELGREKDCNRVQLSESRRELQELKAS 372
|
330
....*....|..
gi 568926925 850 IAAFTEQKEHMQ 861
Cdd:pfam07888 373 LRVAQKEKEQLQ 384
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
577-870 |
2.72e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 51.76 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 577 QELLEkssRIEEQNDKIsdliernqRYVEQSNLMmeKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQV----SH 652
Cdd:PRK04778 85 EEQLF---EAEELNDKF--------RFRKAKHEI--NEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLkdlyRE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 653 LQLKMTAH-------------QKKETELQLQLTDNLKET----------DLLRGHVTRLQADLSELREASEQTQTKFKSE 709
Cdd:PRK04778 152 LRKSLLANrfsfgpaldelekQLENLEEEFSQFVELTESgdyveareilDQLEEELAALEQIMEEIPELLKELQTELPDQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 710 ----KQSRRQLE-----LKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQA-EAEMDEI----------RKSHQEE 769
Cdd:PRK04778 232 lqelKAGYRELVeegyhLDHLDIEKEIQDLKEQIDENLALLEELDLDEAEEKNEEiQERIDQLydilerevkaRKYVEKN 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 770 LDRLRQLLKKARVSTDQAAAE--------QLTLAQAELQSQWEAKCEQLLAsardehlqQYREVCAQRDAHQQKLALLQD 841
Cdd:PRK04778 312 SDTLPDFLEHAKEQNKELKEEidrvkqsyTLNESELESVRQLEKQLESLEK--------QYDEITERIAEQEIAYSELQE 383
|
330 340 350
....*....|....*....|....*....|...
gi 568926925 842 ECLALQAQIAAFTEQ----KEHMQRLEKTKSQA 870
Cdd:PRK04778 384 ELEEILKQLEEIEKEqeklSEMLQGLRKDELEA 416
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
576-775 |
2.80e-06 |
|
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: 49.92 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 576 KQELLEKSSRIEEQNDKISDLIERNQRYVEQsnlmMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQL 655
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAE----LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 656 KMTAHqKKETELQ-LQltdnlKETDLLRGHVTRLQADLSELREASEQTQTKFKsekqsrrQLELKVTSLEEELTDLRAEk 734
Cdd:COG1579 81 QLGNV-RNNKEYEaLQ-----KEIESLKRRISDLEDEILELMERIEELEEELA-------ELEAELAELEAELEEKKAE- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568926925 735 tsleknLSERKKKSAQERCQAEAEMDEIRKSHQEEL----DRLRQ 775
Cdd:COG1579 147 ------LDEELAELEAELEELEAEREELAAKIPPELlalyERIRK 185
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
686-913 |
3.14e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 686 TRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKkksaQERCQAEAEMDEIrks 765
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLE----EELEQARSELEQL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 766 hQEELDRLRQLLKKARVSTDQAAaEQLTLAQAELQSqweakceqlLASARDEHLQQYREVCAQRDAHQQKLALLQDECLA 845
Cdd:COG4372 79 -EEELEELNEQLQAAQAELAQAQ-EELESLQEEAEE---------LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568926925 846 LQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEFELEESYDGGTILRTI 913
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
566-928 |
3.22e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 566 QRIIQENERLKQELL---EKSS-RIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTAT----ENTQARILHAE---- 633
Cdd:pfam05483 112 RKIIEAQRKAIQELQfenEKVSlKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKkyeyEREETRQVYMDlnnn 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 634 -QEKAKVTEEL--AAATAQVS-HLQLKMTAH--QKKETELQLQLTDNLKETDLLRGHVTRLQADLSEL-------REASE 700
Cdd:pfam05483 192 iEKMILAFEELrvQAENARLEmHFKLKEDHEkiQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtflleesRDKAN 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 701 QTQTKFKSEKQSRRQLELKVTSLEEELTDLR-------AEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQE----- 768
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKKDHLTKELEDIKmslqrsmSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAhsfvv 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 769 -ELD----RLRQLLK--KARVSTDQaaaEQLTLAQAELQSQW-------------EAKCEQLLAS-ARDEHL----QQYR 823
Cdd:pfam05483 352 tEFEattcSLEELLRteQQRLEKNE---DQLKIITMELQKKSseleemtkfknnkEVELEELKKIlAEDEKLldekKQFE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 824 EVCAQRDAHQQKLALL----QDECLALQAQIAAFTEQKEH-MQRLEKTKSQAPagraaadpSEKVKKI---MNQVFQSLR 895
Cdd:pfam05483 429 KIAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEHyLKEVEDLKTELE--------KEKLKNIeltAHCDKLLLE 500
|
410 420 430
....*....|....*....|....*....|...
gi 568926925 896 GEFELEESYDggtilrtimhtikmVTLQLLNHQ 928
Cdd:pfam05483 501 NKELTQEASD--------------MTLELKKHQ 519
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
589-864 |
3.62e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.49 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 589 QNDKISDLIERNQRYVeQSNLMM---EKRNNSLQTAT-ENTQA---RILHAEQEK-AKVTEELAAATAQVSHLQlkmTAH 660
Cdd:COG3096 254 DRDLFKHLITEATNYV-AADYMRhanERRELSERALElRRELFgarRQLAEEQYRlVEMARELEELSARESDLE---QDY 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 661 QKKETELQLQLTdNLKetdlLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKN 740
Cdd:COG3096 330 QAASDHLNLVQT-ALR----QQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 741 LSE------------RKKKSAQERCQ--------AEAEMDEIRKSHQEELDRLRQLlkKARVSTDQAAAEQLTLAQAELQ 800
Cdd:COG3096 405 LDVqqtraiqyqqavQALEKARALCGlpdltpenAEDYLAAFRAKEQQATEEVLEL--EQKLSVADAARRQFEKAYELVC 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 801 S---------QWEAKCEQLLASARDEHL--------QQYREvcAQRDAHQQKLA--LLQDECLALQAQIAAFTEQKEHMQ 861
Cdd:COG3096 483 KiageversqAWQTARELLRRYRSQQALaqrlqqlrAQLAE--LEQRLRQQQNAerLLEEFCQRIGQQLDAAEELEELLA 560
|
...
gi 568926925 862 RLE 864
Cdd:COG3096 561 ELE 563
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
686-945 |
3.63e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 686 TRLQADLSELREASEQTQtKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLseRKKKSAQERCQAEAEMDEIrks 765
Cdd:COG4717 71 KELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLL--QLLPLYQELEALEAELAEL--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 766 hQEELDRLRQllKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDE---HLQQYREVCAQRDAHQQKLALLQDE 842
Cdd:COG4717 145 -PERLEELEE--RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 843 CLALQAQIAAFTEQKEHMQRLE---------------------------------------------------KTKSQAP 871
Cdd:COG4717 222 LEELEEELEQLENELEAAALEErlkearlllliaaallallglggsllsliltiagvlflvlgllallflllaREKASLG 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568926925 872 AGRAAADPSEKVKKIMNQVFQSLRGEFELEESYDGGTILRTIMHTIKMVTLQLLNHQEEEEEEEEEEEEEKKPL 945
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
552-824 |
3.80e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 552 MSVTMETSM---IMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQAR 628
Cdd:COG1340 1 SKTDELSSSleeLEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 629 ILHAEQEKaKVTEELAAATAQVSHLQLKMTAHQKKETEL-QL---QLTDNL---KETDLLRgHVTRLQADLSELREASEQ 701
Cdd:COG1340 81 DELNEKLN-ELREELDELRKELAELNKAGGSIDKLRKEIeRLewrQQTEVLspeEEKELVE-KIKELEKELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 702 ------TQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKS---AQERCQAEAEMDEIRKSH---QEE 769
Cdd:COG1340 159 neklkeLRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEAdelHKEIVEAQEKADELHEEIielQKE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568926925 770 LDRLRQLLKKARvstDQAAAEQLTLAQAELQSQWEAKCEQLLASAR---DEHLQQYRE 824
Cdd:COG1340 239 LRELRKELKKLR---KKQRALKREKEKEELEEKAEEIFEKLKKGEKlttEELKLLQKS 293
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
495-863 |
4.06e-06 |
|
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: 51.27 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 495 HFQGSGDMMSFLMteaRQHNTEIRMAVNKVADKMDHLmtkvEELQKHSSGNSMLLPSMSvtmetsmiMSNIQRIIQENER 574
Cdd:pfam15921 214 HFRSLGSAISKIL---RELDTEISYLKGRIFPVEDQL----EALKSESQNKIELLLQQH--------QDRIEQLISEHEV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 575 LKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENtqariLHAEQEKAKVTEElaaatAQVSHLQ 654
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQ-----LRSELREAKRMYE-----DKIEELE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 655 LKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADL----SELREASEQTQTKFKSEKQS-------RRQLE---LKV 720
Cdd:pfam15921 349 KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLhkreKELSLEKEQNKRLWDRDTGNsitidhlRRELDdrnMEV 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 721 TSLEEELTDLRAE-KTSLEKNLS--ERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQllKKARVSTDQAAAEQLTLAQA 797
Cdd:pfam15921 429 QRLEALLKAMKSEcQGQMERQMAaiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTA--KKMTLESSERTVSDLTASLQ 506
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568926925 798 ELQSQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQQklalLQDECLALQAQIAA-------FTEQKEHMQRL 863
Cdd:pfam15921 507 EKERAIEATNAEItkLRSRVDLKLQELQHLKNEGDHLRN----VQTECEALKLQMAEkdkvieiLRQQIENMTQL 577
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
565-865 |
4.29e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.12 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 565 IQRIIQENERLKQ---ELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTE 641
Cdd:TIGR00618 565 MQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 642 ELAAATAQVSHLQLKMTAHQKKETELQLQLTD-NLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKV 720
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSIRVLPKELLAsRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 721 TSLEEELTDLRAEKTSLEKNLSERKKKsAQERCQAEAEMDEiRKSHQE-----ELDRLRQLLKKARVSTDQAAAEQLTLA 795
Cdd:TIGR00618 725 NASSSLGSDLAAREDALNQSLKELMHQ-ARTVLKARTEAHF-NNNEEVtaalqTGAELSHLAAEIQFFNRLREEDTHLLK 802
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568926925 796 QAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDA------HQQKLALLQD-ECLALQAQiaAFTEQKEHMQRLEK 865
Cdd:TIGR00618 803 TLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEeksatlGEITHQLLKYeECSKQLAQ--LTQEQAKIIQLSDK 877
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
569-868 |
4.53e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 569 IQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQsnlmmEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATA 648
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-----EDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 649 QVSHLQLKMTAHQKKETELQLqltdnlkETDLLRGHVTRLQADLSELreaseqtqtkfkseKQSRRQLElKVTSLEEELT 728
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEE-------EAEEAREEVAELNSKLAEL--------------KERIESLE-RIRTLLAAIA 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 729 DLRAEKTSLeknlserkkksaQERCQAEAEMDEIRKSHQEEL-DRLRQL---LKKARVSTDQAAAEQLTLAQAELqsqwe 804
Cdd:PRK02224 603 DAEDEIERL------------REKREALAELNDERRERLAEKrERKRELeaeFDEARIEEAREDKERAEEYLEQV----- 665
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568926925 805 akceqllasarDEHLQQYREvcaQRDAhqqklalLQDECLALQAQIAAFTEQKEHMQRLEKTKS 868
Cdd:PRK02224 666 -----------EEKLDELRE---ERDD-------LQAEIGAVENELEELEELRERREALENRVE 708
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
565-803 |
4.86e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 565 IQRIIQENERLKQELLEKSS-----RIEEQNDKISDLIERNQRYVEQSNLMmekrnnSLQTATENTQARILHAEQEKAKV 639
Cdd:COG3206 158 AEAYLEQNLELRREEARKALefleeQLPELRKELEEAEAALEEFRQKNGLV------DLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 640 TEELAAATAQVSHLQlkmtahqkKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASE----------QTQTKFKS- 708
Cdd:COG3206 232 RAELAEAEARLAALR--------AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpdviALRAQIAAl 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 709 EKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERcQAEAEMDEIrkshQEELDRLRQLLKKArvstdQAA 788
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP-ELEAELRRL----EREVEVARELYESL-----LQR 373
|
250
....*....|....*
gi 568926925 789 AEQLTLAQAELQSQW 803
Cdd:COG3206 374 LEEARLAEALTVGNV 388
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
521-734 |
5.02e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.23 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 521 VNKVADKMDHLMTKVEELQKHSSGNSML---LPSMSVTMETSM---IMSNIQRIIQ-ENERLKQELLEKSSRIEEQNDKI 593
Cdd:COG5022 894 ISSLKLVNLELESEIIELKKSLSSDLIEnleFKTELIARLKKLlnnIDLEEGPSIEyVKLPELNKLHEVESKLKETSEEY 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 594 SDLIERNQRYVEQSNLMMEKRNNSLQTATE-NTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLT 672
Cdd:COG5022 974 EDLLKKSTILVREGNKANSELKNFKKELAElSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKG 1053
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568926925 673 DNLKEtdllrghVTRLQADLSELREASEQTQTKFKSEKQSRRQ--LELKVTSLEEELTDLRAEK 734
Cdd:COG5022 1054 LLLLE-------NNQLQARYKALKLRRENSLLDDKQLYQLESTenLLKTINVKDLEVTNRNLVK 1110
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
648-857 |
7.70e-06 |
|
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: 50.24 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 648 AQVSHLQLKMTAHQKKETELQLQLtdnlketDLLRGHVTRLQADLSELREASEQTQTKFKS-------EKQSRRQLELKv 720
Cdd:pfam09726 402 QDIKKLKAELQASRQTEQELRSQI-------SSLTSLERSLKSELGQLRQENDLLQTKLHNavsakqkDKQTVQQLEKR- 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 721 tsLEEEltdlRAEKTSLEKNLSERKK-------KSAQERCQAEA---EMDEIRKSHQEELD-RLRQLLKKARVSTDQAAa 789
Cdd:pfam09726 474 --LKAE----QEARASAEKQLAEEKKrkkeeeaTAARAVALAAAsrgECTESLKQRKRELEsEIKKLTHDIKLKEEQIR- 546
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568926925 790 eqltlaqaelqsQWEAKCEQllasardehLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQK 857
Cdd:pfam09726 547 ------------ELEIKVQE---------LRKYKESEKDTEVLMSALSAMQDKNQHLENSLSAETRIK 593
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
641-881 |
9.55e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 9.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 641 EELAAATAQVSHLQLKMTAHQKKETELQLQLtDNLKET-DLLRGHVTR--------LQADLSELREASEQTQTKFKSEKQ 711
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQL-EQAKEGlSALNRLLPRlnlladetLADRVEEIREQLDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 712 SRRQLELkvtsLEEELTDLRAEktsleknlserkkksaqercqaEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAA--- 788
Cdd:PRK04863 916 HGNALAQ----LEPIVSVLQSD----------------------PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrra 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 789 ------AEQLTLAQAELQSQWEAKCEQlLASARDEHLQQYREVCAQrdaHQQKLALLQDeclaLQAQIAAFTEQ-KEHMQ 861
Cdd:PRK04863 970 hfsyedAAEMLAKNSDLNEKLRQRLEQ-AEQERTRAREQLRQAQAQ---LAQYNQVLAS----LKSSYDAKRQMlQELKQ 1041
|
250 260
....*....|....*....|...
gi 568926925 862 RLEKTKSQAPAG---RAAADPSE 881
Cdd:PRK04863 1042 ELQDLGVPADSGaeeRARARRDE 1064
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
564-800 |
1.31e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 564 NIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERN-----QRYVEQSNLMMEKRNNSLQTATENTQarilhaeqekak 638
Cdd:PRK11281 74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNdeetrETLSTLSLRQLESRLAQTLDQLQNAQ------------ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 639 vtEELAAATAQVSHLQLK-------MTAHQKKETELQLQLTDNLKETDLLRG-HVTRLQADLS------ELREASEQTQT 704
Cdd:PRK11281 142 --NDLAEYNSQLVSLQTQperaqaaLYANSQRLQQIRNLLKGGKVGGKALRPsQRVLLQAEQAllnaqnDLQRKSLEGNT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 705 KFKSEKQSRRQL-ELKVTSLEEELTDLRAEKTslEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVS 783
Cdd:PRK11281 220 QLQDLLQKQRDYlTARIQRLEHQLQLLQEAIN--SKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKA 297
|
250
....*....|....*..
gi 568926925 784 TDQAAaeqlTLAQAELQ 800
Cdd:PRK11281 298 TEKLN----TLTQQNLR 310
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
573-752 |
1.51e-05 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 49.06 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 573 ERLKQELLEKSSR-------IEEQNDKISDLIErnqryvEQSNLMMEKR--NNSLQTATE---NTQARILHAEQEKAKVT 640
Cdd:pfam15066 345 EKKVKELQMKITKqqvfvdiINKLKENVEELIE------DKYNVILEKNdiNKTLQNLQEilaNTQKHLQESRKEKETLQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 641 EELAAATAQVSHLQLK-MTAHQKKETE----LQLQLTDNLKEtdllrGHVTRLQADLSELREASEQTQTKFKSEKQSRRQ 715
Cdd:pfam15066 419 LELKKIKVNYVHLQERyITEMQQKNKSvsqcLEMDKTLSKKE-----EEVERLQQLKGELEKATTSALDLLKREKETREQ 493
|
170 180 190
....*....|....*....|....*....|....*...
gi 568926925 716 LELkvtSLEEELTdlRAEKtsleKNLSERKK-KSAQER 752
Cdd:pfam15066 494 EFL---SLQEEFQ--KHEK----ENLEERQKlKSRLEK 522
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
641-824 |
1.56e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 641 EELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTrlqaDLSELREASEQTQtKFKSEKQSRRQLELKV 720
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE----DEEELRAALEQAE-EYQELKEELEELEEQL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 721 TSLEEELTDLRAEKTslEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQ 800
Cdd:COG4717 412 EELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
170 180
....*....|....*....|....
gi 568926925 801 SQWEAKceQLLASARDEHLQQYRE 824
Cdd:COG4717 490 EEWAAL--KLALELLEEAREEYRE 511
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
571-871 |
1.72e-05 |
|
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: 49.26 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 571 ENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLmmekrnnslqtATENTQARILHAEQEKAKVTEEL-AAATAQ 649
Cdd:pfam05667 223 EEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAAL-----------AGTEATSGASRSAQDLAELLSSFsGSSTTD 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 650 VSHLQLKMTAHQKKET---ELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEE 726
Cdd:pfam05667 292 TGLTKGSRFTHTEKLQftnEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 727 LTDLRAEKTSLEKNLsERKKKSAQERCQAEAEMDEirkshqeeldrLRQLLkkarvstdQAAAEQLtlaqAELQSQWEAK 806
Cdd:pfam05667 372 LEELKEQNEELEKQY-KVKKKTLDLLPDAEENIAK-----------LQALV--------DASAQRL----VELAGQWEKH 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 807 CEQLLasardEHLQQYREVCA-QRDAHQQKLA---LLQDECLalqaQIAAFTEQKEHMQR-LEKTKSQAP 871
Cdd:pfam05667 428 RVPLI-----EEYRALKEAKSnKEDESQRKLEeikELREKIK----EVAEEAKQKEELYKqLVAEYERLP 488
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
641-904 |
1.87e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.18 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 641 EELAAATAQVSHLQLKMTAHQKKETELQLQLtDNLKET-DLLR---GHVTRL-QADLSELREASEQTQTKFKSEKQSRRQ 715
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQL-DQLKEQlQLLNkllPQANLLaDETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 716 LELKVTSLEEELTDLRAEKTS---LEKNLSERKKKSAQERCQAEAeMDEI--RKSH-------------QEELDRLRQLL 777
Cdd:COG3096 915 HGKALAQLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFA-LSEVvqRRPHfsyedavgllgenSDLNEKLRARL 993
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 778 KKArvstdQAAAEQLTLAQAELQSQWeAKCEQLLASARdehlqqyrevcAQRDAHQQKLALLQDECLALQAQIAAFTEQK 857
Cdd:COG3096 994 EQA-----EEARREAREQLRQAQAQY-SQYNQVLASLK-----------SSRDAKQQTLQELEQELEELGVQADAEAEER 1056
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 568926925 858 --EHMQRLEktkSQAPAGRAAADPSEKVKKIMNQVFQSLRGEF-ELEESY 904
Cdd:COG3096 1057 arIRRDELH---EELSQNRSRRSQLEKQLTRCEAEMDSLQKRLrKAERDY 1103
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
573-848 |
1.88e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.18 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 573 ERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMmEKRNNSL-------QTATENTQARILHAEQ-----EKAK-- 638
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAA-EEEVDSLksqladyQQALDVQQTRAIQYQQavqalEKARal 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 639 ----------VTEELAA-------ATAQVSHLQLKMT----AHQKKETELQL------------------QLTDNLKETD 679
Cdd:COG3096 429 cglpdltpenAEDYLAAfrakeqqATEEVLELEQKLSvadaARRQFEKAYELvckiageversqawqtarELLRRYRSQQ 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 680 LLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSlEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEM 759
Cdd:COG3096 509 ALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 760 DEIRKshqeeldRLRQLLKKARV-STDQAAAEQLtlaqaELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLAL 838
Cdd:COG3096 588 EQLRA-------RIKELAARAPAwLAAQDALERL-----REQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQA 655
|
330
....*....|
gi 568926925 839 LQDECLALQA 848
Cdd:COG3096 656 LESQIERLSQ 665
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
569-867 |
2.13e-05 |
|
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: 49.20 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 569 IQENERLKqELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTatentqarilhaeqekakvtEELAAATA 648
Cdd:pfam02463 169 RKKKEALK-KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL--------------------ELEEEYLL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 649 QVSHLQLkmtaHQKKETELQLQLTDNLKETDLLRGhvtrlqadLSELREASEQTQTKFKSEkqsrrqlELKVTSLEEE-- 726
Cdd:pfam02463 228 YLDYLKL----NEERIDLLQELLRDEQEEIESSKQ--------EIEKEEEKLAQVLKENKE-------EEKEKKLQEEel 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 727 -LTDLRAEKTSLEKNLSERKKKSAQErcQAEAEMDEIRKsHQEELDRLRQLLKKARVS-TDQAAAEQLTLAQAELQSQWE 804
Cdd:pfam02463 289 kLLAKEEEELKSELLKLERRKVDDEE--KLKESEKEKKK-AEKELKKEKEEIEELEKElKELEIKREAEEEEEEELEKLQ 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568926925 805 AKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFtEQKEHMQRLEKTK 867
Cdd:pfam02463 366 EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA-RQLEDLLKEEKKE 427
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
643-880 |
2.89e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 643 LAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTkfksekqsrrqlelKVTS 722
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA--------------EIDK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 723 LEEELTDLRAEKTSLEKNLSERkKKSAQERCQAEAEMDEI--RKSHQEELDRLrQLLKKArVSTDQAAAEQLTLAQAELQ 800
Cdd:COG3883 70 LQAEIAEAEAEIEERREELGER-ARALYRSGGSVSYLDVLlgSESFSDFLDRL-SALSKI-ADADADLLEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 801 SQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAAD 878
Cdd:COG3883 147 AKKAELEAKLaeLEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
..
gi 568926925 879 PS 880
Cdd:COG3883 227 AA 228
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
561-820 |
2.92e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 561 IMSNIQRIIQENERLKQELLEKSSRIEEQNDKI---SDLIERNQRYVEQSNLMMEKRNNSLqtaTENTQARILHAEQEKA 637
Cdd:COG3096 925 LVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfalSEVVQRRPHFSYEDAVGLLGENSDL---NEKLRARLEQAEEARR 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 638 KVTEELAAATAQV-----------SHLQLKMTAHQKKETELQ---LQLTDNLKETdlLRGHVTRLQADLSELReaseqtq 703
Cdd:COG3096 1002 EAREQLRQAQAQYsqynqvlaslkSSRDAKQQTLQELEQELEelgVQADAEAEER--ARIRRDELHEELSQNR------- 1072
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 704 tkfksekqSRRqlelkvTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEaemdeirkSHQEELDRLRQLLKKARVS 783
Cdd:COG3096 1073 --------SRR------SQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVV--------QAKAGWCAVLRLARDNDVE 1130
|
250 260 270
....*....|....*....|....*....|....*...
gi 568926925 784 TDQAAAEQLTLAQAELQSQWEAKCEQL-LASARDEHLQ 820
Cdd:COG3096 1131 RRLHRRELAYLSADELRSMSDKALGALrLAVADNEHLR 1168
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
576-896 |
3.15e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 576 KQELLEKSSRIEEQNDKISDLIERnQRYVEQSNLMMEKRNNSLQTATENtQARILHAEQEKAKVTEELAAATAQVSHLQL 655
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTALRQ-QEKIERYQEDLEELTERLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 656 kmtahQKKETELQLQLTDnlKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQL---ELKVTSLEEELTDLRA 732
Cdd:COG3096 376 -----QLAEAEARLEAAE--EEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCglpDLTPENAEDYLAAFRA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 733 EKTSLEKNLSERKKK---SAQERCQAEAEMDEIRK-----SHQEELDRLRQLLKKARvsTDQAAAEQLT-----LAQAE- 798
Cdd:COG3096 449 KEQQATEEVLELEQKlsvADAARRQFEKAYELVCKiagevERSQAWQTARELLRRYR--SQQALAQRLQqlraqLAELEq 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 799 -LQSQWEAK-------------------CEQLLASA---RDEHLQQYREVCAQRDAHQQKLAllqdeclALQAQIAAFTe 855
Cdd:COG3096 527 rLRQQQNAErlleefcqrigqqldaaeeLEELLAELeaqLEELEEQAAEAVEQRSELRQQLE-------QLRARIKELA- 598
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568926925 856 qkehmqrlektkSQAPAGRAAADPSEKVKKIMNQVFQSLRG 896
Cdd:COG3096 599 ------------ARAPAWLAAQDALERLREQSGEALADSQE 627
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
630-821 |
3.66e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 48.21 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 630 LHAEQEKAKVTE--ELAAATAQVSHLQLKmtahqKKETELQLQLT-DNLKETDLLRGHVTRLQADLSELreaSEQTQTKF 706
Cdd:pfam09731 236 EKAQSLAKLVDQykELVASERIVFQQELV-----SIFPDIIPVLKeDNLLSNDDLNSLIAHAHREIDQL---SKKLAELK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 707 KSEKQsrrQLELKVTSLEEELTDLRAEktsLEKNLSE-RKKKSAQERCQAEAEMDEIRKSHQEEldrLRQLLKKARVSTD 785
Cdd:pfam09731 308 KREEK---HIERALEKQKEELDKLAEE---LSARLEEvRAADEAQLRLEFEREREEIRESYEEK---LRTELERQAEAHE 378
|
170 180 190
....*....|....*....|....*....|....*.
gi 568926925 786 QAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQ 821
Cdd:pfam09731 379 EHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLK 414
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
509-747 |
4.03e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 509 EARQHNTEIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMetsmiMSNIQRIIQENERLKQELLEKSSRIEE 588
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDEL-----VEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 589 QNDKISDLierNQRYVEQSNLM--------MEKRNNSLQTATENtqariLHAEQEK-AKVTEELAAATAQVShlqlKMTA 659
Cdd:PHA02562 253 PSAALNKL---NTAAAKIKSKIeqfqkvikMYEKGGVCPTCTQQ-----ISEGPDRiTKIKDKLKELQHSLE----KLDT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 660 HQKKETELQLQLTDNLKEtdllrghVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEK 739
Cdd:PHA02562 321 AIDELEEIMDEFNEQSKK-------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
....*...
gi 568926925 740 NLSERKKK 747
Cdd:PHA02562 394 TKSELVKE 401
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
656-801 |
4.12e-05 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 46.05 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 656 KMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQtqtkFKSEKQSRRQLELKVTSLEEELTDLRAEKt 735
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN----YEKDKQSLKNLKARLKVLEKELKDLKWEH- 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568926925 736 sleKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKaRVstdQAAAEQLTLAQAELQS 801
Cdd:pfam13851 109 ---EVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEK-KL---QALGETLEKKEAQLNE 167
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
561-817 |
4.18e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 561 IMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIER-NQRYVEQSNLMMEKR-------NNSLQTATENTQARILHA 632
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDElNGELSAADAAVAKDRselealeDQHGAFLDADIETAAADQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 633 EQ------EKAKVTEELAAATAQVSHLQLKMTA-HQKKETELQLQLTDNLKETDLLRGHVTR--------LQADLSELRE 697
Cdd:pfam12128 347 EQlpswqsELENLEERLKALTGKHQDVTAKYNRrRSKIKEQNNRDIAGIKDKLAKIREARDRqlavaeddLQALESELRE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 698 ASEQTQTKFKSEKQ--SRRQLELK-----VTSLEEELTDLRAEKTSLEknlserKKKSAQERCQAEAEmdeirkSHQEEL 770
Cdd:pfam12128 427 QLEAGKLEFNEEEYrlKSRLGELKlrlnqATATPELLLQLENFDERIE------RAREEQEAANAEVE------RLQSEL 494
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568926925 771 DRLRQLLKKARVSTDQA--AAEQLTLAQAELQSQWEAKCEQLLASARDE 817
Cdd:pfam12128 495 RQARKRRDQASEALRQAsrRLEERQSALDELELQLFPQAGTLLHFLRKE 543
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
632-903 |
4.42e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 47.72 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 632 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQlqltdnlKETDLLRGHVTRLQADLSElrEASEQTQTKFKSEKQ 711
Cdd:pfam05701 61 AEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAK-------QDSELAKLRVEEMEQGIAD--EASVAAKAQLEVAKA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 712 SRRQLELKVTSLEEELTDLRAEKTSLeknLSERkKKSAQERCQAEAEMDEIRKSHQE---ELDRLRQLLKKARVSTDQAA 788
Cdd:pfam05701 132 RHAAAVAELKSVKEELESLRKEYASL---VSER-DIAIKRAEEAVSASKEIEKTVEEltiELIATKESLESAHAAHLEAE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 789 AEQLTLAQAELQ--SQWEAKCEQLlasarDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQK-----EHMQ 861
Cdd:pfam05701 208 EHRIGAALAREQdkLNWEKELKQA-----EEELQRLNQQLLSAKDLKSKLETASALLLDLKAELAAYMESKlkeeaDGEG 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568926925 862 RLEKTKSQAPAGRAAADPS-EKVK----------KIMNQVFQSLRGEFELEES 903
Cdd:pfam05701 283 NEKKTSTSIQAALASAKKElEEVKaniekakdevNCLRVAAASLRSELEKEKA 335
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
509-902 |
4.64e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 509 EARQHNTEIRM-AVNKV--ADKMDHLMTKVEELQKHSSGNSMLLPSMSVtmetsmiMSNIQRIIQENERLKQELLEKSsr 585
Cdd:PTZ00121 1216 EARKAEDAKKAeAVKKAeeAKKDAEEAKKAEEERNNEEIRKFEEARMAH-------FARRQAAIKAEEARKADELKKA-- 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 586 ieEQNDKISDLIERNQ-RYVEQSNLMME--KRNNSLQTATENTQ--ARILHAEQEKAKVTEELAAATAQVSHLQLKMTAH 660
Cdd:PTZ00121 1287 --EEKKKADEAKKAEEkKKADEAKKKAEeaKKADEAKKKAEEAKkkADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 661 QKKETELQlqltdnlKETDLLRGHVTRLQADlsELREASEqtqTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKN 740
Cdd:PTZ00121 1365 KAEAAEKK-------KEEAKKKADAAKKKAE--EKKKADE---AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK 1432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 741 LSERKKKSAQERCQAEA--EMDEIRKSHQ-----EELDRLRQLLKKA----RVSTDQAAAEQLTLAQAELQSQWEA--KC 807
Cdd:PTZ00121 1433 ADEAKKKAEEAKKADEAkkKAEEAKKAEEakkkaEEAKKADEAKKKAeeakKADEAKKKAEEAKKKADEAKKAAEAkkKA 1512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 808 EQLLASARDEHLQQYREVCAQRDAHQQKLAllQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKKIM 887
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
410
....*....|....*
gi 568926925 888 NQVFQSLRGEFELEE 902
Cdd:PTZ00121 1591 EARIEEVMKLYEEEK 1605
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
595-773 |
5.22e-05 |
|
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: 45.31 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 595 DLIERNQRYVEQSNLMmEKRNNSLQTATEN-TQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTD 673
Cdd:pfam08614 4 ELIDAYNRLLDRTALL-EAENAKLQSEPESvLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 674 nlketdllrghvtrLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEEL-------TDLRAEKTSLEKNLSerkk 746
Cdd:pfam08614 83 --------------LNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELrekrklnQDLQDELVALQLQLN---- 144
|
170 180
....*....|....*....|....*..
gi 568926925 747 ksaqercQAEAEMDEIRKSHQEELDRL 773
Cdd:pfam08614 145 -------MAEEKLRKLEKENRELVERW 164
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
573-856 |
5.40e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 573 ERLKQELLEKSSRIEEQN---DKISDLIERNQRYVEQSNLMMEKRNNSL---QTATENTQARIL---HAEQ--EKAKVTE 641
Cdd:PRK04863 351 ERYQADLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVQQTRAIqyqQAVQalERAKQLC 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 642 ELAAATA-QVSHLQLKMTAHQKKETELQLQLTDNLKETD-----------LLR---GHVTR------------------- 687
Cdd:PRK04863 431 GLPDLTAdNAEDWLEEFQAKEQEATEELLSLEQKLSVAQaahsqfeqayqLVRkiaGEVSRseawdvarellrrlreqrh 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 688 -------LQADLSELREASEQTQTKFKSEKQSRRQLELKVTSlEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAemd 760
Cdd:PRK04863 511 laeqlqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEARERRMALRQ--- 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 761 eirksHQEELD-RLRQLLKKARV-STDQAAAEQLtlaqaELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLAL 838
Cdd:PRK04863 587 -----QLEQLQaRIQRLAARAPAwLAAQDALARL-----REQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
330
....*....|....*...
gi 568926925 839 LQDECLALQAQIAAFTEQ 856
Cdd:PRK04863 657 LDEEIERLSQPGGSEDPR 674
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
565-869 |
5.73e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.84 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 565 IQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRyvEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELA 644
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQ--AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 645 AATAQVSHLQLKMTAHQKKETELQLQltdnlKEtdllrghvtRLQADLSELREASEQTQtkfksekqsrrqlelkvtsle 724
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEE-----KE---------REIARLRAQQEKAQDEK--------------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 725 EELTDLRAEKTsLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELdRLRQLLKKARVSTDQAAAEQLTLAQAELQSQwe 804
Cdd:pfam13868 201 AERDELRAKLY-QEEQERKERQKEREEAEKKARQRQELQQAREEQI-ELKERRLAEEAEREEEEFERMLRKQAEDEEI-- 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568926925 805 akcEQLLASARDEHLQQYR-EVCAQ-RDAHQQKLALLQDEclaLQAQIAAFTEQKEHMQRLEKTKSQ 869
Cdd:pfam13868 277 ---EQEEAEKRRMKRLEHRrELEKQiEEREEQRAAEREEE---LEEGERLREEEAERRERIEEERQK 337
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
571-821 |
6.16e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.51 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 571 ENERLKQELLEKSSRIEEQNDkisDLIERNQRYVEQSNLMMEKRNNSLQTATENTqARILHAEQEKAkVTEELAAATAQV 650
Cdd:NF041483 503 ESERVRTEAIERATTLRRQAE---ETLERTRAEAERLRAEAEEQAEEVRAAAERA-ARELREETERA-IAARQAEAAEEL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 651 SHLQlkmTAHQKKETELQLQLTDNLKETDLLRghvtrlqadlselREASEQTQtKFKSEKQSR-RQLElkvTSLEEELTD 729
Cdd:NF041483 578 TRLH---TEAEERLTAAEEALADARAEAERIR-------------REAAEETE-RLRTEAAERiRTLQ---AQAEQEAER 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 730 LRAEKTS-LEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQwEAKCE 808
Cdd:NF041483 638 LRTEAAAdASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQEEAARR-RREAE 716
|
250
....*....|...
gi 568926925 809 QLLASARDEHLQQ 821
Cdd:NF041483 717 ETLGSARAEADQE 729
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
584-802 |
9.09e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 584 SRIEEQNDKISDLIERNQRYVEQSNLMMEKRNnSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQ--LKMTAHQ 661
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELE-ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReeLGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 662 KKETELQLQLTDNLKE----TDLLR---------GHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELT 728
Cdd:COG3883 95 LYRSGGSVSYLDVLLGsesfSDFLDrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568926925 729 DLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQ 802
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
944-1129 |
1.16e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 944 PLRPSLEQPGPATPGMPPAPPSGETQEAPEvlpeqvvgettPLPLQALPTPENGAQTrkgePAEAEVPSEIKDSSLPPQP 1023
Cdd:PHA03247 2923 PPPPPQPQPPPPPPPRPQPPLAPTTDPAGA-----------GEPSGAVPQPWLGALV----PGRVAVPRFRVPQPAPSRE 2987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 1024 AGIPA-HRVLGPPTSIPPKPPGPVTMDSESEEMLAADQRTVQPNgllgeEHVREVATDGLLQGNSRRLSL-TPDPEKGEP 1101
Cdd:PHA03247 2988 APASStPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTLWPP-----DDTEDSDADSLFDSDSERSDLeALDPLPPEP 3062
|
170 180
....*....|....*....|....*....
gi 568926925 1102 PalDPESQGGEAQPPECKQAEDVSSS-GP 1129
Cdd:PHA03247 3063 H--DPFAHEPDPATPEAGARESPSSQfGP 3089
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
632-743 |
1.16e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 43.01 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 632 AEQEKAKVTEELAAATAQVSHLQLKM--------TAHQKKETELQLQlTDNLKETDLLRGHVTRLQADLSELREASEQTQ 703
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLekqaeiarEAQQNYERELVLH-AEDIKALQALREELNELKAEIAELKAEAESAK 84
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568926925 704 TKFKSEKQSrrqlelkvtsLEEELTDLRAEKTSLEKNLSE 743
Cdd:pfam07926 85 AELEESEES----------WEEQKKELEKELSELEKRIED 114
|
|
| Tig |
COG0544 |
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ... |
185-250 |
1.19e-04 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440310 [Multi-domain] Cd Length: 424 Bit Score: 45.89 E-value: 1.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568926925 185 LVAAEGPAvETGDSLEVAYTGWllqnhVLGQVFDSTANKDKPLrlKLGSGKVVKGLEDGLLGMKKG 250
Cdd:COG0544 151 LVPVERAA-EEGDRVTIDFEGT-----IDGEEFEGGKAEDYSL--ELGSGSFIPGFEEQLVGMKAG 208
|
|
| tig |
TIGR00115 |
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ... |
185-255 |
1.22e-04 |
|
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]
Pssm-ID: 272913 [Multi-domain] Cd Length: 410 Bit Score: 46.01 E-value: 1.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568926925 185 LVAAEGPAVETGDSLEVAYTGwllqnHVLGQVFDSTANKDkpLRLKLGSGKVVKGLEDGLLGMKKGGKRLI 255
Cdd:TIGR00115 141 LVPVERGAAEKGDRVTIDFEG-----FIDGEAFEGGKAEN--FSLELGSGQFIPGFEEQLVGMKAGEEKEI 204
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
577-778 |
1.26e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.58 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 577 QELLEKSSRIEEQNDKISDLIERNQRYVEQ-----------------SNLMMEKRNNSLQTATENTQAR---ILHAEQEK 636
Cdd:TIGR01612 1489 KEHIDKSKGCKDEADKNAKAIEKNKELFEQykkdvtellnkysalaiKNKFAKTKKDSEIIIKEIKDAHkkfILEAEKSE 1568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 637 AKVTE--------ELAAATAQVSH-----LQLKMTAHQKKE---TELQLQLTDNLKETDLLRGHVTRLQAD-----LSEL 695
Cdd:TIGR01612 1569 QKIKEikkekfriEDDAAKNDKSNkaaidIQLSLENFENKFlkiSDIKKKINDCLKETESIEKKISSFSIDsqdteLKEN 1648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 696 REASEQTQTKFKSEKQSRRQLELKVTsleeELTDLRAEKTSLEKNLSERKKKsaQERCQAEaEMDEIRKSHQEELDRLRQ 775
Cdd:TIGR01612 1649 GDNLNSLQEFLESLKDQKKNIEDKKK----ELDELDSEIEKIEIDVDQHKKN--YEIGIIE-KIKEIAIANKEEIESIKE 1721
|
...
gi 568926925 776 LLK 778
Cdd:TIGR01612 1722 LIE 1724
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
570-772 |
1.33e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 570 QENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQsnlmmekrnnsLQTATENTQARilhAEQEKAKVTEELAAATaq 649
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE-----------LKKAEEENKIK---AAEEAKKAEEDKKKAE-- 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 650 vshlQLKMTAHQKKETELQLQL-TDNLKETDLLRGHVTRLQADLSELREASEQT-----QTKFKSEKQSRRQLELKVtsl 723
Cdd:PTZ00121 1679 ----EAKKAEEDEKKAAEALKKeAEEAKKAEELKKKEAEEKKKAEELKKAEEENkikaeEAKKEAEEDKKKAEEAKK--- 1751
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568926925 724 EEEltdlraEKTSLEKNLSERKKKSAQERCQAEA----EMDEIRKSHQEELDR 772
Cdd:PTZ00121 1752 DEE------EKKKIAHLKKEEEKKAEEIRKEKEAvieeELDEEDEKRRMEVDK 1798
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
518-868 |
1.45e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.35 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 518 RMAVNK-----VADKMDHLMTKVEELQK----HSSGNSMLLPSMSVT------METSMIMS--NIQRIIQENERLKQE-- 578
Cdd:pfam10174 54 RISVLKeqyrvTQEENQHLQLTIQALQDelraQRDLNQLLQQDFTTSpvdgedKFSTPELTeeNFRRLQSEHERQAKElf 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 579 LLEKS-----SRIEEQndkisdliernqryvEQSnlmMEKRNNSLQTATENTQARIL--HAEQEKAKVTEELAAATAQVS 651
Cdd:pfam10174 134 LLRKTleemeLRIETQ---------------KQT---LGARDESIKKLLEMLQSKGLpkKSGEEDWERTRRIAEAEMQLG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 652 HLQLKMtahQKKETELQlqltdNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLeeeltdlr 731
Cdd:pfam10174 196 HLEVLL---DQKEKENI-----HLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQML-------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 732 aeKTSLEKNLSERkkksaqercQAEAEMDEIRKSH----QEELDRLRQLL--KKARVSTDQAAAEQLTLAQAElqsqwea 805
Cdd:pfam10174 260 --KTNGLLHTEDR---------EEEIKQMEVYKSHskfmKNKIDQLKQELskKESELLALQTKLETLTNQNSD------- 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568926925 806 kCEQllasardeHLQQYREVCAqrdAHQQKLALLQDECLALQAQI----AAFTEQKEHMQRLEKTKS 868
Cdd:pfam10174 322 -CKQ--------HIEVLKESLT---AKEQRAAILQTEVDALRLRLeekeSFLNKKTKQLQDLTEEKS 376
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
557-821 |
1.46e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.68 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 557 ETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKIsdlIERNQRYVEQSNLMMEKRNnslqtatentqARILHAEQEK 636
Cdd:pfam13868 99 EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEF---NEEQAEWKELEKEEEREED-----------ERILEYLKEK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 637 AKVTEELAaatAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRghVTRLQADLSE-----LREASEQTQTKFKSEKQ 711
Cdd:pfam13868 165 AEREEERE---AEREEIEEEKEREIARLRAQQEKAQDEKAERDELR--AKLYQEEQERkerqkEREEAEKKARQRQELQQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 712 SRR-QLELKVTSLEEELTDLRAEKtslEKNLSERKKKSAQERCQAEAEMdEIRKSHQEELDRLRQLLKKARvstdqAAAE 790
Cdd:pfam13868 240 AREeQIELKERRLAEEAEREEEEF---ERMLRKQAEDEEIEQEEAEKRR-MKRLEHRRELEKQIEEREEQR-----AAER 310
|
250 260 270
....*....|....*....|....*....|.
gi 568926925 791 QLTLAQAELQSQWEAKCEQLLASARDEHLQQ 821
Cdd:pfam13868 311 EEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
615-816 |
1.60e-04 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 46.00 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 615 NNSLQTATENTQA---RILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQAD 691
Cdd:COG5283 13 KSALESAKQRVAAlaqALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQLSAAQRRLRSS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 692 LSELREASEQTQTKFKSEKQSRRQLelkvTSLEEELTDLRAEKTSLEkNLSERKKKSAQERCQAEAEMDEIRKSHQ---- 767
Cdd:COG5283 93 LEQTNRQLERQQQRLARLGARQDRL----KAARARLQRLAGAGAAAA-AIGAALAASVKPAIDFEDAMADVAATVDldks 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568926925 768 -EELDRLRQLLKKA----RVSTDQAAAEQLTLAQAELQSQweakceQLLASARD 816
Cdd:COG5283 168 sEQFKALGKQARELsaqtPQSADDIAAGQAALAQAGVSAE------DILAFTPT 215
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
619-805 |
1.74e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 619 QTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSE---- 694
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 695 -----------------------------LREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERK 745
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 746 KKSAQERcQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEA 805
Cdd:COG3883 175 AQQAEQE-ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
717-865 |
1.84e-04 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 43.74 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 717 ELKVTSLEEELTDL--RAEKTSLE----KNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARvSTDQAAAE 790
Cdd:pfam15619 10 LHKIKELQNELAELqsKLEELRKEnrllKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ-EKERDLER 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568926925 791 QLTLAQAELQSQwEAKCEQLLASARDEHLqqyrevcAQRDAHQQKLALLQDEclaLQaqiaaftEQKEHMQRLEK 865
Cdd:pfam15619 89 KLKEKEAELLRL-RDQLKRLEKLSEDKNL-------AEREELQKKLEQLEAK---LE-------DKDEKIQDLER 145
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
505-906 |
2.05e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 505 FLMTearqHNTEIRMAVNKVADKMDHLMTKVEELqKHSSGNSMLLPSMsVTMETSMIMSNIQRIiqENER---------L 575
Cdd:PRK04863 220 YLLP----ENSGVRKAFQDMEAALRENRMTLEAI-RVTQSDRDLFKHL-ITESTNYVAADYMRH--ANERrvhleealeL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 576 KQELLE-KSSRIEEQNDKIS-----DLIERNQRYVEQSNLMMEKRNNSLQTAtENTQARILHAEQEKAKVTEELAAATAQ 649
Cdd:PRK04863 292 RRELYTsRRQLAAEQYRLVEmarelAELNEAESDLEQDYQAASDHLNLVQTA-LRQQEKIERYQADLEELEERLEEQNEV 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 650 VShlqlkmTAHQKKEtELQLQLTDNLKETDllrghvtRLQADLSELREASEQTQTKFKSEKQSRRQLE----------LK 719
Cdd:PRK04863 371 VE------EADEQQE-ENEARAEAAEEEVD-------ELKSQLADYQQALDVQQTRAIQYQQAVQALErakqlcglpdLT 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 720 VTSLEEELTDLRA-EKTSLEKNLS-ERKKKSAQE-RCQAEAEMDEIRK-----SHQEELDRLRQLLKKARvsTDQAAAEQ 791
Cdd:PRK04863 437 ADNAEDWLEEFQAkEQEATEELLSlEQKLSVAQAaHSQFEQAYQLVRKiagevSRSEAWDVARELLRRLR--EQRHLAEQ 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 792 LT-----LAQAELQSQWEAKCEQLLASARDEHLQQYR---EVCAQRDAHQQKLALLQDECLALQAQ-IAAFTEQKEHMQR 862
Cdd:PRK04863 515 LQqlrmrLSELEQRLRQQQRAERLLAEFCKRLGKNLDdedELEQLQEELEARLESLSESVSEARERrMALRQQLEQLQAR 594
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 568926925 863 LEKTKSQAPAGRAAADPSEKV-----------KKIMNQVFQSLRGEFELEESYDG 906
Cdd:PRK04863 595 IQRLAARAPAWLAAQDALARLreqsgeefedsQDVTEYMQQLLERERELTVERDE 649
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
515-785 |
2.08e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 515 TEIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMETSMIMS--NIQRIiQENERLKQELLEKSSRIEEQNDK 592
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRaaHEARI-RELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 593 ISDLIER--NQRYVEQSnlmmEKRNnsLQTATENTQA--RILHAEQEKAKVTEELAAATAQ-----VSHLQLKMTAHQKK 663
Cdd:pfam07888 155 MKERAKKagAQRKEEEA----ERKQ--LQAKLQQTEEelRSLSKEFQELRNSLAQRDTQVLqlqdtITTLTQKLTTAHRK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 664 ETELQLQLTD--NLKE--------TDLLRG----------------HVTRLQA-----DLSELREASEQTQTKFKSEKQS 712
Cdd:pfam07888 229 EAENEALLEElrSLQErlnaserkVEGLGEelssmaaqrdrtqaelHQARLQAaqltlQLADASLALREGRARWAQERET 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 713 RRQ-----------LELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKS--------------HQ 767
Cdd:pfam07888 309 LQQsaeadkdriekLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASlrvaqkekeqlqaeKQ 388
|
330
....*....|....*...
gi 568926925 768 EELDRLRQLLKKARVSTD 785
Cdd:pfam07888 389 ELLEYIRQLEQRLETVAD 406
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
679-779 |
2.31e-04 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 42.99 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 679 DLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQ----LELKVTSLEEELTDLRAEKTSLE---KNLSERKKKSAQE 751
Cdd:pfam09744 39 ESLASRNQEHNVELEELREDNEQLETQYEREKALRKRaeeeLEEIEDQWEQETKDLLSQVESLEeenRRLEADHVSRLEE 118
|
90 100
....*....|....*....|....*...
gi 568926925 752 RcqaEAEMDEIRKSHQEeldRLRQLLKK 779
Cdd:pfam09744 119 K---EAELKKEYSKLHE---RETEVLRK 140
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
566-805 |
2.45e-04 |
|
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: 44.75 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 566 QRIIQENERLKQELLEKSSRieeqndkisdliernqryveqsnlmmekrnNSLQTATENTqARILHAEQEKAKVTEELAA 645
Cdd:pfam09787 17 ARILQSKEKLIASLKEGSGV------------------------------EGLDSSTALT-LELEELRQERDLLREEIQK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 646 ATAQVSHLQlkmtahqkkeTELQlqltdnlkETDllrghvTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEE 725
Cdd:pfam09787 66 LRGQIQQLR----------TELQ--------ELE------AQQQEEAESSREQLQELEEQLATERSARREAEAELERLQE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 726 ELTDLRAEKtsleknlsERKKKSAQERCQaeaemdeirkSHQEELDRLR-QLLKKARVSTDQAAAE----QLTLAQAELQ 800
Cdd:pfam09787 122 ELRYLEEEL--------RRSKATLQSRIK----------DREAEIEKLRnQLTSKSQSSSSQSELEnrlhQLTETLIQKQ 183
|
....*
gi 568926925 801 SQWEA 805
Cdd:pfam09787 184 TMLEA 188
|
|
| PLC-beta_C |
pfam08703 |
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ... |
687-826 |
2.46e-04 |
|
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.
Pssm-ID: 462571 [Multi-domain] Cd Length: 176 Bit Score: 43.13 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 687 RLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEM------- 759
Cdd:pfam08703 9 RLEQELLELREEQYEQEKKRKEQHLTEQIQKLKELAREKQAAELKALKESSESEKKEMKKKLERKRLESIQEAkkrtsdk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 760 -------DEIRKSH-QEELDRLRQL----------LKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARdEHLQQ 821
Cdd:pfam08703 89 aaqerlkKEINNSHiQEVVQSIKQLeekqkrrqekLEEKQAECLQQIKEEEPQLQAELNAEYEEKLKGLPAEVR-ESVKS 167
|
....*
gi 568926925 822 YREVC 826
Cdd:pfam08703 168 CLKEG 172
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
563-751 |
2.86e-04 |
|
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: 45.44 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 563 SNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNL---------------MMEKRNN----------- 616
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklteeyaelkeeLEDLRAEleevdkefaet 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 617 -----SLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQAD 691
Cdd:TIGR02169 384 rdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 692 LSELREASEQTQTKFksekqsrRQLELKVTSLEEELTDLRAEKTSLEKnlSERKKKSAQE 751
Cdd:TIGR02169 464 LSKYEQELYDLKEEY-------DRVEKELSKLQRELAEAEAQARASEE--RVRGGRAVEE 514
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
601-824 |
3.02e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 601 QRYVEQSNLmmeKRNNSLQTATENtQARILHAEQEKAKVTEELAAATaqvshlQLKMTAHQKKEtELQLQLTDNLKETDL 680
Cdd:pfam01576 811 QRELEEARA---SRDEILAQSKES-EKKLKNLEAELLQLQEDLAASE------RARRQAQQERD-ELADEIASGASGKSA 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 681 LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTdlrAEKTSLEKNLS-----ERKKKSAQERCQa 755
Cdd:pfam01576 880 LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELA---AERSTSQKSESarqqlERQNKELKAKLQ- 955
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568926925 756 eaEMD-EIRKSHQEELDRLRQLLKKARVSTDQAAAEQltLAQAELQSQWEAKCEQLLASARDE--HLQQYRE 824
Cdd:pfam01576 956 --EMEgTVKSKFKSSIAALEAKIAQLEEQLEQESRER--QAANKLVRRTEKKLKEVLLQVEDErrHADQYKD 1023
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
521-769 |
3.33e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.21 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 521 VNKVADKMDHLMTKVEELQ----KHSSGNSMLLPSMSVTMETSMIMSNIQ--------------RIIQENERL------K 576
Cdd:PTZ00440 2317 VKLYIENITHLLNRINTLIndldNYQDENYGKDKNIELNNENNSYIIKTKekinnlkeefskllKNIKRNNTLcnnnniK 2396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 577 QELLEKSSRIEEQNDKISDLIERNQRYV-------EQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQ 649
Cdd:PTZ00440 2397 DFISNIGKSVETIKQRFSSNLPEKEKLHqieenlnEIKNIMNETKRISNVDAFTNKILQDIDNEKNKENNNMNAEKIDDL 2476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 650 VSHLqlkmTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQS-RRQLELKVTSLEE--- 725
Cdd:PTZ00440 2477 IENV----TSHNEKIKSELLIINDALRRVKEKKDEMNKLFNSLTENNNNNNNSAKNIVDNSTYiINELESHVSKLNElls 2552
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568926925 726 ----ELTDLRAEKTSLEKNL---SERKKKSAQERCQAEAEMDEIRKSHQEE 769
Cdd:PTZ00440 2553 yidnEIKELENEKLKLLEKAkieESRKERERIESETQEDNTDEEQINRQQQ 2603
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
569-781 |
3.51e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 569 IQENERLKQEllekssrieeQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQA------RILHAEQEKAKVTEE 642
Cdd:TIGR00606 417 LQSKERLKQE----------QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegssdRILELDQELRKAERE 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 643 LAAA--TAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQ--------- 711
Cdd:TIGR00606 487 LSKAekNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRhsdeltsll 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 712 ----SRRQLELKVTSL-------EEELTDLRAEKTSLEKNL----SERKKKSAQERCQAEAEMDEIRKSHQE-ELDRLRQ 775
Cdd:TIGR00606 567 gyfpNKKQLEDWLHSKskeinqtRDRLAKLNKELASLEQNKnhinNELESKEEQLSSYEDKLFDVCGSQDEEsDLERLKE 646
|
....*.
gi 568926925 776 LLKKAR 781
Cdd:TIGR00606 647 EIEKSS 652
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
618-798 |
3.72e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.86 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 618 LQTATENTQARILHAEQEKAKVTEElaaATAQVSHLqlkmtahqKKETELQlqlTDNLKETDLLRGHvtrlqadlSELRE 697
Cdd:PRK00106 26 MKSAKEAAELTLLNAEQEAVNLRGK---AERDAEHI--------KKTAKRE---SKALKKELLLEAK--------EEARK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 698 ASEQTQTKFKSEKQSRRQLELKVT----SLEEELTDLRAEKTSL---EKNLSErKKKSAQERcqaEAEMDEIRKSHQEEL 770
Cdd:PRK00106 84 YREEIEQEFKSERQELKQIESRLTeratSLDRKDENLSSKEKTLeskEQSLTD-KSKHIDER---EEQVEKLEEQKKAEL 159
|
170 180
....*....|....*....|....*...
gi 568926925 771 DRLRQLlkkarvstDQAAAEQLTLAQAE 798
Cdd:PRK00106 160 ERVAAL--------SQAEAREIILAETE 179
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
565-869 |
4.18e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 565 IQRIIQENER---LKQELLEKSSRIEEQNDKISDLIE---------------RNQRYVEQSNLMMEKRNNSLQTATENTQ 626
Cdd:TIGR04523 67 EEKINNSNNKikiLEQQIKDLNDKLKKNKDKINKLNSdlskinseikndkeqKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 627 ARILHAE--------------------------QEKAKVTEELAAATAQVSHLQLKMTAHQKKE---TELQLQLTDNLKE 677
Cdd:TIGR04523 147 IKKKEKEleklnnkyndlkkqkeelenelnlleKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIqknKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 678 TDLLRGHVTRLQADLSELREASEQTQTKFKSEKQS---------RRQLEL-----KVTSLEE-------ELTDLRAEKTS 736
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkikkqlsEKQKELeqnnkKIKELEKqlnqlksEISDLNNQKEQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 737 -LEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLK--KARVSTDQAAAEQLTLAQAELQS------QWEAKC 807
Cdd:TIGR04523 307 dWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKelTNSESENSEKQRELEEKQNEIEKlkkenqSYKQEI 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568926925 808 EQLLASARD--EHLQQYREVCAQRDahqQKLALLQDECLALQAQI----AAFTEQKEHMQRLEKTKSQ 869
Cdd:TIGR04523 387 KNLESQINDleSKIQNQEKLNQQKD---EQIKKLQQEKELLEKEIerlkETIIKNNSEIKDLTNQDSV 451
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
694-869 |
4.34e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.56 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 694 ELREASEQTQTKFKSEKQSRRQLELKVTSLEEEltdLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKsHQEELDRL 773
Cdd:pfam15709 356 EQEEQRRLQQEQLERAEKMREELELEQQRRFEE---IRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQ-QQEEFRRK 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 774 RQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYRevcaQRDAHQQKlALLQDECLALQAQIAAF 853
Cdd:pfam15709 432 LQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQR----QKQEAEEK-ARLEAEERRQKEEEAAR 506
|
170
....*....|....*.
gi 568926925 854 TEQKEHMQRLEKTKSQ 869
Cdd:pfam15709 507 LALEEAMKQAQEQARQ 522
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
511-779 |
4.85e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.43 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 511 RQHNTEIRMAVNKVADKMDHLMTKVEELQKHSS--GNSML-LPSMSVTMETSMIMSNIQRIIQENERLKQELLEKSSRI- 586
Cdd:pfam10174 474 KKENKDLKEKVSALQPELTEKESSLIDLKEHASslASSGLkKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTn 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 587 EEQNDKISDLIERNQRYVEQSN--------LM-----MEKRNNSLQTATENTQARILHAEQEKAKvteelaaATAQVSHL 653
Cdd:pfam10174 554 PEINDRIRLLEQEVARYKEESGkaqaeverLLgilreVENEKNDKDKKIAELESLTLRQMKEQNK-------KVANIKHG 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 654 QLKMtahQKKETELqlqLTDNLKETDLLRGHVTRLQadLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAE 733
Cdd:pfam10174 627 QQEM---KKKGAQL---LEEARRREDNLADNSQQLQ--LEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAE 698
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568926925 734 KtslEKNLSERKKKSAQERCQAEAEMD------EI----RKSHQEEL-------DRLRQLLKK 779
Cdd:pfam10174 699 R---RKQLEEILEMKQEALLAAISEKDaniallELssskKKKTQEEVmalkrekDRLVHQLKQ 758
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
632-779 |
5.77e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.59 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 632 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQlqltdNLKEtdllrgHVTRLQADLSELREASEQTQTKFKSEKQ 711
Cdd:pfam13851 52 IQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLK-----NLKA------RLKVLEKELKDLKWEHEVLEQRFEKVER 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568926925 712 SRRQLELKvtsLEEELTDLRaEKTSLEKNLSERKKKSAQERC-QAEAEMDEIRKSHQEELDRLRQLLKK 779
Cdd:pfam13851 121 ERDELYDK---FEAAIQDVQ-QKTGLKNLLLEKKLQALGETLeKKEAQLNEVLAAANLDPDALQAVTEK 185
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
713-862 |
6.07e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 713 RRQLELKVTSLEEELTDLRAEKTSLEKnlserkkksAQERCQAEAEMDEIRKSHQE---ELDRLRQLLKKARVSTDQAAA 789
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALED---------AREQIELLEPIRELAERYAAareRLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568926925 790 EQLTLAQAELQSQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQ-QKLAllqdeclALQAQIAAFTEQKEHMQR 862
Cdd:COG4913 291 ELLEAELEELRAELARLEAELerLEARLDALREELDELEAQIRGNGgDRLE-------QLEREIERLERELEERER 359
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
689-877 |
6.89e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 689 QADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEmdEIRKSHQE 768
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAA--AAKAKAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 769 ELDRLRQLLKKARVSTD-QAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLAllqdecLALQ 847
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKkKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA------EAKA 225
|
170 180 190
....*....|....*....|....*....|
gi 568926925 848 AQIAAFTEQKEHMQRLEKTKSQAPAGRAAA 877
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
561-822 |
7.31e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 561 IMSNIQRIIQENERLKQELL--------EKSSRIEEQNDKISDLIERN---QRYVEQSN-------LMMEKRNNSLQTAT 622
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEeldldeaeEKNEEIQERIDQLYDILEREvkaRKYVEKNSdtlpdflEHAKEQNKELKEEI 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 623 ENTQA--RILHAEQEKAK-VTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKE-TDLLRGHVtRLQADLSELRea 698
Cdd:PRK04778 334 DRVKQsyTLNESELESVRqLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQlEEIEKEQE-KLSEMLQGLR-- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 699 seqtqtkfKSEKQSRRQLELKVTSLEEelTDLRAEK---TSLEKNLSERKKKSAQERCQAEAEMDEIRKshqeELDRLRQ 775
Cdd:PRK04778 411 --------KDELEAREKLERYRNKLHE--IKRYLEKsnlPGLPEDYLEMFFEVSDEIEALAEELEEKPI----NMEAVNR 476
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568926925 776 LLKKArvstdQAAAEQLtlaqaelqsqwEAKCEQLLASAR-DEHLQQY 822
Cdd:PRK04778 477 LLEEA-----TEDVETL-----------EEETEELVENATlTEQLIQY 508
|
|
| PRK11570 |
PRK11570 |
peptidyl-prolyl cis-trans isomerase; Provisional |
185-285 |
7.75e-04 |
|
peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 183207 [Multi-domain] Cd Length: 206 Bit Score: 42.09 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 185 LVAAEGPAVETGDSLEVAYTGWLLQnhvlGQVFDSTANKDKPLRLKLGSgkVVKGLEDGLLGMKKGGKRLIITPSACAAG 264
Cdd:PRK11570 109 LTQGEGAIPARTDRVRVHYTGKLID----GTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYG 182
|
90 100
....*....|....*....|.
gi 568926925 265 SEGViGWTQPTDSILVFEVEV 285
Cdd:PRK11570 183 ERGA-GASIPPFSTLVFEVEL 202
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
566-803 |
7.96e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.89 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 566 QRIIQENERLKQELLEKssrIEEQNDKISDL------IERNQRYVEQSNLMMEKRN-------------NSL-QTATENT 625
Cdd:PRK10929 71 QQVIDNFPKLSAELRQQ---LNNERDEPRSVppnmstDALEQEILQVSSQLLEKSRqaqqeqdrareisDSLsQLPQQQT 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 626 QARILHAEQE---KAKVTEELAAATAQVSHLQLKMTAHQKKETELQL-QLTDNLKE------TDLLRGHVTRLQADLSEL 695
Cdd:PRK10929 148 EARRQLNEIErrlQTLGTPNTPLAQAQLTALQAESAALKALVDELELaQLSANNRQelarlrSELAKKRSQQLDAYLQAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 696 ReaseqTQTKFKSEKQSRRQLElKVTSLEEELTDLRAEKTS-LEKN--LSERKKKSAQercqaeaEMDEIrKSHQEeldr 772
Cdd:PRK10929 228 R-----NQLNSQRQREAERALE-STELLAEQSGDLPKSIVAqFKINreLSQALNQQAQ-------RMDLI-ASQQR---- 289
|
250 260 270
....*....|....*....|....*....|....*
gi 568926925 773 lrqllkkarvstdQAAAEQLTLAQA----ELQSQW 803
Cdd:PRK10929 290 -------------QAASQTLQVRQAlntlREQSQW 311
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
561-999 |
8.04e-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: 43.85 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 561 IMSNIQRIIQEnerlKQELLEKSSRIEEQ--NDKISDLierNQRYVEQSNLMMEKRNNSLQTAT-ENTQARILHAEQEKA 637
Cdd:NF033838 63 VESHLEKILSE----IQKSLDKRKHTQNValNKKLSDI---KTEYLYELNVLKEKSEAELTSKTkKELDAAFEQFKKDTL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 638 KVTEELAAATAQVSHLQLKmtAHQKKETELQLQLTDNLK--ETDLLRGHVTRLQADLSELREASEQTQtkfksEKQSRRQ 715
Cdd:NF033838 136 EPGKKVAEATKKVEEAEKK--AKDQKEEDRRNYPTNTYKtlELEIAESDVEVKKAELELVKEEAKEPR-----DEEKIKQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 716 LELKVTSLEEELTDLRAEKTSLEKnlSERKKKSAQERCQAEAEMDEIRKSHQE------------ELDRLRQLLKKARvS 783
Cdd:NF033838 209 AKAKVESKKAEATRLEKIKTDREK--AEEEAKRRADAKLKEAVEKNVATSEQDkpkrrakrgvlgEPATPDKKENDAK-S 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 784 TDQAAAEQlTLAQAELqsqweaKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAqiaAFTEQKEHMQRL 863
Cdd:NF033838 286 SDSSVGEE-TLPSPSL------KPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKTLELEI---AESDVKVKEAEL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 864 EKTKSQAPAGRAaadpSEKVKKIMNQVfQSLRGEfeleesydgGTILRTIMHTIKmvtlqllnhqEEEEEEEEEEEEEKK 943
Cdd:NF033838 356 ELVKEEAKEPRN----EEKIKQAKAKV-ESKKAE---------ATRLEKIKTDRK----------KAEEEAKRKAAEEDK 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568926925 944 PLRPSLEQPGPATPGMP--PAP--------PSGE---TQEAPEVLPEQVVGETTPLPLQALPTPENGAQ 999
Cdd:NF033838 412 VKEKPAEQPQPAPAPQPekPAPkpekpaeqPKAEkpaDQQAEEDYARRSEEEYNRLTQQQPPKTEKPAQ 480
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
563-775 |
9.04e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 563 SNIQRIiqenERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNL--------MMEKRNNSLQTATENTQARILH--- 631
Cdd:COG4913 607 DNRAKL----AALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeysWDEIDVASAEREIAELEAELERlda 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 632 -------AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETD-LLRGHVTRLQADLSELREASEQTq 703
Cdd:COG4913 683 ssddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaAEDLARLELRALLEERFAAALGD- 761
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568926925 704 tkfKSEKQSRRQLELKVTSLEEELTDLRAEktsLEKNLSERKKKSAQERCQAEAEMDEIRkSHQEELDRLRQ 775
Cdd:COG4913 762 ---AVERELRENLEERIDALRARLNRAEEE---LERAMRAFNREWPAETADLDADLESLP-EYLALLDRLEE 826
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
531-826 |
1.08e-03 |
|
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: 43.19 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 531 LMTKVEELQK----HSSGNSmllpsmSVTMETSMIMSNIQRIIQENERLKQELLEKSSRIEEQndkiSDLIERNQRYVeq 606
Cdd:pfam05557 281 LSRRIEQLQQreivLKEENS------SLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRH----KALVRRLQRRV-- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 607 snLMMEKRNNSLQTATENtqariLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQkkeTELQLQLTDNLKETDLLRGHVT 686
Cdd:pfam05557 349 --LLLTKERDGYRAILES-----YDKELTMSNYSPQLLERIEEAEDMTQKMQAHN---EEMEAQLSVAEEELGGYKQQAQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 687 RLQADLSELREASEQTQTKFKSEKQSrrQLELKVTSLEEELTDLRAEKTSLEKNLSER---------KKKSAQERCQAEA 757
Cdd:pfam05557 419 TLERELQALRQQESLADPSYSKEEVD--SLRRKLETLELERQRLREQKNELEMELERRclqgdydpkKTKVLHLSMNPAA 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 758 EMDEIRKSH----QEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEHL--------QQYREV 825
Cdd:pfam05557 497 EAYQQRKNQleklQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLkevfqakiQEFRDV 576
|
.
gi 568926925 826 C 826
Cdd:pfam05557 577 C 577
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
571-869 |
1.09e-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: 43.27 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 571 ENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQ-SNLmmEKRNNSLQTATENTQARILHAEQ---EKAKVTEELAaa 646
Cdd:pfam10174 381 EIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQlAGL--KERVKSLQTDSSNTDTALTTLEEalsEKERIIERLK-- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 647 taqvshlqlkmTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSE----LREASEQTQTKFKS--EKQSR-RQLELK 719
Cdd:pfam10174 457 -----------EQREREDRERLEELESLKKENKDLKEKVSALQPELTEkessLIDLKEHASSLASSglKKDSKlKSLEIA 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 720 VTSLEEELTDLRAE-KTSLEKNLSERKKKSAQERCQA-EAEM----DEIRKShQEELDRLRQLLKKA---RVSTDQ--AA 788
Cdd:pfam10174 526 VEQKKEECSKLENQlKKAHNAEEAVRTNPEINDRIRLlEQEVarykEESGKA-QAEVERLLGILREVeneKNDKDKkiAE 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 789 AEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDEclalqaqiaafteqkEHMQRLEKTKS 868
Cdd:pfam10174 605 LESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLE---------------ELMGALEKTRQ 669
|
.
gi 568926925 869 Q 869
Cdd:pfam10174 670 E 670
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
575-806 |
1.10e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 575 LKQELLEKSSRIEEQNDKISDLIER----NQRYVEQSNLMMEKRNNSLQTATENTQ--ARILHAEQEKAKVTEELAAata 648
Cdd:PRK11637 52 IQQDIAAKEKSVRQQQQQRASLLAQlkkqEEAISQASRKLRETQNTLNQLNKQIDElnASIAKLEQQQAAQERLLAA--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 649 qvshlQLKMTAHQKKETELQLqltdnlketdLLRGHVT----RLQADLSELREASEQTQTKFKsekQSRRQLELKVTSLE 724
Cdd:PRK11637 129 -----QLDAAFRQGEHTGLQL----------ILSGEESqrgeRILAYFGYLNQARQETIAELK---QTREELAAQKAELE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 725 EE-------LTDLRAEKTSLEKNLSERKK------KSAQERCQAEAEMdeirksHQEElDRLRQLLKKARVSTDQAAAEQ 791
Cdd:PRK11637 191 EKqsqqktlLYEQQAQQQKLEQARNERKKtltgleSSLQKDQQQLSEL------RANE-SRLRDSIARAEREAKARAERE 263
|
250
....*....|....*
gi 568926925 792 LTLAQAELQSQWEAK 806
Cdd:PRK11637 264 AREAARVRDKQKQAK 278
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
639-889 |
1.16e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 639 VTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLEL 718
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 719 KVTSLEEELTDLRAEKTSLEKNLSERKKKsaqercqaEAEMDEIRKSHQ-------------EELDRLRQLLKKARVSTD 785
Cdd:COG1340 86 KLNELREELDELRKELAELNKAGGSIDKL--------RKEIERLEWRQQtevlspeeekelvEKIKELEKELEKAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 786 QAAAEQLTLAQA-ELQSQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQI----AAFTEQKE 858
Cdd:COG1340 158 KNEKLKELRAELkELRKEAEEIHKKIkeLAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAdelhEEIIELQK 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 568926925 859 HMQRLEKT-----KSQAPAGRAAADPS--EKVKKIMNQ 889
Cdd:COG1340 238 ELRELRKElkklrKKQRALKREKEKEEleEKAEEIFEK 275
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
562-713 |
1.16e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 562 MSNIQRIIQENERLKQELLEKSSRIEEQN-------DKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQ 634
Cdd:COG4717 346 IEELQELLREAEELEEELQLEELEQEIAAllaeagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 635 EKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDL--LRGHVTRLQADLSEL----------REASEQT 702
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELaeLLQELEELKAELRELaeewaalklaLELLEEA 505
|
170
....*....|.
gi 568926925 703 QTKFKSEKQSR 713
Cdd:COG4717 506 REEYREERLPP 516
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
569-812 |
1.17e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 569 IQENE-RLKQELLEKSSRIEEQNDKISDLIERNQryvEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAAT 647
Cdd:TIGR00606 370 IQSLAtRLELDGFERGPFSERQIKNFHTLVIERQ---EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKK 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 648 AQVSHLQLKMtahQKKETELQlQLTDNLKETDLLRGHVTRLQADLSELREAS--EQTQTKFKSEKQSRRQLELKVTSLEE 725
Cdd:TIGR00606 447 EILEKKQEEL---KFVIKELQ-QLEGSSDRILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQ 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 726 ELTDLRAEKTSLEKNLSERKKKSaqercQAEAEMDEIRKSHQEEL--------------DRLRQLLKKARVSTDQAAAEQ 791
Cdd:TIGR00606 523 EMEQLNHHTTTRTQMEMLTKDKM-----DKDEQIRKIKSRHSDELtsllgyfpnkkqleDWLHSKSKEINQTRDRLAKLN 597
|
250 260
....*....|....*....|....*.
gi 568926925 792 LTLAQAE-----LQSQWEAKCEQLLA 812
Cdd:TIGR00606 598 KELASLEqnknhINNELESKEEQLSS 623
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
557-900 |
1.26e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.97 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 557 ETSMIMSNIQRIIQENERLKQELleKSSRIEE--------------QNDKI----SDLIERNQRYVEQSN---------- 608
Cdd:pfam15964 136 ELSEMKQRVQVVVLENEKLQQEL--KSQTQEEtlreqtlldssgnmQNSWCtpedSRVHQTSKRPASHNLaerlksattg 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 609 ------LMMEKRNNSLQTATENTQARILHAEQ---EKAKVTEEL------------AAATAQVSHLQLKMTAHQ----KK 663
Cdd:pfam15964 214 edekwrLELEKLKLLYEAKTEVLESQVKSLRKdlaESQKTCEDLkerlkhkeslvaASTSSRVGGLCLKCAQHEavlaQT 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 664 ETELQLQLTDNL-KETDLLRGHVTRLQADLSEL--REASEQTQTKFKSEKQSRRQLElKVTSL---EEELTDLRAEKTSL 737
Cdd:pfam15964 294 HTNVHMQTIERLtKERDDLMSALVSVRSSLAEAqqRESSAYEQVKQAVQMTEEANFE-KTKALiqcEQLKSELERQKERL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 738 EKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQ------AAAEQLTLAQAELQSQwEAKCEQLL 811
Cdd:pfam15964 373 EKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKvtreknSLVSQLEEAQKQLASQ-EMDVTKVC 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 812 ASAR----------DEHLQQYREVCA-------------------------QRDAHQQKLALLQDECLALqAQIAAFTEQ 856
Cdd:pfam15964 452 GEMRyqlnqtkmkkDEAEKEHREYRTktgrqleikdqeieklglelseskqRLEQAQQDAARAREECLKL-TELLGESEH 530
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 568926925 857 KEHMQRLEKTKSQAPAGRAAAdpsekvkkimNQVFQSLRGEFEL 900
Cdd:pfam15964 531 QLHLTRLEKESIQQSFSNEAK----------AQALQAQQREQEL 564
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
741-912 |
1.30e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 41.47 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 741 LSERKKKSAQERCQAEAEMDEIRKSHQEELDRLR-QLLKKARVSTDQAAAEQltLAQAELQSQweakceQLLASARDEHL 819
Cdd:COG1390 12 LEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKeEILEKAEREAEREKRRI--ISSAELEAR------KELLEAKEELI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 820 QQYREvcaqrdahqqklallqdeclALQAQIAAFTEQKEHMQRLEKT----KSQAPAGRAAADPSEKVKKIMNQVFQSLR 895
Cdd:COG1390 84 EEVFE--------------------EALEKLKNLPKDPEYKELLKKLlkeaAEELGSGDLVVYVNEKDKELLEELLKELK 143
|
170 180
....*....|....*....|.
gi 568926925 896 GE-FELEE---SYDGGTILRT 912
Cdd:COG1390 144 KKgLEVSEediDILGGVIVES 164
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
631-882 |
1.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 631 HAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEK 710
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 711 QSRRQLELKVTSLE-----EELTDLrAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKkarvstd 785
Cdd:COG3883 93 RALYRSGGSVSYLDvllgsESFSDF-LDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 786 qaaaeQLTLAQAELQSQWEAKcEQLLASARdehlqqyrevcAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEK 865
Cdd:COG3883 165 -----ELEAAKAELEAQQAEQ-EALLAQLS-----------AEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250
....*....|....*..
gi 568926925 866 TKSQAPAGRAAADPSEK 882
Cdd:COG3883 228 AAAAAAAAAAAAAAAAA 244
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
648-869 |
1.35e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 648 AQVSHLQLKMTAHQK-KETELQLQLTDNLKETDL-LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLE---LKVTS 722
Cdd:TIGR00606 187 ALETLRQVRQTQGQKvQEHQMELKYLKQYKEKACeIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnlSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 723 LEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQ 802
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELL 346
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568926925 803 WEAKCEQLLASARDEHLQQYrEVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQ 869
Cdd:TIGR00606 347 VEQGRLQLQADRHQEHIRAR-DSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQ 412
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
569-951 |
1.36e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 569 IQENERLKQELlekssRIEEQNDKISDlIERNQRYVEQsnlmmeKRNNSLQTATENTQARILHAEQEKAKVTEELAAATA 648
Cdd:COG5185 127 KSEIVALKDEL-----IKVEKLDEIAD-IEASYGEVET------GIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 649 QVSHLQLKMTAHQKKETELQLQLTDNLKETdllrghvtrlqADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELT 728
Cdd:COG5185 195 LKKAEPSGTVNSIKESETGNLGSESTLLEK-----------AKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 729 DLRAEKTSLEKNLSERKKKsaqercQAEAEMDEIRKsHQEELDRlrqllkkarvSTDQAAAEQLTLaqaELQSQWEAkce 808
Cdd:COG5185 264 DLRLEKLGENAESSKRLNE------NANNLIKQFEN-TKEKIAE----------YTKSIDIKKATE---SLEEQLAA--- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 809 qllASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQApagRAAADPSEKVKKIMN 888
Cdd:COG5185 321 ---AEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEL---DSFKDTIESTKESLD 394
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568926925 889 QVFQSLRGEFELeesydggtILRTIMHTIKMVTLQLLNHQEEEEEEEEEEEEEKKPLRPSLEQ 951
Cdd:COG5185 395 EIPQNQRGYAQE--------ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISE 449
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
662-777 |
1.39e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.93 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 662 KKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSE--KQSR-----RQLELKVTSLEEELTDLRAEK 734
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERElvLHAEdikalQALREELNELKAEIAELKAEA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568926925 735 TSLEKNLSERKKKSAQERCQAEAEMDEIRKSHqEELDRLRQLL 777
Cdd:pfam07926 81 ESAKAELEESEESWEEQKKELEKELSELEKRI-EDLNEQNKLL 122
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
704-906 |
1.41e-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: 43.29 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 704 TKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKksaqercQAEAEMDEIRKSHQEELDRLRQLLKKARVS 783
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSA-------ELNQLLRTLDDQWKEKRDELNGELSAADAA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 784 TdqaaaeqltlaqaelqsqweAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRL 863
Cdd:pfam12128 317 V--------------------AKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAK 376
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568926925 864 EKTKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEFELEESYDG 906
Cdd:pfam12128 377 YNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQA 419
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
662-897 |
1.46e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 662 KKETELQLQLTDNLKETDLLRGHVtrLQADLSElreaSEQTQTKFKSEKQS--RRQLELKVTSLEEELTDLRAEKTSLE- 738
Cdd:COG5022 823 QKTIKREKKLRETEEVEFSLKAEV--LIQKFGR----SLKAKKRFSLLKKEtiYLQSAQRVELAERQLQELKIDVKSISs 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 739 -KNLSERKKKSAQE-RCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQ---WEAKCEQL--L 811
Cdd:COG5022 897 lKLVNLELESEIIElKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVeskLKETSEEYedL 976
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 812 ASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQiaafTEQKEHMQR-------LEKTKSQAPAGRAAADPSEKVK 884
Cdd:COG5022 977 LKKSTILVREGNKANSELKNFKKELAELSKQYGALQES----TKQLKELPVevaelqsASKIISSESTELSILKPLQKLK 1052
|
250
....*....|...
gi 568926925 885 KIMNQVFQSLRGE 897
Cdd:COG5022 1053 GLLLLENNQLQAR 1065
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
626-802 |
1.71e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 626 QARILHAEQEKAKVTEElAAATAQVshlqlkmtahQKKETELQLQltdnlKETDLLRghvTRLQADLSELREASEQTQTK 705
Cdd:PRK12704 30 EAKIKEAEEEAKRILEE-AKKEAEA----------IKKEALLEAK-----EEIHKLR---NEFEKELRERRNELQKLEKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 706 FKSEKQS-RRQLELkVTSLEEELTDLRAEKTSLEKNLSERKKksaqercqaeaEMDEIRKSHQEELDRLRQLlkkarvST 784
Cdd:PRK12704 91 LLQKEENlDRKLEL-LEKREEELEKKEKELEQKQQELEKKEE-----------ELEELIEEQLQELERISGL------TA 152
|
170
....*....|....*...
gi 568926925 785 DQAAAEQLTLAQAELQSQ 802
Cdd:PRK12704 153 EEAKEILLEKVEEEARHE 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
751-870 |
1.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 751 ERCQAEAEMDEIrKSHQEELDRLRQLLKKARvstdqaaaeqltlAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRD 830
Cdd:COG4913 219 EEPDTFEAADAL-VEHFDDLERAHEALEDAR-------------EQIELLEPIRELAERYAAARERLAELEYLRAALRLW 284
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568926925 831 AHQQKLALLQDECLALQAQIAAFTEQKEhmqRLEKTKSQA 870
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELE---RLEARLDAL 321
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
571-781 |
1.75e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 571 ENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILhaeqEKAKVT--EELAAATA 648
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL----AEAGVEdeEELRAALE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 649 QVSHLQlkmtAHQKKETELQLQLTDNLKETDLLRGhvtrlQADLSELREASEQTQTKfksekqsRRQLELKVTSLEEELT 728
Cdd:COG4717 393 QAEEYQ----ELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEE-------LEELEEELEELREELA 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568926925 729 DLRAEKTSLEKNLSERKKKSAQERCQAEAE---------------MDEIRKSHQEEldRLRQLLKKAR 781
Cdd:COG4717 457 ELEAELEQLEEDGELAELLQELEELKAELRelaeewaalklalelLEEAREEYREE--RLPPVLERAS 522
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
559-798 |
1.82e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.63 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 559 SMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSL---QTATENTQARILHAEQ- 634
Cdd:pfam06008 8 TGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLakaQQVNAESERTLGHAKEl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 635 -EKAK-VTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREAS---EQTQTKFKSE 709
Cdd:pfam06008 88 aEAIKnLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQdllSRIQTWFQSP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 710 KQSRRQLElkvTSLEEELTDLRAEKTSLEKNLSE--RKKKSAQERCQAEAEMDEIRKSHQEELDRLR----QLLKKARVS 783
Cdd:pfam06008 168 QEENKALA---NALRDSLAEYEAKLSDLRELLREaaAKTRDANRLNLANQANLREFQRKKEEVSEQKnqleETLKTARDS 244
|
250
....*....|....*
gi 568926925 784 TDQAAaeqLTLAQAE 798
Cdd:pfam06008 245 LDAAN---LLLQEID 256
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
692-810 |
2.03e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 39.98 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 692 LSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDL-------RAEKTSLEKNLSERKKK---SAQERCQAEA---- 757
Cdd:pfam12718 2 MNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLthknqqlEEEVEKLEEQLKEAKEKaeeSEKLKTNNENltrk 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568926925 758 ------EMDEIRKSHQEELDRLRQllkkarvsTDqAAAEQLTLAQAELQS---QWEAKCEQL 810
Cdd:pfam12718 82 iqlleeELEESDKRLKETTEKLRE--------TD-VKAEHLERKVQALEQerdEWEKKYEEL 134
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
571-824 |
2.03e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 571 ENERLKQELLEKSSRIEEQNDKISDLIER-NQRYVEQSNLmmEKRNNSLQTATENTQARI------LHAEQEKAKVTEEL 643
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERfGDAPVDLGNA--EDFLEELREERDELREREaeleatLRTARERVEEAEAL 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 644 AAA---------TAQVSHLQLKMTAHQKKEtELQLQLTDNLKETDLLRGHVTRLqadlSELREASEQTQTKFKSEKQSRR 714
Cdd:PRK02224 449 LEAgkcpecgqpVEGSPHVETIEEDRERVE-ELEAELEDLEEEVEEVEERLERA----EDLVEAEDRIERLEERREDLEE 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 715 QLELKVTSLEEE---LTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEI------RKSHQEELDRLRqllkkaRVSTD 785
Cdd:PRK02224 524 LIAERRETIEEKrerAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVaelnskLAELKERIESLE------RIRTL 597
|
250 260 270
....*....|....*....|....*....|....*....
gi 568926925 786 QAAAEQLTLAQAELQSQWEAKCEqlLASARDEHLQQYRE 824
Cdd:PRK02224 598 LAAIADAEDEIERLREKREALAE--LNDERRERLAEKRE 634
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
638-880 |
2.19e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.24 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 638 KVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQtkfksekQSRRQLE 717
Cdd:pfam06008 16 KINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTL-------GHAKELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 718 LKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERcQAEAE--MDEIRKshqeeldrlRQLLKKARVSTDQAAAEQLTLA 795
Cdd:pfam06008 89 EAIKNLIDNIKEINEKVATLGENDFALPSSDLSRM-LAEAQrmLGEIRS---------RDFGTQLQNAEAELKAAQDLLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 796 QA-ELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGR 874
Cdd:pfam06008 159 RIqTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETL 238
|
....*.
gi 568926925 875 AAADPS 880
Cdd:pfam06008 239 KTARDS 244
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
654-865 |
2.19e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 654 QLKMTAHQKKETELQLQLTDnlketdllrghvtrLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEEltdlRAE 733
Cdd:PRK02224 191 QLKAQIEEKEEKDLHERLNG--------------LESELAELDEEIERYEEQREQARETRDEADEVLEEHEER----REE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 734 KTSLEKNLSE-RKKKSAQERcQAEAEMDEIRkSHQEELDRLRQLLKKARVST--DQAAAEQLTLAQAELQSQwEAKCEQL 810
Cdd:PRK02224 253 LETLEAEIEDlRETIAETER-EREELAEEVR-DLRERLEELEEERDDLLAEAglDDADAEAVEARREELEDR-DEELRDR 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568926925 811 LASAR---DEHLQQYREVCAQRDAHQQKLALLQDECLALQAQI----AAFTEQKEHMQRLEK 865
Cdd:PRK02224 330 LEECRvaaQAHNEEAESLREDADDLEERAEELREEAAELESELeearEAVEDRREEIEELEE 391
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
302-497 |
2.24e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 42.45 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 302 SSRDSAAPSPIPASDSLSADPVVTPLPLPLKPGEPGLRsksnslseqlTVNSNPDTVKAKLISRMAKMgQPMLPILPPQl 381
Cdd:pfam03154 192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT----------LIQQTPTLHPQRLPSPHPPL-QPMTQPPPPS- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 382 dSNDSETEDATVLRGAGQSLVTP-SIQPSLQPaHPVLPQMASQAPQPSGSglQTPSAAlmqavsldshsavsgnaqnfQP 460
Cdd:pfam03154 260 -QVSPQPLPQPSLHGQMPPMPHSlQTGPSHMQ-HPVPPQPFPLTPQSSQS--QVPPGP--------------------SP 315
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568926925 461 YAGVQAYAYPQTPSVTSQLQP-----VRPLYPAPLSQaPHFQ 497
Cdd:pfam03154 316 AAPGQSQQRIHTPPSQSQLQSqqpprEQPLPPAPLSM-PHIK 356
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
601-869 |
2.56e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 601 QRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAataqvshLQLKMTAHQkketelqlqltdnlketdl 680
Cdd:PRK10246 238 AQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAA-------LSLAQPARQ------------------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 681 LRGHVTRLQ---ADLSELREASEQTQTKFKSEKQSRRQLElkvTSLEEELTDLRAEKTSLEKNLSE--RKKKSAQERCQA 755
Cdd:PRK10246 292 LRPHWERIQeqsAALAHTRQQIEEVNTRLQSTMALRARIR---HHAAKQSAELQAQQQSLNTWLAEhdRFRQWNNELAGW 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 756 EAEMDEiRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAElqsqweakceqlLASARDEHLQQ--YRE----VCAQR 829
Cdd:PRK10246 369 RAQFSQ-QTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADE------------VAAALAQHAEQrpLRQrlvaLHGQI 435
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568926925 830 DAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQ 869
Cdd:PRK10246 436 VPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQ 475
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
606-878 |
2.59e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 606 QSNLMMEKRNNSLQTATENTQARilHAEQEkakvtEELAAATAQVSHLQLKMT--AHQKKETELQLQLTDNLKETDLLRG 683
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREK--QAAAE-----EQLVQANGELEKASREETfaRTALKNARLDLRRLFDEKQSEKDKK 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 684 HvtrlQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNL-SERKKKSAQ-------ERCQA 755
Cdd:pfam12128 670 N----KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVeGALDAQLALlkaaiaaRRSGA 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 756 EAEMDEIRKSHQEELDRLR-QLLKKARVSTDQAAAEQlTLAQAelqsqweAKCEQLLASARDEHLQQYREvcaQRDAHQQ 834
Cdd:pfam12128 746 KAELKALETWYKRDLASLGvDPDVIAKLKREIRTLER-KIERI-------AVRRQEVLRYFDWYQETWLQ---RRPRLAT 814
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568926925 835 KLALLQDECLALQAQIAAFTEQKEhmQRLEKTKSQAPAGRAAAD 878
Cdd:pfam12128 815 QLSNIERAISELQQQLARLIADTK--LRRAKLEMERKASEKQQV 856
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
681-779 |
2.61e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.61 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 681 LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQercqaeaemd 760
Cdd:pfam11559 64 LEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAH---------- 133
|
90
....*....|....*....
gi 568926925 761 EIRKsHQEELDRLRQLLKK 779
Cdd:pfam11559 134 EVKK-RDREIEKLKERLAQ 151
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
684-866 |
2.74e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 41.09 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 684 HVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRaekTSLEKnlsERKKKSAQeRCQAEAEMDEIR 763
Cdd:pfam15397 61 NKKQLQQAKAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLS---TYKDK---EYPVKAVQ-IANLVRQLQQLK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 764 KSHQEELDRLRQLLKKARvstdqaaaeqltlaqAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLAllqdEC 843
Cdd:pfam15397 134 DSQQDELDELEEMRRMVL---------------ESLSRKIQKKKEKILSSLAEKTLSPYQESLLQKTRDNQVML----KE 194
|
170 180
....*....|....*....|...
gi 568926925 844 LALQAQIAAftEQKEHMQRLEKT 866
Cdd:pfam15397 195 IEQFREFID--ELEEEIPKLKAE 215
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
562-856 |
2.74e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 562 MSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEkrnnSLQTATE--------NTQARILHAE 633
Cdd:TIGR00606 321 LVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQ----SLATRLEldgfergpFSERQIKNFH 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 634 QEKAKVTEELAAATAQ-VSHLQLKMTAHQKKETELQLQLTDNLKetdLLRGHVTRLQADLSELREASEQTQtkfKSEKQS 712
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQlCADLQSKERLKQEQADEIRDEKKGLGR---TIELKKEILEKKQEELKFVIKELQ---QLEGSS 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 713 RRQLElkvtsLEEELTDLRAEKTSLEKN-LSERKKKSAQERCQAEAEMDEIRKSHQEELDRLR---------QLLKKARV 782
Cdd:TIGR00606 471 DRILE-----LDQELRKAERELSKAEKNsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttrtqmEMLTKDKM 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 783 STDQAAAEQLTLAQAELQSQ-----WEAKCEQLLASARDEhLQQYREVCAQRDAHQQKLALLQ----DECLALQAQIAAF 853
Cdd:TIGR00606 546 DKDEQIRKIKSRHSDELTSLlgyfpNKKQLEDWLHSKSKE-INQTRDRLAKLNKELASLEQNKnhinNELESKEEQLSSY 624
|
...
gi 568926925 854 TEQ 856
Cdd:TIGR00606 625 EDK 627
|
|
| PRK15095 |
PRK15095 |
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
214-266 |
3.24e-03 |
|
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
Pssm-ID: 237908 [Multi-domain] Cd Length: 156 Bit Score: 39.69 E-value: 3.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568926925 214 GQVFDSTANKDKPLRLKLGSGKVVKGLEDGLLGMKKGGKRLIITPSACAAGSE 266
Cdd:PRK15095 22 GSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVP 74
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
533-779 |
3.55e-03 |
|
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: 41.54 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 533 TKVEELQKH-SSGNSMLLpsmSVTMETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDL--------------- 596
Cdd:TIGR04523 482 QNLEQKQKElKSKEKELK---KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLedelnkddfelkken 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 597 ----IERNQRYVEQsnlmMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLT 672
Cdd:TIGR04523 559 lekeIDEKNKEIEE----LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 673 DnlketdllrghvtrLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDL-RAEKTSL-EKNLSERKKKSAQ 750
Cdd:TIGR04523 635 N--------------IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIiELMKDWLkELSLHYKKYITRM 700
|
250 260
....*....|....*....|....*....
gi 568926925 751 ERCQAEAEMDEIRKSHQEELDRLRQLLKK 779
Cdd:TIGR04523 701 IRIKDLPKLEEKYKEIEKELKKLDEFSKE 729
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
668-800 |
4.27e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.82 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 668 QLQLTDNLKET----DLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTslekNLSE 743
Cdd:pfam10473 5 QLHVLEKLKESerkaDSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLV----TLRS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568926925 744 RKKKSAQERCQAEAEMDEIRKSHqEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQ 800
Cdd:pfam10473 81 EKENLTKELQKKQERVSELESLN-SSLENLLEEKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
562-864 |
4.30e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 562 MSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSlqtatENTQARILHAEQEKAKVTE 641
Cdd:PRK01156 182 ISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNL-----KSALNELSSLEDMKNRYES 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 642 ELAAATAQVSHLQLKMTAHQKKETELQlQLTDN--LKETDLLRGHVTrLQADLSELREASEQTQTKFKSEKQSRRQLEL- 718
Cdd:PRK01156 257 EIKTAESDLSMELEKNNYYKELEERHM-KIINDpvYKNRNYINDYFK-YKNDIENKKQILSNIDAEINKYHAIIKKLSVl 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 719 ------------KVTSLEEELTDLRAEKT---SLEKNLSERKKKSAQERCQAE---AEMDEIRKSHQEELDRLRQLLKKA 780
Cdd:PRK01156 335 qkdyndyikkksRYDDLNNQILELEGYEMdynSYLKSIESLKKKIEEYSKNIErmsAFISEILKIQEIDPDAIKKELNEI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 781 RVSTDQAAAEqltlaQAELQSQWEAKCEQLLASARDEHLQQYREVCAQ-------------RDAHQQKLALLQDECLALQ 847
Cdd:PRK01156 415 NVKLQDISSK-----VSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgttlgeeksnhiINHYNEKKSRLEEKIREIE 489
|
330
....*....|....*..
gi 568926925 848 AQIAAFTEQKEHMQRLE 864
Cdd:PRK01156 490 IEVKDIDEKIVDLKKRK 506
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
570-842 |
4.35e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.74 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 570 QENERLKQELLEKSSRIEEQNDKISDLIERN----QRYVEQSNLMMEKRNNSLQTATENT--QARI------LHAEQEKA 637
Cdd:PTZ00440 560 KLKRSMKNDIKNKIKYIEENVDHIKDIISLNdeidNIIQQIEELINEALFNKEKFINEKNdlQEKVkyilnkFYKGDLQE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 638 KVTEEL------------AAATAQVSHLQLKMTAHQKKETELQL----QLTDNLKetdllrghvTRLQaDLSELREA--S 699
Cdd:PTZ00440 640 LLDELShflddhkylyheAKSKEDLQTLLNTSKNEYEKLEFMKSdnidNIIKNLK---------KELQ-NLLSLKENiiK 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 700 EQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLE---KNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQL 776
Cdd:PTZ00440 710 KQLNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEvykHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTI 789
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 777 LKKARVSTDQAAA--EQLTLAQAELQSqWEAKCEQLLASAR--DEHLQQYREVCAQRDahqQKLALLQDE 842
Cdd:PTZ00440 790 LNKENKISNDINIlkENKKNNQDLLNS-YNILIQKLEAHTEknDEELKQLLQKFPTED---ENLNLKELE 855
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
574-824 |
4.38e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 40.78 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 574 RLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQ---TATENTQARILHAEQEKAKVTEELAAATAQV 650
Cdd:pfam04849 87 RIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQiysNDAEESETESSCSTPLRRNESFSSLHGCVQL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 651 SHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADL-SELREASeqTQTKFKSEkqsrrQLELKVtsleEELTD 729
Cdd:pfam04849 167 DALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCvEQLSEAN--QQMAELSE-----ELARKM----EENLR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 730 LRAEKTSLEKNLSErkkksAQERCqaeaemdeirKSHQEELDRLRQLLKKARvstdqAAAEQLTLAQAELQSQWeAKCEQ 809
Cdd:pfam04849 236 QQEEITSLLAQIVD-----LQHKC----------KELGIENEELQQHLQASK-----EAQRQLTSELQELQDRY-AECLG 294
|
250
....*....|....*
gi 568926925 810 LLASARDEhLQQYRE 824
Cdd:pfam04849 295 MLHEAQEE-LKELRK 308
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
512-708 |
4.51e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 40.03 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 512 QHNTEIRMAVNKVADKMDHLMTKVEE---LQKHSSgnsmllpsmsvTMETSmimsniqriIQENERLKQELLEK----SS 584
Cdd:pfam15665 22 AHEEEIQQILAETREKILQYKSKIGEeldLKRRIQ-----------TLEES---------LEQHERMKRQALTEfeqyKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 585 RIEEQNDKISDliERNQRYVEQSNLMMEKRNN---SLQTATENTQArilhAEQEKAKVTEELAAATAQ-VSHLQLKMTAH 660
Cdd:pfam15665 82 RVEERELKAEA--EHRQRVVELSREVEEAKRAfeeKLESFEQLQAQ----FEQEKRKALEELRAKHRQeIQELLTTQRAQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568926925 661 QKKETELQLQLTDNLK-ETDLLRGHVTRLQADLSELREASEQTQTKFKS 708
Cdd:pfam15665 156 SASSLAEQEKLEELHKaELESLRKEVEDLRKEKKKLAEEYEQKLSKAQA 204
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
566-884 |
4.70e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 566 QRIIQEN----ERLKQELLEKSSRIEEQNDKisDLIERNQ---RYVEQSNLMMEKrnnsLQTATEnTQARILhAEQEKAK 638
Cdd:NF041483 104 QRILQEHaehqARLQAELHTEAVQRRQQLDQ--ELAERRQtveSHVNENVAWAEQ----LRARTE-SQARRL-LDESRAE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 639 VTEELAAATAQVShlQLKMTAHQKKETELQLQLTDnlKETDLLRGHVTR---LQADLSELREAS---EQTQTKFKSE-KQ 711
Cdd:NF041483 176 AEQALAAARAEAE--RLAEEARQRLGSEAESARAE--AEAILRRARKDAerlLNAASTQAQEATdhaEQLRSSTAAEsDQ 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 712 SRRQL-------ELKVTSLEEELTDLRAEKtslEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVST 784
Cdd:NF041483 252 ARRQAaelsraaEQRMQEAEEALREARAEA---EKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEAL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 785 dQAAAEQLtLAQAelqsqwEAKCEQLLASARDehlqQYREVCAQRDAHQ-QKLALLQDECLA-----LQAQIAAFTEQKE 858
Cdd:NF041483 329 -KAEAEQA-LADA------RAEAEKLVAEAAE----KARTVAAEDTAAQlAKAARTAEEVLTkasedAKATTRAAAEEAE 396
|
330 340
....*....|....*....|....*....
gi 568926925 859 HMQRlektKSQAPAGR---AAADPSEKVK 884
Cdd:NF041483 397 RIRR----EAEAEADRlrgEAADQAEQLK 421
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
679-781 |
4.88e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 679 DLLRGHVTRLQADLSELREASEQTQTKFKSEKQSR-RQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEA 757
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEERELTEEEEEiRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100
....*....|....*....|....*.
gi 568926925 758 EMDEIRK--SHQEELDRLRQLLKKAR 781
Cdd:COG2433 460 EIRKDREisRLDREIERLERELEEER 485
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
633-752 |
6.06e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.81 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 633 EQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTD-----NLKETDL---------LRGHVTRLQADLSELREA 698
Cdd:pfam05911 694 KSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASlkesnSLAETQLkcmaesyedLETRLTELEAELNELRQK 773
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568926925 699 SEQTQTKFKSEKQSRRQLELKVTSLEEELTdlRAEKTSLEKNL-SERKKKSAQER 752
Cdd:pfam05911 774 FEALEVELEEEKNCHEELEAKCLELQEQLE--RNEKKESSNCDaDQEDKKLQQEK 826
|
|
| SYCE1 |
pfam15233 |
Synaptonemal complex central element protein 1; This family of proteins includes synaptonemal ... |
628-764 |
6.17e-03 |
|
Synaptonemal complex central element protein 1; This family of proteins includes synaptonemal complex central element protein 1, a component of the synaptonemal complex involved in meiosis, and synaptonemal complex central element protein 1-like, which may be involved in meiosis.
Pssm-ID: 464575 [Multi-domain] Cd Length: 152 Bit Score: 38.64 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 628 RILHAEQEKAKVTEELAAATAQVSHLQ------------LKMTAHQKKETELQLQLTDNLKETDLLRGHvtrlqADLSEL 695
Cdd:pfam15233 13 RINELQQAKKKSSEELGEAQALWEALQreldslngekvhLEEVLNKKQEALRILQLHCQEKESEAQRQH-----TLNEEC 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568926925 696 REASEQTQTKFKSEKQSRRQLELKVtslEEELTDLraekTSLEKNLSE--RKKKSAQERCQAEAEMDEIRK 764
Cdd:pfam15233 88 KQRIEQYTFQIQEEKLKHRKQRMDF---EEQLEDL----MEQHKDLWEfhVPQRLAREIRALESSKEQLLK 151
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
620-877 |
6.23e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.94 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 620 TATENTQARILHAEQEK-----AKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQA---- 690
Cdd:PRK10246 407 TADEVAAALAQHAEQRPlrqrlVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTiceq 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 691 -----DLSELRE-----------------ASEQTQTKFKSEKQSRR-QLELKVTSLEEELTDLRAEKTSLEKNLsERKKK 747
Cdd:PRK10246 487 earikDLEAQRAqlqagqpcplcgstshpAVEAYQALEPGVNQSRLdALEKEVKKLGEEGAALRGQLDALTKQL-QRDES 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 748 SAQERCQAEAEM------------------DEI------RKSHQEELDRLRQllKKARVSTDQAAAEQLTLAQAELQSQW 803
Cdd:PRK10246 566 EAQSLRQEEQALtqqwqavcaslnitlqpqDDIqpwldaQEEHERQLRLLSQ--RHELQGQIAAHNQQIIQYQQQIEQRQ 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 804 EAKCEQLLA---------------SARDEHLQQYREVCAQRDAHQQKLALLQ---------------------------- 840
Cdd:PRK10246 644 QQLLTALAGyaltlpqedeeaswlATRQQEAQSWQQRQNELTALQNRIQQLTplletlpqsddlphseetvaldnwrqvh 723
|
330 340 350
....*....|....*....|....*....|....*...
gi 568926925 841 DECLALQAQIAAFTEQK-EHMQRLEKTKSQAPAGRAAA 877
Cdd:PRK10246 724 EQCLSLHSQLQTLQQQDvLEAQRLQKAQAQFDTALQAS 761
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
565-784 |
7.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 565 IQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQsnlMMEKRN--NSLQTATENTQARILHAEQEKAKVTEE 642
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE---AEEKREaaAEAEEEAEEAREEVAELNSKLAELKER 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 643 L-------------AAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRG-----HVTRLQADLSELREASEQTQT 704
Cdd:PRK02224 588 IeslerirtllaaiADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAefdeaRIEEAREDKERAEEYLEQVEE 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 705 KFKSEKQSRRQLELKVTSLEEELTDLraektsleKNLSERkKKSAQERCQA-EAEMDEIrkshqEELD----RLRQLLKK 779
Cdd:PRK02224 668 KLDELREERDDLQAEIGAVENELEEL--------EELRER-REALENRVEAlEALYDEA-----EELEsmygDLRAELRQ 733
|
....*
gi 568926925 780 ARVST 784
Cdd:PRK02224 734 RNVET 738
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
507-783 |
7.16e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 507 MTEARQHNTEIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMETSMImsniqriiqenERLkQELLEKSSRI 586
Cdd:PRK04863 839 LRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLA-----------DRV-EEIREQLDEA 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 587 EEqnDKISdlIERNQRYVEQsnlmMEKRNNSLQTATEN---TQARILHAEQEKAKVTEELAAATAQVSHLqlkmtAHQKK 663
Cdd:PRK04863 907 EE--AKRF--VQQHGNALAQ----LEPIVSVLQSDPEQfeqLKQDYQQAQQTQRDAKQQAFALTEVVQRR-----AHFSY 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 664 ETELQLqLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKF----------KSEKQSRRQLelkVTSLEEELTDL--- 730
Cdd:PRK04863 974 EDAAEM-LAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLaqynqvlaslKSSYDAKRQM---LQELKQELQDLgvp 1049
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568926925 731 ---------RAEKTSLEKNLSE-RKKKSAQERCQA--EAEMDEIRK---SHQEELDRLRQLLKKARVS 783
Cdd:PRK04863 1050 adsgaeeraRARRDELHARLSAnRSRRNQLEKQLTfcEAEMDNLTKklrKLERDYHEMREQVVNAKAG 1117
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
302-495 |
7.33e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.69 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 302 SSRDSAAPSPIPASDSLSADPVVTPLPLPLKPGEPGlrskSNSLSEQLTVNSNPDTVKAKLISRMAKMGQPMLPILPPQ- 380
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHP----PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQr 2682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 381 ----------------LDSNDSETEDATVLRGAGQSLVTPSIQPSLQPAHPVLPqmASQAPQPSGSGLQTPSAALMQAvs 444
Cdd:PHA03247 2683 prrraarptvgsltslADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALP--AAPAPPAVPAGPATPGGPARPA-- 2758
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568926925 445 ldSHSAVSGNAQNFQPYAGVQAYAYPQTPSVTSQLQPVRPLYPAPLSQAPH 495
Cdd:PHA03247 2759 --RPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP 2807
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
508-785 |
7.39e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 508 TEARQHNT---EIRMAVNKVADKMDHLMTKV----EELQKHSSgnsmllpsmsvtmETSMIMSNIQRIIQENERLKQELL 580
Cdd:COG1340 22 EEIEELKEkrdELNEELKELAEKRDELNAQVkelrEEAQELRE-------------KRDELNEKVKELKEERDELNEKLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 581 EKSSRIEEQN-------------DKISDLIERNQRYVEQSNLMMEKRNNSLQTATEntQARILHAEQEKAKVTEELAAAT 647
Cdd:COG1340 89 ELREELDELRkelaelnkaggsiDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKE--LEKELEKAKKALEKNEKLKELR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 648 AQVSHLQLKM-TAHQKKET------ELQLQLTDNLKETDllrghvtrlqadlsELREASEQTQTKFKSEKQSRRQLELKV 720
Cdd:COG1340 167 AELKELRKEAeEIHKKIKElaeeaqELHEEMIELYKEAD--------------ELRKEADELHKEIVEAQEKADELHEEI 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568926925 721 TSLEEELTDLRAEKTSLEKNLSERKKKSAQErcqaeaemdEIRKSHQEELDRLRqllKKARVSTD 785
Cdd:COG1340 233 IELQKELRELRKELKKLRKKQRALKREKEKE---------ELEEKAEEIFEKLK---KGEKLTTE 285
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
672-831 |
7.48e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.58 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 672 TDNLKETDLLRGHVTRLQADL-SELREASEQTQTKFKSEKQSRR-----QLELKVTSLEEELTDLRAEK----TSLEKNL 741
Cdd:NF041483 909 SDAAAQADRLIGEATSEAERLtAEARAEAERLRDEARAEAERVRadaaaQAEQLIAEATGEAERLRAEAaetvGSAQQHA 988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 742 SERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTlaqaELQSQWEAKCEQLLASARDEHLQQ 821
Cdd:NF041483 989 ERIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQAD----TLITEAAAEADQLTAKAQEEALRT 1064
|
170
....*....|
gi 568926925 822 YREVCAQRDA 831
Cdd:NF041483 1065 TTEAEAQADT 1074
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
632-840 |
7.80e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 39.28 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 632 AEQEKAKVTEELAAATAQV--SHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQaDLSELREASEQTQTKFKSe 709
Cdd:pfam04012 34 MQSELVKARQALAQTIARQkqLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEKK-SLEKQAEALETQLAQQRS- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 710 kqSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKkksaqercqaeaemdeirksHQEELDrlrQLLKKARVSTDQAAA 789
Cdd:pfam04012 112 --AVEQLRKQLAALETKIQQLKAKKNLLKARLKAAK--------------------AQEAVQ---TSLGSLSTSSATDSF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568926925 790 EQLTLAQAELQSQWEAKCEqlLASARDEhLQQYREVCAQRDAHQQKLALLQ 840
Cdd:pfam04012 167 ERIEEKIEEREARADAAAE--LASAVDL-DAKLEQAGIQMEVSEDVLARLK 214
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
718-852 |
8.29e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 718 LKVTSLEEELTDLRAEKTSLEKnlserkkksaqERCQAEAEMDEirkSHQEELDRLRQLLKKARvstdqaaaEQLtlaqA 797
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEI-----------EKEALKKEQDE---ASFERLAELRDELAELE--------EEL----E 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568926925 798 ELQSQWEakceqllasARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAA 852
Cdd:COG0542 458 ALKARWE---------AEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAE 503
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
696-809 |
8.42e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 38.48 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 696 REASEQT----QTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKnlsERKKKSAQERCQAEAEMDEIRKSHQEELD 771
Cdd:pfam05672 21 RQAREQRereeQERLEKEEEERLRKEELRRRAEEERARREEEARRLEE---ERRREEEERQRKAEEEAEEREQREQEEQE 97
|
90 100 110
....*....|....*....|....*....|....*...
gi 568926925 772 RLRQLLKKARVSTdQAAAEQLTLAQAELQSQWEAKCEQ 809
Cdd:pfam05672 98 RLQKQKEEAEAKA-REEAERQRQEREKIMQQEEQERLE 134
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
309-501 |
9.13e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.69 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 309 PSPIPASDSLSADPVVTPLPL--PLKPGEPglrsksnsLSEQLTVNSNPDTVKAKLISRMAKMGQPMLPilpPQLDSnds 386
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLggSVAPGGD--------VRRRPPSRSPAAKPAAPARPPVRRLARPAVS---RSTES--- 2897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 387 etedatvlrgagQSLVTPSIQPSLQPAHPVLPQMASQAPQPSGSGLQTPSAALMQA-VSLDSHSAVSGNAQNFQPYAGVQ 465
Cdd:PHA03247 2898 ------------FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPpLAPTTDPAGAGEPSGAVPQPWLG 2965
|
170 180 190
....*....|....*....|....*....|....*.
gi 568926925 466 AYAYPQTPSVTSQLQPVRPLYPAPLSQAPHFQGSGD 501
Cdd:PHA03247 2966 ALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSL 3001
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
570-777 |
9.43e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.52 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 570 QENERLkQEL-------LEKSSRIEEQND----KISDLIERNQRYVEQSNLMMEK-----RNNSLQTATENTQARI---- 629
Cdd:pfam00038 1 NEKEQL-QELndrlasyIDKVRFLEQQNKlletKISELRQKKGAEPSRLYSLYEKeiedlRRQLDTLTVERARLQLeldn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 630 --LHAEQEKAKVTEELA-----------------AATAQVSHLQLKMTA-----------HQKKETELQLQLTDN--LKE 677
Cdd:pfam00038 80 lrLAAEDFRQKYEDELNlrtsaendlvglrkdldEATLARVDLEAKIESlkeelaflkknHEEEVRELQAQVSDTqvNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 678 TDLLRGhvTRLQADLSELR------------EASEQTQTKF-----------------KSE-KQSRRQLElkvtSLEEEL 727
Cdd:pfam00038 160 MDAARK--LDLTSALAEIRaqyeeiaaknreEAEEWYQSKLeelqqaaarngdalrsaKEEiTELRRTIQ----SLEIEL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568926925 728 TDLRAEKTSLEKNLSERKKKSAQERCQA-------EAEMDEIRKSHQEELDRLRQLL 777
Cdd:pfam00038 234 QSLKKQKASLERQLAETEERYELQLADYqeliselEAELQETRQEMARQLREYQELL 290
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
664-779 |
9.48e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 664 ETELQLQLTDNLKETDLLRGHVTRLQADLSELR-------EASEQTQTKFKSEKQSRRQLELKvtslEEELTDLRAEKTS 736
Cdd:COG2433 401 KEHEERELTEEEEEIRRLEEQVERLEAEVEELEaeleekdERIERLERELSEARSEERREIRK----DREISRLDREIER 476
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568926925 737 LEKNLserkkksaqercqaeAEMDEIRKSHQEELDRLRQLLKK 779
Cdd:COG2433 477 LEREL---------------EEERERIEELKRKLERLKELWKL 504
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
570-951 |
9.51e-03 |
|
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: 40.34 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 570 QENERLKQEL-LEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQtatentQARILHAEQEKAKVTEELAAATA 648
Cdd:TIGR00618 386 QQKTTLTQKLqSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQ------QRYAELCAAAITCTAQCEKLEKI 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 649 QVSHLQLKMTAHQKKETELQlQLTDNLKETDLLRGHVTRLQADL------SELREASEQTQTKFKSEKQSR-RQLELKVT 721
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKE-QIHLQETRKKAVVLARLLELQEEpcplcgSCIHPNPARQDIDNPGPLTRRmQRGEQTYA 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 722 SLEEELTDLRAEKTSLEKNLSERKKKsAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQaELQS 801
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQ-MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC-EQHA 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 802 QWEAKCEQLlasaRDEHLQQYREVCAQRDahQQKLALLQDECLALQAQiaaftEQKEHMQRLEKTKSQAPAGRAAADPSE 881
Cdd:TIGR00618 617 LLRKLQPEQ----DLQDVRLHLQQCSQEL--ALKLTALHALQLTLTQE-----RVREHALSIRVLPKELLASRQLALQKM 685
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 882 KVKKimnqvfQSLRGEFELeesydggtilrtimhtikmvtlqlLNHQEEEEEEEEEEEEEKKPLRPSLEQ 951
Cdd:TIGR00618 686 QSEK------EQLTYWKEM------------------------LAQCQTLLRELETHIEEYDREFNEIEN 725
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
638-824 |
9.76e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 38.40 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 638 KVTEELAAATAQVSHLQLKMtAHQKKETELQLqltdnLKETDLLRGhvtRLQADLSELREASEQTQTKFKSEKQSR-RQL 716
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQL-GPVAQELVDRL-----EKETEALRE---RLQKDLEEVRAKLEPYLEELQAKLGQNvEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926925 717 ELKVTSLEEELTDLRAEKT-SLEKNLSErkkKSAQERCQAEAEMDEIRKSHQEELDRLRQLLkKARVstdQAAAEQLTLA 795
Cdd:pfam01442 72 RQRLEPYTEELRKRLNADAeELQEKLAP---YGEELRERLEQNVDALRARLAPYAEELRQKL-AERL---EELKESLAPY 144
|
170 180
....*....|....*....|....*....
gi 568926925 796 QAELQSQWEAKCEQLLASArDEHLQQYRE 824
Cdd:pfam01442 145 AEEVQAQLSQRLQELREKL-EPQAEDLRE 172
|
|
|